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Molecular chaperones in cellular protein folding
scientific article (publication date: 13 June 1996)
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scholarly article
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review article
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Europe PubMed Central
title
Molecular chaperones in cellular protein folding
(English)
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PubMed
reference URL
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retrieved
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main subject
protein folding
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molecular chaperones
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author
Franz-Ulrich Hartl
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object named as
Hartl FU
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language of work or name
English
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23 April 2017
publication date
13 June 1996
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PubMed
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retrieved
23 April 2017
published in
Nature
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PubMed
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592
retrieved
23 April 2017
volume
381
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PubMed
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23 April 2017
page(s)
571-9
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PubMed
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23 April 2017
issue
6583
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PubMed
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retrieved
23 April 2017
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Peptide-binding specificity of the molecular chaperone BiP
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Homologous plant and bacterial proteins chaperone oligomeric protein assembly
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A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene
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Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
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Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
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Understanding how proteins fold: the lysozyme story so far.
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Global suppression of protein folding defects and inclusion body formation
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Protein folding in the cell: competing models of chaperonin function.
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Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
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The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
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Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
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Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
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Refolding of denatured lactate dehydrogenase by Escherichia coli ribosomes
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Cotranslational folding and calnexin binding during glycoprotein synthesis
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A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE.
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The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology
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NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.
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1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78)
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Crossref
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7 January 2021
based on heuristic
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A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.
1 reference
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Crossref
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7 January 2021
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Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.
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Different peptide binding specificities of hsp70 family members.
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Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences
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Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding
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Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.
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DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.
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The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
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Kinetics of molecular chaperone action
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based on heuristic
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Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
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ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.
1 reference
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The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates
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Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
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based on heuristic
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The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
1 reference
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based on heuristic
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Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones
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7 January 2021
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Protein disaggregation mediated by heat-shock protein Hsp104.
1 reference
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based on heuristic
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Roles of molecular chaperones in protein degradation
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7 January 2021
based on heuristic
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Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
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7 January 2021
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The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
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Mitochondrial Hsp70/MIM44 complex facilitates protein import
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based on heuristic
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What drives the translocation of proteins?
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7 January 2021
based on heuristic
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Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44
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7 January 2021
based on heuristic
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Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
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Crossref
reference URL
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7 January 2021
based on heuristic
inferred from DOI database lookup
The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria.
1 reference
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Crossref
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7 January 2021
based on heuristic
inferred from DOI database lookup
Identification of GroEL as a constituent of an mRNA-protection complex in Escherichia coli
1 reference
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7 January 2021
based on heuristic
inferred from DOI database lookup
A polypeptide bound by the chaperonin groEL is localized within a central cavity
1 reference
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7 January 2021
based on heuristic
inferred from DOI database lookup
ATP induces large quaternary rearrangements in a cage-like chaperonin structure.
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
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The crystal structure of the bacterial chaperonin GroEL at 2.8 A
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https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
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The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S
1 reference
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7 January 2021
based on heuristic
inferred from DOI database lookup
Residues in chaperonin GroEL required for polypeptide binding and release
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https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
1 reference
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7 January 2021
based on heuristic
inferred from DOI database lookup
Characterization of a functionally important mobile domain of GroES.
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
1 reference
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Crossref
reference URL
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7 January 2021
based on heuristic
inferred from DOI database lookup
Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
The hydrophobic nature of GroEL-substrate binding
1 reference
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Crossref
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https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Prevention of protein denaturation under heat stress by the chaperonin Hsp60
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https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2F381571A0
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7 January 2021
based on heuristic
inferred from DOI database lookup
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
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7 January 2021
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inferred from DOI database lookup
Protein folding. Secrets of a double-doughnut.
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Protein folding in the central cavity of the GroEL-GroES chaperonin complex
1 reference
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7 January 2021
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Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
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7 January 2021
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Cooperativity in ATP hydrolysis by GroEL is increased by GroES
1 reference
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Crossref
reference URL
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7 January 2021
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Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.
1 reference
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Crossref
reference URL
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7 January 2021
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Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.
1 reference
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Crossref
reference URL
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7 January 2021
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Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding
1 reference
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Crossref
reference URL
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7 January 2021
based on heuristic
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Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.
1 reference
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Crossref
reference URL
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7 January 2021
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The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle
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7 January 2021
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Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.
1 reference
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Crossref
reference URL
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7 January 2021
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Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.
1 reference
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Crossref
reference URL
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7 January 2021
based on heuristic
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Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.
1 reference
stated in
Crossref
reference URL
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7 January 2021
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The formation of symmetrical GroEL-GroES complexes in the presence of ATP.
1 reference
stated in
Crossref
reference URL
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7 January 2021
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Symmetric complexes of GroE chaperonins as part of the functional cycle
1 reference
stated in
Crossref
reference URL
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7 January 2021
based on heuristic
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Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Proper and improper folding of proteins in the cellular environment
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Unfolding protein folding
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
To fold or not to fold....
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Molecular chaperones. Opening and closing the Anfinsen cage.
1 reference
stated in
Crossref
reference URL
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7 January 2021
based on heuristic
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Revisiting the Anfinsen cage
1 reference
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reference URL
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7 January 2021
based on heuristic
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Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Refolding of barnase in the presence of GroE
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
1 reference
stated in
Crossref
reference URL
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7 January 2021
based on heuristic
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Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin
1 reference
stated in
Crossref
reference URL
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7 January 2021
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A cytoplasmic chaperonin that catalyzes beta-actin folding
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
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TCP1 complex is a molecular chaperone in tubulin biogenesis
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Specificity in chaperonin-mediated protein folding
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Structure of a molecular chaperone from a thermophilic archaebacterium
1 reference
stated in
Crossref
reference URL
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7 January 2021
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Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains.
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
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Primary structure of the thermosome from Thermoplasma acidophilum.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms
1 reference
stated in
Crossref
reference URL
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7 January 2021
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Calnexin: a membrane-bound chaperone of the endoplasmic reticulum
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
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Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Sequencing and analysis of bacterial genomes
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Successive action of Escherichia coli chaperones in vivo.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Synthesis of chloramphenicol acetyltransferase in a coupled transcription-translation in vitro system lacking the chaperones DnaK and DnaJ.
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese. Analysis by fluorescence.
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
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Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
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Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
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Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
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A protein complex required for signal-sequence-specific sorting and translocation
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
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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
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F381571A0
retrieved
7 January 2021
based on heuristic
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Intracellular protein trafficking defects in human disease
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
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Resting places on folding pathways
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
How chaperones tell wrong from right
1 reference
stated in
Crossref
reference URL
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7 January 2021
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Identifiers
DOI
10.1038/381571A0
2 references
stated in
PubMed
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592
retrieved
23 April 2017
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
40127
Dimensions Publication ID
1029280955
0 references
OpenCitations bibliographic resource ID
40127
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
40127
PubMed ID
8637592
2 references
stated in
PubMed
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=8637592
retrieved
23 April 2017
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
40127
Springer Nature article ID
10.1038/381571a0
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