(Q58360990)

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10 February 2020

title

Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain (English)

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10 February 2020

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13

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10 February 2020

Chrisostomos Prodromou

14

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10 February 2020

15

Len Neckers

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10 February 2020

10

Jane B Trepel

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10 February 2020

5

Bradley T Scroggins

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10 February 2020

author name string

Shinji Tsutsumi

1

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10 February 2020

Mehdi Mollapour

2

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10 February 2020

Christian Graf

3

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10 February 2020

Chung-Tien Lee

4

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10 February 2020

Wanping Xu

6

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10 February 2020

Lenka Haslerova

7

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10 February 2020

Martin Hessling

8

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10 February 2020

Anna A Konstantinova

9

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10 February 2020

Barry Panaretou

11

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10 February 2020

Johannes Buchner

12

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10 February 2020

publication date

18 October 2009

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Nature Structural & Molecular Biology

10 February 2020

published in

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volume

16

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10 February 2020

issue

11

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10 February 2020

page(s)

1141-1147

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https://scigraph.springernature.com/pub.10.1038/nsmb.1682

10 February 2020

exact match

0 references

cites work

Hsp90 inhibitors as novel cancer chemotherapeutic agents

1 reference

Structure and mechanism of the Hsp90 molecular chaperone machinery

21 January 2018

1 reference

The Hsp90 chaperone machinery

21 January 2018

1 reference

Heat-shock protein 90, a chaperone for folding and regulation

21 January 2018

1 reference

Hsp90 inhibitors: small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation

21 January 2018

1 reference

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.

21 January 2018

1 reference

Conformational dynamics of the molecular chaperone Hsp90 in complexes with a co-chaperone and anticancer drugs.

21 January 2018

1 reference

Apo-Hsp90 coexists in two open conformational states in solution.

21 January 2018

1 reference

Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements

21 January 2018

1 reference

Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle

21 January 2018

1 reference

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

21 January 2018

1 reference

Structure of an Hsp90-Cdc37-Cdk4 complex.

21 January 2018

1 reference

21 January 2018

1 reference

The charged region of Hsp90 modulates the function of the N-terminal domain

21 January 2018

1 reference

Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast

21 January 2018

1 reference

Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis

21 January 2018

1 reference

The heat-shock protein receptors: some answers and more questions

21 January 2018

1 reference

Induction of heat shock proteins in B-cell exosomes.

21 January 2018

1 reference

Transforming growth factor alpha (TGFalpha)-stimulated secretion of HSP90alpha: using the receptor LRP-1/CD91 to promote human skin cell migration against a TGFbeta-rich environment during wound healing

21 January 2018

1 reference

Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine

21 January 2018

1 reference

Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

21 January 2018

1 reference

Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

The Hsp90 of Candida albicans can confer Hsp90 functions in Saccharomyces cerevisiae: a potential model for the processes that generate immunogenic fragments of this molecular chaperone in C. albicans infections

21 January 2018

1 reference

Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis

21 January 2018

1 reference

p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules

21 January 2018

1 reference

Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions

21 January 2018

1 reference

Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions.

21 January 2018

1 reference

High-sensitivity mass spectrometry for imaging subunit interactions: hydrogen/deuterium exchange

21 January 2018

1 reference

An acetylation site in the middle domain of Hsp90 regulates chaperone function

21 January 2018

1 reference

A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor

21 January 2018

1 reference

Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu

21 January 2018

1 reference

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

21 January 2018

1 reference

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

21 January 2018

1 reference

Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange.

21 January 2018

1 reference

Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation.

21 January 2018

1 reference

Coordinated ATP hydrolysis by the Hsp90 dimer

21 January 2018

1 reference

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

21 January 2018

1 reference

Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicol

31 March 2020

1 reference

The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes

31 March 2020

1 reference

Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex

31 March 2020

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19838189

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NSMB.1682

1 reference

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10 February 2020

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