(Q43000739)

English

Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1.

scientific article published in January 2002

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scholarly article

1 reference

Europe PubMed Central

12 November 2017

Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. (English)

1 reference

Europe PubMed Central

12 November 2017

molecular chaperones

0 references

author name string

Xinguo Qian

1

1 reference

Europe PubMed Central

12 November 2017

Wenbo Hou

2

1 reference

Europe PubMed Central

12 November 2017

Li Zhengang

3

1 reference

Europe PubMed Central

12 November 2017

Bingdong Sha

4

1 reference

Europe PubMed Central

12 November 2017

language of work or name

0 references

publication date

1 January 2002

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Europe PubMed Central

12 November 2017

number of pages

8

1 reference

based on heuristic

inferred from page(s)

Biochemical Journal

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Europe PubMed Central

12 November 2017

361

1 reference

Europe PubMed Central

12 November 2017

27-34

1 reference

Europe PubMed Central

12 November 2017

Pt 1

1 reference

Europe PubMed Central

12 November 2017

An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Probing protein-protein interactions in real time.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

The Hsp70 and Hsp60 chaperone machines

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Structural analysis of substrate binding by the molecular chaperone DnaK

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Molecular chaperones in cellular protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Direct observation of enzyme activity with the atomic force microscope.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Protein folding in the cell

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

The emergence of the chaperone machines

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1222294

26 May 2018

Peptide-binding specificity of the molecular chaperone BiP

1 reference

https://pubmed.ncbi.nlm.nih.gov/11743879

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell

1 reference

https://pubmed.ncbi.nlm.nih.gov/11743879

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria

1 reference

https://pubmed.ncbi.nlm.nih.gov/11743879

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1042/0264-6021:3610027

1 reference

Europe PubMed Central

12 November 2017

1 reference

Europe PubMed Central

12 November 2017

1 reference

Europe PubMed Central

12 November 2017

ResearchGate publication ID

0 references

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