N. Que

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

B. Blagg, D. Gewirth, Vincent M Crowley, 2018, Journal of medicinal chemistry.

NECA derivatives exploit the paralog-specific properties of the Site 3 side pocket of Grp94, the ER Hsp90

G. Chiosis, R. Immormino, D. Gewirth, 2019 .

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

M. Gleave, Rendong Yang, P. Rennie, 2017, Molecular Cancer Therapeutics.

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

Pallav D. Patel, Weilin Sun, Tony Taldone, 2013, Nature chemical biology.

Paralog-selective Hsp 90 inhibitors define tumor-specific regulation of Her 2

Pallav D. Patel, Weilin Sun, Tony Taldone, 2014 .

Selective inhibition of hsp90 paralogs: Structure and binding studies uncover the role of helix 1 in Grp94-selective ligand binding

G. Chiosis, D. Gewirth, P. Seidler, 2023, bioRxiv.

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

Pallav D. Patel, Weilin Sun, Tony Taldone, 2013, Nature chemical biology.