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Cerebral Amyloid Angiopathy, App-Related OMIM

A number sign (#) is used with this entry because cerebral amyloid angiopathy (CAA) can be caused by mutation in the gene encoding the amyloid precursor protein (APP; 104760). Mutations in the APP gene can also cause autosomal dominant Alzheimer disease-1 (AD1; 104300), which shows overlapping clinical and neuropathologic features. ... Revesz et al. (2003) reviewed the pathology and genetics of APP-related CAA and discussed the different neuropathologic consequences of different APP mutations. ... In 4 affected members of an Italian family with cerebral amyloid angiopathy, Obici et al. (2005) identified a mutation in the APP gene (104760.0019). In 2 brothers from an extensive Iowa kindred with progressive dementia and cerebroarterial amyloidosis, Grabowski et al. (2001) identified a heterozygous mutation in the APP gene (N694D; 104760.0016). ... Human APP mRNA was detected in neurons and neuronal processes, but not in vessel walls. ... Herzig et al. (2006) extended their earlier studies by developing several murine models of APP-related CAA and APP-related parenchymal amyloid deposition.

APP, APOE, PAOX, SMOX, DELEC1, TSHZ1, SCRN1, BHLHE40, TGFBR2, TGFB1, PSEN1, SERPINF2, SERPINF1, NOTCH3, SMAD2, LAMC2, CST3, CSF2, CRP, LINC01672
- Abeta Amyloidosis, Iowa Type Orphanet
  
  This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.
- Abeta Amyloidosis, Dutch Type Orphanet
  
  Etiology HCHWA-D is due to a mutation in the APP gene on chromosome 21q21.2, encoding the beta-amyloid precursor protein. ... Genetic testing reveals a mutation in the APP gene. Differential diagnosis Differential diagnoses include other conditions that could cause intracerebral hemorrhage such as coagulopathies, vasculitis (see these terms), CNS neoplasms, cerebral vascular malformations, ischemic stroke and antecedent trauma.
- Hereditary Cerebral Amyloid Angiopathy MedlinePlus
  
  The Dutch type is the most common, with over 200 affected individuals reported in the scientific literature. Causes Mutations in the APP gene are the most common cause of hereditary cerebral amyloid angiopathy. APP gene mutations cause the Dutch, Italian, Arctic, Iowa, Flemish, and Piedmont types of this condition. ... Familial British and Danish dementia are caused by mutations in the ITM2B gene. The APP gene provides instructions for making a protein called amyloid precursor protein. ... Additionally, the ITM2B protein may be involved in processing the amyloid precursor protein. Mutations in the APP , CST3 , or ITM2B gene lead to the production of proteins that are less stable than normal and that tend to cluster together (aggregate). ... Learn more about the genes associated with Hereditary cerebral amyloid angiopathy APP CST3 ITM2B Inheritance Pattern Hereditary cerebral amyloid angiopathy caused by mutations in the APP , CST3 , or ITM2B gene is inherited in an autosomal dominant pattern , which means one copy of the altered gene in each cell is sufficient to cause the disorder.
- Abetal34v Amyloidosis Orphanet
  
  This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.
- Abetaa21g Amyloidosis Orphanet
  
  This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.
- Abeta Amyloidosis, Arctic Type Orphanet
  
  This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.
- Abeta Amyloidosis, Italian Type Orphanet
  
  This subtype is due to a mutation in the APP gene (21q21.2), encoding the beta-amyloid precursor protein.
Inclusion Body Myositis OMIM

The authors discussed the abnormalities of APP processing, the role of abnormal intracellular protein folding, oxidative stress, and the potential role of cholesterol in the pathogenic cascade of IBM. ... Accumulation of the amyloid-beta peptide, which is derived from proteolysis of the larger beta-APP, seems to be an early pathologic event in both Alzheimer disease and IBM; in the latter, it occurs predominantly intracellularly within affected myofibers. To elucidate the possible role of beta-APP mismetabolism in the pathogenesis of IBM, Sugarman et al. (2002) selectively targeted beta-APP overexpression to skeletal muscle in transgenic mice, using the muscle creatine kinase promoter. They reported that older (more than 10 months) transgenic mice exhibited intracellular immunoreactivity to beta-APP and its proteolytic derivatives in skeletal muscle. In this transgenic model, selective overexpression of beta-APP led to the development of a subset of other histopathologic and clinical features characteristic of IBM, including centric nuclei, inflammation, and deficiencies in motor performance.

GNE, NT5C1A, APP, TARDBP, HLA-DRB1, SQSTM1, APOE, KHDRBS1, NUP62, DCTN4, GTF2H1, SDC1, CDR3, GSN, MAPT, TRBV20OR9-2, HLA-C, PLAAT4, FYCO1, MSTN, TNFRSF12A, NFAT5, CCR2, UBB, MALAT1, VCP, RBM45, AOC3, DCD, UCN2, DNAJB6, OPTN, KLRG1, MAP1LC3A, LILRB1, KDELR1, ICOSLG, SYNM, ROBO3, DDX58, CHMP1B, PABPC1, TIMP1, RRM2B, TWNK, FOXP3, KRT20, TTR, ACTB, THBS1, CST3, HLA-DQA1, HK1, H1-0, NR3C1, EPHB2, EMD, DES, CD47, TGFB1, CD38, CD36, CD34, MS4A1, CAPN3, BCL2, AOC2, HLA-DRB3, HMGB1, IFN1@, IFNG, TRIM21, AGER, MOK, PTPRC, PSME1, PSMB10, MAPK1, POLG, PMP22, MMP9, MMP1, MLF1, LMNA, IL6, IL1B, LOC102723996
- Inclusion Body Myositis Orphanet
  
  Inclusion body myositis (IBM) is a slowly progressive degenerative inflammatory disorder of skeletal muscles characterized by late onset weakness of specific muscles and distinctive histopathological features. Epidemiology IBM has a highly variable prevalence according to geographic, ethnic and age criteria. Prevalence in the general population ranges from 1:1,000,000 to 1:14,000 but a three-fold increase is observed when considering only a population over 50 years. Underdiagnosis may be an explanation for the high ethno-geographic variation. Male-to-female ratio is 2:1 on average (0.5 to 6.5:1). Clinical description IBM onset is over 50 years but may also occur earlier, in the 5th decade.
- Inclusion Body Myositis Wikipedia
  
  Inflammatory muscle disease in older adults This article needs additional citations for verification . Please help improve this article by adding citations to reliable sources . Unsourced material may be challenged and removed. Find sources: "Inclusion body myositis" – news · newspapers · books · scholar · JSTOR ( September 2009 ) ( Learn how and when to remove this template message ) Inclusion body myositis Other names sIBM Specialty Rheumatology Inclusion body myositis ( IBM ) ( / m aɪ oʊ ˈ s aɪ t ɪ s / ) (sometimes called sporadic inclusion body myositis , sIBM ) is the most common inflammatory muscle disease in older adults. [1] The disease is characterized by slowly progressive weakness and wasting of both proximal muscles (closest to the body's midline) and distal muscles (the limbs), most apparent in the finger flexors and knee extensors . [2] IBM is often confused with an entirely different class of diseases, called hereditary inclusion body myopathies (hIBM). [3] [4] The "M" in hIBM is an abbreviation for "myopathy" while the "M" in IBM is an abbreviation for "myositis". These diseases should not be confused with each other. In IBM, two processes appear to occur in the muscles in parallel, one autoimmune and the other degenerative. Inflammation is evident from the invasion of muscle fibers by immune cells .
- Idiopathic Inflammatory Myopathy MedlinePlus
  
  Idiopathic inflammatory myopathy is a group of disorders characterized by inflammation of the muscles used for movement (skeletal muscles). Idiopathic inflammatory myopathy usually appears in adults between ages 40 and 60 or in children between ages 5 and 15, though it can occur at any age. The primary symptom of idiopathic inflammatory myopathy is muscle weakness, which develops gradually over a period of weeks to months or even years. Other symptoms include joint pain and general tiredness (fatigue). There are several forms of idiopathic inflammatory myopathy, including polymyositis, dermatomyositis, and sporadic inclusion body myositis. Polymyositis and dermatomyositis involve weakness of the muscles closest to the center of the body (proximal muscles), such as the muscles of the hips and thighs, upper arms, and neck.
- Inclusion Body Myositis GARD
  
  Inclusion body myositis (IBM) is a progressive muscle disorder characterized by muscle inflammation, weakness, and atrophy (wasting). It is a type of inflammatory myopathy . IBM develops in adulthood, usually after age 50. The symptoms and rate of progression vary from person to person. The most common symptoms include progressive weakness of the legs, arms, fingers, and wrists. Some people also have weakness of the facial muscles (especially muscles controlling eye closure), or difficulty swallowing (dysphagia). Muscle cramping and pain are uncommon, but have been reported in some people.
Angioedema Induced By Ace Inhibitors, Susceptibility To OMIM

Clinical Features Blais et al. (1999) and Adam et al. (2002) reported significantly lower plasma aminopeptidase P (APP) activities in patients with a history of AEACEI. ... Measured genotype analysis strongly suggested that the linkage signal for APP activity at this locus was accounted for predominantly by the SNP association. ... There was a significant association between the -2399A allele and decreased serum APP activity in both men and women, but the APP activity was lower in men regardless of genotype. ... This haplotype was associated with decreased plasma APP activity and decreased luciferase gene expression compared to other haplotypes of these SNPs. Cilia La Corte et al. (2011) concluded that the ATG haplotype of XPNPEP2 is functional and contributes to the development of ACEi-angioedema through a reduction in APP activity.

SERPING1, KNG1, ACE, AGT
- Acquired Angioedema GARD
  
  Acquired angioedema (AAE) is a rare disorder that causes recurrent episodes of swelling (edema) of the face or body, lasting several days. People with AAE may have swelling of the face, lips, tongue, limbs, or genitals. People with AAE can have edema of the lining of the digestive tract, which can cause abdominal pain and nausea, as well as edema of the upper airway, which can be life-threatening. Swelling episodes may have various triggers, such as mild trauma (such as dental work), viral illness, cold exposure, pregnancy, certain foods, or emotional stress. The frequency of episodes is unpredictable and can vary widely. There are two forms of AAE.
- Acquired Angioedema Orphanet
  
  A rare disease characterized by the occurrence of transitory and recurrent subcutaneous and/or submucosal edemas resulting in swelling and/or abdominal pain due to an acquired C1 inhibitor (C1-INH) deficiency. Epidemiology Prevalence is unknown. Clinical description Onset most commonly occurs after 50 years of age. Patients present with white, circumscribed nonpruritic edemas that remain for a period of 48 to 72 hours and recur with variable frequency. The edemas may involve the digestive tract resulting in a clinical picture similar to that seen in intestinal occlusion syndrome, sometimes associated with ascites and hypovolemic shock. Laryngeal edema can be life-threatening with a risk of death of 25% in the absence of appropriate treatment.
- Acquired C1 Esterase Inhibitor Deficiency Wikipedia
  
  Acquired C1 esterase inhibitor deficiency Other names Acquired angioedema Specialty Hematology Acquired C1 esterase inhibitor deficiency presents with symptoms indistinguishable from hereditary angioedema , but generally with onset after the fourth decade of life. [1] : 153 C4 levels are low and C3 levels are normal. [2] See also [ edit ] Hereditary Angioedema Wheal response Urticaria Skin lesion List of cutaneous conditions References [ edit ] ^ James, William; Berger, Timothy; Elston, Dirk (2005). Andrews' Diseases of the Skin: Clinical Dermatology . (10th ed.). Saunders. ISBN 0-7216-2921-0 . ^ Markovic SN, Inwards DJ, Frigas EA, Phyliky RP (January 2000). "Acquired C1 esterase inhibitor deficiency". Ann. Intern. Med . 132 (2): 144–50. doi : 10.7326/0003-4819-132-2-200001180-00009 . PMID 10644276 . External links [ edit ] Classification D ICD - 10 : D84.1 ( ILDS D84.112) MeSH : C538173 External resources eMedicine : article/104888 v t e Lymphoid and complement disorders causing immunodeficiency Primary Antibody / humoral ( B ) Hypogammaglobulinemia X-linked agammaglobulinemia Transient hypogammaglobulinemia of infancy Dysgammaglobulinemia IgA deficiency IgG deficiency IgM deficiency Hyper IgM syndrome ( 1 2 3 4 5 ) Wiskott–Aldrich syndrome Hyper-IgE syndrome Other Common variable immunodeficiency ICF syndrome T cell deficiency ( T ) thymic hypoplasia : hypoparathyroid ( Di George's syndrome ) euparathyroid ( Nezelof syndrome Ataxia–telangiectasia ) peripheral: Purine nucleoside phosphorylase deficiency Hyper IgM syndrome ( 1 ) Severe combined (B+T) x-linked: X-SCID autosomal: Adenosine deaminase deficiency Omenn syndrome ZAP70 deficiency Bare lymphocyte syndrome Acquired HIV/AIDS Leukopenia : Lymphocytopenia Idiopathic CD4+ lymphocytopenia Complement deficiency C1-inhibitor ( Angioedema / Hereditary angioedema ) Complement 2 deficiency / Complement 4 deficiency MBL deficiency Properdin deficiency Complement 3 deficiency Terminal complement pathway deficiency Paroxysmal nocturnal hemoglobinuria Complement receptor deficiency This cutaneous condition article is a stub .
Alzheimer Disease 18 OMIM

Q170H and R181G mutant mice showed significant attenuation of APP processing compared to wildtype, with a decrease in APP-CTF-alpha levels and an increase in sAPP-beta levels, indicating that the mutations attenuated Adam10 alpha-secretase activity on APP. Crossing these Adam10 mutant mice with the Tg2576 AD mouse model showed that the Adam10 mutations increased amyloidogenic APP processing, as manifest by a shift from the alpha-secretase to the amyloidogenic beta-secretase pathway. ... Collectively, these findings suggested that diminished alpha-secretase activity of ADAM10 on APP resulting from mutations in the ADAM10 prodomain can cause AD-related pathology.

