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Molecular chaperones--cellular machines for protein folding
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scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
review article
1 reference
stated in
Europe PubMed Central
title
Molecular chaperones--cellular machines for protein folding
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
main subject
protein folding
0 references
molecular chaperones
0 references
author name string
Stefan Walter
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
Johannes Buchner
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
publication date
1 April 2002
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
published in
Angewandte Chemie
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
volume
41
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
issue
7
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
page(s)
1098-1113
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
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Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin
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Protein folding in the cell
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Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
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21 January 2018
Protein Folding: A Perspective from Theory and Experiment.
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The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain
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Principles that govern the folding of protein chains
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Nucleation, rapid folding, and globular intrachain regions in proteins
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21 January 2018
Folding and association of proteins
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21 January 2018
Dominant forces in protein folding
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Some factors in the interpretation of protein denaturation
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Proteins as molecular chaperones.
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21 January 2018
Identification of the predominant non-native histidine ligand in unfolded cytochrome c.
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21 January 2018
GroEL-mediated protein folding
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21 January 2018
Chaperonin-mediated protein folding
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21 January 2018
Review: a structural view of the GroE chaperone cycle
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21 January 2018
The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
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21 January 2018
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
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Characterization of a functionally important mobile domain of GroES.
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21 January 2018
The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli
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21 January 2018
Binding of chaperonins.
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21 January 2018
Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.
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21 January 2018
The formation of symmetrical GroEL-GroES complexes in the presence of ATP.
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21 January 2018
Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
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21 January 2018
Group II chaperonins: new TRiC(k)s and turns of a protein folding machine
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21 January 2018
Residues in chaperonin GroEL required for polypeptide binding and release
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21 January 2018
A structural model for GroEL-polypeptide recognition
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21 January 2018
The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity
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21 January 2018
Structural changes in GroEL effected by binding a denatured protein substrate
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21 January 2018
Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.
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21 January 2018
Folding of malate dehydrogenase inside the GroEL-GroES cavity
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21 January 2018
Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding
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21 January 2018
The Hsp70 and Hsp60 chaperone machines
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21 January 2018
The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.
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21 January 2018
Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes
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21 January 2018
Protein folding in the central cavity of the GroEL-GroES chaperonin complex
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21 January 2018
Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.
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21 January 2018
GroEL/GroES-mediated folding of a protein too large to be encapsulated
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21 January 2018
Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.
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21 January 2018
Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding
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21 January 2018
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.
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21 January 2018
A thermodynamic coupling mechanism for GroEL-mediated unfolding
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21 January 2018
Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.
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21 January 2018
Chaperonin function: folding by forced unfolding
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21 January 2018
Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.
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21 January 2018
Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism
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21 January 2018
Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
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21 January 2018
Molecular chaperones in cellular protein folding
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21 January 2018
Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
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21 January 2018
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
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21 January 2018
Structural analysis of substrate binding by the molecular chaperone DnaK
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21 January 2018
Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein
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21 January 2018
Kinetics of molecular chaperone action
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21 January 2018
Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.
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21 January 2018
Specificity of DnaK-peptide binding
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Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
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BiP binding sequences in antibodies.
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21 January 2018
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
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21 January 2018
DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70.
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21 January 2018
The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.
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21 January 2018
Inhibition of transforming activity of tyrosine kinase oncogenes by herbimycin A.
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21 January 2018
Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation
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21 January 2018
Hsp90: chaperoning signal transduction
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21 January 2018
Hsp90 & Co. - a holding for folding
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21 January 2018
Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90
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21 January 2018
Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent
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21 January 2018
A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
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21 January 2018
Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
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21 January 2018
Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence
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21 January 2018
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
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21 January 2018
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
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21 January 2018
The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains
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21 January 2018
The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions
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21 January 2018
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
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21 January 2018
Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
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21 January 2018
The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell
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21 January 2018
Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor
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21 January 2018
Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties
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21 January 2018
Localization of the chaperone domain of FKBP52.
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21 January 2018
In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
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21 January 2018
Expression of human papilloma virus E7 protein causes apoptosis and inhibits DNA synthesis in primary hepatocytes via increased expression of p21(Cip-1/WAF1/MDA6).
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21 January 2018
Hsp90 chaperones protein folding in vitro.
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21 January 2018
Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
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21 January 2018
Crystal structure of a small heat-shock protein
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21 January 2018
The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure
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Crossref
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21 January 2018
Alpha-crystallin can function as a molecular chaperone
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21 January 2018
Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones
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21 January 2018
A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
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Crossref
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21 January 2018
Stabilization of proteins and peptides in diagnostic immunological assays by the molecular chaperone Hsp25.
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21 January 2018
Hsp26: a temperature-regulated chaperone
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21 January 2018
Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.
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21 January 2018
Cells overexpressing Hsp27 show accelerated recovery from heat-induced nuclear protein aggregation.
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Crossref
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21 January 2018
A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
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Crossref
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21 January 2018
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
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21 January 2018
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
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21 January 2018
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.
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21 January 2018
The primary pathway of protein export in E. coli
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21 January 2018
Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins
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Crossref
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21 January 2018
SecB, a molecular chaperone with two faces
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Crossref
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21 January 2018
Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.
1 reference
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Crossref
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21 January 2018
Prions
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21 January 2018
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
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Crossref
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21 January 2018
Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae.
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Crossref
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21 January 2018
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.
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Crossref
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21 January 2018
Conformational stability of globular proteins
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21 January 2018
Hsp90 as a capacitor for morphological evolution
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Crossref
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21 January 2018
The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle
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21 January 2018
The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
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Crossref
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21 January 2018
Identification of in vivo substrates of the chaperonin GroEL
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21 January 2018
Peptide-binding specificity of the molecular chaperone BiP
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21 January 2018
Protein misassembly in vitro.
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21 January 2018
Protein folding
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Crossref
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21 January 2018
The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State
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21 January 2018
The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitor
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21 January 2018
Structure and function in GroEL-mediated protein folding
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Crossref
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21 January 2018
Symmetric complexes of GroE chaperonins as part of the functional cycle
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21 January 2018
Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer
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Crossref
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21 January 2018
The hydrophobic nature of GroEL-substrate binding
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Crossref
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21 January 2018
Analysis of GroE-assisted folding under nonpermissive conditions
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21 January 2018
Limits of protein folding inside GroE complexes
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Crossref
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21 January 2018
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
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21 January 2018
Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies
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21 January 2018
C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle
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21 January 2018
In vitro evidence that hsp90 contains two independent chaperone sites
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21 January 2018
Chaperone function of Hsp90-associated proteins
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21 January 2018
Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
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21 January 2018
The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
1 reference
stated in
Crossref
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21 January 2018
Identifiers
DOI
10.1002/1521-3773(20020402)41:7<1098::AID-ANIE1098>3.0.CO;2-9
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
PubMed ID
12491239
1 reference
stated in
Europe PubMed Central
PubMed ID
12491239
retrieved
31 July 2017
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