Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101.

about

P2860

Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101.

Item

http://www.wikidata.org/entity/Q42820720

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101.

@en

Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101.

@nl

type

Item

label

Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101.

@en

Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101.

@nl

prefLabel

Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101.

@en

Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101.

@nl

P1433

Q42820720-CE570F07-13A6-40C8-87BE-B1191323DE62

P1476

Q42820720-83E9C5FF-A7BD-4F4A-ABF1-0CEE6F1CE172

P2093

Q42820720-0435910A-CE41-4554-9D1F-760FD93FC8E3

Q42820720-1DE164D3-CB74-40E2-80F0-068E9DB76557

Q42820720-D7E0DC50-644D-4C83-9192-15531AEA9F2C

P2860

Q42820720-0574190D-32BE-44AF-8DBA-EA1C50719627

Q42820720-07C22CD7-AA1F-4EC5-AA23-E500DFF2A269

Q42820720-09416DA4-547A-40C1-A9FA-2FE1F1977A4F

Q42820720-1368C3F8-B7D8-4242-B6FC-C13964F146B1

Q42820720-1D90E01F-F610-4710-A595-62DF2CFFA568

Q42820720-1F5C9E7B-034A-4934-AAEB-81F9F1B514D5

Q42820720-30E06ABB-FB91-42FF-ADE9-82BF67FBFFEC

Q42820720-38F1A25F-58AC-4BE0-8B70-7535A3CCA3F6

Q42820720-3CB19A75-D4C3-4D59-A2C4-2CE227826DE8

Q42820720-3E9778D4-9C0F-436E-B76C-D84A0E2697DD

P304

Q42820720-BB481B2D-E390-480E-9934-F2681CA53A5A

P31

Q42820720-52AB9239-D65A-495F-A1C6-97EFA6802E20

P356

Q42820720-D3894E19-E9FF-401B-9035-1709BDA7053A

P407

Q42820720-0B98E3D6-43E9-466E-A3F9-C5DF961B9D3F

P433

Q42820720-F458A681-9C49-469B-A6AB-207CA80A41E6

P4510

Q42820720-21913E00-3B84-443A-A4AA-E59019FAC96C

Q42820720-5012E9B0-C88E-449E-B3D5-AEC2D86C231A

Q42820720-955F5662-2212-4276-BBCF-9C2AE96A5506

Q42820720-E53C6B47-5ACB-45D5-8696-31A5B0C2B7BF

P478

Q42820720-30E01B0C-5C65-4EC3-BEBA-59407A7F6150

P577

Q42820720-9973C2A7-1CAC-4C74-BC94-74EDCF5D2EA9

P698

Q42820720-C4535A8B-DAD6-4FB2-92E5-091567D18724

P921

Q42820720-0886449A-FD79-4937-8BAD-ABDCFB229DB3

P356

BJ20120911

P1433

Biochemical Journal

P1476

Pex5p stabilizes Pex14p: a study using a newly isolated pex5 CHO cell mutant, ZPEG101.

@en

P2093

Kanji Okumoto

http://www.w3.org/2001/XMLSchema#string

Ryuichi Natsuyama

http://www.w3.org/2001/XMLSchema#string

Yukio Fujiki

http://www.w3.org/2001/XMLSchema#string

P2860

Molecular anatomy of the peroxin Pex12p: ring finger domain is essential for Pex12p function and interacts with the peroxisome-targeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p

Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTs1 receptor

Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders

PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14

Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import.

Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I

Involvement of Pex13p in Pex14p localization and peroxisomal targeting signal 2-dependent protein import into peroxisomes

Crystal structure of the conserved N-terminal domain of the peroxisomal matrix protein import receptor, Pex14p

Saccharomyces cerevisiae PTS1 receptor Pex5p interacts with the SH3 domain of the peroxisomal membrane protein Pex13p in an unconventional, non-PXXP-related manner.

Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol.

P304

195-207

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1042/BJ20120911

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P4510

P478

449

http://www.w3.org/2001/XMLSchema#string

P577

2013-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

23009329

http://www.w3.org/2001/XMLSchema#string

P921

cell line