(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

page(s)

430-434

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1 June 2018

issue

6

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1 June 2018

Protein folding in the cell

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Assisted protein folding

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Protein folding and the regulation of signaling pathways

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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A structural model for GroEL-polypeptide recognition

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

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

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

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

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

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Assessment of the ATP binding properties of Hsp90.

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

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

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Protein-peptide interactions

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Residues in chaperonin GroEL required for polypeptide binding and release

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GroEL-mediated protein folding

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

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Structural analysis of substrate binding by the molecular chaperone DnaK

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Chaperone function of Hsp90-associated proteins

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

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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

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

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Targeted replacement of the mouse apolipoprotein E gene with the common human APOE3 allele enhances diet-induced hypercholesterolemia and atherosclerosis

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

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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

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31 March 2020

Identifiers

DOI

10.1038/NSB0697-430

1 reference

1 June 2018

PubMed ID

9187647

1 reference

1 June 2018