ADAM10, PSEN2
Infantile Myofibromatosis Orphanet

Clinical description Infantile myofibromatosis (IM) presents at birth or develops shortly thereafter, with 90% of cases occurring before the age of 2 years. IM is characterized by solitary or multiple nodules that are firm, flesh-colored to purple (''myofibroma''), and usually painless (except in case of compression of adjacent nerves). ... Etiology Most of these tumors are sporadic and isolated. Rare familial cases of IM have been described and 2 genes have been identified as disease causing: PDGFRB and NOTCH3 which encode PDGFRB and NOTCH3 respectively. ... Histopathology remains the gold standard for the diagnosis of IM. Biopsy reveals interlacing fascicles of spindle cells (myofibroblasts) in the periphery. ... Antenatal diagnosis Prenatal diagnosis is achieved by ultrasound examination and confirm by fetal MRI. Genetic counseling IM is mostly isolated and sporadic. In cases of familial and multifocal lesions, IM can be inherited as an autosomal recessive or dominant trait (incomplete penetrance and variable expressivity).

PDGFRB, NOTCH3, ACTB, SMUG1, S100A1, NDRG4, LRIT1, VIM, SMS, S100B, PECAM1, ACVR1, PAM, DES, COX8A, CD34, ACAN, SHCBP1
- Infantile Myofibromatosis Wikipedia
  
  Infantile myofibromatosis Other names Congenital generalized fibromatosis, [1] and Congenital multicentric fibromatosis [1] Specialty Oncology Infantile myofibromatosis is the most common fibrous tumor of infancy, in which eighty percent of patients have solitary lesions with half of these occurring on the head and neck, and 60% are present at or soon after birth. [2] : 606 Less commonly, infantile myofibromatosis presents as multiple lesions of skin, muscle, and bone with about 1/3 of these cases also having lesions in their visceral organs. All of these cases have an excellent prognosis with their tumors sometimes regressing spontaneously except for those cases in which there is visceral involvement where the prognosis is poor. [3] Infantile myofibromatosis and the classic form of mesoblastic nephroma have been suggested to be the same disease because of their very similar histology. However, studies on the distribution of cell-type markers (i.e. cyclin D1 and Beta-catenin ) indicate that the two neoplasms likely have different cellular origins. [4] [5] See also [ edit ] Skin lesion List of cutaneous conditions mesoblastic nephroma References [ edit ] ^ a b Rapini, Ronald P.; Bolognia, Jean L.; Jorizzo, Joseph L. (2007). Dermatology: 2-Volume Set . St. Louis: Mosby. ISBN 978-1-4160-2999-1 . ^ James, William; Berger, Timothy; Elston, Dirk (2005). Andrews' Diseases of the Skin: Clinical Dermatology . (10th ed.). Saunders.
- Myofibromatosis, Infantile, 1 OMIM
  
  A number sign (#) is used with this entry because infantile myofibromatosis-1 (IMF1) is caused by heterozygous mutation in the PDGFRB gene (173410) on chromosome 5q32. Description Infantile myofibromatosis is a rare mesenchymal disorder characterized by the onset of nodules in the skin, striated muscles, bones, and, more rarely, visceral organs. Subcutaneous or soft tissue nodules commonly involve the skin of the head, neck, and trunk. Skeletal and muscular lesions occur in about 50% of patients. Lesions may be solitary or multicentric, and they may be present at birth or become apparent in early infancy or occasionally in adult life (summary by Arcangeli and Calista, 2006). Genetic Heterogeneity of Infantile Myofibromatosis See also IMF2 (615293), caused by mutation in the NOTCH3 gene (600276).
- Myofibromatosis, Infantile, 2 OMIM
  
  Clinical Features Martignetti et al. (2013) reported a 2-generation family (IM-9) in which 9 individuals had infantile myofibromatosis.
Early-Onset Alzheimer's Disease Wikipedia

This loss of brain volume affects ones ability to live and function properly, ultimately being fatal. [5] Beta-amyloid is a small piece of a larger protein called the amyloid precursor protein (APP). Once APP is activated, it is cut into smaller sections of other proteins. ... Alpha-secretase cleavage of APP, which precludes the production of Aβ, is the most common processing event for APP. 21 allelic mutations have been discovered in the APP gene. These guarantee onset of early-onset familial Alzheimer disease and all occur in the region of the APP gene that encodes the Aβ domain. ... "A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid". ... PMID 16817891 . ^ Chow VW, Mattson MP, Wong PC, Gleichmann M (March 2010). "An overview of APP processing enzymes and products" .
Alzheimer Disease OMIM

See also APP-related cerebral amyloid angiopathy (CAA; 605714), which shows overlapping clinical and neuropathologic features. ... Genetic analysis identified a mutation in the APP gene (V717I; 104760.0002). Farlow et al. (1994) reviewed the clinical characteristics of the disorder in the AD family reported by Murrell et al. (1991) in which affected members had a mutation in the APP gene (V717F; 104760.0003). ... Rovelet-Lecrux et al. (2006) estimated that in their whole cohort of 65 ADEOAD families, the frequency of the APP locus duplication was roughly 8% (5 of 65), which corresponds to half of the contribution of APP missense mutations to ADEOAD. ... Revesz et al. (2003) reviewed the pathology and genetics of APP-related CAA and discussed the different neuropathologic consequences of different APP mutations. ... Further studies indicated that suppression of PPARGC1A in hyperglycemia resulted in activation of the FOXO3A (602681) transcription factor, which inhibits nonamyloidogenic secretase processing of APP and promotes amyloidogenic processing of APP.

TOMM40, TREM2, ABCA7, APP, APOE, PSEN2, PSEN1, MAPT, SORL1, PRNP, CASP3, BACE1, GSK3B, NCSTN, IDE, IL1B, HFE, A2M, ACE, DHCR24, BIN1, ESR1, ADAM10, ADAMTS1, PGRMC1, VEGFA, ARC, CYP46A1, SLC30A4, VSNL1, PICALM, HMOX1, HLA-DRB5, IGF1R, IGF1, INPP5D, IGF2, MPO, NPY, NOS3, PLAU, PLCG2, PPARG, RELN, MTHFR, PYY, NECTIN2, SLC2A4, IGF2R, SOD2, MAOB, TF, LEP, TFAM, INSR, INS, TNF, TPI1, EPHA1, F2, ENO1, CR1, CASS4, ATP5F1A, CLU, CHRNB2, CHRNA7, MIR766, CD33, IQCK, EIF2S1, MIR505, APOC1, CALM1, MIR100, MIR146A, BDNF, BCL2, MIR375, MIR296, BCHE, MIR708, TPP1, SLC30A6, SNAR-I, DPYSL2, ACHE, CD2AP, GAPDHS, PCDH11X, CYP2D6, MIR4467, CRH, MIR3622B, BAX, AMFR, ABI3, CST3, MS4A4A, WWOX, BRCA2, FANCD2, TFF1, TAS2R64P, CTNNB1, SUCLA2, SNCA, CTSD, RNR2, NEFL, TAS2R62P, SOD1, ITPR3, ITPR2, ITPR1, FLAD1, PSENEN, TP53, CDK5R1, EIF2AK3, UBQLN1, ALG3, PIK3CG, PIK3CA, PIK3CD, SERPINA3, PIK3CB, DOCK3, APLP1, OGDH, CREB1, NOTCH1, CASP6, NGF, CCND1, FOS, DLX4, DLG4, DDIT3, RABGEF1, PEBP1, PYCARD, DAPK2, KCNIP3, CTSB, CSF2, CRMP1, CTSG, EHMT2, ENO2, ERBB4, TMED10, TERF2IP, PTK2B, FCN2, PTGES3, FGF2, ACKR1, DNM1L, SDC3, G6PD, GCHFR, ITM2B, CREBBP, MAP3K8, TRPM7, ADI1, MTCO2P12, UPK3B, ACTB, AKT1, AKT2, ANXA1, APBB1, DNLZ, STS, MIR34A, BRCA1, MIR137, C5AR1, DDR1, CAMK4, TMED10P1, MPEG1, C9orf72, ESCO1, CDCA5, PRRT2, MAP1LC3B, CAT, EHMT1, CNR2, SPPL2B, RAB9A, NRXN3, GFAP, SYNJ1, SERPINB5, CD99, MME, MNAT1, CCL2, RRAS, RPS27, RPS21, RAP1A, PYCR1, COX2, PTS, PTGS2, MTHFD1, MMUT, NCAM1, NFIA, NFIB, MAPK8, MAPK3, PRKCB, PRKCA, PPBP, MED1, NFIC, PPARA, NFIX, PKD1, NOTCH3, NRGN, MEOX2, MEF2A, SPRR2A, TTC3, GRIN2A, DENR, GRIN2B, RAB7A, LRP8, HPRT1, HSP90AA1, VIM, IDUA, UTRN, SUMO1, UBE2I, TTK, TPT1, SULT1E1, IL1A, IL6, IL12A, TSPAN6, TIE1, TGFB1, TG, KNG1, LAMC2, LGALS3, TERT, TERC, STIM1, H3P17
- Alzheimer Disease 13 OMIM
  
  For a general phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease, see 104300. Mapping Liu et al. (2007) conducted a genome screen of 103 patients with late-onset AD who were ascertained as part of the Genetic Research in Isolated Populations (GRIP) program that was conducted in an isolated population from the southwestern area of the Netherlands. Genealogic information resulted in an extremely large and complex pedigree of 4,645 members. The pedigree was split into 35 subpedigrees to reduce the computational burden of linkage analysis. The strongest evidence for linkage, hlod = 5.20 at marker D1S498, was obtained at chromosome 1q21 (AD13).
- Early-Onset Autosomal Dominant Alzheimer Disease GARD
  
  There are three subtypes of early-onset familial AD which are each associated with changes (mutations) in unique genes: (1) Alzheimer disease, type 1 is caused by mutations in the APP gene (2) Alzheimer disease, type 3 is caused by mutations in the PSEN1 gene (3) Alzheimer disease, type 4 is caused by mutations in the PSEN2 gene.
- Alzheimer Disease 11 OMIM
  
  For a general phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping By genomewide linkage analysis of 466 families with late-onset AD, including 730 affected sib pairs, Pericak-Vance et al. (2000) identified a candidate disease locus on chromosome 9p22.1 (nonparametric maximum lod score of 2.97 at marker D9S741). Analysis of a subset of 199 families in which there was at least 1 autopsy-confirmed AD case yielded a higher lod score of 4.31 at the same marker. Scott et al. (2003) reexamined 437 white AD families included in the original report by Pericak-Vance et al. (2000) by considering age of onset as a covariate. Ordered-subsets analysis included continuous covariates in linkage analysis by rank ordering families by a covariate and summing lod scores.
- Alzheimer Disease 6 OMIM
  
  In HEK293 cells with an AD-associated APP mutation (104760.0008), overexpression of SORCS1 resulted in a significant decrease in amyloid-beta-40 and -beta-42 secretion, whereas suppression of SORCS1 in HEK293 cells increased beta-amyloid-40 levels. The findings indicated that SORCS1 can influence APP processing, and Reitz et al. (2011) suggested that variation in the SORCS1 gene may be associated with risk of LOAD. ... The findings indicated a role for calcium signaling in APP (104760) processing and suggested that variations in the CALHM1 gene may influence susceptibility to late-onset AD.
- Alzheimer Disease 5 OMIM
  
  For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping In a late-onset form of familial Alzheimer disease (AD), Pericak-Vance et al. (1997) identified linkage to a locus on chromosome 12. From a series of multiplex families affected with late-onset AD (at least 60 years) ascertained during the previous 14 years and for which DNA had been obtained, Pericak-Vance et al. (1997) selected a subset of 16 families (with 52 AD patients) to use for a genomewide screen. A second subset of 38 families (with 89 AD patients) was used for a follow-up analysis. Linkage analysis was performed using both genetic model-dependent (lod score) and model-independent methods.
- Alzheimer Disease, Familial Early-Onset, With Coexisting Amyloid And Prion Pathology OMIM
  
  Clinical Features Leuba et al. (2000) described a Swiss family whose members presented with standard clinical and neuropathologic features of Alzheimer disease (104300) and, in particular, severe neurofibrillary tangle degeneration present in the hippocampus and in several cortical areas, together with a large number of beta-amyloid deposits and senile plaques. The brain pathology of 5 deceased members of this family, from 2 generations, represented a coexisting beta-amyloid and prion protein (PrP; 176640) pathology. Frequent beta-amyloid-positive senile plaques were observed, together with senile plaques stained by the monoclonal antibody against PrP(106-126). In all 5 cases, the cerebral cortex showed spongiform changes, mainly in the superficial layers, with some degree of gliosis. Successive sections showed that both beta-amyloid- and PrP-positive senile plaques were deposited in all layers of the frontal and temporal cortex.
- Alzheimer Disease 8 OMIM
  
  Within this candidate region, 1 gene of particular interest was that encoding cystatin-3 (CST3; 604312), because it is known to be an amyloidogenic protein and is codeposited with the amyloid-beta precursor protein (APP; 104760) in amyloid plaques in the brain of AD patients. Using a covariate-based linkage method, Olson et al. (2001) showed that the APP region on chromosome 21q21 is strongly linked to AD-affected sib pairs of the oldest current age (i.e., age either at last exam or at death) who lacked E4 alleles at the apolipoprotein E (APOE; 107741) locus. ... Two-locus analysis provided evidence of strong epistasis between 20p and the APP region, limited to the oldest age group and to those lacking E4 alleles at the APOE locus.
- Alzheimer Disease 2 OMIM
  
  Onset was early in 4 other families tested; 2 had chromosome 21 APP (104760) mutations and 2 showed linkage to chromosome 14, thus representing AD1 (104300) and AD3 (607822), respectively.
- Early-Onset Autosomal Dominant Alzheimer Disease Orphanet
  
  Etiology EOAD is the consequence of either PSEN1 mutations (69%), APP mutations (13%), or APP duplication (7,5%), and exceptionally of PSEN2 mutations (2%).
- Alzheimer Disease 4 OMIM
  
  A number sign (#) is used with this entry because Alzheimer disease-4 (AD4) is caused by heterozygous mutation in the presenilin-2 gene (PSEN2; 600759) on chromosome 1q42. For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease, see 104300. Clinical Features Bird et al. (1988) described 5 German kindreds with an autosomal dominant early-onset form of Alzheimer disease. All families were descendants of a group of immigrants, known as the Volga Germans, who came to the United States between 1870 and 1920. Their ancestors had moved from Germany to the southern Volga region of Russia in the 1760s.
- Familial Alzheimer Disease GARD
  
