Inhibitory effects of HSP70 chaperones on nascent polypeptides

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http://www.wikidata.org/entity/Q36277498

description

1992 nî lūn-bûn

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1992年の論文

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年学术文章

@zh-my

1992年学术文章

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1992年學術文章

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1992年學術文章

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1992年學術文章

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name

Inhibitory effects of HSP70 chaperones on nascent polypeptides

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Inhibitory effects of HSP70 chaperones on nascent polypeptides

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Item

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Inhibitory effects of HSP70 chaperones on nascent polypeptides

@ast

Inhibitory effects of HSP70 chaperones on nascent polypeptides

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prefLabel

Inhibitory effects of HSP70 chaperones on nascent polypeptides

@ast

Inhibitory effects of HSP70 chaperones on nascent polypeptides

@en

P1476

Inhibitory effects of HSP70 chaperones on nascent polypeptides

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P2093

C Ryan

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

M J Schlesinger

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

T H Stevens

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P2860

Structure and expression of the human gene encoding major heat shock protein HSP70

Production of infectious RNA transcripts from Sindbis virus cDNA clones: mapping of lethal mutations, rescue of a temperature-sensitive marker, and in vitro mutagenesis to generate defined mutants

Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase

In vitro proteolytic processing of a diubiquitin and a truncated diubiquitin formed from in vitro-generated mRNAs.

Heat shock and the sorting of luminal ER proteins.

A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides.

Speculations on the functions of the major heat shock and glucose-regulated proteins.

Rapid purification of mammalian 70,000-dalton stress proteins: affinity of the proteins for nucleotides

P304

980-985

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scholarly article

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10.1002/PRO.5560010803

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P478

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1992-08-01T00:00:00Z

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21852091

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P698

1304386

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P921

molecular chaperones

P932

2142165

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