An enzyme trafficking defect in two patients with primary hyperoxaluria type 1: peroxisomal alanine/glyoxylate aminotransferase rerouted to mitochondria.
about
Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide productionPeroxisomal import of human alanine:glyoxylate aminotransferase requires ancillary targeting information remote from its C terminusIdentification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codonMistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutationEnzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregationStructural implications of a G170R mutation of alanine:glyoxylate aminotransferase that is associated with peroxisome-to-mitochondrion mistargetingFunctional 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 treatmentA single amino acid substitution within the mature sequence of ornithine aminotransferase obstructs mitochondrial entry of the precursorOptical Control of Peroxisomal TraffickingCellular transfection to deliver alanine-glyoxylate aminotransferase to hepatocytes: a rational gene therapy for primary hyperoxaluria-1 (PH-1).Traffic jam: a compendium of human diseases that affect intracellular transport processes.Different types of peroxisomes in human duodenal epithelium.Pharmacologic rescue of an enzyme-trafficking defect in primary hyperoxaluria 1.Mitochondrial biogenesis and turnover.Studies on a unique organelle localization of a liver enzyme, serine:pyruvate (or alanine:glyoxylate) aminotransferase.Import of proteins into peroxisomes and other microbodies.Phenotype-Genotype Correlations and Estimated Carrier Frequencies of Primary Hyperoxaluria.High throughput cell-based assay for identification of glycolate oxidase inhibitors as a potential treatment for Primary Hyperoxaluria Type 1ATP-dependent degradation of a mutant serine: pyruvate/alanine:glyoxylate aminotransferase in a primary hyperoxaluria type 1 casePeroxisomal diseases.The many roles of oxalate in nature.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.Alternative topogenic signals in peroxisomal citrate synthase of Saccharomyces cerevisiae.Mitochondrial protein import and human health and disease.Two novel AGXT mutations identified in primary hyperoxaluria type-1 and distinct morphological and structural difference in kidney stonesVitamin B6 in primary hyperoxaluria I: first prospective trial after 40 years of practice.Glycine metabolism in animals and humans: implications for nutrition and health.Protein homeostasis defects of alanine-glyoxylate aminotransferase: new therapeutic strategies in primary hyperoxaluria type I.AGXT2: a promiscuous aminotransferase.Primary hyperoxalurias: diagnosis and treatment.Biochemical analyses are instrumental in identifying the impact of mutations on holo and/or apo-forms and on the region(s) of alanine:glyoxylate aminotransferase variants associated with primary hyperoxaluria type I.Separate information required for nuclear and subnuclear localization: additional complexity in localizing an enzyme shared by mitochondria and nucleiCorrection of an enzyme trafficking defect in hereditary kidney stone disease in vitro.Molecular adaptation of alanine:glyoxylate aminotransferase targeting in primates.Molecular basis for the dual mitochondrial and cytosolic localization of alanine:glyoxylate aminotransferase in amphibian liver cells.Mammalian alanine/glyoxylate aminotransferase 1 is imported into peroxisomes via the PTS1 translocation pathway. Increased degeneracy and context specificity of the mammalian PTS1 motif and implications for the peroxisome-to-mitochondrion mistargetiInhibition of alanine:glyoxylate aminotransferase 1 dimerization is a prerequisite for its peroxisome-to-mitochondrion mistargeting in primary hyperoxaluria type 1.Reconstruction of human hepatocyte glyoxylate metabolic pathways in stably transformed Chinese-hamster ovary cells.