  There are three subtypes of early-onset familial AD which are each associated with changes (mutations) in unique genes: (1) Alzheimer disease, type 1 is caused by mutations in the APP gene (2) Alzheimer disease, type 3 is caused by mutations in the PSEN1 gene (3) Alzheimer disease, type 4 is caused by mutations in the PSEN2 gene.
- Alzheimer Disease 15 OMIM
  
  For a general phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease, see 104300. Mapping Liu et al. (2007) conducted a genome screen of 103 patients with late-onset AD who were ascertained as part of the Genetic Research in Isolated Populations (GRIP) program that was conducted in an isolated population from the southwestern area of the Netherlands. Genealogic information resulted in an extremely large and complex pedigree of 4,645 members. The pedigree was split into 35 subpedigrees to reduce the computational burden of linkage analysis. They found significant evidence of linkage of AD to 3q22-q24 (AD15), in a region of 18 cM from D3S3514 to D3S3626 that reached a maximum hlod of 4.44 at marker D3S1579.
- Alzheimer Disease 14 OMIM
  
  For a general phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease, see 104300. Mapping In a genome screen of individuals from an isolated population from the southwestern area of the Netherlands, ascertained as part of the Genetic Research in Isolated Populations (GRIP) program, Liu et al. (2007) found the strongest evidence of linkage for chromosome 1q21 (AD13; 611152). Approximately 30 cM upstream of this locus, at 1q25, another peak (AD14) was found (hlod = 4.0 at marker D1S218). Liu et al. (2007) noted that these 2 loci were in a linkage region spanning 1q21-q31 identified by Zubenko et al. (1998), Hiltunen et al. (2001), Myers et al. (2002), and Blacker et al. (2003). Haplotype analysis showed that the 2 linkage peaks on chromosome 1q21 and 1q25 are explained by different haplotypes, of 15 cM and 21 cM, respectively, segregating in different families.
- Alzheimer Disease 12 OMIM
  
  For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping Giedraitis et al. (2006) conducted a genome scan with 369 microsatellite markers in 12 extended families collected in Sweden. Age at disease onset ranged from 53 to 78 years, but in 10 of the families there was at least 1 member with age at onset of less than 65 years. Mutations in known early-onset Alzheimer disease susceptibility genes were excluded. All persons were genotyped for APOE (107741), but no clear linkage with the E4 allele was observed.
- Alzheimer Disease 3 OMIM
  
  In 2 Belgian families with early-onset autosomal dominant AD, Van Broeckhoven et al. (1987) excluded linkage to the APP locus on chromosome 21q. One pedigree contained 36 patients in 6 generations, and the second had 22 patients spanning 5 generations.
- Alzheimer Disease 10 OMIM
  
  For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping In an extended multiplex family, ascertained in a population-based study of early-onset AD in the northern Netherlands, Rademakers et al. (2005) obtained conclusive evidence of linkage of AD with a candidate region of 19.7 cM at 7q36. They identified a shared haplotype at 7q36 between the index family and 3 of 6 multiplex AD-affected families from the same geographic region, which was indicative of a founder effect and defined a priority region of 9.3 cM. Mutation analysis of coding exons of 29 candidate genes identified only an exonic silent mutation in the PAXIP1 gene (608254), 38030G-C in the exon 10 genomic sequence, which affected codon 626. It remained to be determined whether PAXIP1 has a functional role in the expression of AD in the index family or whether another mutation at this locus explained the observed linkage and sharing.
- Alzheimer Disease 7 OMIM
  
  For a phenotypic description and a discussion of genetic heterogeneity of Alzheimer disease (AD), see 104300. Mapping In a systematic survey of the human genome in patients with AD, Zubenko et al. (1998) identified D10S1423, located at 10p13, as a candidate susceptibility locus. The allelic associations in this survey were observed in independent samples of autopsied AD cases and controls from geographically disparate sites (Boston and Pittsburgh). Majores et al. (2000) replicated these findings by identifying an association of the D10S1423 234-bp allele with AD in an ethnically homogeneous group of 397 German AD cases and controls. Zubenko et al. (2001) described a prospective, longitudinal, double-blind assessment of the age-specific risk of AD encountered by 325 asymptomatic first-degree relatives of AD probands who carried the D10S1423 234-bp allele, the APOE E4 allele (107741), or both, after 11.5 years of systematic follow-up.
Congenital Disorder Of Glycosylation, Type Im OMIM

A number sign (#) is used with this entry because of evidence that congenital disorder of glycosylation type Im (CDG1M), also known as dolichol kinase deficiency, is caused by homozygous mutation in the DOLK gene (610746), which encodes the enzyme responsible for the final step of the de novo biosynthesis of dolichol phosphate, on chromosome 9q34. ... Helander et al. (2013) reported 2 sibs, born of consanguineous Syrian Turkish parents, with CDG type Im. The patients presented at age 4 months with severe intractable seizures and hypsarrhythmia, consistent with a clinical diagnosis of West syndrome (see 308350). ... In 2 sibs, born of consanguineous Syrian Turkish parents, with CDG type Im and a purely neurologic phenotype, Helander et al. (2013) identified a homozygous mutation in the initiating methionine codon of the DOLK gene (610746.0006). ... Kranz et al. (2007) suggested that since dolichol kinase deficiency can be detected by isoelectric focusing (IEF) of serum transferrin, the disorder could be included in the CDG I group with the designation CDG Im. INHERITANCE - Autosomal recessive GROWTH Height - Normal birth length Weight - Normal birth weight Other - Failure to thrive HEAD & NECK Head - Normal birth head circumference - Microcephaly, acquired Eyes - Sparse eyebrows - Sparse eyelashes CARDIOVASCULAR Heart - Dilated cardiomyopathy SKIN, NAILS, & HAIR Skin - Ichthyosis Hair - Sparse eyebrows - Sparse eyelashes - Minimal hair growth NEUROLOGIC Central Nervous System - Hypotonia, profound muscular (in some patients) - Seizures (in some patients) - Hypsarrhythmia (in some patients) METABOLIC FEATURES - Hypoketotic hypoglycemia (in some patients) LABORATORY ABNORMALITIES - Abnormal transferrin isoelectric focusing (IEF) - Increased disialo- and asialotransferrin - Decreased lipid-linked oligosaccharides (LLO) MISCELLANEOUS - Death in early infancy (in some patients) - Some patients present with apparent nonsyndromic dilated cardiomyopathy in early childhood MOLECULAR BASIS - Caused by mutation in the transmembrane protein 15 gene (TMEM15, 610746.0001 ) ▲ Close

DOLK
- Dolk-Congenital Disorder Of Glycosylation MedlinePlus
  
  DOLK -congenital disorder of glycosylation ( DOLK -CDG, formerly known as congenital disorder of glycosylation type Im) is an inherited condition that often affects the heart but can also involve other body systems.
- Dk1-Cdg Orphanet
  
  DK1-CDG is characterised by muscular hypotonia and ichthyosis. It has been described in four children from two consanguineous families. All the affected children died during early infancy, two from dilated cardiomyopathy. The syndrome is caused by a deficiency in dolichol kinase 1 (DK1), an enzyme involved in the de novo biosynthesis of dolichol phosphate. The mutations identified in the DK1 gene led to a 96 to 98% reduction in DK activity.
- Dolichol Kinase Deficiency Wikipedia
  
  Dolichol kinase deficiency Other names Hypotonia and ichthyosis due to dolichol phosphate deficiency [1] This condition is inherited in an autosomal recessive manner. Dolichol kinase deficiency is a cutaneous condition caused by a mutation in the dolichol kinase gene. [2] [3] It is also known as Congenital disorder of glycosylation 1m. See also [ edit ] CEDNIK syndrome List of cutaneous conditions References [ edit ] ^ RESERVED, INSERM US14-- ALL RIGHTS. "Orphanet: DK1 CDG" . www.orpha.net . Retrieved 11 April 2019 . ^ Rapini, Ronald P.; Bolognia, Jean L.; Jorizzo, Joseph L. (2007). Dermatology: 2-Volume Set . St. Louis: Mosby. ISBN 978-1-4160-2999-1 . ^ Kranz C, Jungeblut C, Denecke J, et al.
Alzheimer's Disease Wikipedia

The hypothesis holds that an amyloid-related mechanism that prunes neuronal connections in the brain in the fast-growth phase of early life may be triggered by ageing-related processes in later life to cause the neuronal withering of Alzheimer's disease. [64] N-APP, a fragment of APP from the peptide's N-terminus , is adjacent to beta-amyloid and is cleaved from APP by one of the same enzymes. N-APP triggers the self-destruct pathway by binding to a neuronal receptor called death receptor 6 (DR6, also known as TNFRSF21 ). [64] DR6 is highly expressed in the human brain regions most affected by Alzheimer's, so it is possible that the N-APP/DR6 pathway might be hijacked in the ageing brain to cause damage. ... Osaka mutation A Japanese pedigree of familial Alzheimer's disease was found to be associated with a deletion mutation of codon 693 of APP. [65] This mutation and its association with Alzheimer's disease was first reported in 2008. [66] This mutation is known as the Osaka mutation. ... A β is a fragment from the larger amyloid precursor protein (APP). APP is a transmembrane protein that penetrates through the neuron's membrane. APP is critical to neuron growth, survival, and post-injury repair. [103] [104] In Alzheimer's disease, gamma secretase and beta secretase act together in a proteolytic process which causes APP to be divided into smaller fragments. [105] One of these fragments gives rise to fibrils of amyloid beta, which then form clumps that deposit outside neurons in dense formations known as senile plaques . [98] [106] AD is also considered a tauopathy due to abnormal aggregation of the tau protein .

