(Q33840775)

29 July 2017

1 reference

title

Protein folding in vivo: the importance of molecular chaperones (English)

1 reference

29 July 2017

0 references

0 references

Feldman DE

1

1 reference

PubMed ID

10679467

29 July 2017

Frydman J

series ordinal

2

1 reference

29 July 2017

1 February 2000

1 reference

Current Opinion in Structural Biology

29 July 2017

1 reference

29 July 2017

10

1 reference

29 July 2017

26-33

1 reference

29 July 2017

1

1 reference

Principles that govern the folding of protein chains

29 July 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Molecular chaperones: avoiding the crowd

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Recombination of protein domains facilitated by co-translational folding in eukaryotes.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Co-translational folding of an alphavirus capsid protein in the cytosol of living cells

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Contribution of cotranslational folding to the rate of formation of native protein structure

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Protein folding in the cell

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

The Hsp70 and Hsp60 chaperone machines

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

The translation machinery and 70 kd heat shock protein cooperate in protein synthesis

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

In vivo newly translated polypeptides are sequestered in a protected folding environment

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Escherichia coli dnaK null mutants are inviable at high temperature

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Trigger factor depletion or overproduction causes defective cell division but does not block protein export

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

A novel protein complex promoting formation of functional alpha- and gamma-tubulin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Group II chaperonins: new TRiC(k)s and turns of a protein folding machine

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

In vivo observation of polypeptide flux through the bacterial chaperonin system.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Identification of in vivo substrates of the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Chaperonin-mediated folding of actin and tubulin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Myosin II folding is mediated by a molecular chaperonin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Protein folding in vivo: unraveling complex pathways

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Molecular chaperones: pathways and networks

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Growing up in a dangerous environment: a network of multiple targeting and folding pathways for nascent polypeptides in the cytosol

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Protein folding in the cell: competing models of chaperonin function.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

The J-domain family and the recruitment of chaperone power

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Zuotin, a ribosome-associated DnaJ molecular chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Interaction of the protein import and folding machineries of the chloroplast

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Interaction of homologues of Hsp70 and Cpn60 with ferredoxin-NADP+ reductase upon its import into chloroplasts.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Hsp90's secrets unfold: new insights from structural and functional studies

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Chaperones get in touch: the Hip-Hop connection

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Ribosomes and ribosomal RNA as chaperones for folding of proteins.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Chaperone properties of bacterial elongation factor EF-Tu

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Effects of macromolecular crowding on protein folding and aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

Eukaryotic type II chaperonin CCT interacts with actin through specific subunits

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2900044-5

7 January 2021

10.1016/S0959-440X(99)00044-5

Identifiers

DOI

1 reference

29 July 2017

1 reference

PubMed ID

10679467