Inhibition of alanine:glyoxylate aminotransferase 1 dimerization is a prerequisite for its peroxisome-to-mitochondrion mistargeting in primary hyperoxaluria type 1.
about
Peroxisomal import of human alanine:glyoxylate aminotransferase requires ancillary targeting information remote from its C terminusMolecular cloning of Aralar, a new member of the mitochondrial carrier superfamily that binds calcium and is present in human muscle and brainPEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14Protein trafficking defects in inherited kidney diseasesStructural implications of a G170R mutation of alanine:glyoxylate aminotransferase that is associated with peroxisome-to-mitochondrion mistargetingMolecular Requirements for Peroxisomal Targeting of Alanine-Glyoxylate Aminotransferase as an Essential Determinant in Primary Hyperoxaluria Type 1Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non-PTS1, import pathway into peroxisomes that is dependent on Pex5p.The cytosolic DnaJ-like protein djp1p is involved specifically in peroxisomal protein import.Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutationsMolecular etiology of primary hyperoxaluria type 1: new directions for treatmentProtein structure and import into the peroxisomal matrix.Cellular transfection to deliver alanine-glyoxylate aminotransferase to hepatocytes: a rational gene therapy for primary hyperoxaluria-1 (PH-1).Pharmacologic rescue of an enzyme-trafficking defect in primary hyperoxaluria 1.Allele-specific characterization of alanine: glyoxylate aminotransferase variants associated with primary hyperoxaluriaPeroxisomal targeting, import, and assembly of alcohol oxidase in Pichia pastorisPex20p of the yeast Yarrowia lipolytica is required for the oligomerization of thiolase in the cytosol and for its targeting to the peroxisome.Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing complex into peroxisomes of Yarrowia lipolytica.Four of the most common mutations in primary hyperoxaluria type 1 unmask the cryptic mitochondrial targeting sequence of alanine:glyoxylate aminotransferase encoded by the polymorphic minor allele.Mitochondrial protein import and human health and disease.Peroxisomal catalase in the methylotrophic yeast Candida boidinii: transport efficiency and metabolic significance.Molecular Insight into the Synergism between the Minor Allele of Human Liver Peroxisomal Alanine:Glyoxylate Aminotransferase and the F152I MutationCorrection of an enzyme trafficking defect in hereditary kidney stone disease in vitro.Pnc1 piggy-back import into peroxisomes relies on Gpd1 homodimerisation.Molecular basis for the dual mitochondrial and cytosolic localization of alanine:glyoxylate aminotransferase in amphibian liver cells.The energetics of Pex5p-mediated peroxisomal protein import.Implications of genotype and enzyme phenotype in pyridoxine response of patients with type I primary hyperoxaluria.Folding Defects Leading to Primary Hyperoxaluria.Mutational analyses of a type 2 peroxisomal targeting signal that is capable of directing oligomeric protein import into tobacco BY-2 glyoxysomes
P2860
Q24303519-EFCAB2BF-00CE-4BC1-AEF5-7F61B2A188F5Q24309242-36F8B3DE-3C17-4F41-86D9-44299C33E33AQ24339454-F3E10632-DBF9-4663-83E6-ED42B5850E0BQ27012909-6E6FB252-542B-48FA-B352-7D599A51C067Q27660137-9DE5D5E6-237E-4E2A-8056-21628021999FQ27678710-76B5D552-0570-4D1D-9D11-137797CA2335Q27933990-6CEE74DB-7C32-4245-B003-5D8F72BB780FQ27934680-F159FB4F-739B-4628-9A45-309B6340DA51Q28144619-6615C449-0386-473B-812F-EFF247129862Q28257183-389F4490-1C86-475B-8735-E81B08FC17D2Q30332454-EED04863-2B2D-4B63-ADCB-05F64E562CA1Q31162712-28EF156D-5068-4C5E-BE3A-CB674D0C5482Q34407663-58A261F0-4A17-40EF-851C-1559C1D0B22BQ35144060-BC7C3684-3376-44E4-96A2-5435594081F5Q36254940-DF37A78C-1DFF-4B07-90F6-463B4E1F2849Q36256275-AE41EBF9-3EDC-47A0-BA24-43D7A26FC4FDQ36324201-2C9A1FF1-D492-4F28-BFDB-22B5B3387F86Q36562007-7EFDCBD7-2956-4D5F-932B-148D887CCA1EQ36735868-E46A03DA-CB14-4924-90E3-E2A2C6C67982Q39529849-8F18CCB4-815F-49C5-B0B6-CFEC3241BBB6Q42103822-5816ABC1-E413-4926-A83F-CC227D894F7CQ42213400-024784A5-BBA7-4129-9542-BFCE408DE97BQ42320896-BFB98B55-9B11-4FCE-B19C-911440AD0C8EQ42663187-F65C1D88-00A9-44B4-A640-CD38B0D3C8D4Q44529197-835A4B9F-1BD5-402C-81FF-B37DDB662AFEQ46453748-AA501C57-ECFB-4AF8-A1CA-C41DD817B18FQ47602222-D86BBCF5-5B22-4457-B9B2-4FBC966F0736Q58451079-FA698A9C-3B79-4212-83AE-A080E799AC5E
P2860
Inhibition of alanine:glyoxylate aminotransferase 1 dimerization is a prerequisite for its peroxisome-to-mitochondrion mistargeting in primary hyperoxaluria type 1.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Inhibition of alanine:glyoxyla ...... primary hyperoxaluria type 1.
@en
Inhibition of alanine:glyoxyla ...... primary hyperoxaluria type 1.
@nl
type
label
Inhibition of alanine:glyoxyla ...... primary hyperoxaluria type 1.
@en
Inhibition of alanine:glyoxyla ...... primary hyperoxaluria type 1.
@nl
prefLabel
Inhibition of alanine:glyoxyla ...... primary hyperoxaluria type 1.
@en
Inhibition of alanine:glyoxyla ...... primary hyperoxaluria type 1.
@nl
P2093
P2860
P356
P1476
Inhibition of alanine:glyoxyla ...... primary hyperoxaluria type 1.
@en
P2093
P2860
P304
P356
10.1083/JCB.135.4.939
P407
P577
1996-11-01T00:00:00Z