APP, ACE, TREM2, ADAM10, APOE, PSEN1, GSK3B, HFE, MAPT, PLAU, NPY, BCL2, CASP3, BDNF, IDE, INSR, IL1B, LEP, BACE1, IGF2, IGF1R, ATP5F1A, INS, BAX, CR1, A2M, ABCA7, TOMM40, CD2AP, BIN1, EPHA1, CLU, PICALM, NOS3, PSEN2, APOC1, MPO, SORL1, VSNL1, INPP5D, NECTIN2, MS4A4A, PCDH11X, CASS4, BCHE, MIR146A, CYP46A1, DHCR24, CHRNA7, NCSTN, VEGFA, DPYSL2, PRNP, ESR1, PPARG, RELN, HMOX1, ACHE, CST3, MAOB, TNF, MTHFR, IGF1, CD33, TFAM, IL6, CYP2D6, CRH, SOD2, UNC5C, PLCG2, TF, ABI3, WWOX, SLC30A6, CHRNB2, ARC, PGRMC1, F2, CALM1, EIF2S1, HLA-DRB5, ENO1, TPI1, IGF2R, SLC30A4, MIR296, SLC2A4, MIR100, IQCK, MIR375, AMFR, SNAR-I, ADAMTS1, MAPK14, PIN1, PYY, PTGS2, S100B, PPARGC1A, NOS2, NGFR, NGF, NFE2L2, SOD1, SYP, CDK5, NGB, MIR505, GAPDHS, MME, MAP2, CTNNB1, TPP1, LRP1, IRS1, CHAT, GAPDH, MIR4467, MIR3622B, AGER, MIR766, MIR708, CAV1, NTRK2, PTGS1, APLP2, ADAM17, MFN2, DNM1, HSF1, GSR, IL33, CCR5, HSPD1, HSPB1, CIB1, CASP8, IKBKB, SERPINF1, ATP7A, MT2A, ADAM9, INS-IGF2, BCL2L2, CASP9, GAB2, PTK2B, PLCB1, ABCA1, GRN, CASP12, SQSTM1, FERMT2, HLA-DRB1, NFIC, CSF1R, APOB, MARK4, HSPG2, MS4A6A, CELF1, VCP, SYNJ1, ZCWPW1, MS4A4E, APH1B, APOC2, F13A1, EXOC3L2, PLXNA4, ADAMTS4, AKAP9, MADD, DST, PILRA, FRMD4A, LAMP1, SLC24A4, GLIS3, SPON1, CADPS2, IL34, COL18A1, TRIP4, SPI1, TGFB2, BCL3, MTHFD1L, AICDA, IL6R, DCHS2, MEGF10, SLC16A7, EPHX2, NDUFAF6, DSG2, OSBPL6, CELF2, UBE2L3, SPPL2A, MAPK7, CDH13, LAMA1, SGK1, SUCLG2, LUZP2, PTPRG, ST6GAL1, AP2A2, RBFOX1, SORCS3, TSPOAP1-AS1, TLN2, ZAP70, ALDH1A2, TCF7L2, FMN2, OTOF, EXOC4, HSD17B10, DNM1L, ALOX5, GULOP, HTR2A, AHCYL1, SDR42E2, HTR6, GTF2H1, GRM5, IAPP, AHSA1, STAG3, ALB, FARP1, TSHZ1, HRES1, AGFG2, DCAF7, SIGMAR1, BCKDK, RTN3, TPPP, HSPA4, HCLS1, HSP90AA1, G3BP1, PGAM5P1, BACE1-AS, KHDRBS1, ALDH2, CFH, HCRT, GPC6, ABCA8, GLP1R, NR3C1, TNRC6A, IL19, PARVB, DDX25, BZW2, FCN2, FGF10, GOLIM4, LINC00476, HPGDS, FANCD2, PDE7B, SIGLEC7, TSPAN16, TRPC4AP, POLDIP2, CNTNAP2, RNF19A, BACE2, UBQLN1, ITSN2, GRIN2B, ZGLP1, BCAS3, EPDR1, TMED9, ENO2, CYCS, ANXA1, EPHB2, EPO, RAPGEF6, APH1A, LARS1, EYA4, SNX9, ESR2, WAC, SLC8A1-AS1, DCTN4, RMDN1, QPCT, MTOR, SGK3, FBXL7, SZT2, GIP, ACSL6, WWC1, CLEC16A, KAZN, LINC01672, PRRC2C, COLGALT2, PLD3, HECW1, ZNF292, MYO16, DKK1, SIRT2, ACOT7, PSIP1, CLASRP, LINC00271, SIRT3, SIRT1, GFAP, NUP62, FYN, CBLC, INHCAP, TRIM51CP, GABPA, GABRA2, GABRG3, DAPK2, SMUG1, GAP43, GATA1, GCG, GCHFR, TARDBP, NCS1, GDNF, HDAC6, RAB3D, MVP, OGG1, LINC02268, LINC02325, SOAT1, ACTG2, ACTG1, SNCG, SNCA, SNCB, SNAP25, NOS1, ACTB, MEF2C-AS1, SLC6A4, NPC1, SLC6A3, GEMIN7-AS1, SLC1A2, LINC01508, LINC01725, NEFL, COX2, TNFRSF1B, STAG3L5P, TLR4, TLR2, MSH2, THY1, MT3, TH, SST, STAG3L5P-PVRIG2P-PILRB, TGFB1, TFF1, RNR2, LINC02653, LINC01712, TCF3, NRGN, CX3CL1, ELMO1, CCL2, PIK3CG, ABCA2, PLA2G1B, EIF2AK2, SERPINA3, PLG, MAPK8, MAPK1, PRKCB, PRKCA, PRKAB1, PRKAA2, PRKAA1, PMS2P1, POLD1, PTPA, PON1, PIK3CD, PIK3CB, PIK3CA, MOK, UPK3B, SORT1, ROS1, SERPINE1, REST, REN, RELB, RAC1, LINC01965, PVR, PVALB, PTPRA, LINC00972, ABCB1, LINC02008, MTCO2P12, TP53, OVCH1-AS1, MOBP, MNAT1, SLC4A8, AGT, INSIG1, AZIN1-AS1, EIF3E, FHL5, IRF2, GSTO1, ITM2B, GRAP2, LIPG, ADIPOQ, KL, MSC, LRAT, AP4M1, CCRL2, IL18, IL17A, IL12A, ST18, IFNG, ARL17B, AKT1, AIF1, KRBOX1, IGFALS, HDAC9, PHF14, IL10, IL1A, ALOX12-AS1, MICAL2, IL2RB, IL4, CLOCK, CXCL8, KCNN2, MPZL1, HERC2, VDR, TFEB, MAOA, COX10-AS1, ZNF232, YWHAZ, VLDLR, PARP1, UTRN, BCAM, UCHL1, UBB, TYROBP, AFF1, TTR, TRPM1, MMP9, AIMP2, LTBP2, KNG1, CRADD, CACNA1G, LAMC2, RPSA, CDK5R1, SUCLA2, LCN2, LDLR, BECN1, LPL, PDE5A, ABCB11, APOC4-APOC2, KHSRP, DENR, AGPS, LPA, CDKAL1, PPARA, MEIKIN, COL4A4, CRK, CEACAM22P, SCIMP, CREB1, CR1L, ZNF862, SH2D4B, CP, PNPLA7, SIMC1, GGACT, COMT, COL12A1, FAM181A, BRCA2, PPP1R37, GPR141, TENM3-AS1, CNR2, L3MBTL4, UBXN11, ACKR2, TMEM132C, CASTOR3, CLPTM1, STRADA, FNIP1, CDCA5, NLRP3, APOA1, CRMP1, KAT8, CSMD1, CLMN, PINK1, CYP8B1, AHNAK, MIR132, MIR107, CUX1, POTEM, PPP1R3B, FAS, SAP30L, ANKRD55, CTSD, CTSB, GEMIN7, EHMT1, LINC01184, CTNNA2, LINC01185, TMC5, THSD4, CCDC134, SP6, LINC01567, PDCD1LG2, SETD7, APOD, BHMG1, CSF2, HYI, BLOC1S3, TSPO, CHRNA4, CHRNA2, TAS2R62P, C3orf67, C9orf72, CCDC83, CCDC89, KDM1B, CD14, TGM6, ATXN7L1, RSPO4, ADGRF2, STH, TAS2R64P, CALHM1, RUNX1T1, PPP1R42, ALPK2, PCSK9, CAT, ANKRD31, CASP6, NKAIN3, TRIQK, CALB1, STEAP1B, CASP1, EPHA1-AS1, CAPN1, APOC4, FAM181A-AS1, NKPD1, SPRED2, CD36, SCARB1, PLPP4, MED12L, ARAP2, CHN2, CHI3L1, ACTBL2, C10orf71, MCIDAS, LRRK2, AKR1C4, ANO4, AGBL1, CEACAM20, ZNF813, RMDN3, CETP, CDR1, LINC00343, TCAM1P, APOC1P1, IGSF23, RMDN2, CDK1, SLC25A48, NKAIN2, FSIP1, CD68, BMPER, C3, CD40, CYP19A1, CRP, NIT2, ANO3, DLG4, ARHGAP20, RCAN1, WDR41, NDUFA12, STK32B, EDEM2, DSCAML1, RNF165, SH3RF1, DYRK1A, MIR29A, SYBU, AQP4, APBB1, DLX5, DBN1, PALM2AKAP2, CEACAM19, DPP4, IL6-AS1, ARVCF, CDC42SE2, DMXL1, TULP4, DAPK1, PMS2CL, POTEKP, MIR34A, VAT1L, OLR1, HDAC2, LRP8, GSN, CCL11, S100A9, COL25A1, POTEF, KLK6, BLMH, HSD17B7, P2RX7, COX8A, ABCB6, PRRT2, IL2, SORCS1, NR1I2, MAPK3, ITGAM, CASR, ATP7B, VDAC1, EGR1, PDE4A, RAB5A, SUMO1, NRG1, OXER1, NTRK1, TFCP2, ANK1, CSNK1D, DLST, APLP1, BLVRA, NFIB, IL1RN, HTT, ACAT1, PLA2G4A, NFIX, NLRP1, GPRC6A, HMGCR, PPID, LPAR3, FZD4, REG1A, MRGPRX1, LRP2, DBH, PSENEN, VPS35, ESCO1, HSD11B1, VN1R17P, SOX2, AGTR1, XBP1, MIR155, MRGPRX4, MRGPRX3, GAL, GPR151, IL13, PAEP, OGDH, GPR166P, STAT3, SET, NFIA, PLB1, AR, LGR6, DHRS11, ABCG2, C4A, KCNIP3, HSD17B13, ABCG1, TTBK1, NOTCH1, EIF2AK3, SLCO6A1, CHMP2B, RBM45, CD44, RIPK1, APBA1, GSTK1, ADNP, ICAM1, BRCA1, APCS, TNFRSF1A, NFKB1, CNTF, MMP3, KLC1, LBP, CTNNA3, SGSM3, FGF2, C4B, HIF1A, CREBBP, SERPINA1, TMEM106B, GRIA1, GRIA2, ECE1, C4B_2, GSAP, OGA, TFRC, PLA2G6, ST3GAL4, PAWR, MFAP1, KAT5, GSTM1, APRT, COX1, HP, NTF3, MIR206, FPR2, CDC42, FUS, MARK1, FGF1, PREP, C5AR1, PON2, MIR29C, CALB2, PDIK1L, SYK, S100A1, CH25H, SREBF2, COX5A, GRIN2A, VCAM1, TMED10, GSTP1, KLK8, PHF1, CXCL10, MEFV, SP1, GJA1, IGFBP3, SLC17A7, CYP3A4, FOXO3, HMGA1, SLC11A2, XPR1, MARK2, PPIF, CRHR1, SHANK3, MYC, CD40LG, CPOX, FKBP5, ANPEP, CAST, C1D, FKBP4, HSPA1A, FLT1, MIF, PLA2G2A, CX3CR1, CSF3, IFNB1, KALRN, PLTP, STXBP3, DDR1, PWAR1, PRDX2, TP63, VIM, IL23A, F2RL3, MMP14, MEF2C, TREM1, TMED10P1, NAT2, MIR342, SAMD9, RAB7A, PGR-AS1, TRPM2, EGFR, ADRB2, CLDN5, ETS2, SYT1, TIMP1, NME8, ELANE, F2R, CD59, EPHA4, CBS, MSMB, APLN, MMP2, MYCL, CALML5, SYN1, XRCC1, TGM2, EEF2, PLA2G7, ELAVL2, EDN1, TMEM97, HMGB1, MIR455, HTRA1, BPIFA2, SLC52A2, NQO1, TUBA1B, FOS, CRYAB, SLC2A1, GPR3, LGMN, SLC2A3, RIDA, FN1, ABCA4, HSPA1B, PECAM1, PTEN, HSPA8, HLA-A, PTPN1, HAMP, TXNIP, GRM2, P4HB, LIN28A, PSPH, GSTT1, CCN2, DECR1, CPLX1, BCYRN1, NES, POU5F1P4, MIR21, GRK5, POU5F1, NTSR1, MIR212, PRKN, LINC02210-CRHR1, HSPA5, DLD, DAB1, HTRA2, POU5F1P3, MIR137, DNAH8, MAPK10, GH1, SERPING1, ADAMTS2, EEF2K, GSTO2, ROCK2, NEDD9, SPTBN1, NTN1, CEBPD, GDF2, CEBPB, PWAR4, SYNM, IGFBP2, GLUL, ABCC9, ATM, PSPN, PTPRC, MIR29B1, RANBP9, NDRG2, CNR1, RTN4R, PTBP1, AQP1, PDK1, MIR106B, PDE4D, ARNTL, PRDX1, ADM, RENBP, POMC, PTPN4, MS, PDGFRB, P2RY2, MIR142, PDE9A, SSTR4, KLK3, BCL2A1, C2, SRPK2, NFATC2, ADCYAP1, LRRTM3, PLD1, NUBP1, MIR424, ATF4, BSG, MIR29B2, PPY, BMP4, TBP, SLC18A3, POLB, NOTCH3, SLC18A2, NPTX2, MTR, SI, MIR222, SH3GL2, ND2, NR4A2, SELENOP, CXCL12, CCL5, ATXN1, CALM3, ITGAX, IFNA13, DISC1, OPTN, HTR1F, HTR4, WNT3A, COL11A2, C20orf181, IFNA1, KEAP1, HDAC4, KLK4, SEMA6A, LRRC4, CRTC1, IL9, DAO, ALOX15, AGTR2, IDO1, SLC25A27, ABCG4, CD55, APOA4, MCOLN1, REM1, ATCAY, EBPL, HSPB2, HSPA9, PLK2, GAD1, NANOG, DCX, COASY, UBE2K, DDIT3, TREML2, APBB2, MAP1LC3B, SRRM2, GZMB, FXN, HNRNPA1, HPSE, RAB10, CIP2A, FOLH1, STIM2, DIO2, MMP24, CEBPZ, GBA, CDR2, ITPR3, CDKN2A, MELTF, SLC30A3, ADRA2B, FTO, FNDC5, GGA3, XPNPEP1, VGF, NR1H2, UGCG, MFGE8, MGAT3, CXCR4, TLR9, APOC3, GPT, ELK3, NEAT1, ADORA2A, MMEL1, TRPC6, EIF4E, CAMK2A, MS4A6E, SRR, HSPA14, IRS2, MGAM, C1orf52, HDAC3, PABPC4, ACKR3, LGALS3, FAM20C, WNK1, DRD4, CYP2C9, MBTPS1, DRD1, LRP6, GRK2, CYP2B6, OGT, LIPA, AD11, GORASP1, PTGDS, SPEN, MIR200B, NPTXR, DNMBP, MIR200A, NCOA6, MIR181C, RBP4, RELA, OPN1LW, EFHD2, MIR188, TPH1, HNRNPA1P10, CTNNBL1, SLC40A1, PNO1, CHCHD2, SDF4, RETN, GOLM1, PPP3R1, PYCARD, PAG1, CCR2, DDIT4, RCBTB1, SBNO1, PPARD, CD274, PCBP4, ACE2, PROS1, PRND, PPP1R15A, CIZ1, MIR26B, TPSG1, GGA1, CFAP97, MAP2K1, AATF, SHANK2, PRL, RBMS3, LOC107987479, MAP2K2, PAXIP1, CHCHD10, SBNO2, PTGES, SPHK1, LPAR2, PPIG, NRXN3, MED23, SPP1, MAPK8IP1, BAG3, APBA3, TAP2, PRDX6, CARTPT, SNAP91, SV2A, MALAT1, MAK16, SYVN1, GDF11, TAC1, TAT, SLC6A2, TRPV1, CISD3, TPT1, TSC2, TM7SF2, TXN, UBE2I, TLE1, TIMP2, XK, CNTN2, TGFBR2, YY1, GOLGA6A, ANP32A, TAM, TERT, DCP1B, TNFSF10, PPP1R1B, GPHN, RGS2, ADAM30, SAA1, METAP2, IMMT, SDS, ADAP1, RYR3, ECHDC3, RYR2, RXRA, SCD, RPS6KB1, CIT, RPS6, CTXN3, LMTK2, NLGN1, ROCK1, RGS4, ATXN2, SRL, STUB1, SHBG, LILRB2, AKR1A1, OLFM1, SKIL, SLC9A6, CREB3, PITRM1, SCGN, CXCR6, OCM, RIN3, SGCA, SFPQ, NCKAP1, CPLX2, TP73, EDAR, CCL3, NPS, BEST1, HPS1, CXCL1, GLO1, LIF, CDH1, LHCGR, CDK4, PCNA, PCK1, L1CAM, GPR42, GPX1, GRB2, ANGPT1, ANGPT2, CETN1, MYD88, GLB1, AKT2, LMNA, DNMT3B, TSC22D3, CD38, PER1, CD69, DRD3, LOX, CD74, LMNB1, DNM2, GAS6, AVP, GC, DMRT1, SARDH, GRIN1, ANXA5, BACH1, P2RY1, INPPL1, CSF1, CS, NEFM, NTS, APEX1, STS, HTC2, NEUROD1, NPTX1, NPPA, ATF2, HTR2C, ARRB2, IGFBP7, HMGCS2, CLK1, CKB, APBA2, CYP17A1, GSTM3, CHGA, CYBB, JUN, CTSS, ORM1, ITPR1, CHRM1, CHRM2, OPRK1, OPRD1, CTRL, HK1, ADRB1, LAMP2, CASP2, EDNRA, PLD2, CAPN2, F2RL1, ACO1, ERBB4, FAT1, FGFR3, CALM2, BRS3, CALCA, CAD, EGF, CASP4, FCGR3B, FDPS, LYZ, FCGR3A, FLNA, MECP2, FABP3, ADRA1A, PLXNA2, MBP, FAAH, ENPEP, F12, BAG1, MEOX2, HOMER1, ITGB2, DBA2, ITGAL, ITGB1, AIM2, AZIN2, CD80, ITIH4, CD46, VIP, CHRNA3, ATG5, TREML1, MCL1, GPRASP2, VWF, APOA5, TMEM119, KLF4, SOCS6, WNT1, XBP1P1, FOXQ1, C3AR1, OPN4, USF1, C1QA, CXCR2, VPS26A, MOGAT3, CCR3, IL6ST, IL5, IL1RAP, LMF2, IL1R1, CREB3L1, UNG, MCU, CLSTN3, SNPH, IL9R, NPEPPS, NAPSA, USF2, MEF2A, ING1, CGB8, FTMT, CHM, VAV1, IMPA1, C1R, ILK, ADAMTS3, IL16, MAP3K5, IL15, GDF15, CGB5, CA2, KCNB1, TSPOAP1, SMAD2, DPPA2, SGO1, LIG3, IFNL3, TNK1, CP20, APCDD1, HSD17B6, CDKN1A, TTBK2, CDKN1B, SLC2A14, CFLAR, STMN1, LIPC, TAB3, CHIT1, BRAP, SPARCL1, MLKL, PTCRA, CD47, LGR5, CD8A, CCT, NR4A3, USP9X, MSRB3, CDR3, CCK, LNPEP, CASP7, CHRFAM7A, CAMP, PER3, YES1, CGA, MARK3, CGB3, SYNGR1, CALCR, IL1RL1, ARHGEF2, PER2, SLC33A1, TPH2, CHEK1, RAB7B, NOG, MBL2, CFL2, HSPB6, AHSA2P, SLC30A1, CD200R1, SOCS3, KDR, KIF5A, HAP1, CALR, CES1, TRPA1, HSPB3, WASF1, SLC32A1, ARHGEF7, CAMK4, COL3A1, H3P40, SCRN1, PTCD1, SPHK2, ATN1, PPIL2, POU2F1, FOSB, GCA, FLT4, SH2B1, APPL1, DNMT1, FLG, FOXO1, DUSP1, DUSP6, HHAT, HSPB8, E2F1, PLXNA3, DOCK2, PNPLA2, ADI1, GMFB, GPI, GPC1, KIF21B, NMNAT2, TRIB3, ALS2, DLG2, DLG3, GLS, PDSS2, ASTN2, MCF2L, GLI2, KIDINS220, CBLIF, SYNE1, DMD, GGT1, FKBP1A, SIT1, SV2C, GDE1, FOXP3, ASCC1, TMED7, FIS1, PRLH, CRYL1, ADIPOR1, LSR, F11, MBL3P, SIRT6, TRMO, NRN1, LCMT1, PRRX2, ERN1, BIN2, UBR5, HEBP1, GEMIN4, PDCD4, TBK1, SLC25A38, FGF14, PCSK1N, TRPM7, DLL1, FLVCR1, AHI1, SETD2, ELK1, IL22, NCAPH2, ELN, PADI1, BPTF, NRBF2, FABP5, EP300, PLA2G3, GRHL3, CXCR3, NAV3, SIRPB1, FLOT1, MET, KCNMB2, CRISPLD2, ARHGAP24, HNMT, SNX27, NPL, BHLHB9, TRIM13, HMOX2, KLF2, CSNK1E, LPAL2, CPQ, PPP1R2C, RAPGEF3, TET1, CRYZ, SORBS3, CTBP1, BCL2L11, COL17A1, NCAPD2, COX10, UBASH3B, NR1I3, ACOT8, PTPN5, PPP1R9B, TOM1, MINDY4, CPE, HTR7, NR1H3, HTR1B, HTR1A, LRPPRC, PDIA6, RHBDD1, NAA25, HLA-C, TPX2, BCAN, ADAMTS13, MOAP1, TNMD, GRIA3, NEUROD6, CHEK2, PADI2, HRH3, PHB2, SIL1, MGLL, FFAR1, GADD45A, MMRN1, DEFA1, IL21, NLRC4, GPR17, AZI2, HHIP, CTF1, HCRTR2, HLA-B, CTNND2, HHEX, HGF, CTSG, HDAC1, CTCF, DHX40, PTGES3, STIP1, CTSZ, CXADR, CARD14, CYP1A2, PDE10A, LILRB1, EHMT2, PDIA2, UMOD, ANGPT4, MIR339, SYN2, MSD, ACP3, APEH, ST8SIA1, AZU1, PI4KA, NCAM1, MIR144, SMIM10L2B, MSI1, NAP1L1, PRSS3, PEBP1, MASP1, SIM2, TIA1, MIR15B, ATD, RPL29, ABCC1, NCAM2, MIR125A, TLR5, SERPINF2, TNFAIP1, CXADRP1, MAPK9, ZFHX3, GGTLC4P, AD10, SGCG, MIR451A, CDR1-AS, TPTEP2-CSNK1E, MIR384, ITSN1, CBSL, MPZ, NFATC4, PKM, NCL, NTF4, LOC643