Chaperone-assisted folding of newly synthesized proteins in the cytosol (Q36069355)

12 August 2017

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title

Chaperone-assisted folding of newly synthesized proteins in the cytosol (English)

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12 August 2017

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2

Bernd Bukau

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12 August 2017

1

Elke Deuerling

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12 August 2017

publication date

1 September 2004

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Critical Reviews in Biochemistry and Molecular Biology

12 August 2017

published in

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12 August 2017

volume

39

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12 August 2017

issue

5-6

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12 August 2017

page(s)

261-277

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Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed

12 August 2017

cites work

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Principles that govern the folding of protein chains

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Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit

21 January 2018

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The complete atomic structure of the large ribosomal subunit at 2.4 A resolution

21 January 2018

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The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions

21 January 2018

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The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity

21 January 2018

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

21 January 2018

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Getting newly synthesized proteins into shape.

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

The Hsp70 and Hsp60 chaperone machines

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

GroEL/GroES-mediated folding of a protein too large to be encapsulated

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

Folding of malate dehydrogenase inside the GroEL-GroES cavity

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

An insertional mutation in theBTF3 transcription factor gene leads to an early postimplantation lethality in mice

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

Trigger Factor and DnaK possess overlapping substrate pools and binding specificities

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

From Levinthal to pathways to funnels

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

Understanding protein folding via free-energy surfaces from theory and experiment

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

The structural basis of protein targeting and translocation in bacteria.

21 January 2018

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https://api.crossref.org/works/10.1080%2F10409230490892496

Proteins as molecular chaperones.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Principles of protein folding in the cellular environment

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Cotranslational protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

GroEL-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Protein folding and unfolding at atomic resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Folding of newly translated proteins in vivo: the role of molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

A cytoplasmic chaperonin that catalyzes beta-actin folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

A functional chaperone triad on the yeast ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

In vivo analysis of the overlapping functions of DnaK and trigger factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Role and regulation of the ER chaperone BiP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Three-dimensional structures of translating ribosomes by Cryo-EM.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Folding of a nascent peptide on the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Random circular permutation of DsbA reveals segments that are essential for protein folding and stability

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Chaperone rings in protein folding and degradation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The major pathways of protein translocation across membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Diffusion control in an elementary protein folding reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

L23 protein functions as a chaperone docking site on the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Interaction of trigger factor with the ribosome

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Hsp70 chaperone machines.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Molecular basis for interactions of the DnaK chaperone with substrates.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Mechanisms of protein folding: molecular chaperones and their application in biotechnology

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Chaperone selection during glycoprotein translocation into the endoplasmic reticulum.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The ribosomal exit tunnel functions as a discriminating gate

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Protein import into mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The protein import motor of mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The structural basis of ribosome activity in peptide bond synthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Three-state equilibrium of Escherichia coli trigger factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Binding specificity of Escherichia coli trigger factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Versatility of the mitochondrial protein import machinery

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Mitochondrial protein import: two membranes, three translocases

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Co-translocational misfolding in the ER of living cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Initial characterization of the nascent polypeptide-associated complex in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Nascent-polypeptide-associated complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Interaction of Hsp70 chaperones with substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Conformational changes studied by cryo-electron microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Fast folding of the two-domain semliki forest virus capsid protein explains co-translational proteolytic activity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Common principles of protein translocation across membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Molecular chaperones as HSF1-specific transcriptional repressors

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Chaperonin function: folding by forced unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

SecB is a bona fide generalized chaperone in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Effects of macromolecular crowding on protein folding and aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

The nascent polypeptide-associated complex (NAC) of yeast functions in the targeting process of ribosomes to the ER membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

A protein complex required for signal-sequence-specific sorting and translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Structure of the 30S ribosomal subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

GroEL/GroES: structure and function of a two-stroke folding machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Zuotin, a ribosome-associated DnaJ molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Macromolecular crowding: biochemical, biophysical, and physiological consequences

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

Identification of in vivo substrates of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1080%2F10409230490892496

10.1080/10409230490892496

21 January 2018

Identifiers

DOI

1 reference

12 August 2017

1 reference