Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

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BiP clustering facilitates protein folding in the endoplasmic reticulum Protein accumulation in aleurone cells, sub-aleurone cells and the center starch endosperm of cereals.

P2860

Q31171777-905192F7-4245-4E00-A767-40D24E576765 Q38229495-75A26AD1-FEAA-4909-B24B-2FDD86584C1A

P2860

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

Item

http://www.wikidata.org/entity/Q42096150

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2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

@en

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

@nl

type

Item

label

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

@en

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

@nl

prefLabel

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

@en

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

@nl

P1476

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

@en

P2093

A Robinson

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

C Young

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

L Petzold

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

M Griesemer

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

P2860

LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum

Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions

Hsp70 chaperones: cellular functions and molecular mechanism

Global analysis of protein localization in budding yeast.

Global analysis of protein expression in yeast

A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum.

Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation.

Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.

Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.

A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors

P304

54-63

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P31

scholarly article

P356

10.1049/IET-SYB.2011.0006

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P433

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

P478

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

P577

2012-04-01T00:00:00Z

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

P5875

224808022

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

P698

22519358

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

P921

molecular chaperones

endoplasmic reticulum

P932

4564256

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

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

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P2860

P2860

Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932