387, SLC1A3, APOA2, THAS, PSMB6, SERPINB6, PSMB9, RHOA, ARMCX5-GPRASP2, SMPD1, REG3A, ATP4A, MIR193B, RFC1, NOTCH4, SLPI, PGF, AEBP1, MIR214, MIR219A1, SLC19A1, MIR22, PCSK1, ALPP, AMD1, MTNR1A, TGFBR1, COX3, ATP12A, NM, ADD3, PSD, TGM1, ARR3, NPM1, PAK1, TMED7-TICAM2, PNP, MIR195, MTHFD1, ADH1B, AMPH, ND4, AMD1P2, ARG1, SULT2A1, RRAS, PDE7A, TTPA, TYK2, TXNRD1, PPP1R1A, PPP1R10, SPG7, SPAST, RAB4A, PPP2CA, OTC, PPP2R2B, MMP1, ARMS2, RAB3A, GGTLC3, RTL1, P2RX4, ST13, SPARC, ALAS1, PPP3CA, NEFH, SEL1L, TYR, RAB6A, MICB, PPIA, CCL4, BST1, TICAM2, BNIP3, MIR326, OPRL1, PON3, BMP6, OPRM1, AHSG, H3P17, SDC2, AGRN, TYRP1, PPP1CA, BMI1, TYRO3, PNMT, DEFA1B, GGT2, ORI6, SMIM10L2A, CISD2, ARSA, EIF2AK4, PRKAR1A, LRP1-AS, SRSF2, MIR98, MIRLET7B, CD200, PDCD1, RAP1A, GGTLC5P, CCND1, ANXA6, FXYD1, S100A6, NFATC3, PLK1, ABO, PTGER3, APC, S100A12, ASL, HSP90B2P, SETMAR, PRRX1, PZP, STAT1, ODC1, CFB, CDNF, ZBTB4, PARK16, SUGP1, DIO1, SORCS2, MAGEE1, ALDH1A1, MIR1306, DES, DIAPH1, LSM2, MIR1229, XPO5, HCN3, CFD, MIR664A, KIF17, WDR48, MTRNR2L12, PRX, DHFR, EPG5, SEPTIN1, FAS-AS1, RNF213, MIR320E, MIR1908, HECW2, LINC00672, NUFIP2, ABCD1, DLG1, QRFP, ZNF410, AOC2, NBEAL1, CYP11A1, OPN1MW2, AD6, P2RY12, NMNAT1, DEPTOR, TNS3, CYP2D7, FAM72A, NUCKS1, CLEC7A, CYP26A1, ARAP3, GREM2, CDKN2B-AS1, CYP2J2, UBE2Z, MIR1246, TSPY3, MIR632, CTSK, GTDC1, CTSL, MIR650, MIR660, SNORD118, TNFAIP8L2, LYNX1, MUL1, PAGR1, CYLD, MAPKAP1, APOF, PDCL3, CYP2C19, NOC3L, CYP27A1, DPEP2, MFT2, PROK2, HPSE2, AD14, AKR1C2, ALPI, TRPV4, NTN4, PRM3, PDF, JAM2, ALOX5AP, TSPY10, DEFB4A, DEFB4B, ALOX12, PTBP2, DCN, NECAB3, FKBPL, NEUROG2, DGKQ, SLC25A4, MIR873, MIR301B, CENPK, DAXX, GFRA4, GOLPH3, ERVK-6, MTUS1, DBI, MIR937, ANG, ACE3P, SOD2-OT1, ANK3, DRD2, ZNF608, NAT10, DYM, LOC102724334, TRIT1, EIF4G2, TET2, EIF5, SERPINB1, ELAVL4, PDP1, ACO2, THRA1/BTR, UGT1A1, CCHCR1, CPVL, SMOX, TOLLIP, TERF2IP, SNTG1, EMP1, LOC102723407, EIF4EBP1, MIR6845, EIF2S3, ADCY2, NUDT11, EGR2, MSTO1, ADARB1, SLC6A15, ADA, TAPBPL, TESC, MIR6840, ACVRL1, FOCAD, EIF4A1, CASZ1, QRICH1, PGPEP1, EIF4A2, NDE1, ASIC2, CTTN, ACADVL, GSKIP, LNCRNA-ATB, ATP6V1H, H3P7, TDP2, ERBB2, CINP, ZCCHC17, H3P13, DTL, GPRC5B, ERCC1, DCDC2, NAT8B, GULP1, H3P23, ERG, H3P28, H3P11, PPIL1, STIN2-VNTR, NANS, EPHA8, H2BS1, POLE3, ACACA, SLC29A1, FXYD6, LRP1B, CST12P, SIRT1-AS, INPP5K, MSRB1, ARID4B, EPOR, ABL1, AAVS1, NR2F6, ERVK-32, LOC110366354, MNS16A, EFNA5, SLC47A1, ALAD, EEF1A1, SNHG19, MICA, DNTT, SOX21-AS1, DOCK3, DPYSL3, MIR626, XAB2, MFF, DUSP22, ARNTL2, SPPL2B, MCCC1, TMX2-CTNND1, ANKS1B, DPYSL5, FXYD6-FXYD2, BARHL1, DSC1, TWSG1, TLE5, DNASE1, DNA2, OCLN, NLN, AMIGO1, AHR, PLEKHG5, SLC24A3, SPC25, TTC7A, PELI1, JAG1, TMEM159, RTN4, APMAP, CD177, CAMK1D, PLAAT1, NR0B1, TIGAR, P2RX5-TAX1BP3, PARD3, GKN1, ADH6, INAVA, CDK5RAP2, OGDHL, LINC01080, ATF7IP, IPO9, VAC14, DVL1, PPP4R3A, OPN1MW3, EBM, OTUB1, SOX6, SLC30A10, SMPD3, MEG3, PLIN2, FBXW7, TDP1, ADORA1, DSC3, ACSS2, BTNL2, KIAA1217, ZNF253, CFC1, MIR4668, DSG1, APOM, MYO5C, MIR4487, NOTCH2NLC, USE1, SELENOS, GDNF-AS1, DSPP, ADCY10, ADRA2A, ZNF415, LINC-ROR, NARS2, CSF2RB, MIR616, MIR20A, CDC25C, PROM2, ATP6V1E1, IL23R, GLIS1, PM20D1, PHF13, CDH2, ZNF569, MIR191, CDK9, MIR192, PRIMA1, CDKN2D, MIR196A1, OR2AG1, LAYN, PIWIL4, MIR19B1, GPBAR1, CDC25B, GDF7, ZDHHC15, MIR139, CD63, SGMS2, MIR140, TMPRSS6, RHBDL3, AVPR2, MIR15A, CBLL2, MIR186, PRUNE2, AMOTL1, CD81, MIR18A, SLC2A12, CDA, MIR181A2, ATP5PO, SESN3, ATP6V1B2, UBR1, ATP5PF, PPME1, MIR224, LYZL4, KCNH8, MTERF4, MIR23A, CPO, ACMSD, MIR23B, BHLHE23, MIR25, CFL1, OSCAR, SPNS2, SEZ6, SLC38A10, MSI2, CFTR, MIR27A, MIR223, ALDH7A1, MIR221, SELENOM, ATP5MC2, CACUL1, HECTD2, SREK1, CTCFL, CBLN4, CDSN, ATP5MC1, DEFB104A, OCIAD2, MAGEC3, MIR210, CEACAM5, CECR, PPARGC1B, ATP5F1B, IL31RA, GNPDA2, SCARB2, NSMCE1, SOCS4, UBE2L1, BNC1, CACNA1C, SLC25A20, SERPINA13P, BLM, SREK1IP1, MIF-AS1, C20orf203, SYPL2, ZNF763, CCL4L1, BID, BGN, ZSCAN1, ZADH2, SMIM20, MILR1, PGP, GOLGA6L2, TMEM189-UBE2V1, TMEM189, IL31, C4BPA, BTK, AMIGO2, HCN1, NHLRC2, ATP9B, SBSN, BMP1, OSTN, C5, CFAP410, BARHL2, NANOS3, C9, STING1, GADL1, ARMH1, VPS51, HCAR2, CAPG, LINC00639, TMEM201, LIN28B, CD5L, MIR127, CD19, KIF6, MS4A1, MS4A3, HYLS1, STOX1, FOLH1B, OR8J1, TRIML2, CD28, KHDRBS2, GAPT, CENPV, KLHDC8B, MIR134, CD86, PIKFYVE, SLC29A4, CCNC, KRIT1, PTF1A, DAOA-AS1, BDKRB2, HCA1, BRD3OS, ASPM, BCS1L, SGMS1, BCR, MIRLET7D, MIR122, RUNX1, ANKK1, BCL6, PHYHD1, BAK1, MIR10A, EBF3, CCKAR, MIR28, FRMD6, MIR613, ADAMTS10, TMEM175, XIAP, MAF1, BIRC3, SLA2, ANTXR1, ASCC2, CRHBP, EVA1A, QRFPR, MAGT1, NCALD, LOC646506, ROPN1L, L3MBTL2, GMNC, SCFV, CSE1L, RNF146, PHF6, HOOK3, BRSK1, MBOAT4, COX15, MIR497, MFSD2A, MIR501, ACCS, ARG2, FAM126A, CPB1, CPN1, ECSCR, MAP1LC3A, MIR484, AQP9, CPS1, SNORD35B, CPT1A, ABLIM2, FASLG, NETO1, DOCK8, RNFT2, C1QBP, TM2D3, ASRGL1, PTGES2, PANK2, MIR590, SCD5, CSNK2A1, VCAN, ZC3H14, CSPG4, CTBS, MIR592, MIR598, CAMKMT, CTNS, SLTM, PTCD2, CTNND1, MIR603, NUBPL, WDR26, SPHKAP, GSTT2B, TMEM163, NCF1, LBH, SPAG11A, SFTPA1, CSF3R, ZNF436, CSN2, NDFIP1, MIR545, SLC44A4, SLC19A3, FAM72B, AIRE, IQCJ, CSNK1G2, DNAJC5, CSNK1G3, LINGO1, ATG4C, ATP2B4, MIR346, SERPINC1, CISH, ASPA, CLC, UCN3, TMEM54, ASS1P1, CLCN3, NACC1, ASIP, STX1B, IFT43, MIR133B, MIR151A, CLK2, TP53INP1, MIR330, MIR335, MIR338, MIR93, SLC26A7, OMA1, CHGB, PLD4, TDRD9, CHD1, MIR299, ATIC, ATHS, H4-16, LRIG3, EXOSC6, CHRM3, MIR30B, MIR30E, AGAP2, MIR31, MIR34C, MIR9-1, GRIN3B, GRIN3A, ASAH1, MIR369, H2BC12, KPRP, LRSAM1, MIR429, H4C15, SHF, GADD45GIP1, COL11A1, ZNF628, MIR431, HNP1, NAV2, MIR409, SLC31A1, RPPH1, SNORD14E, SNORD14D, SNORD14C, SNORD14B, COX6B1, MIR485, CNTN1, DNM1P33, CNTFR, CHRDL1, CLN3, MIR361, MYOCD, PRDM6, DNER, SPECC1, MIR377, CLN5, EXOC3L4, CNP, MIR425, ARRB1, ZNF804A, BDNF-AS, NLRP12, CCR6, ABCC2, DEFB104B, LRRC15, POU3F4, HOOK1, TERC, NAT1, MCM2, EZR, MDH1, VEGFC, MDH2, MDM4, MEF2D, UVRAG, UROD, UQCRC1, UGT1A, SLC35A2, UCP2, UBTF, UBP1, MID1, UBE3A, UBE2V1, CXCL9, ATXN3, UBE2D2, UBE2A, UBC, MAP3K10, MC1R, WARS1, WAS, ZMYM2, MANF, SCG2, FZD5, SMAD7, MAG, MAP3K12, MAP1A, MAP1B, ZNF236, ZNF224, ZNF217, RNF112, WEE1, MZF1, ZIC1, MARS1, MAS1, MAT1A, MAT2A, MAZ, XIST, WT1, WNT2B, WNT5A, UBA52, KMT2A, MLLT3, THBS1, TLR3, TLE3, MSH3, TKT, TIMP4, TIMP3, MSR1, MSRA, THRA, THOP1, THBS4, CYTB, MRE11, NUDT1, TGFBI, TGFB3, ND1, TFF3, TFDP1, MTNR1B, MTRR, TRNL1, MUC1, TERF2, TSPAN7, MRC1, TWIST1, TRAF2, TUBA4A, NR3C2, TTN, TSPY1, TSHR, TSG101, TSC1, MMP7, MMP8, TRPC1, TRH, NR2C2, TNFAIP6, MMP13, TPM1, MOG, MOV10, TP53BP2, TP53BP1, MPG, TNR, TNNI3, MPI, MPST, SLBP, REEP5, DEK, SNX3, TNFRSF6B, RAB11A, LDHA, LEPR, LGALS4, LGALS9, GPAA1, RNMT, GBF1, ADAM19, URI1, TRADD, LCK, B3GALT4, LIFR, LIG1, SOCS1, NUMB, LIMS1, AOC3, PDE8B, USO1, TNFSF11, STK16, LCT, CES2, KMO, KLRC1, BRSK2, KCNQ1, KIR2DL2, NOL3, ATP6V0E1, SELENBP1, USP13, KLKB1, CDK5R2, RAB29, MBD2, KIF11, TMEM11, ENDOU, EIF2S2, TAX1BP1, NAE1, KRT14, KRT18, LAMC1, LBR, PROM1, LCAT, SOCS2, PRKRA, DEGS1, DDX39B, PABPN1, EOMES, BAP1, LTF, H4C9, COLQ, DYSF, CHAF1B, LYN, NRIP1, COIL, SLC7A5, AD5, H4C1, FGF23, ADAM12, BRD3, PSCA, ARHGEF5, TFPI2, FZD3, GHS, M6PR, MARCKS, SMAD1, LTC4S, H4C4, BHLHE40, IRS4, MAPKAPK5, LMO4, LOXL1, CST7, DDO, DGKZ, GAS7, PIK3R3, PKP4, PPFIA1, LRPAP1, SORBS2, H4C6, CUL4A, GNPAT, LTB, H4C14, H4C13, H4C5, H4C2, H4C8, H4C3, H4C11, H4C12, TERF1, MUC4, KCNMA1, TDO2, PCP4, CDK18, RBM3, RBL2, RBBP6, RB1, RASGRF1, RASA1, RARRES2, RAN, RAF1, RAD52, PCYT1A, RAD23B, RAC2, PDB1, RAB27B, RAB27A, PDC, PDE2A, PURA, PDGFB, ENPP2, PDYN, PTPN13, PC, PAX6, PARN, RPL15, P2RX1, S100A8, P2RX3, P2RX5, P2RY4, RREB1, RPS23, RPS21, RPS6KB2, P2RY6, RPS3A, RPL13, RET, RPA1, PAFAH1B2, RORA, ROM1, SNORD15A, BRD2, RNASE1, RHO, RHD, PAK3, TRIM27, PTPN11, PENK, PTN, PMM2, PLAUR, PLCL1, PLEK, PRKCE, PRKCD, PLP1, PRKAR1B, PRKACB, PRKACA, PLXNB1, PML, PRG2, PLAT, PMP22, PRB1, PPT1, PPP2R5E, POLG, PPP2R1A, PPP1CB, PPL, PPIC, PPIB, POR, MAP2K3, PLAG1, PFDN5, PSMD2, PFKFB3, PTGER2, PTGER1, PGD, PTGDR, PTCH1, PGR, PHB, PSMD9, PSMD7, PSMD3, PSMB2, PITX2, SERPINE2, SERPINI1, KLK10, PIK3C3, PIK3R1, KLK7, PIK3R2, PRS, PROS2P, PIN4, PROC, S100A10, OXT, OXA1L, SQLE, STAR, ST14, ST2, NDUFA6, SSTR3, SSTR2, NDUFA9, NDUFB8, SRM, SRF, NEDD4, SEPTIN2, STC1, SP4, NEU1, SOX5, SOX3, SOS2, SOS1, SOD3, NFE2L1, NFKB2, SNRPG, SNRNP70, NDUFA5, STIM1, NME1, MYH9, TRBV20OR9-2, TCP1, TCN2, MMUT, MUTYH, TCF4, ELOC, TBX2, MX1, MYH6, TARBP2, MAP3K7, STK11, MYO6, TACR2, NACA, VAMP2, VAMP1, SURF1, ABCC8, SUOX, NDP, STXBP1, STX1A, NINJ2, NME2, SAA2, OMP, SFTPC, TRA2B, SRSF6, SRSF5, SRSF3, SRSF1, SFRP1, OCA2, MAP2K4, ODF1, SELE, OPA1, OAS3, CXCL11, CCL21, CCL20, CCL19, CCL8, CCL1, SCP2, SCN1A, ORM2, OSM, TSPAN31, OAT, SGSH, SUMO2, SLC8A3, SMPD2, SLN, SLIT3, SLC22A5, SLC22A2, NQO2, SLC18A1, SLC16A1, SLC12A3, SLC11A1, SLC10A2, SLC8A1, NUP98, SLC6A12, NPHP1, SLC6A1, SLC5A2, NRCAM, NRDC, SLC1A1, NRF1, PMEL, YBX1, NT5E, NAT8, SEMA5A, ESRRA, RAB31, MACF1, HEY2, BRD4, TRAM1, CBX5, ANGPTL2, OPN1MW, GRIP1, KCNH4, MSTN, GFER, GFRA1, SIRT5, COTL1, GFRA3, GHR, ZNF629, UBR4, GHSR, WASHC4, GLI1, NUP160, CLUH, GLI3, SCFD1, KCTD2, CLCF1, SEC14L2, NR5A1, SLC24A2, PRPF6, TFIP11, MAFF, EID1, RAB38, FSHR, TMEFF2, PLA2G15, SLC7A11, FTH1, SNHG1, TSPAN15, GAST, ACKR1, G6PD, GAB1, NTSR2, GABBR1, GAD2, GALNS, DDAH1, PADI4, GART, NBEAL2, GMPR, PLEKHM2, WDHD1, GPR39, CARD8, ARHGEF15, AAK1, SYNPO, GPX4, ECD, PARK7, KLF8, TREX1, WIF1, WDR45, ATF6, CORO1A, TBC1D8, SLC7A9, GRIA4, FAF1, GRIK4, RER1, GRM1, STMN2, RAPGEF4, ADRM1, MSRB2, RAB3GAP1, GNA12, ZNF423, ATG4B, UBXN4, RCOR1, SEPTIN8, STAB1, GNAI1, MAPK8IP3, GRAMD4, GNB3, NFASC, KIF1B, GOLGA2, GPER1, SETX, GOLGA4, PDZD2, SAMD4A, KDM1A, GPM6A, RAB21, GPR6, P2RX2, GPR20, SNW1, FRK, FBXO7, BRI3, SNX12, SOCS7, CD209, FABP6, TBX21, NOP53, FABP7, SLC2A8, UBQLN2, A1CF, PSAT1, FANCG, HOOK2, DELEC1, FASN, SNX8, NPC1L1, BLNK, MS4A2, FCGR1A, FCGR2A, MYLIP, SCG3, DROSHA, TMEM230, NOX4, PCA3, SPCS1, VRK3, ETFA, SLC25A37, TLR8, SLC22A17, ECSIT, CD320, EZH2, DNAJC27, CLEC1B, NT5C3A, MZB1, F2RL2, HP1BP3, F3, F9, IRAK4, SAR1B, UTP11, F13B, SH3GLB1, SIDT2, SHANK1, TRAT1, F11R, RGCC, TMEM176B, NOCT, FBXO2, NPTN, TPK1, VCX, GREM1, FKBP1AP2, FKBP1AP3, AGO1, SEZ6L2, FKBP1AP4, FGF21, CLDN17, NOC2L, SND1, FOXM1, EPC2, ATRNL1, LRP10, FLNB, FMR1, POU2F3, TXN2, FBXL2, FOLR1, FOLR2, FKBP1AP1, B3GAT1, IGHV1-68, TNFRSF21, FEB1, FES, FGF9, RABGEF1, PRPF19, FGF13, FGFR1, FGFR4, PDLIM3, RND1, KLHL20, COQ2, CACYBP, HCAR1, FHL2, VPS4A, IL37, GLS2, NAAA, CYTH4, DKK2, DKK3, BBC3, SDCBP2, GRM3, IL24, SPAG9, CXCL2, PCLAF, IGFBP1, ACAP1, IGFBP5, SART3, KDM4A, IGHG3, SDC3, SH3PXD2A, RGS6, SNCAIP, TCL1B, IL4R, IL7, BCAR1, CCL4L2, CXCR1, BAG2, IL12B, BAG5, TMEM59, TBPL1, GAL3ST1, AKAP5, STX8, PIEZO1, BMS1, PTDSS1, IDH1, SH2D3C, GNE, SH2B3, IRF8, SRA1, TANK, KCNE3, HNRNPDL, CCS, NUP153, MED12, HS3ST1, TOMM20, RBM8A, IDH2, CFI, SV2B, TECPR2, IFI27, TOMM70, KIAA0319, IFIT3, IFNAR1, IGBP1, INSRR, PCYT1B, IL27RA, CCNE2, NOLC1, TIAF1, JUND, ZMYM3, KCNC4, KCNJ13, HGS, SYNGR3, ATG12, CBFA2T2, RABEP1, P2RX6, RAB11B, SLC16A3, SLC16A4, ATP6V0D1, RGN, USP10, USP2, USP14, DNAJA3, CLDN1, CLDN8, ARTN, JUNB, GPR50, PICK1, ITPKB, IRAK1, HOMER2, IREB2, IRF3, IRF6, IRF7, ITGAV, CYP7B1, ITGB3, NRXN1, SLC22A8, ITPR2, AIMP1, JAG2, ITGBL1, LHX2, SLIT2, TAOK2, CD163, JAK2, GPR37L1, PIWIL1, MAPKAPK2, PDLIM7, IARS1, TNC, IL18BP, CCT2, HCK, NRG3, USP39, DCTN6, CD226, HDC, HDLBP, CAMKK2, HIP1, TXNRD2, NPC2, SLC35A1, HBG2, PRDX4, ZNRD2, HYOU1, HLA-DQA1, SEMA4D, HLA-DQB1, NXF1, HLA-DRA, ATP5PD, COG5, GPNMB, CHL1, HAS3, FAM3C, GYPA, GSK3A, COPS5, GSM1, GSTM2, EBNA1BP2, PRSS21, PRDX3, GSTZ1, GTS, GUSB, C1QL1, GYPB, HAS1, GYPC, CCL27, ALDH1L1, GYPE, HAGH, WASF3, HSPH1, GJB6, HARS1, ARPP19, DHS, HLA-DRB4, HLA-G, PQBP1, MPHOSPH6, STAM2, GLYAT, HOXA@, RABEPK, HPCA, CALCOCO2, HRC, OLIG2, DDX39A, TOPORS, EIF1, HSD17B1, RAMP2, WASF2, HSD17B4, HSPA2, HSP90AB1, DNAJB1, NAMPT, BCAP31, CTDSP2, TSPAN3, ACTR2, CERT1, ABCC4, HNRNPK, HMBS, NPM3, CFDP1, PRMT5, HMGB2, YAP1, IFITM3, SPAG11B, PEMT, RACK1, SYCP2, TUBB4B, SEMA3A, WARS2, HNRNPC, FOXA1, CCL26, TLR6, FOXA2, LAMC3, LANCL1, HNF4A, TCIRG1, APBB3, APC2, HNRNPA2B1, MTCH2
- Alzheimer's Disease Mayo Clinic
  
