(Q54565103)

1 June 2018

title

Capturing the misfolds: chaperone-peptide-binding motifs. (English)

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1 June 2018

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Joachimiak A

1

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1 June 2018

publication date

1 June 1997

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1 June 2018

Nature structural biology

published in

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1 June 2018

volume

4

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1 June 2018

issue

6

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1 June 2018

page(s)

430-434

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1 June 2018

Protein folding in the cell

cites work

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Chaperone-assisted protein folding.

21 January 2018

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21 January 2018

Assisted protein folding

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Protein folding and the regulation of signaling pathways

21 January 2018

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

A structural model for GroEL-polypeptide recognition

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

Heat-induced chaperone activity of HSP90.

21 January 2018

1 reference

Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent

21 January 2018

1 reference

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

21 January 2018

1 reference

Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function.

21 January 2018

1 reference

Assessment of the ATP binding properties of Hsp90.

21 January 2018

1 reference

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

21 January 2018

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Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein GP96/GRP94.

21 January 2018

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Protein-peptide interactions

21 January 2018

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Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

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GroEL-mediated protein folding

21 January 2018

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Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain

31 March 2020

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Structural analysis of substrate binding by the molecular chaperone DnaK

31 March 2020

1 reference

Chaperone function of Hsp90-associated proteins

31 March 2020

1 reference

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

31 March 2020

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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

31 March 2020

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Isolation of Hsp90 mutants by screening for decreased steroid receptor function

31 March 2020

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Interaction of glucocorticosteroid receptor and wild-type or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells

31 March 2020

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Interaction of Endoplasmic Reticulum Chaperone GRP94 with Peptide Substrates Is Adenine Nucleotide-independent

31 March 2020

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Targeted Replacement of the Mouse Apolipoprotein E Gene with the Common Human APOE3 Allele Enhances Diet-induced Hypercholesterolemia and Atherosclerosis

31 March 2020

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

31 March 2020

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Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants

31 March 2020

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Crystal structure of an H-2Kb-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove

31 March 2020

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The structural basis of sequence-independent peptide binding by OppA protein

31 March 2020

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Structural basis of pilus subunit recognition by the PapD chaperone.

31 March 2020

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The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC

31 March 2020

1 reference

31 March 2020

Identifiers

DOI

10.1038/NSB0697-430

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1 June 2018

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1 June 2018