Molecular chaperones--cellular machines for protein folding (Q34165962)

31 July 2017

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title

Molecular chaperones--cellular machines for protein folding (English)

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31 July 2017

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Stefan Walter

1

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31 July 2017

Johannes Buchner

series ordinal

2

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31 July 2017

publication date

1 April 2002

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31 July 2017

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31 July 2017

volume

41

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31 July 2017

issue

7

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31 July 2017

page(s)

1098-1113

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Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin

31 July 2017

cites work

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Protein folding in the cell

21 January 2018

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Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding

21 January 2018

1 reference

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Protein Folding: A Perspective from Theory and Experiment.

21 January 2018

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The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain

21 January 2018

1 reference

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Principles that govern the folding of protein chains

21 January 2018

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Nucleation, rapid folding, and globular intrachain regions in proteins

21 January 2018

1 reference

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Folding and association of proteins

21 January 2018

1 reference

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Dominant forces in protein folding

21 January 2018

1 reference

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Some factors in the interpretation of protein denaturation

21 January 2018

1 reference

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Proteins as molecular chaperones.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Identification of the predominant non-native histidine ligand in unfolded cytochrome c.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

GroEL-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Chaperonin-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Review: a structural view of the GroE chaperone cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Characterization of a functionally important mobile domain of GroES.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

21 January 2018

Binding of chaperonins.

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Group II chaperonins: new TRiC(k)s and turns of a protein folding machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

A structural model for GroEL-polypeptide recognition

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Structural changes in GroEL effected by binding a denatured protein substrate

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Folding of malate dehydrogenase inside the GroEL-GroES cavity

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

A thermodynamic coupling mechanism for GroEL-mediated unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Chaperonin function: folding by forced unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Molecular chaperones in cellular protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

21 January 2018

1 reference

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Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

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Specificity of DnaK-peptide binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

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BiP binding sequences in antibodies.

21 January 2018

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70.

21 January 2018

1 reference

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The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Inhibition of transforming activity of tyrosine kinase oncogenes by herbimycin A.

21 January 2018

1 reference

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Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation

21 January 2018

1 reference

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Hsp90: chaperoning signal transduction

21 January 2018

1 reference

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Hsp90 & Co. - a holding for folding

21 January 2018

1 reference

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Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

21 January 2018

1 reference

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Localization of the chaperone domain of FKBP52.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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).

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Hsp90 chaperones protein folding in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Crystal structure of a small heat-shock protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Alpha-crystallin can function as a molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Stabilization of proteins and peptides in diagnostic immunological assays by the molecular chaperone Hsp25.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Hsp26: a temperature-regulated chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Cells overexpressing Hsp27 show accelerated recovery from heat-induced nuclear protein aggregation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The primary pathway of protein export in E. coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

SecB, a molecular chaperone with two faces

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Conformational stability of globular proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Hsp90 as a capacitor for morphological evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Identification of in vivo substrates of the chaperonin GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Protein misassembly in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitor

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Structure and function in GroEL-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Symmetric complexes of GroE chaperonins as part of the functional cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The hydrophobic nature of GroEL-substrate binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Analysis of GroE-assisted folding under nonpermissive conditions

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Limits of protein folding inside GroE complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

In vitro evidence that hsp90 contains two independent chaperone sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Chaperone function of Hsp90-associated proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F1521-3773%2820020402%2941%3A7%3C1098%3A%3AAID-ANIE1098%3E3.0.CO%3B2-9

10.1002/1521-3773(20020402)41:7<1098::AID-ANIE1098>3.0.CO;2-9

21 January 2018

Identifiers

DOI

1 reference

31 July 2017

1 reference