Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
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Mutation in PEX16 is causal in the peroxisome-deficient Zellweger syndrome of complementation group D.Peroxisome synthesis in the absence of preexisting peroxisomesPEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein importMutations in the peroxin Pex26p responsible for peroxisome biogenesis disorders of complementation group 8 impair its stability, peroxisomal localization, and interaction with the Pex1p x Pex6p complexAlternative splicing suggests extended function of PEX26 in peroxisome biogenesis.A deleterious mutation in SAMD9 causes normophosphatemic familial tumoral calcinosisNDUFS6 mutations are a novel cause of lethal neonatal mitochondrial complex I deficiencyCloning and characterization of the gene encoding the human peroxisomal assembly protein Pex3pIdentification of PEX10, the gene defective in complementation group 7 of the peroxisome-biogenesis disordersClofibrate-inducible, 28-kDa peroxisomal integral membrane protein is encoded by PEX11PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of PEX12pPhenotype-genotype relationships in complementation group 3 of the peroxisome-biogenesis disordersPEX13 is mutated in complementation group 13 of the peroxisome-biogenesis disorders.Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group IDisruption of a PEX1-PEX6 interaction is the most common cause of the neurologic disorders Zellweger syndrome, neonatal adrenoleukodystrophy, and infantile Refsum diseasePeroxisomes in brain development and functionZellweger spectrum disorders: clinical overview and management approachSPATA5 mutations cause a distinct autosomal recessive phenotype of intellectual disability, hypotonia and hearing lossThe Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits.ATM functions at the peroxisome to induce pexophagy in response to ROS.Functional association of the AAA complex and the peroxisomal importomer.A new horizon of moyamoya disease and associated health risks explored through RNF213The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysisCatalase-less peroxisomes. Implication in the milder forms of peroxisome biogenesis disorderPEX1 mutations in complementation group 1 of Zellweger spectrum patients correlate with severity of diseaseNovel PEX1 mutations and genotype-phenotype correlations in Australasian peroxisome biogenesis disorder patientsIdentification of the molecular defect in patients with peroxisomal mosaicism using a novel method involving culturing of cells at 40 degrees C: implications for other inborn errors of metabolismAAA+ proteins: have engine, will workMolecular snapshots of the Pex1/6 AAA+ complex in action.Genomic structure and identification of 11 novel mutations of the PEX6 (peroxisome assembly factor-2) gene in patients with peroxisome biogenesis disorders.Peroxisome biogenesis and peroxisome biogenesis disorders.Characterization of two common 5' polymorphisms in PEX1 and correlation to survival in PEX1 peroxisome biogenesis disorder patients.Therapeutic developments in peroxisome biogenesis disorders.Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export.Genetic and molecular bases of peroxisome biogenesis disorders.Plasma very long chain fatty acids in 3,000 peroxisome disease patients and 29,000 controls.AAA+ ATPases: achieving diversity of function with conserved machinery.Rational diagnostic strategy for Zellweger syndrome spectrum patientsUnique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy.An Arabidopsis indole-3-butyric acid-response mutant defective in PEROXIN6, an apparent ATPase implicated in peroxisomal function.
P2860
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P2860
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
description
1997 nî lūn-bûn
@nan
1997 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@ast
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@en
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@en-gb
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@nl
type
label
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@ast
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@en
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@en-gb
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@nl
prefLabel
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@ast
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@en
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@en-gb
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@nl
P2093
P3181
P356
P1433
P1476
Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders
@en
P2093
B E Reuber
C S Collins
E Germain-Lee
J C Morrell
R Ameritunga
P2888
P3181
P356
10.1038/NG1297-445
P407
P577
1997-12-01T00:00:00Z
P5875
P6179
1005476781