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Hsp90 Co-chaperones as Drug Targets in Cancer: Current Perspectives

https://doi.org/10.1007/7355_2015_99

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The tetratricopeptide repeat: a structural motif mediating protein-protein interactions

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Role of HSP90, CDC37, and CRM1 as modulators of P16INK4A activity in rat liver carcinogenesis and human liver cancer†

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Gedunin, a limonoid from Xylocarpus granatum, inhibits the growth of CaCo‐2 colon cancer cell line In Vitro

inferredcites →https://doi.org/10.1007/978-1-61779-295-3_4openalex-snapshot

The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function

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Hsp70/Hsp90 Organising Protein (Hop): Beyond Interactions with Chaperones and Prion Proteins

inferredcites →https://doi.org/10.1007/978-3-319-11731-7_5openalex-snapshot

Cdc37 as a Co-chaperone to Hsp90

inferredcites →https://doi.org/10.1007/978-3-319-11731-7_6openalex-snapshot

p23 and Aha1

inferredcites →https://doi.org/10.1007/978-3-642-61122-3_18openalex-snapshot

Genetic Approaches to Defining Signaling by the CML-Associated Tyrosine kinase BCR-ABL1

inferredcites →https://doi.org/10.1007/s00109-004-0549-9openalex-snapshot

Targeting multiple signal transduction pathways through inhibition of Hsp90

inferredcites →https://doi.org/10.1007/s00109-006-0066-0openalex-snapshot

Modulation of Hsp90 function in neurodegenerative disorders: a molecular-targeted therapy against disease-causing protein

inferredcites →https://doi.org/10.1007/s10254-003-0021-1openalex-snapshot

Hsp70 and Hsp90—a relay team for protein folding

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Cucurbitacin D induces cell cycle arrest and apoptosis by inhibiting STAT3 and NF-κB signaling in doxorubicin-resistant human breast carcinoma (MCF7/ADR) cells

inferredcites →https://doi.org/10.1007/s12192-010-0211-0openalex-snapshot

Increased expression of co-chaperone HOP with HSP90 and HSC70 and complex formation in human colonic carcinoma

inferredcites →https://doi.org/10.1007/s13277-012-0549-2openalex-snapshot

Cucurbitacin D induces growth inhibition, cell cycle arrest, and apoptosis in human endometrial and ovarian cancer cells

inferredcites →https://doi.org/10.1016/0092-8674(94)90442-1openalex-snapshot

Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila

inferredcites →https://doi.org/10.1016/j.bbamcr.2011.08.007openalex-snapshot

TRAP-1, the mitochondrial Hsp90

inferredcites →https://doi.org/10.1016/j.bbamcr.2011.08.013openalex-snapshot

Approaches for defining the Hsp90-dependent proteome

inferredcites →https://doi.org/10.1016/j.bbamcr.2011.09.003openalex-snapshot

The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones

inferredcites →https://doi.org/10.1016/j.bbamcr.2011.09.020openalex-snapshot

Evolution and function of diverse Hsp90 homologs and cochaperone proteins

inferredcites →https://doi.org/10.1016/j.bbamcr.2011.10.013openalex-snapshot

GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum

inferredcites →https://doi.org/10.1016/j.bbamcr.2011.11.006openalex-snapshot

Chaperoning steroidal physiology: Lessons from mouse genetic models of Hsp90 and its cochaperones

inferredcites →https://doi.org/10.1016/j.bbamcr.2011.12.006openalex-snapshot

HSP90 as a platform for the assembly of more effective cancer chemotherapy

inferredcites →https://doi.org/10.1016/j.bbamcr.2012.02.004openalex-snapshot

Preface to Hsp90

inferredcites →https://doi.org/10.1016/j.bbamcr.2012.03.014openalex-snapshot

Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins

inferredcites →https://doi.org/10.1016/j.bmc.2010.07.042openalex-snapshot

Design and synthesis of Hsp90 inhibitors: Exploring the SAR of Sansalvamide A derivatives

inferredcites →https://doi.org/10.1016/j.bmcl.2011.06.083openalex-snapshot

Synthesis and evaluation of biotinylated sansalvamide A analogs and their modulation of Hsp90

inferredcites →https://doi.org/10.1016/j.bmcl.2014.12.048openalex-snapshot

Exploring in vitro and in vivo Hsp90 inhibitors activity against human protozoan parasites

