Chaperone-assisted protein folding. (Q54571596)

1 June 2018

review article

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title

Chaperone-assisted protein folding. (English)

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1 June 2018

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2

F U Hartl

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1 June 2018

J Martin

1

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1 June 2018

publication date

1 February 1997

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1 June 2018

Current Opinion in Structural Biology

published in

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1 June 2018

volume

7

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1 June 2018

issue

1

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1 June 2018

page(s)

41-52

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1 June 2018

Molecular chaperones in protein folding and translocation

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

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Structural analysis of substrate binding by the molecular chaperone DnaK

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The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology

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Specificity of DnaK-peptide binding

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Peptide-binding specificity of the molecular chaperone BiP

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Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

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Kinetics of molecular chaperone action

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Conformational characterization of DnaK and its complexes by small-angle X-ray scattering

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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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Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain

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NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone

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7 January 2021

A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding

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7 January 2021

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

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7 January 2021

The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone

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7 January 2021

A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein

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7 January 2021

Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40.

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A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.

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7 January 2021

Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone

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7 January 2021

Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1.

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7 January 2021

The role of ATP in the functional cycle of the DnaK chaperone system

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7 January 2021

Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes

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7 January 2021

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

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7 January 2021

The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates

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7 January 2021

Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle

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7 January 2021

Mutational analysis of the hsp70-interacting protein Hip

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7 January 2021

Characterization of functional domains of the eukaryotic co-chaperone Hip

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7 January 2021

Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein

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7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

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7 January 2021

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

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https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

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7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

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7 January 2021

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

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7 January 2021

Molecular chaperones in protein folding: the art of avoiding sticky situations

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7 January 2021

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

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7 January 2021

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

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7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

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7 January 2021

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1 reference

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7 January 2021

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

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7 January 2021

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

1 reference

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7 January 2021

Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure.

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7 January 2021

Characterization of a functionally important mobile domain of GroES.

1 reference

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7 January 2021

Interplay of structure and disorder in cochaperonin mobile loops

1 reference

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7 January 2021

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Molecular chaperones. Opening and closing the Anfinsen cage.

1 reference

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7 January 2021

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

A thermodynamic coupling mechanism for GroEL-mediated unfolding

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Release of both native and non-native proteins from a cis-only GroEL ternary complex

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Fluorescence detection of symmetric GroEL14(GroES7)2 heterooligomers involved in protein release during the chaperonin cycle

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Symmetric complexes of GroE chaperonins as part of the functional cycle

1 reference

https://api.crossref.org/works/10.1016/S0959-440X(97)80006-1

7 January 2021

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

1 reference

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7 January 2021

Whole-genome random sequencing and assembly of Haemophilus influenzae Rd

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7 January 2021

The Minimal Gene Complement of Mycoplasma genitalium

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7 January 2021

Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

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7 January 2021

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

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7 January 2021

Identification of the prolyl isomerase domain of Escherichia coli trigger factor

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7 January 2021

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

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7 January 2021

A dnaK homolog in the archaebacterium Methanosarcina mazei S6.

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7 January 2021

Complete Genome Sequence of the Methanogenic Archaeon, Methanococcus jannaschii

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7 January 2021

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

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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

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

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7 January 2021

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

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7 January 2021

A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin

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7 January 2021

Quasi-native Chaperonin-bound Intermediates in Facilitated Protein Folding

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7 January 2021

Pathway leading to correctly folded beta-tubulin

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7 January 2021

Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization

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7 January 2021

The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

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7 January 2021

Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi ]

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7 January 2021

Support for the prion hypothesis for inheritance of a phenotypic trait in yeast

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7 January 2021

10.1016/S0959-440X(97)80006-1

Identifiers

DOI

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1 June 2018

release_vyhmmpy2ojg2zj6gep2mutqfre

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24 November 2022

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1 June 2018