(Q51042630)

27 March 2018

title

The HSP90 chaperone machinery. (English)

1 reference

27 March 2018

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Florian H Schopf

1

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27 March 2018

Maximilian M Biebl

series ordinal

2

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27 March 2018

Johannes Buchner

series ordinal

3

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27 March 2018

publication date

21 April 2017

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27 March 2018

Nature Reviews Molecular Cell Biology

published in

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27 March 2018

volume

18

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27 March 2018

issue

6

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27 March 2018

page(s)

345-360

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27 March 2018

https://scigraph.springernature.com/pub.10.1038/nrm.2017.20

exact match

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cites work

Discovery of the heat shock response

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Steroid receptor interactions with heat shock protein and immunophilin chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Identification of a transformation-specific antigen induced by an avian sarcoma virus

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Regulation of human hsp90alpha gene expression

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Evolution and function of diverse Hsp90 homologs and cochaperone proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

HEAT SHOCK PROTEIN 90C is a bona fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 as a capacitor for morphological evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 as a capacitor of phenotypic variation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 and environmental stress transform the adaptive value of natural genetic variation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Cryptic variation in morphological evolution: HSP90 as a capacitor for loss of eyes in cavefish.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90: breaking the symmetry.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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/10.1038%2FNRM.2017.20

The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 & Co. - a holding for folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The charged linker region is an important regulator of Hsp90 function

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Multidomain structure and correlated dynamics determined by self-consistent FRET networks

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

GHKL, an emergent ATPase/kinase superfamily

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

ATP-binding properties of human Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Stimulation of the weak ATPase activity of human hsp90 by a client protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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/10.1038%2FNRM.2017.20

Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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/10.1038%2FNRM.2017.20

Designed Hsp90 heterodimers reveal an asymmetric ATPase-driven mechanism in vivo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Importance of cycle timing for the function of the molecular chaperone Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Mechanisms of Hsp90 regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Defining the Essential Function of Yeast Hsf1 Reveals a Compact Transcriptional Program for Maintaining Eukaryotic Proteostasis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Chaperone regulation of the heat shock protein response

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The chaperone Hsp90: changing partners for demanding clients

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Post-translational modifications of Hsp90 and their contributions to chaperone regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Dynamic activation of endothelial nitric oxide synthase by Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 is regulated by a switch point in the C-terminal domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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/10.1038%2FNRM.2017.20

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/10.1038%2FNRM.2017.20

The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hop modulates Hsp70/Hsp90 interactions in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Substrate transfer from the chaperone Hsp70 to Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Dynamics of the regulation of Hsp90 by the co-chaperone Sti1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hop/Sti1 phosphorylation inhibits its co-chaperone function

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Stress-inducible phosphoprotein 1 has unique cochaperone activity during development and regulates cellular response to ischemia via the prion protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp70 and Hsp90 of E. coli Directly Interact for Collaboration in Protein Remodeling

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Modulation of the Hsp90 chaperone cycle by a stringent client protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Global functional map of the p23 molecular chaperone reveals an extensive cellular network

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 and p23 Molecular Chaperones Control Chromatin Architecture by Maintaining the Functional Pool of the RSC Chromatin Remodeler.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Cns1 is an activator of the Ssa1 ATPase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

MZB1 is a GRP94 cochaperone that enables proper immunoglobulin heavy chain biosynthesis upon ER stress

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

pERp1 is significantly up-regulated during plasma cell differentiation and contributes to the oxidative folding of immunoglobulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis Mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Global analysis of protein expression in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Chaperoning steroid hormone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Heat-shock protein hsp90 governs the activity of pp60v-src kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Reduced levels of hsp90 compromise steroid receptor action in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Regulation of Ubiquitin-like with Plant Homeodomain and RING Finger Domain 1 (UHRF1) Protein Stability by Heat Shock Protein 90 Chaperone Machinery