inferredcites →https://doi.org/10.1016/j.canlet.2011.03.004openalex-snapshot

RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation

inferredcites →https://doi.org/10.1016/j.canlet.2012.09.021openalex-snapshot

Knockdown of Hop downregulates RhoC expression, and decreases pseudopodia formation and migration in cancer cell lines

inferredcites →https://doi.org/10.1016/j.cell.2012.06.047openalex-snapshot

Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition

inferredcites →https://doi.org/10.1016/j.celrep.2015.07.004openalex-snapshot

c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells

inferredcites →https://doi.org/10.1016/j.ejcb.2008.09.003openalex-snapshot

Knockdown of the co-chaperone Hop promotes extranuclear accumulation of Stat3 in mouse embryonic stem cells

inferredcites →https://doi.org/10.1016/j.gde.2004.12.011openalex-snapshot

Hsp90 and Cdc37 – a chaperone cancer conspiracy

inferredcites →https://doi.org/10.1016/j.jbiosc.2012.02.016openalex-snapshot

Cytotoxic activity to acute myeloid leukemia cells by Antp-TPR hybrid peptide targeting Hsp90

inferredcites →https://doi.org/10.1016/j.jchromb.2010.08.016openalex-snapshot

High-yield expression and purification of the Hsp90-associated p23, FKBP52, HOP and SGTα proteins

inferredcites →https://doi.org/10.1016/j.jmb.2004.05.007openalex-snapshot

Biochemical and Structural Studies of the Interaction of Cdc37 with Hsp90

inferredcites →https://doi.org/10.1016/j.jmb.2005.11.085openalex-snapshot

The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins

inferredcites →https://doi.org/10.1016/j.jmb.2005.12.008openalex-snapshot

Substrate Transfer from the Chaperone Hsp70 to Hsp90

inferredcites →https://doi.org/10.1016/j.jmb.2008.02.013openalex-snapshot

Structural Studies on the Co-chaperone Hop and Its Complexes with Hsp90

inferredcites →https://doi.org/10.1016/j.molcel.2006.07.016openalex-snapshot

Structure of an Hsp90-Cdc37-Cdk4 Complex

inferredcites →https://doi.org/10.1016/j.molcel.2010.01.006openalex-snapshot

Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1

inferredcites →https://doi.org/10.1016/j.molcel.2011.05.029openalex-snapshot

Global Functional Map of the p23 Molecular Chaperone Reveals an Extensive Cellular Network

inferredcites →https://doi.org/10.1016/j.molonc.2014.08.014openalex-snapshot

The co‐chaperone p23 promotes prostate cancer motility and metastasis

inferredcites →https://doi.org/10.1016/j.tcb.2005.09.003openalex-snapshot

Modulating molecular chaperone Hsp90 functions through reversible acetylation

inferredcites →https://doi.org/10.1016/j.tips.2015.04.005openalex-snapshot

FDA-approved small-molecule kinase inhibitors

inferredcites →https://doi.org/10.1016/j.virol.2008.04.040openalex-snapshot

Hsp90 inhibitors reduce influenza virus replication in cell culture

inferredcites →https://doi.org/10.1016/s0021-9258(18)42471-4openalex-snapshot

Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1.

inferredcites →https://doi.org/10.1016/s0092-8674(00)80830-2openalex-snapshot

Structure of TPR Domain–Peptide Complexes

inferredcites →https://doi.org/10.1016/s0092-8674(00)81588-3openalex-snapshot

Repression of Heat Shock Transcription Factor HSF1 Activation by HSP90 (HSP90 Complex) that Forms a Stress-Sensitive Complex with HSF1

inferredcites →https://doi.org/10.1016/s0092-8674(03)01027-4openalex-snapshot

The Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50cdc37

inferredcites →https://doi.org/10.1016/s0163-7258(98)00013-8openalex-snapshot

The 90-kDa Molecular Chaperone Family

inferredcites →https://doi.org/10.1016/s0378-1119(97)00206-0openalex-snapshot

Isolation of a mouse cDNA encoding mSTI1, a stress-inducible protein containing the TPR motif

inferredcites →https://doi.org/10.1016/s0960-0760(00)00037-6openalex-snapshot

Control of estrogen receptor ligand binding by Hsp90

inferredcites →https://doi.org/10.1016/s1097-2765(02)00785-2openalex-snapshot

Activation of the ATPase Activity of Hsp90 by the Stress-Regulated Cochaperone Aha1