  Overview Alzheimer's disease is a brain disorder that gets worse over time. It's characterized by changes in the brain that lead to deposits of certain proteins. Alzheimer's disease causes the brain to shrink and brain cells to eventually die. Alzheimer's disease is the most common cause of dementia — a gradual decline in memory, thinking, behavior and social skills. These changes affect a person's ability to function. About 6.5 million people in the United States age 65 and older live with Alzheimer's disease.
- Alzheimer Disease MedlinePlus
  
  Researchers have found that this form of the disorder can result from mutations in the APP , PSEN1 , or PSEN2 genes. When any of these genes is altered, large amounts of a toxic protein fragment called amyloid beta peptide are produced in the brain. ... As a result, people with Down syndrome have three copies of many genes in each cell, including the APP gene, instead of the usual two copies. ... Learn more about the genes associated with Alzheimer disease APOE APP PSEN1 PSEN2 Inheritance Pattern Early-onset familial Alzheimer disease is inherited in an autosomal dominant pattern , which means one copy of an altered gene in each cell is sufficient to cause the disorder.
Neurogenic Inflammation Wikipedia

PMID 18079356 . S2CID 1001915 . ^ Chiu IM, von Hehn CA, Woolf CJ (July 2012). ... PMID 22837035 . ^ Fig. 3 of article Chiu IM, von Hehn CA, Woolf CJ (2012). "Neurogenic inflammation and the peripheral nervous system in host defense and immunopathology" .