P2860
Q24292756-DF05D3A5-F4EF-42C2-B7D2-4F5421D5154AQ24303519-639B032A-9E5A-4A52-A78A-517132120C44Q24306643-E9657338-BBBE-491D-BAA7-573FABD5D7E7Q24339516-0830B42A-4E92-41E8-917C-BE62F8BA9AA1Q24559970-60617BE6-E220-44D3-8E70-7FF375FEF933Q24670805-807F5691-D76B-4A62-A6E1-6BF5F286814AQ27660137-2D948178-DAF2-425D-9D12-0FC3BC7D8697Q28144619-CD31CA8C-C4EE-47FF-B3A3-DD86985D6FADQ28257183-E05C2B9F-D5A7-4E10-8A4A-16D308522449Q28297087-4A150802-EA7B-46DF-BB6C-C39D46393656Q30751156-3415030B-40BB-4B2E-8504-3D4558B23220Q31162712-E2C1A0BC-C000-4CB7-95A7-AA55D0E9A4A1Q34156525-967DF897-CEED-4DDD-BFF6-5DB1D18D6D82Q34394021-1FBBCDBC-DC80-4F70-9D27-95DBB45CEFD5Q34407663-A40031FD-48D7-445F-9E04-3DA22FAC77D0Q34590193-6428764F-CE23-4DC1-A837-E4D60223D801Q35193133-06EC7B56-6D40-45A7-94AF-0C6623DF415CQ35450111-39AFE74C-65BC-4B41-8C7E-1E381C7A524EQ36104822-2C6E9FD9-2623-4313-B20D-5D5C4C766344Q36145370-3F9FF580-C3DD-440E-BD4E-D0CAA2B1E297Q36233567-E83EDB39-6A35-4A58-BB55-841793D3A354Q36307328-A4E6683C-A7E4-4C21-9265-B3E04E746668Q36372388-305E6E60-2ABC-421A-A375-8FAFE8E659EFQ36562007-8CA80B64-82EC-48CD-BA29-62AE2F059611Q36706888-5809142E-43A4-4CF7-973E-0C2A22CBFDDAQ36735868-862676D2-ADE1-42C4-8FD6-E7AD9081394CQ37267462-67D2EDED-2E74-4A90-9D1D-F24974F54F1BQ37621553-3E5804D3-0A5D-4BFA-BFD2-030E2FD44455Q38101481-623F2C06-2F9E-42AF-823E-F09D43CDFA04Q38129886-2345DE38-B6BD-4F81-83FD-30F0AD622089Q38257983-4E8AA4A1-8ECC-4C42-84C9-09F957B9467CQ38292247-C9CB4BAF-2621-4B5A-8CC0-D18326F5C2ACQ40821949-947EA2FA-21C4-4A8C-939A-17ABF5EA9AB2Q42077413-26EC2F2F-550A-4885-B42A-242818DBBB65Q42213400-9AA2C837-AE39-4CB6-9EC5-47988F971D51Q42621887-48B5CDBE-2477-4DFB-9A9F-5DD1226BAD47Q42663187-B4CFEBF6-86CD-49EB-BEAD-405501DF312BQ42771608-C5A72329-C5CE-4BF5-B29C-6254409D891DQ42798924-B2FA20F5-DCEA-4F56-9E94-36D40F7CB73CQ43246859-4CA224C3-BC15-44AC-9F0D-70885A502504
P2860
An enzyme trafficking defect in two patients with primary hyperoxaluria type 1: peroxisomal alanine/glyoxylate aminotransferase rerouted to mitochondria.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
An enzyme trafficking defect i ...... rase rerouted to mitochondria.
@ast
An enzyme trafficking defect i ...... rase rerouted to mitochondria.
@en
type
label
An enzyme trafficking defect i ...... rase rerouted to mitochondria.
@ast
An enzyme trafficking defect i ...... rase rerouted to mitochondria.
@en
prefLabel
An enzyme trafficking defect i ...... rase rerouted to mitochondria.
@ast
An enzyme trafficking defect i ...... rase rerouted to mitochondria.
@en
P2093
P2860
P356
P1476
An enzyme trafficking defect i ...... rase rerouted to mitochondria.
@en
P2093
P2860
P304
P356
10.1083/JCB.108.4.1345
P407
P577
1989-04-01T00:00:00Z