(Q48956947)

17 February 2018

title

Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms. (English)

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17 February 2018

author name string

G W Farr

1

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17 February 2018

E C Scharl

2

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17 February 2018

R J Schumacher

3

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17 February 2018

S Sondek

4

1 reference

17 February 2018

A L Horwich

5

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17 February 2018

language of work or name

English

0 references

publication date

1 June 1997

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17 February 2018

published in

Cell

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17 February 2018

volume

89

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17 February 2018

page(s)

927-937

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17 February 2018

issue

6

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17 February 2018

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

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GroEL-mediated protein folding

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

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A cytoplasmic chaperonin that catalyzes beta-actin folding

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

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A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin

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

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Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed

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Molecular chaperones in cellular protein folding

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The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol.

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Actin is the naturally occurring inhibitor of deoxyribonuclease I

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Chaperonin-mediated folding of actin and tubulin

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Reversible interaction of beta-actin along the channel of the TCP-1 cytoplasmic chaperonin

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The effect of macromolecular crowding on chaperonin-mediated protein folding

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Effect of monoclonal antibody binding on alpha-beta gamma subunit interactions in the rod outer segment G protein, Gt

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Amino acid sequence of the alpha subunit of transducin deduced from the cDNA sequence

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

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

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Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

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The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound

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Identification of a guanine binding domain peptide of the GTP binding site of glutamate dehydrogenase: isolation with metal-chelate affinity chromatography

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Mapping of effector binding sites of transducin alpha-subunit using G alpha t/G alpha i1 chimeras

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7 January 2021

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

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7 January 2021

Specificity in chaperonin-mediated protein folding

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7 January 2021

Quasi-native chaperonin-bound intermediates in facilitated protein folding

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7 January 2021

Pathway leading to correctly folded beta-tubulin

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7 January 2021

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

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7 January 2021

The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes

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7 January 2021

A yeast TCP-1-like protein is required for actin function in vivo

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7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

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7 January 2021

TCP1 complex is a molecular chaperone in tubulin biogenesis

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7 January 2021

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Identifiers

DOI

1 reference

17 February 2018

PubMed ID

9200611

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17 February 2018