inferredcites →https://doi.org/10.1016/s1097-2765(02)00793-1openalex-snapshot

Aha, Another Regulator for Hsp90 Chaperones

inferredcites →https://doi.org/10.1016/s1097-2765(03)00065-0openalex-snapshot

Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

inferredcites →https://doi.org/10.1021/acs.jnatprod.5b00054openalex-snapshot

Cucurbitacin D Is a Disruptor of the HSP90 Chaperone Machinery

inferredcites →https://doi.org/10.1021/bi051423mopenalex-snapshot

Cdk2: A Genuine Protein Kinase Client of Hsp90 and Cdc37

inferredcites →https://doi.org/10.1021/cb200203mopenalex-snapshot

Macrocycles That Inhibit the Binding between Heat Shock Protein 90 and TPR-Containing Proteins

inferredcites →https://doi.org/10.1021/cb200539uopenalex-snapshot

Celastrol Analogues as Inducers of the Heat Shock Response. Design and Synthesis of Affinity Probes for the Identification of Protein Targets

inferredcites →https://doi.org/10.1021/cb800162xopenalex-snapshot

A Novel Class of Small Molecule Inhibitors of Hsp90

inferredcites →https://doi.org/10.1021/jm8007486openalex-snapshot

Gedunin, a Novel Hsp90 Inhibitor: Semisynthesis of Derivatives and Preliminary Structure−Activity Relationships

inferredcites →https://doi.org/10.1021/ml900003topenalex-snapshot

Mechanistic Studies of Sansalvamide A-Amide: An Allosteric Modulator of Hsp90

inferredcites →https://doi.org/10.1021/mp200346yopenalex-snapshot

A Compound That Inhibits the HOP–Hsp90 Complex Formation and Has Unique Killing Effects in Breast Cancer Cell Lines

inferredcites →https://doi.org/10.1021/pr400321xopenalex-snapshot

The Anticancer Drug AUY922 Generates a Proteomics Fingerprint That Is Highly Conserved among Structurally Diverse Hsp90 Inhibitors

inferredcites →https://doi.org/10.1038/emboj.2011.472openalex-snapshot

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

inferredcites →https://doi.org/10.1038/emboj.2012.37openalex-snapshot

Dynamics of the regulation of Hsp90 by the co‐chaperone Sti1

inferredcites →https://doi.org/10.1038/nature01913openalex-snapshot

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

inferredcites →https://doi.org/10.1038/nature04716openalex-snapshot

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

inferredcites →https://doi.org/10.1038/nchembio.1212openalex-snapshot

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

inferredcites →https://doi.org/10.1038/ncomms1070openalex-snapshot

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

inferredcites →https://doi.org/10.1038/ncomms6484openalex-snapshot

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

inferredcites →https://doi.org/10.1038/nrc1716openalex-snapshot

HSP90 and the chaperoning of cancer

inferredcites →https://doi.org/10.1038/onc.2008.380openalex-snapshot

Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors

inferredcites →https://doi.org/10.1038/onc.2013.127openalex-snapshot

Genome-wide functional screening identifies CDC37 as a crucial HSP90-cofactor for KIT oncogenic expression in gastrointestinal stromal tumors

inferredcites →https://doi.org/10.1038/onc.2013.519openalex-snapshot

Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins

inferredcites →https://doi.org/10.1038/sj.emboj.7600060openalex-snapshot

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

inferredcites →https://doi.org/10.1038/sj.emboj.7600141openalex-snapshot

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

inferredcites →https://doi.org/10.1038/sj.leu.2403764openalex-snapshot

Synergistic activity of imatinib and 17-AAG in imatinib-resistant CML cells overexpressing BCR-ABL – Inhibition of P-glycoprotein function by 17-AAG

inferredcites →https://doi.org/10.1038/sj.onc.1201036openalex-snapshot

Interaction between Cdc37 and Cdk4 in human cells

inferredcites →https://doi.org/10.1038/sj.onc.1203561openalex-snapshot

Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia

inferredcites →https://doi.org/10.1042/bj20041283openalex-snapshot

Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation

inferredcites →https://doi.org/10.1046/j.1432-1033.2003.03610.xopenalex-snapshot

Comparative analysis of the ATP‐binding sites of Hsp90 by nucleotide affinity cleavage: a distinct nucleotide specificity of the C‐terminal ATP‐binding site