TNF, TACR1, TAC1, APP, POMC, CALCA, PTGS2, AMN, PNOC, NGF, MCAM, CIRBP, IL2, TNFRSF1A, TNFRSF1B, RXRA, TRPV1, TRPV4
Coronary Artery Anomaly Wikipedia

AA = antero-left; AR = antero-right; Cx = circumfles artery; IM = intramural; IS = intraseptal; LAD = left anterior descending artery; M = mitral valve; P = posterior; PP = prepulmonic; RA = retroaortic; RC = retrocardiac; RCA = right coronary artery; T = tricuspid valve. R-ACAOS-IM [2] is observed in a higher percentage of cases (0.35% of adolescents) than L-ACAOS-IM [3] but is less likely to be associated with sudden cardiac death in athletes. ... Assessment of severity of stenosis is best achieved by intravascular ultrasound (IVUS) imaging and it should be considered in known carriers of ACAOS-IM or that have symptoms or positive stress test results or are involved in competitive exercises. ... Importantly, untreated carriers of significant ACAOS should not generally engage in competitive sports or strenuous activities. Treatment options for ACAOS-IM include both catheter-based procedures ( percutaneous coronary intervention [PCI]) and surgical interventions. PCI consists of stent angioplasty of the proximal, intramural segment by placing a thin metal tube (a stent) in order to keep open the narrowed artery. PCI of R-ACAOS-IM is feasible and quite successful, but further experience is needed in L-ACAOS-IM since few cases have been treated percutaneously, while surgery is the recommended treatment in this subpopulation, at this time.

PCYT1A, POFUT1, CERNA3
Pustular Psoriasis Wikipedia

This skin eruption is often accompanied by a fever , muscle aches , nausea , and an elevated white blood cell count . [1] Annular pustular psoriasis (APP), a rare form of GPP, is the most common type seen during childhood. [6] APP tends to occur in women more frequently than in men, and is usually less severe than other forms of generalized pustular psoriasis such as impetigo herpetiformis. [6] This form of psoriasis is characterized by ring-shaped plaques with pustules around the edges and yellow crusting. [6] APP most often affects the torso, neck, arms, and legs. [6] Diagnosis [ edit ] Classification [ edit ] Pustular psoriasis is classified into two major forms: localized and generalized pustular psoriasis . [1] Within these two categories there are several variants: Classification of Localized and Generalized Pustular Psoriasis Localized pustular psoriasis Palmoplantar pustulosis (acute and chronic) Acrodermatitis continua (of Hallopeau) Generalized pustular psoriasis (von Zumbusch) acute generalized pustular psoriasis Acute generalized pustular psoriasis of pregnancy ( impetigo herpetiformis ) Infantile and juvenile Subacute circinate and annular Management [ edit ] injection of methotrexate This section is empty.

IL36RN, IL1B, CARD14, IL1A, IL1RL2, IL17A, PI3, TNF, IL22, AP1S3, TLR3, TNFAIP3, MOG, TNIP1, LDHA, IL23A, NOD2, IL1F10
- Pustular Psoriasis GARD
  
  Pustular psoriasis is a rare form of psoriasis that is characterized by widespread pustules and reddish skin. This condition can occur alone or with plaque-type psoriasis . Most cases of pustular psoriasis are thought to be " multifactorial " or associated with the effects of multiple genes in combination with lifestyle and environmental factors. There are several triggers for this conditions including withdrawal from corticosteroids, exposure to various medications and/or infections. Some cases of the generalized form are caused by changes (mutations) in the IL36RN gene and are inherited in an autosomal recessive pattern. In severe cases, hospitalization may be required. Treatment aims to alleviate the associated symptoms and may include certain medications and/or phototherapy.
Problematic Smartphone Use Wikipedia

Contents 1 History and terminology 2 Prevalence 3 Effects 3.1 Social 3.2 Health 3.3 Psychological 3.4 Neural 3.5 Distracted driving 4 Tools to prevent or treat mobile phone overuse 4.1 Behavioral 4.2 Phone settings 4.3 Phone apps 4.4 Research-based 4.5 Bans on mobile phone use 5 Psychological symptoms of phone usage 6 Depression 7 Isolation 8 Low self-esteem and anxiety 9 See also 10 References 11 Further reading History and terminology [ edit ] It is also known as smartphone overuse , smartphone addiction , mobile phone overuse , or cell phone dependency . ... For 3-4 year-old children: 180 minutes physical activity, 1 hour screen time, 10–13 hours of sleep time per day. [81] Phone settings [ edit ] Many smartphone addiction activists (such as Tristan Harris) recommend turning one's phone screen to grayscale mode, which helps reduce time spent on mobile phones by making them boring to look at. [82] Other phone settings alterations for mobile phone non-use included turning on airplane mode, turning off cellular data and/or Wi-Fi, turning off the phone, removing specific apps, and factory resetting. [83] Phone apps [ edit ] German psychotherapist and online addiction expert Bert te Wildt recommends using apps such as Offtime and Menthal to help prevent mobile phone overuse. [84] In fact, there are many apps available on Android and iOS stores which help track mobile usage. ... In Android a similar feature called "digital wellbeing" has been implemented to keep track of cell phone usage. [85] These apps usually work by doing one of two things: increasing awareness by sending user usage summaries, or notifying the user when he/she has exceeded some user-defined time-limit for each app or app category. ... The researchers implement an Android app that combined these three intervention types and found that users reduced their time with the apps they feel are a poor use of time by 21% while their use of the apps they feel are a good use of time remained unchanged. [86] AppDetox allows users to define rules that limit their usage of specific apps. [87] PreventDark detects and prevents problematic usage of smartphones in the dark. [88] Using vibrations instead of notifications to limit app usage has also been found to be effective. [89] Further, researchers have found group-based interventions that rely on users sharing their limiting behaviors with others to be effective. [90] Bans on mobile phone use [ edit ] See also: Mobile phone use in schools In some places in the world the use of mobile phones was banned in classes during instructional time, for example, in France , Ontario . ... International Journal of Interactive Mobile Technologies . 11 (6): 103–111. doi : 10.3991/ijim.v11i6.7453 . ^ Gardner, Howard; Davis, Katie (22 October 2013). The App Generation: How Today's Youth Navigate Identity, Intimacy, and Imagination in a Digital World .
Fraxe Intellectual Disability Orphanet

A rare X-linked syndromic intellectual disability characterized by a variable clinical picture including developmental delay, mild to moderate intellectual disability, learning difficulties, communication deficits, and behavioral problems (such as aggression, attention deficit, hyperactivity, and autistic features). Personality disorder and psychotic behavior have also been reported.

AFF2, FMR1, APP, SERPINA1, FRAXE, AFM, FRAXA, GTF2A1L, STON1, KIAA1109, STON1-GTF2A1L
- Fragile Xe Syndrome MedlinePlus
  
  Fragile XE syndrome is a genetic disorder that impairs thinking ability and cognitive functioning. Most affected individuals have mild intellectual disability. In some people with this condition, cognitive function is described as borderline, which means that it is below average but not low enough to be classified as an intellectual disability. Females are rarely diagnosed with fragile XE syndrome, likely because the signs and symptoms are so mild that the individuals function normally. Learning disabilities are the most common sign of impaired cognitive function in people with fragile XE syndrome. The learning disabilities are likely a result of communication and behavioral problems, including delayed speech, poor writing skills, hyperactivity, and a short attention span.
- Mental Retardation, X-Linked, Associated With Fragile Site Fraxe OMIM
  
  A number sign (#) is used with this entry because this form of X-linked mental retardation is caused by disruption of the FMR2 gene (AFF2; 300806), either by expansion of a CCG repeat in the 5-prime untranslated region or by deletion. Description FRAXE mental retardation is a form of mild to moderate mental retardation associated with learning difficulties, communication deficits, attention problems, hyperactivity, and autistic behavior (summary by Bensaid et al., 2009). FRAXE is associated with a fragile site on chromosome Xq28 and is the cause of nonsyndromic X-linked mental retardation in 1 of 50,000 newborn males. The disorder can be caused either by silencing of the FMR2 gene as a consequence of a CCG expansion located upstream of this gene or by deletion within the gene (Stettner et al., 2011). Clinical Features Knight et al. (1996) provided clinical details of 1 FRAXE male identified through a screening study as well as 3 other FRAXE individuals identified through previous referrals for fragile X syndrome testing.
- Fragile Xe Syndrome GARD
  
  Fragile XE syndrome (FRAXE) is a genetic condition associated with mild to borderline intellectual disabilities with physical features differing from person to person. The characteristic features are learning difficulties, often a consequence of communication problems (speech delay, poor writing skills), hyperactivity, and a shortened attention span. Nearly all cases of FRAXE are caused by a specific type of mutation, called a trinucleotide repeat expansion , in the AFF2 gene, which is located on the X chromosome. A trinucleotide repeat expansion occurs when there is an abnormally large number of repeats of a specific sequence of three nucleotides (building block of DNA) within our DNA. The repeating nucleotides in FRAXE syndrome are CCG. When the number of CCG repeats is over 200, people typically have the signs and symptoms seen in FRAXE.
Fragile X Syndrome GARD

Fragile X syndrome is a genetic condition involving changes in part of the X chromosome. This condition causes a range of developmental problems including learning disabilities and cognitive impairment. It is the most common form of inherited intellectual disability in males and a significant cause of intellectual disability in females. Other signs and symptoms may include symptoms of autism spectrum disorders , seizures, and characteristic physical features. Fragile X syndrome is caused by a change (mutation) in the FMR1 gene and is inherited in an X-linked dominant manner.

FMR1, APP, AFF2, FMR1-IT1, NUFIP2, GRM5, FRAXA, FRAXE, MMP9, ACTB, ARSD, PVALB, BDNF, FXN, FXR1, FMR1-AS1, G6PD, FXR2, PGD, RBMS3, CYFIP2, SRRM2, PNO1, MFAP1, MAK16, EIF4E, F9, PIK3CA, APRT, PIK3CD, PIK3CG, PTBP1, LINC01672, RAC1, PIK3CB, MECP2, IGF2, IL6, ST14, NCS1, SDC2, MLH1, CYFIP1, RPS6KB1, MSH2, NR1H4, VEGFA, PDE4D, SHANK1, FOSL1, IDS, LIMK1, SOD1, BMPR2, GRIK1, RIC8A, CD44, GRM1, CPEB1, PCSK9, DLG3, RABEP2, KIAA1109, HSPG2, C9orf72, RSS, SLC36A1, ST8SIA4, DGKK, WNT7A, PTPN5, VIP, USF2, MIR219A1, PKP4, USF1, UBE3A, TWIST1, MIR510, ICAM5, SYN1, STXBP1, STATH, C20orf181, SRY, SPARC, MAGT1, YTHDF2, WASF1, DICER1, CHMP4A, INPP5K, MED18, CHD7, MBD5, NBEA, SHC2, TWNK, SNRPN, BRD4, TARDBP, SIRT1, ARHGEF9, TOP3B, ADARB1, KCNT1, CLSTN1, DSTN, RAI1, CTCF, PDLIM5, ABCB6, HDAC6, MED12, PCA3, NRXN1, TDRD3, APOA1, SMS, HTC2, GRN, GRIN2A, ADCYAP1, GSK3B, GSN, HTT, NRG1, HTR2A, SLC12A2, IAPP, IGF1, IGFALS, IRF6, KCNH1, KCNQ2, LGALS4, GRIA2, GABRD, GABPA, AKT1, AVP, BCR, BRCA2, CAT, CD47, CRHR1, DLD, DLG4, DSCAM, RCAN1, ELAVL2, FBN1, ANG, ALPP, ALPI, LMNA, CAPRIN1, MAOA, PDE2A, ADAM10, PPP2R5E, MAPK3, PTEN, ANXA1, RANGAP1, REST, RGS4, ATXN8OS, SCN2A, SHBG, SKI, SLC1A2, SLC6A4, SLC6A8, CFP, PAX3, MAS1, PAK1, MBS1, MDM2, MEF2A, ATXN3, ADCY1, PPP1R12A, NF1, NFE2L1, NFE2L2, NHS, NNAT, NOS1, NRF1, NTRK2, NUP98, PLCG1
- Fragile X Syndrome Wikipedia
  
