(Q38549374)

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The chaperone cofactor Hop/p60 interacts with the cytosolic chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities

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scholarly article

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Europe PubMed Central

PubMed publication ID

4 September 2017

The chaperone cofactor Hop/p60 interacts with the cytosolic chaperonin-containing TCP-1 and affects its nucleotide exchange and protein folding activities (English)

1 reference

Europe PubMed Central

PubMed publication ID

4 September 2017

protein folding

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molecular chaperones

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author name string

Gebauer M

1

1 reference

Europe PubMed Central

PubMed publication ID

4 September 2017

Melki R

2

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Europe PubMed Central

PubMed publication ID

4 September 2017

Gehring U

3

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Europe PubMed Central

PubMed publication ID

4 September 2017

language of work or name

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publication date

1 November 1998

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Europe PubMed Central

PubMed publication ID

4 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

4 September 2017

273

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Europe PubMed Central

PubMed publication ID

4 September 2017

45

1 reference

Europe PubMed Central

PubMed publication ID

4 September 2017

29475-29480

1 reference

Europe PubMed Central

PubMed publication ID

4 September 2017

Protein folding in vivo: unraveling complex pathways

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

The Hsp70 and Hsp60 chaperone machines

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

The ins and outs of a molecular chaperone machine.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Mammalian protein RAP46: an interaction partner and modulator of 70 kDa heat shock proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

BAG-1 modulates the chaperone activity of Hsp70/Hsc70.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

ATP-dependent protein refolding activity in reticulocyte lysate. Evidence for the participation of different chaperone components

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Cytoplasmic chaperonin containing TCP-1: structural and functional characterization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Hop modulates Hsp70/Hsp90 interactions in protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Purification and characterization of a 66-kDa protein from rabbit reticulocyte lysate which promotes the recycling of hsp 70.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

ATP Binding Induces Large Conformational Changes in the Apical and Equatorial Domains of the Eukaryotic Chaperonin Containing TCP-1 Complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.45.29475

21 January 2018

Identifiers

10.1074/JBC.273.45.29475

1 reference

Europe PubMed Central

PubMed publication ID

4 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

4 September 2017

ResearchGate publication ID

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