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Regulation of Hsp90 client proteins by a Cullin5-RING E3 ubiquitin ligase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Soluble guanylyl cyclase requires heat shock protein 90 for heme insertion during maturation of the NO-active enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Defining fundamental steps in the assembly of the Drosophila RNAi enzyme complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The hsp90 molecular chaperone modulates multiple telomerase activities

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Oncogenic mutations reduce the stability of SRC kinase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Isolation of Hsp90 mutants by screening for decreased steroid receptor function

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Phosphorylation and hsp90 binding mediate heat shock stabilization of p53

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 chaperones wild-type p53 tumor suppressor protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The client protein p53 adopts a molten globule-like state in the presence of Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Dynamic Interaction of Hsp90 with Its Client Protein p53.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90-Tau complex reveals molecular basis for specificity in chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Nucleotide-Free sB-Raf is Preferentially Bound by Hsp90 and Cdc37 In Vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Bipartite Role of Heat Shock Protein 90 (Hsp90) Keeps CRAF Kinase Poised for Activation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 promotes kinase evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Disassembly of transcriptional regulatory complexes by molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Structural and functional basis of protein phosphatase 5 substrate specificity

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Unusual Suspects in the Twilight Zone Between the Hsp90 Interactome and Carcinogenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

High HSP90 expression is associated with decreased survival in breast cancer

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Improving survival by exploiting tumour dependence on stabilized mutant p53 for treatment

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Tumor selectivity of Hsp90 inhibitors: the explanation remains elusive

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The epichaperome is an integrated chaperome network that facilitates tumour survival

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Microglia in the aging brain: relevance to neurodegeneration

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Broad action of Hsp90 as a host chaperone required for viral replication

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Heat shock protein 90 from neglected protozoan parasites

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virus

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Leishmania donovani P23 protects parasites against HSP90 inhibitor-mediated growth arrest

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Heat shock protein 90 homeostasis controls stage differentiation in Leishmania donovani

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

HSP90 Shapes the Consequences of Human Genetic Variation

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf-1-MEK-mitogen-activated protein kinase signalling pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Development of Radicicol Analogues

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

HSP90 and the chaperoning of cancer

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Anticancer Inhibitors of Hsp90 Function: Beyond the Usual Suspects

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Targeting the dynamic HSP90 complex in cancer

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

HSP90 Inhibitor-SN-38 Conjugate Strategy for Targeted Delivery of Topoisomerase I Inhibitor to Tumors

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Targeting Hsp90 prevents escape of breast cancer cells from tyrosine kinase inhibition

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Regulation of organismal proteostasis by transcellular chaperone signaling

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The Hsp90 cochaperone p23 is essential for perinatal survival.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Hsp90, an unlikely ally in the war on cancer

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Essential role of the first intron in the transcription of hsp90beta gene

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

From a ratchet mechanism to random fluctuations evolution of Hsp90's mechanochemical cycle

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Post-translational modification of heat-shock protein 90: impact on chaperone function

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Chaperone function of Hsp90-associated proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Studies with Purified Chaperones Advance the Understanding of the Mechanism of Glucocorticoid Receptor-hsp90 Heterocomplex Assembly

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

The stabilization mechanism of mutant-type p53 by impaired ubiquitination: the loss of wild-type p53 function and the hsp90 association

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Heat shock protein 90 in neurodegenerative diseases

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

STA-8666, a novel HSP90 inhibitor/SN-38 drug conjugate, causes complete tumor regression in preclinical mouse models of pediatric sarcoma

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRM.2017.20

Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70

31 March 2020

1 reference

12 December 2020

A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23

1 reference

12 December 2020

Disruption of functions of wild-type p53 by hetero-oligomerization.

1 reference

12 December 2020

Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes

1 reference

12 December 2020

The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies

1 reference

12 December 2020

Identifiers

DOI

10.1038/NRM.2017.20

1 reference

27 March 2018

PubMed ID

28429788

1 reference

27 March 2018