  X-linked dominant genetic disorder Fragile X syndrome Other names Martin–Bell syndrome, [1] Escalante syndrome Boy with protruding ears characteristic of fragile X syndrome Specialty Medical genetics , pediatrics , psychiatry Symptoms Intellectual disability , long and narrow face, large ears, flexible fingers, large testicles [1] Complications Autism features, seizures [1] Usual onset Noticeable by age 2 [1] Duration Lifelong [2] Causes Genetic ( X-linked dominant ) [1] Diagnostic method Genetic testing [2] Treatment Supportive care , early interventions [2] Frequency 1 in 4,000 (males), 1 in 8,000 (females) [1] Fragile X syndrome ( FXS ) is a genetic disorder characterized by mild-to-moderate intellectual disability . [1] The average IQ in males is under 55, while about two thirds of affected females are intellectually disabled. [3] [4] Physical features may include a long and narrow face, large ears, flexible fingers, and large testicles . [1] About a third of those affected have features of autism such as problems with social interactions and delayed speech. [1] Hyperactivity is common, and seizures occur in about 10%. [1] Males are usually more affected than females. [1] This disorder and finding of Fragile X syndrome has an X-linked dominant inheritance. [1] It is typically caused by an expansion of the CGG triplet repeat within the FMR1 (fragile X mental retardation 1) gene on the X chromosome . [1] This results in silencing ( methylation ) of this part of the gene and a deficiency of the resultant protein (FMRP), which is required for the normal development of connections between neurons . [1] Diagnosis requires genetic testing to determine the number of CGG repeats in the FMR1 gene. [5] Normally, there are between 5 and 40 repeats; fragile X syndrome occurs with more than 200. [1] A premutation is said to be present when the gene has between 40 and 200 repeats; women with a premutation have an increased risk of having an affected child. [1] Testing for premutation carriers may allow for genetic counseling . [5] There is no cure. [2] Early intervention is recommended, as it provides the most opportunity for developing a full range of skills. [6] These interventions may include special education , speech therapy , physical therapy , or behavioral therapy . [2] [7] Medications may be used to treat associated seizures , mood problems, aggressive behavior, or ADHD . [8] Fragile X syndrome is estimated to occur in 1.4 per 10,000 males and 0.9 per 10,000 females. [9] Contents 1 Signs and symptoms 1.1 Physical phenotype 1.2 Intellectual development 1.3 Autism 1.4 Social interaction 1.5 Mental health 1.6 Vision 1.7 Neurology 1.8 Working memory 1.9 Fertility 2 Causes 2.1 Inheritance 3 Pathophysiology 4 Diagnosis 5 Management 5.1 Medication 6 Prognosis 7 Research 8 History 9 References 10 External links Signs and symptoms [ edit ] Prominent characteristics of the syndrome include an elongated face and large or protruding ears. Most young children do not show any physical signs of FXS. [10] It is not until puberty that physical features of FXS begin to develop. [10] Aside from intellectual disability, prominent characteristics of the syndrome may include an elongated face, large or protruding ears , flat feet, larger testes ( macroorchidism ), and low muscle tone . [11] [12] Recurrent otitis media (middle ear infection) and sinusitis is common during early childhood. Speech may be cluttered or nervous. Behavioral characteristics may include stereotypic movements (e.g., hand-flapping) and atypical social development, particularly shyness, limited eye contact, memory problems, and difficulty with face encoding. Some individuals with fragile X syndrome also meet the diagnostic criteria for autism . Males with a full mutation display virtually complete penetrance and will therefore almost always display symptoms of FXS, while females with a full mutation generally display a penetrance of about 50% as a result of having a second, normal X chromosome. [13] Females with FXS may have symptoms ranging from mild to severe, although they are generally less affected than males.
- Fragile X Syndrome Orphanet
  
  A rare genetic disease associated with mild to severe intellectual deficit that may be associated with behavioral disorders and characteristic physical features including a high forehead, prominent and large ears, hyperextensible finger joints, flat feet with pronation and, in adolescent and adult males, macroorchidism. Epidemiology Prevalence is estimated at approximately 1/2400-1/6000 although the prevalence may vary, depending on where the screening is carried out in the world. Clinical description Fragile X syndrome (FXS) presents with a variable clinical phenotype. In males, the disease presents during childhood with delayed developmental milestones. Intellectual deficit can be of variable severity and may include problems with working and short-term memory, executive function, language, mathematics and visuospatial abilities.
- Fragile X Syndrome OMIM
  
  A number sign (#) is used with this entry because fragile X (FXS) is caused by mutation in the FMR1 gene (309550). The vast majority of cases are caused by a trinucleotide (CGG)n repeat expansion (309550.0004) of greater than 200 repeats. See also fragile X tremor/ataxia syndrome (FXTAS; 300623), which is caused by expanded FMR1 (CGG)n repeats that range in size from 55 to 200 repeats and are referred to as 'premutations.' Description Fragile X syndrome is characterized by moderate to severe mental retardation, macroorchidism, and distinct facial features, including long face, large ears, and prominent jaw. In most cases, the disorder is caused by the unstable expansion of a CGG repeat in the FMR1 gene and abnormal methylation, which results in suppression of FMR1 transcription and decreased protein levels in the brain (Devys et al., 1993).
Transcobalamin Deficiency Orphanet

Management and treatment Treatment of TC involves maintenance of a very high serum cobalamin concentration (1,000-10,000 pg/ml) by intramuscular (IM) administration of hydroxocobalamin. Oral treatment or treatment with cyanocobalamin instead of hydroxocobalamin may result in poorer outcomes. Treatment with IM hydroxocobalamin at least once a week is recommended, with monitoring of biochemical and hematological parameters to ensure that treatment is effective.

TCN2, CBLIF, MMUT, PPBP, TCN1
- Transcobalamin Deficiency MedlinePlus
  
  Transcobalamin deficiency is a disorder that impairs the transport of cobalamin (also known as vitamin B12) within the body. Cobalamin is obtained from the diet; this vitamin is found in animal products such as meat, eggs, and shellfish. An inability to transport cobalamin within the body results in cells that lack cobalamin, which they need for many functions including cell growth and division (proliferation) and DNA production. The absence of cobalamin leads to impaired growth, a shortage of blood cells, and many other signs and symptoms that usually become apparent within the first weeks or months of life. The first signs of transcobalamin deficiency are typically a failure to gain weight and grow at the expected rate (failure to thrive), vomiting, diarrhea, and open sores (ulcers) on the mucous membranes such as the lining inside the mouth.
- Transcobalamin Ii Deficiency OMIM
  
  A number sign (#) is used with this entry because transcobalamin II deficiency is caused by homozygous or compound heterozygous mutation in the gene encoding transcobalamin II (TCN2; 613441) on chromosome 22q12. Description Transcobalamin II deficiency is an autosomal recessive disorder with onset in early infancy characterized by failure to thrive, megaloblastic anemia, and pancytopenia. Other features include methylmalonic aciduria, recurrent infections, and vomiting and diarrhea. Treatment with cobalamin results in clinical improvement, but the untreated disorder may result in mental retardation and neurologic abnormalities (summary by Haberle et al., 2009). Hall (1981) gave a clinically oriented review of congenital defects of vitamin B12 transport, and Frater-Schroder (1983) gave a genetically oriented review.
Gfer Syndrome Wikipedia

Mechanism [ edit ] The most major role of GFER is inside the mitochondria's IMS (it is imported into the mitochondria from the cytosol ). ... These unfolded proteins will not be able to enter the matrix and therefore: The mitochondria will lack various building blocks and its ability to maintain itself will be hindered (e.g., It will not be able to produce cytochrome c oxidase and other building blocks for the ETC, maintenance, correction of errors and splitting). The IMS will become bloated with partially folded proteins with structural damage.
Hereditary Cerebral Hemorrhage With Amyloidosis GARD

Based on the region in which they were first described, the subtypes include: The Dutch , Arctic , Piedmont , Iowa , Flemish , Italian types are caused by mutations in the APP gene The British and Danish types are caused by mutations in the ITM2B gene The Icelandic type is caused by mutations in the CST3 gene All types of HCHWA currently described are inherited in an autosomal dominant manner.

CST3, ITM2B, APP, CTSD, APOE, ACTB, PTPRC, TSHZ1, SYP, SPP1, SDC2, HSPG2, SMAD2, ITGAX, GFAP, FN1, FAP, CD68, HSPB8
- Cerebral Amyloid Angiopathy, Cst3-Related OMIM
  
  A critical piece of evidence indicating a difference between the 2 diseases is the finding by van Duinen et al. (1987) that in the Dutch form of the disease the vascular amyloid deposits have immunohistochemical characteristics of Alzheimer disease-related beta-protein (APP; 104760). Molecular Genetics In Icelandic patients with hereditary cerebral hemorrhage with amyloidosis, Abrahamson et al. (1987) identified a heterozygous mutation in the CST3 gene (L68Q; 604312.0001).
- Hereditary Cerebral Hemorrhage With Amyloidosis Orphanet
  
  Etiology Most forms of HCHWA (Dutch, Arctic, Piedmont, Iowa, Flemish and Italian) are due to a point-mutation in the APP gene on chromosome 21q21.2, which encodes the beta-amyloid precursor protein.
- Cerebral Amyloid Angiopathy Wikipedia
  
  Abnormalities in each of these identified clearance pathways have been linked to CAA. [12] [13] In familial forms of CAA, the cause of Aβ build up is likely due to increased production rather than poor clearance. [14] Mutations in the amyloid precursor protein (APP), Presenilin (PS) 1 and PS2 genes can result in increased rates of cleavage of the APP into Aβ. ... External links [ edit ] Classification D ICD - 10 : I68.0 MeSH : D016657 DiseasesDB : 32874 External resources MedlinePlus : 000719 eMedicine : neuro/628 Scholia has a topic profile for Cerebral amyloid angiopathy . v t e Amyloidosis Common amyloid forming proteins AA ATTR Aβ2M AL Aβ / APP AIAPP ACal APro AANF ACys ABri Systemic amyloidosis AL amyloidosis AA amyloidosis Aβ2M/Haemodialysis-associated AGel/Finnish type AA/Familial Mediterranean fever ATTR/Transthyretin-related hereditary Organ-limited amyloidosis Heart AANF/Isolated atrial Brain Familial amyloid neuropathy ACys+ABri/Cerebral amyloid angiopathy Aβ/Alzheimer's disease Kidney AApoA1+AFib+ALys/Familial renal Skin Primary cutaneous amyloidosis Amyloid purpura Endocrine Thyroid ACal/Medullary thyroid cancer Pituitary APro/Prolactinoma Pancreas AIAPP/Insulinoma AIAPP/Diabetes mellitus type 2 v t e Medicine Specialties and subspecialties Surgery Cardiac surgery Cardiothoracic surgery Colorectal surgery Eye surgery General surgery Neurosurgery Oral and maxillofacial surgery Orthopedic surgery Hand surgery Otolaryngology ENT Pediatric surgery Plastic surgery Reproductive surgery Surgical oncology Transplant surgery Trauma surgery Urology Andrology Vascular surgery Internal medicine Allergy / Immunology Angiology Cardiology Endocrinology Gastroenterology Hepatology Geriatrics Hematology Hospital medicine Infectious disease Nephrology Oncology Pulmonology Rheumatology Obstetrics and gynaecology Gynaecology Gynecologic oncology Maternal–fetal medicine Obstetrics Reproductive endocrinology and infertility Urogynecology Diagnostic Radiology Interventional radiology Nuclear medicine Pathology Anatomical Clinical pathology Clinical chemistry Cytopathology Medical microbiology Transfusion medicine Other Addiction medicine Adolescent medicine Anesthesiology Dermatology Disaster medicine Diving medicine Emergency medicine Mass gathering medicine Family medicine General practice Hospital medicine Intensive care medicine Medical genetics Narcology Neurology Clinical neurophysiology Occupational medicine Ophthalmology Oral medicine Pain management Palliative care Pediatrics Neonatology Physical medicine and rehabilitation PM&R Preventive medicine Psychiatry Addiction psychiatry Radiation oncology Reproductive medicine Sexual medicine Sleep medicine Sports medicine Transplantation medicine Tropical medicine Travel medicine Venereology Medical education Medical school Bachelor of Medicine, Bachelor of Surgery Bachelor of Medical Sciences Master of Medicine Master of Surgery Doctor of Medicine Doctor of Osteopathic Medicine MD–PhD Related topics Alternative medicine Allied health Dentistry Podiatry Pharmacy Physiotherapy Molecular oncology Nanomedicine Personalized medicine Public health Rural health Therapy Traditional medicine Veterinary medicine Physician Chief physician History of medicine Book Category Commons Wikiproject Portal Outline
Estrogen And Neurodegenerative Diseases Wikipedia

In addition, estrogen deprivation is likely to initiate or enhance degenerative changes caused by oxidative stress , and to reduce the brain's ability to maintain synaptic connectivity and cholinergic integrity leading to the cognitive decline seen in aged and disease-afflicted individuals. [5] There is sufficient evidence that estradiol is a powerful neuroprotectant which might have use against AD, stroke and Parkinson's disease both in women and men. [5] Estrogen and Alzheimer's disease [ edit ] This figure shows how APP cleavage produces toxic Abeta in Alzheimer's disease. Amyloid plaques formed by amyloid-β (Aβ) deposition and neurofibrillary tangles formed by tau protein phosphorylation are dominant physiological features of Alzheimer's disease. Amyloid precursor protein (APP) proteolysis is fundamental for production of Aβ peptides implicated in AD pathology. [6] By using a cell line that contains high levels of estrogen receptors, scientists found that treatment with physiological concentrations of 17 beta-estradiol is associated with accumulation in the conditioned medium of an amino-terminal cleavage product of APP (soluble APP or protease nexin-2), indicative of non-amyloidogenic processing. [7] Estrogen and Parkinson's disease [ edit ] Recommendations on the use of postmenopausal hormonal replacement therapy in women with Parkinson's disease or those genetically at risk. [8] But another group of scientists found a positive association between estrogen use and lower symptom severity in women with early PD not yet taking L-dopa . [9] Estrogen and Huntington's disease [ edit ] Huntington's disease (HD) is a polyglutamine disorder based on an expanded CAG triplet repeat [10] leading to cerebral and striatal neurodegeneration. [11] Potential sex differences concerning the age of onset and the course of the disease are poorly defined, as the difficulties of matching female and male HD patients regarding their CAG repeat lengths limit comparability. [12] Estrogen and Amyotrophic lateral sclerosis [ edit ] ALS occurs more commonly in men than in women, and women get the disease later in life compared to men. [13] This suggested the possible protective role of estrogen in ALS. ... "Octyl Gallate Markedly Promotes Anti-amyloidogenic Processing of APP through Estrogen Receptor-Mediated ADAM10 Activation" .
Microvasculature Remodeling Wikipedia

What makes vessels grow with exercise training? J App Physiol 97: 1119–28, 2004. This cardiovascular system article is a stub .