inferredcites →https://doi.org/10.1046/j.1432-1033.2003.03866.xopenalex-snapshot

Sensitivity to Hsp90‐targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast

inferredcites →https://doi.org/10.1073/pnas.0407294102openalex-snapshot

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

inferredcites →https://doi.org/10.1073/pnas.0813394106openalex-snapshot

Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease

inferredcites →https://doi.org/10.1073/pnas.1011867108openalex-snapshot

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

inferredcites →https://doi.org/10.1074/jbc.272.3.1876openalex-snapshot

Stress-inducible, Murine Protein mSTI1

inferredcites →https://doi.org/10.1074/jbc.272.38.23843openalex-snapshot

The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

inferredcites →https://doi.org/10.1074/jbc.273.29.18007openalex-snapshot

Specific Binding of Tetratricopeptide Repeat Proteins to the C-terminal 12-kDa Domain of hsp90

inferredcites →https://doi.org/10.1074/jbc.274.25.17525openalex-snapshot

The Importance of ATP Binding and Hydrolysis by Hsp90 in Formation and Function of Protein Heterocomplexes

inferredcites →https://doi.org/10.1074/jbc.275.5.3305openalex-snapshot

The hsp90-related Protein TRAP1 Is a Mitochondrial Protein with Distinct Functional Properties

inferredcites →https://doi.org/10.1074/jbc.m003410200openalex-snapshot

Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone

inferredcites →https://doi.org/10.1074/jbc.m006864200openalex-snapshot

Sensitivity of Mature ErbB2 to Geldanamycin Is Conferred by Its Kinase Domain and Is Mediated by the Chaperone Protein Hsp90

inferredcites →https://doi.org/10.1074/jbc.m109.051532openalex-snapshot

Characterization of Celastrol to Inhibit Hsp90 and Cdc37 Interaction

inferredcites →https://doi.org/10.1074/jbc.m109.081018openalex-snapshot

Celastrol Inhibits Hsp90 Chaperoning of Steroid Receptors by Inducing Fibrillization of the Co-chaperone p23

inferredcites →https://doi.org/10.1074/jbc.m109002200openalex-snapshot

Ligand Discrimination by TPR Domains

inferredcites →https://doi.org/10.1074/jbc.m112.427328openalex-snapshot

Gedunin Inactivates the Co-chaperone p23 Protein Causing Cancer Cell Death by Apoptosis

inferredcites →https://doi.org/10.1074/jbc.m112.439257openalex-snapshot

Cdc37 (Cell Division Cycle 37) Restricts Hsp90 (Heat Shock Protein 90) Motility by Interaction with N-terminal and Middle Domain Binding Sites

inferredcites →https://doi.org/10.1074/jbc.m114.553255openalex-snapshot

ATPase Activity and ATP-dependent Conformational Change in the Co-chaperone HSP70/HSP90-organizing Protein (HOP)

inferredcites →https://doi.org/10.1074/jbc.m201287200openalex-snapshot

Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50

inferredcites →https://doi.org/10.1074/jbc.m206322200openalex-snapshot

Akt Forms an Intracellular Complex with Heat Shock Protein 90 (Hsp90) and Cdc37 and Is Destabilized by Inhibitors of Hsp90 Function

inferredcites →https://doi.org/10.1074/jbc.m206867200openalex-snapshot

Tetratricopeptide Repeat Motif-mediated Hsc70-mSTI1 Interaction

inferredcites →https://doi.org/10.1074/jbc.m212761200openalex-snapshot

Aha1 Binds to the Middle Domain of Hsp90, Contributes to Client Protein Activation, and Stimulates the ATPase Activity of the Molecular Chaperone

inferredcites →https://doi.org/10.1074/jbc.m305960200openalex-snapshot

Genetic Dissection of p23, an Hsp90 Cochaperone, Reveals a Distinct Surface Involved in Estrogen Receptor Signaling

inferredcites →https://doi.org/10.1074/jbc.m308242200openalex-snapshot

Identification of a Conserved Sequence Motif That Promotes Cdc37 and Cyclin D1 Binding to Cdk4

