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Paralog Specific Hsp90 Inhibitors - A Brief History and a Bright Future

Current topics in medicinal chemistry, 2016-10, Vol.16 (25), p.2779-2791

Gewirth, Daniel T

2016

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Clients and Oncogenic Roles of Molecular Chaperone gp96/grp94

Current topics in medicinal chemistry, 2016-10, Vol.16 (25), p.2765-2778

2016

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Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2

Nature chemical biology, 2013-11, Vol.9 (11), p.677-684

2013

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Chaperome heterogeneity and its implications for cancer study and treatment

The Journal of biological chemistry, 2019-02, Vol.294 (6), p.2162-2179

2019

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Thrombin contributes to cancer immune evasion via proteolysis of platelet-bound GARP to activate LTGF-β

Science translational medicine, 2020-01, Vol.12 (525)

2020

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Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site

Cell reports (Cambridge), 2017-09, Vol.20 (12), p.2800-2809

2017

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Structure Based Design of a Grp94-Selective Inhibitor: Exploiting a Key Residue in Grp94 To Optimize Paralog-Selective Binding

Journal of medicinal chemistry, 2018-04, Vol.61 (7), p.2793-2805

2018

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Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones

Molecular cell, 2007-10, Vol.28 (1), p.41-56

2007

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Structural transitions modulate the chaperone activities of Grp94

Proceedings of the National Academy of Sciences - PNAS, 2024-03, Vol.121 (12), p.e2309326121

2024

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Molecular Stressors Engender Protein Connectivity Dysfunction through Aberrant N-Glycosylation of a Chaperone

Cell reports (Cambridge), 2020-06, Vol.31 (13), p.107840-107840, Article 107840

2020

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Structural Basis of Androgen Receptor Binding to Selective Androgen Response Elements

Proceedings of the National Academy of Sciences - PNAS, 2004-04, Vol.101 (14), p.4758-4763

2004

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NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90

The Journal of biological chemistry, 2019-11, Vol.294 (44), p.16010-16019

2019

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Exploring the Functional Complementation between Grp94 and Hsp90

PloS one, 2016-11, Vol.11 (11), p.e0166271-e0166271

2016

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α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasis

The Journal of biological chemistry, 2013-06, Vol.288 (25), p.18243-18248

2013

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Structures of Hsp90α and Hsp90β bound to a purine‐scaffold inhibitor reveal an exploitable residue for drug selectivity

Proteins, structure, function, and bioinformatics, 2019-10, Vol.87 (10), p.869-877

2019

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Structure–Activity Relationship in a Purine-Scaffold Compound Series with Selectivity for the Endoplasmic Reticulum Hsp90 Paralog Grp94

Journal of medicinal chemistry, 2015-05, Vol.58 (9), p.3922-3943

2015

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Potential impact of combined inhibition of 3α-oxidoreductases and 5α-reductases on prostate cancer

Asian Journal of Urology, 2019-01, Vol.6 (1), p.50-56

2019

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Structural and Quantum Chemical Studies of 8-Aryl-sulfanyl Adenine Class Hsp90 Inhibitors

Journal of medicinal chemistry, 2006-08, Vol.49 (16), p.4953-4960

2006

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Identification of Potent Water Soluble Purine-Scaffold Inhibitors of the Heat Shock Protein 90

Journal of medicinal chemistry, 2006-01, Vol.49 (1), p.381-390

2006

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Experimental and Structural Testing Module to Analyze Paralogue-Specificity and Affinity in the Hsp90 Inhibitors Series

Journal of medicinal chemistry, 2013-09, Vol.56 (17), p.6803-6818

2013

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Selective targeting of GARP-LTGFβ axis in the tumor microenvironment augments PD-1 blockade via enhancing CD8+ T cell antitumor immunity

Journal for immunotherapy of cancer, 2022-09, Vol.10 (9), p.e005433

2022

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The Role of Antibody Polyspecificity and Lipid Reactivity in Binding of Broadly Neutralizing Anti-HIV-1 Envelope Human Monoclonal Antibodies 2F5 and 4E10 to Glycoprotein 41 Membrane Proximal Envelope Epitopes

Journal of Immunology, 2007-04, Vol.178 (7), p.4424-4435

2007

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Characterization of the Grp94/OS-9 Chaperone–Lectin Complex

Journal of molecular biology, 2014-10, Vol.426 (21), p.3590-3605

2014

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Second international symposium on the chaperone code, 2023

Cell stress & chaperones, 2024-02, Vol.29 (1), p.88-96

2024

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Bypassing Drug Resistance Mechanisms of Prostate Cancer with Small Molecules that Target Androgen Receptor-Chromatin Interactions

Molecular cancer therapeutics, 2017-10, Vol.16 (10), p.2281-2291

2017

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Paralog Specific Hsp90 Inhibitors - A Brief History and a Bright Future

Clients and Oncogenic Roles of Molecular Chaperone gp96/grp94

Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2

Chaperome heterogeneity and its implications for cancer study and treatment

Thrombin contributes to cancer immune evasion via proteolysis of platelet-bound GARP to activate LTGF-β

Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site

Structure Based Design of a Grp94-Selective Inhibitor: Exploiting a Key Residue in Grp94 To Optimize Paralog-Selective Binding

Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones

Structural transitions modulate the chaperone activities of Grp94

Molecular Stressors Engender Protein Connectivity Dysfunction through Aberrant N-Glycosylation of a Chaperone

Structural Basis of Androgen Receptor Binding to Selective Androgen Response Elements

NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90

Exploring the Functional Complementation between Grp94 and Hsp90

α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasis

Structures of Hsp90α and Hsp90β bound to a purine‐scaffold inhibitor reveal an exploitable residue for drug selectivity

Structure–Activity Relationship in a Purine-Scaffold Compound Series with Selectivity for the Endoplasmic Reticulum Hsp90 Paralog Grp94

Potential impact of combined inhibition of 3α-oxidoreductases and 5α-reductases on prostate cancer

Structural and Quantum Chemical Studies of 8-Aryl-sulfanyl Adenine Class Hsp90 Inhibitors

Identification of Potent Water Soluble Purine-Scaffold Inhibitors of the Heat Shock Protein 90

Experimental and Structural Testing Module to Analyze Paralogue-Specificity and Affinity in the Hsp90 Inhibitors Series

Selective targeting of GARP-LTGFβ axis in the tumor microenvironment augments PD-1 blockade via enhancing CD8+ T cell antitumor immunity

The Role of Antibody Polyspecificity and Lipid Reactivity in Binding of Broadly Neutralizing Anti-HIV-1 Envelope Human Monoclonal Antibodies 2F5 and 4E10 to Glycoprotein 41 Membrane Proximal Envelope Epitopes

Characterization of the Grp94/OS-9 Chaperone–Lectin Complex

Second international symposium on the chaperone code, 2023

Bypassing Drug Resistance Mechanisms of Prostate Cancer with Small Molecules that Target Androgen Receptor-Chromatin Interactions

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