Sanket J Mishra
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Explore the profile of Sanket J Mishra including associated specialties, affiliations and a list of published articles.
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7
Citations
162
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Recent Articles
1.
Reynolds T, Mishra S, Blagg B
Sci Rep
. 2025 Jan;
15(1):3692.
PMID: 39880847
The heat shock protein 90 (Hsp90) family of molecular chaperones mediates the folding and activation of ~ 400 client proteins, many of which contribute to oncogenesis. As a result, Hsp90...
2.
Mishra S, Reynolds T, Merfeld T, Balch M, Peng S, Deng J, et al.
ACS Med Chem Lett
. 2022 Dec;
13(12):1870-1878.
PMID: 36518703
The heat shock protein 90 (Hsp90) family of molecular chaperones mediates the folding and activation of client proteins associated with all 10 hallmarks of cancer. Herein, the design, synthesis, and...
3.
Rahmy S, Mishra S, Murphy S, Blagg B, Lu X
Front Immunol
. 2022 Nov;
13:1005045.
PMID: 36341371
Response resistance to the immune checkpoint blockade (ICB) immunotherapy remains a major clinical challenge that may be overcome through the rational combination of ICB and specific targeted therapeutics. One emerging...
4.
Mishra S, Khandelwal A, Banerjee M, Balch M, Peng S, Davis R, et al.
Angew Chem Int Ed Engl
. 2021 Feb;
60(19):10547-10551.
PMID: 33621416
The 90 kDa heat shock protein (Hsp90) is a molecular chaperone that processes nascent polypeptides into their biologically active conformations. Many of these proteins contribute to the progression of cancer,...
5.
Mishra S, Liu W, Beebe K, Banerjee M, Kent C, Munthali V, et al.
J Med Chem
. 2021 Jan;
64(3):1545-1557.
PMID: 33428418
The 90 kD heat shock proteins (Hsp90) are molecular chaperones that are responsible for the folding of select proteins, many of which are directly associated with cancer progression. Consequently, inhibition...
6.
Khandelwal A, Kent C, Balch M, Peng S, Mishra S, Deng J, et al.
Nat Commun
. 2018 Feb;
9(1):425.
PMID: 29382832
The 90 kDa heat shock protein (Hsp90) is a molecular chaperone responsible for folding proteins that are directly associated with cancer progression. Consequently, inhibition of the Hsp90 protein folding machinery...
7.
Stothert A, Suntharalingam A, Tang X, Crowley V, Mishra S, Webster J, et al.
Sci Rep
. 2017 Dec;
7(1):17951.
PMID: 29263415
The heat shock protein 90 (Hsp90) family of molecular chaperones regulates protein homeostasis, folding, and degradation. The ER-resident Hsp90 isoform, glucose-regulated protein 94 (Grp94), promotes the aggregation of mutant forms...
8.
Mishra S, Ghosh S, Stothert A, Dickey C, Blagg B
ACS Chem Biol
. 2016 Dec;
12(1):244-253.
PMID: 27959508
Glucose regulated protein 94 kDa, Grp94, is the endoplasmic reticulum (ER) localized isoform of heat shock protein 90 (Hsp90) that is responsible for the trafficking and maturation of toll-like receptors,...