inferredcites →https://doi.org/10.1074/jbc.m309814200openalex-snapshot

The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex

inferredcites →https://doi.org/10.1074/jbc.m311377200openalex-snapshot

Hsp90/p50cdc37 Is Required for Mixed-lineage Kinase (MLK) 3 Signaling

inferredcites →https://doi.org/10.1074/jbc.m410562200openalex-snapshot

Co-chaperone Regulation of Conformational Switching in the Hsp90 ATPase Cycle

inferredcites →https://doi.org/10.1074/jbc.m601759200openalex-snapshot

Localization of Sites of Interaction between p23 and Hsp90 in Solution

inferredcites →https://doi.org/10.1074/jbc.m808436200openalex-snapshot

The Chaperones Hsp90 and Cdc37 Mediate the Maturation and Stabilization of Protein Kinase C through a Conserved PXXP Motif in the C-terminal Tail*

inferredcites →https://doi.org/10.1074/mcp.m600449-mcp200openalex-snapshot

Proteome Analysis of Hepatocellular Carcinoma by Two-dimensional Difference Gel Electrophoresis

inferredcites →https://doi.org/10.1083/jcb.143.4.901openalex-snapshot

In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis

inferredcites →https://doi.org/10.1083/jcb.200210121openalex-snapshot

The Cdc37 protein kinase–binding domain is sufficient for protein kinase activity and cell viability

inferredcites →https://doi.org/10.1083/jcb.200604106openalex-snapshot

Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation

inferredcites →https://doi.org/10.1091/mbc.7.9.1405openalex-snapshot

CDC37 is required for p60v-src activity in yeast.

inferredcites →https://doi.org/10.1091/mbc.e03-07-0480openalex-snapshot

Sti1 and Cdc37 Can Stabilize Hsp90 in Chaperone Complexes with a Protein Kinase

inferredcites →https://doi.org/10.1091/mbc.e07-05-0467openalex-snapshot

Src-mediated Phosphorylation of Hsp90 in Response to Vascular Endothelial Growth Factor (VEGF) Is Required for VEGF Receptor-2 Signaling to Endothelial NO Synthase

inferredcites →https://doi.org/10.1093/emboj/17.16.4829openalex-snapshot

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

inferredcites →https://doi.org/10.1093/emboj/18.3.754openalex-snapshot

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

inferredcites →https://doi.org/10.1093/emboj/19.16.4383openalex-snapshot

The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N‐terminal domains

inferredcites →https://doi.org/10.1093/emboj/19.21.5930openalex-snapshot

Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co‐chaperone p23

inferredcites →https://doi.org/10.1093/jnci/92.3.242openalex-snapshot

Novobiocin and Related Coumarins and Depletion of Heat Shock Protein 90-Dependent Signaling Proteins

inferredcites →https://doi.org/10.1096/fj.13-232280openalex-snapshot

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

inferredcites →https://doi.org/10.1101/gad.10.12.1491openalex-snapshot

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4.

inferredcites →https://doi.org/10.1101/gad.11.14.1775openalex-snapshot

Cdc37 is a molecular chaperone with specific functions in signal transduction.

inferredcites →https://doi.org/10.1101/gad.14.4.422openalex-snapshot

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

inferredcites →https://doi.org/10.1101/gad.1505307openalex-snapshot

Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance

inferredcites →https://doi.org/10.1101/sqb.1994.059.01.067openalex-snapshot

Genetic Approaches to Defining Signaling by the CML-associated Tyrosine Kinase BCR-ABL

inferredcites →https://doi.org/10.1111/igc.0b013e3181a83135openalex-snapshot

Gedunin, a Novel Natural Substance, Inhibits Ovarian Cancer Cell Proliferation

inferredcites →https://doi.org/10.1111/liv.12651openalex-snapshot

Suppressing the CDC 37 cochaperone in hepatocellular carcinoma cells inhibits cell cycle progression and cell growth

inferredcites →https://doi.org/10.1126/science.1073051openalex-snapshot

Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones

inferredcites →https://doi.org/10.1128/mcb.00009-06openalex-snapshot

The Cochaperone p23 Differentially Regulates Estrogen Receptor Target Genes and Promotes Tumor Cell Adhesion and Invasion

inferredcites →https://doi.org/10.1128/mcb.00734-06openalex-snapshot

The Hsp90 Cochaperone p23 Is Essential for Perinatal Survival

inferredcites →https://doi.org/10.1128/mcb.02246-07openalex-snapshot

p23/Sba1p Protects against Hsp90 Inhibitors Independently of Its Intrinsic Chaperone Activity

