Principles of protein folding in the cellular environment (Q33536619)

27 July 2017

1 reference

title

Principles of protein folding in the cellular environment (English)

1 reference

27 July 2017

0 references

2

Hartl FU

1 reference

27 July 2017

Ellis RJ

1

1 reference

27 July 2017

publication date

1 February 1999

1 reference

Current Opinion in Structural Biology

27 July 2017

published in

1 reference

27 July 2017

volume

9

1 reference

27 July 2017

issue

1

1 reference

27 July 2017

page(s)

102-110

1 reference

Principles that govern the folding of protein chains

27 July 2017

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Forty years under the central dogma

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

The Hsp70 and Hsp60 chaperone machines

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Do Molecular Chaperones Have to Be Proteins?

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

1 reference

7 January 2021

Protein memory through altered folding mediated by intramolecular chaperones.

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Unfolded conformations of alpha-lytic protease are more stable than its native state

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

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%2980013-X

7 January 2021

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

1 reference

7 January 2021

Structural aspects of GroEL function

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Molecular chaperones: Avoiding the crowd

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Macromolecular crowding: biochemical, biophysical, and physiological consequences

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

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%2980013-X

7 January 2021

Zuotin, a ribosome-associated DnaJ molecular chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

In vitro evidence that hsp90 contains two independent chaperone sites

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system 1 1Edited by J.Karn

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

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%2980013-X

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%2980013-X

7 January 2021

The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

GroEL-GroES-mediated protein folding requires an intact central cavity

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

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%2980013-X

7 January 2021

In vivo activities of GroEL minichaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

A single ring is sufficient for productive chaperonin-mediated folding in vivo

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II Chaperonin

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Group II chaperonin in an open conformation examined by electron tomography

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

The thermosome: chaperonin with a built-in lid

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

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%2980013-X

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%2980013-X

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%2980013-X

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%2980013-X

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%2980013-X

7 January 2021

Protein Folding In Vivo: Unraveling Complex Pathways

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

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%2980013-X

7 January 2021

Chaperone properties of bacterial elongation factor EF-Tu

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

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%2980013-X

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%2980013-X

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%2980013-X

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%2980013-X

7 January 2021

Engineered biosynthesis of peptide antibiotics

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Genetic Contributions to Understanding Polyketide Synthases

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

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%2980013-X

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Cotranslational protein folding

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

Nascent chains: folding and chaperone interaction during elongation on ribosomes

1 reference

https://api.crossref.org/works/10.1016%2FS0959-440X%2899%2980013-X

7 January 2021

10.1016/S0959-440X(99)80013-X

Identifiers

DOI

1 reference

release_q6x6brn73nbl5kzqam5jmqvgg4

27 July 2017

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/q6x6brn73nbl5kzqam5jmqvgg4

24 November 2022

mapped directly with Wikidata item

1 reference