Principles of protein folding in the cellular environment (Q33536619)

27 July 2017

title

Principles of protein folding in the cellular environment (English)

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27 July 2017

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2

Hartl FU

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27 July 2017

Ellis RJ

1

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27 July 2017

publication date

1 February 1999

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Current Opinion in Structural Biology

27 July 2017

published in

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27 July 2017

volume

9

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27 July 2017

issue

1

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27 July 2017

page(s)

102-110

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publication type of scholarly work

27 July 2017

review article

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Principles that govern the folding of protein chains

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Molecular chaperones in cellular protein folding

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Do Molecular Chaperones Have to Be Proteins?

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Pro Region C-Terminus:Protease Active Site Interactions Are Critical in Catalyzing the Folding of α-Lytic Protease

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

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The J-domain family and the recruitment of chaperone power

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Structural aspects of GroEl function

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Molecular chaperones: Avoiding the crowd

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

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

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

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

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

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Zuotin, a ribosome-associated DnaJmolecular chaperone

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In vitro evidence that hsp90 contains two independent chaperone sites

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

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

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

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7 January 2021

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

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7 January 2021

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

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

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

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

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

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7 January 2021

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

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7 January 2021

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

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In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System

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7 January 2021

In vivo activities of GroEL minichaperones

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7 January 2021

A Single Ring Is Sufficient for Productive Chaperonin-Mediated Folding In Vivo

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7 January 2021

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

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7 January 2021

Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT

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7 January 2021

Group II chaperonin in an open conformation examined by electron tomography

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7 January 2021

The thermosome: chaperonin with a built-in lid

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

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7 January 2021

Protein Folding In Vivo: Unraveling Complex Pathways

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7 January 2021

In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

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7 January 2021

Ribosomes and ribosomal RNA as chaperones for folding of proteins

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7 January 2021

Chaperone Properties of Bacterial Elongation Factor EF-Tu

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Directionality of Polypeptide Transfer in the Mitochondrial Pathway of Chaperone-Mediated Protein Folding

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7 January 2021

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

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7 January 2021

Engineered biosynthesis of peptide antibiotics

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7 January 2021

Genetic Contributions to Understanding Polyketide Synthases

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Cotranslational Protein Folding

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7 January 2021

Nascent chains: folding and chaperone interaction during elongation on ribosomes

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7 January 2021

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

Identifiers

DOI

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release_q6x6brn73nbl5kzqam5jmqvgg4

27 July 2017

Fatcat ID

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

24 November 2022

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