inferredcites →https://doi.org/10.1128/mcb.17.1.318openalex-snapshot

In Vivo Analysis of the Hsp90 Cochaperone Sti1 (p60)

inferredcites →https://doi.org/10.1128/mcb.18.6.3330openalex-snapshot

Genetic and Biochemical Analysis of p23 and Ansamycin Antibiotics in the Function of Hsp90-Dependent Signaling Proteins

inferredcites →https://doi.org/10.1128/mcb.19.3.1661openalex-snapshot

p50cdc37 Acting in Concert with Hsp90 Is Required for Raf-1 Function

inferredcites →https://doi.org/10.1128/mcb.19.5.3748openalex-snapshot

Role for Hsp90-Associated Cochaperone p23 in Estrogen Receptor Signal Transduction

inferredcites →https://doi.org/10.1128/mcb.20.12.4462-4473.2000openalex-snapshot

The Oncoprotein Kinase Chaperone CDC37 Functions as an Oncogene in Mice and Collaborates with Both c- myc and Cyclin D1 in Transformation of Multiple Tissues

inferredcites →https://doi.org/10.1128/mcb.20.3.749-754.2000openalex-snapshot

Cdc37 Promotes the Stability of Protein Kinases Cdc28 and Cak1

inferredcites →https://doi.org/10.1128/mcb.23.15.5132-5142.2003openalex-snapshot

Identification of Cdc37 as a Novel Regulator of the Stress-Responsive Mitogen-Activated Protein Kinase

inferredcites →https://doi.org/10.1128/mcb.26.9.3378-3389.2006openalex-snapshot

Cdc37 Interacts with the Glycine-Rich Loop of Hsp90 Client Kinases

inferredcites →https://doi.org/10.1128/mcb.9.9.3638openalex-snapshot

Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae.

inferredcites →https://doi.org/10.1158/0008-5472.can-07-3162openalex-snapshot

Targeting Cdc37 Inhibits Multiple Signaling Pathways and Induces Growth Arrest in Prostate Cancer Cells

inferredcites →https://doi.org/10.1158/0008-5472.can-07-3268openalex-snapshot

Silencing of HSP90 Cochaperone AHA1 Expression Decreases Client Protein Activation and Increases Cellular Sensitivity to the HSP90 Inhibitor 17-Allylamino-17-Demethoxygeldanamycin

inferredcites →https://doi.org/10.1158/0008-5472.can-08-0644openalex-snapshot

Role of Acetylation and Extracellular Location of Heat Shock Protein 90α in Tumor Cell Invasion

inferredcites →https://doi.org/10.1158/0008-5472.can-10-1590openalex-snapshot

High Levels of Hsp90 Cochaperone p23 Promote Tumor Progression and Poor Prognosis in Breast Cancer by Increasing Lymph Node Metastases and Drug Resistance

inferredcites →https://doi.org/10.1158/1078-0432.ccr-09-0152openalex-snapshot

CUDC-305, a Novel Synthetic HSP90 Inhibitor with Unique Pharmacologic Properties for Cancer Therapy

inferredcites →https://doi.org/10.1158/1535-7163.mct-07-0484openalex-snapshot

A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells

inferredcites →https://doi.org/10.1182/blood-2008-03-143644openalex-snapshot

HDAC6 inhibition enhances 17-AAG–mediated abrogation of hsp90 chaperone function in human leukemia cells

inferredcites →https://doi.org/10.1186/1471-2202-9-s2-s7openalex-snapshot

Heat shock protein 90: translation from cancer to Alzheimer's disease treatment?

