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Daniel T. Gewirth

Affiliations: 
Duke University, Durham, NC 
Area:
Biochemistry
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"Daniel Gewirth"
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Children

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Paul L. Shaffer grad student 2005 Duke
Dwayne E. Dollins grad student 2007 Duke
Robert M. Immormino grad student 2007 Duke

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Publications

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Amankwah YS, Fleifil Y, Unruh E, et al. (2024) Structural transitions modulate the chaperone activities of Grp94. Proceedings of the National Academy of Sciences of the United States of America. 121: e2309326121
Que NLS, Seidler PM, Aw WJ, et al. (2023) Selective inhibition of hsp90 paralogs: Structure and binding studies uncover the role of helix 1 in Grp94-selective ligand binding. Biorxiv : the Preprint Server For Biology
Yan P, Patel HJ, Sharma S, et al. (2020) Molecular Stressors Engender Protein Connectivity Dysfunction through Aberrant N-Glycosylation of a Chaperone. Cell Reports. 31: 107840
Huck JD, Que NLS, Immormino RM, et al. (2019) NECA derivatives exploit the paralog-specific properties of the Site 3 side pocket of Grp94, the ER Hsp90. The Journal of Biological Chemistry
Huck JD, Que NLS, Sharma S, et al. (2019) Structures of Hsp90α and Hsp90β bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity. Proteins
Huck JD, Que NLS, Sharma S, et al. (2019) Structures of Hsp90 alpha and Hsp90 beta bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity. Proteins. 87: 869-877
Wang T, Rodina A, Dunphy MP, et al. (2018) Chaperome heterogeneity and its implications for cancer study and treatment. The Journal of Biological Chemistry
Que NLS, Crowley VM, Duerfeldt AS, et al. (2018) Structure based design of a Grp94-selective inhibitor: Exploiting a key residue in Grp94 to optimize paralog-selective binding. Journal of Medicinal Chemistry
Huck JD, Que NL, Hong F, et al. (2017) 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. 20: 2800-2809
Dalal K, Che M, Que NS, et al. (2017) Bypassing drug-resistance mechanisms of prostate cancer with small-molecules that target androgen receptor chromatin interactions. Molecular Cancer Therapeutics
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