inferredcites →https://doi.org/10.1186/1476-4598-11-59openalex-snapshot

Molecular mechanism of cytotoxicity induced by Hsp90-targeted Antp-TPR hybrid peptide in glioblastoma cells

inferredcites →https://doi.org/10.1186/1477-5956-7-3openalex-snapshot

Identification of pancreatic cancer invasion-related proteins by proteomic analysis

inferredcites →https://doi.org/10.1186/1479-5876-9-8openalex-snapshot

Designed hybrid TPR peptide targeting Hsp90 as a novel anticancer agent

inferredcites →https://doi.org/10.1186/bcr1996openalex-snapshot

NVP-AUY922: a small molecule HSP90 inhibitor with potent antitumor activity in preclinical breast cancer models

inferredcites →https://doi.org/10.1210/me.2012-1056openalex-snapshot

Role of the HSP90-Associated Cochaperone p23 in Enhancing Activity of the Androgen Receptor and Significance for Prostate Cancer

inferredcites →https://doi.org/10.1210/me.9.6.670openalex-snapshot

Binding of p23 and hsp90 during assembly with the progesterone receptor

inferredcites →https://doi.org/10.1371/journal.pone.0036389openalex-snapshot

Regulation of Vascular Endothelial Cell Polarization and Migration by Hsp70/Hsp90-Organizing Protein

inferredcites →https://doi.org/10.1371/journal.pone.0049322openalex-snapshot

The Co-Chaperone Hch1 Regulates Hsp90 Function Differently than Its Homologue Aha1 and Confers Sensitivity to Yeast to the Hsp90 Inhibitor NVP-AUY922

inferredcites →https://doi.org/10.1371/journal.pone.0068394openalex-snapshot

Analysis of Conformational Determinants Underlying HSP90-Kinase Interaction

inferredcites →https://doi.org/10.1379/1466-1268(2003)008<0114:cgbhak>2.0.co;2openalex-snapshot

Cdc37 goes beyond Hsp90 and kinases

inferredcites →https://doi.org/10.1515/bc.2002.152openalex-snapshot

The Hsp90 Co-Chaperones Cdc37 and Sti1 Interact Physically and Genetically

inferredcites →https://doi.org/10.1634/theoncologist.6-3-233openalex-snapshot

STI571: Targeting BCR-ABL as Therapy for CML

inferredcites →https://doi.org/10.2119/molmed.2013.00166openalex-snapshot

Correlation between PDZK1, Cdc37, Akt and Breast Cancer Malignancy: The Role of PDZK1 in Cell Growth through Akt Stabilization by Increasing and Interacting with Cdc37

inferredcites →https://doi.org/10.2174/1567205053585927openalex-snapshot

Development of a High Throughput Drug Screening Assay for the Detection of Changes in Tau Levels - Proof of Concept with HSP90 inhibitors

inferredcites →https://doi.org/10.2174/1568009033481787openalex-snapshot

The Stress Response: Implications for the Clinical Development of Hsp90 Inhibitors

inferredcites →https://doi.org/10.3892/ijo.25.3.579openalex-snapshot

Cyclin D1 overexpression is not a specific grouping marker, but may collaborate with CDC37 in myeloma cells

inferredcites →https://doi.org/10.4049/jimmunol.177.3.1772openalex-snapshot

A Protein Associated with Toll-Like Receptor 4 (PRAT4A) Regulates Cell Surface Expression of TLR4

inferredcites →https://doi.org/10.4161/cc.8.3.7531openalex-snapshot

Targeting CDC37: An alternative, kinase-directed strategy for disruption of oncogenic chaperoning

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Cellular Protein TTC4 and its Cofactor HSP90 are Pro-Viral for Bovine Herpesvirus 1

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Native Mass Spectrometry‐Guided Screening Identifies Hit Fragments for HOP‐HSP90 PPI Inhibition**

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Bimolecular Fluorescence Complementation Assay to Evaluate HSP90-Client Protein Interactions in Cells

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General Structural and Functional Features of Molecular Chaperones

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Hsp70/Hsp90 Organising Protein (Hop): Coordinating Much More than Chaperones

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Identification of nucleotide binding sites and repurposing of potential FDA-approved inhibitors against human HOP

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AHA1 regulates cell migration and invasion via the EMT pathway in colorectal adenocarcinomas

inferred← citeshttps://doi.org/10.1039/d1cc04257bopenalex-snapshot

A native mass spectrometry platform identifies HOP inhibitors that modulate the HSP90–HOP protein–protein interaction

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A native mass spectrometry approach to qualitatively elucidate interfacial epitopes of transient protein–protein interactions

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Disrupting the Hsp90–Cdc37 axis: a selective strategy for targeting oncogenic kinases in cancer

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Ganetespib for small cell lung cancer

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Hsp70-Hsp90 organising protein (HOP/STIP1) is required for KSHV lytic replication

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Targeting extracellular Hsp90: A unique frontier against cancer

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