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Journal of Medicinal Chemistry|August 4, 2006
Structural and quantum chemical studies of 8-aryl-sulfanyl adenine class Hsp90 inhibitorsRobert M Immormino, Yanlong Kang, Gabriela Chiosis, et al.
The Journal of Biological Chemistry|September 13, 2003
Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulationKaren L Soldano, Arif Jivan, Christopher V Nicchitta, et al.
The Journal of Biological Chemistry|May 15, 2013
α7 helix region of αI domain is crucial for integrin binding to endoplasmic reticulum chaperone gp96: a potential therapeutic target for cancer metastasisFeng Hong, Bei Liu, Gabriela Chiosis, et al.
Molecular Cell|October 16, 2007
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperonesD Eric Dollins, Joshua J Warren, Robert M Immormino, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 13, 2006
Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptideAllison H Williams, Robert M Immormino, Daniel T Gewirth, et al.
Cell Reports|September 21, 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 SiteJohn D Huck, Nanette L Que, Feng Hong, et al.
Biorxiv : the Preprint Server for Biology|August 14, 2023
Selective inhibition of hsp90 paralogs: Uncovering the role of helix 1 in Grp94-selective ligand bindingNanette L S Que, Paul M Seidler, Wen J Aw, et al.
Proteins|October 30, 2024
Selective Inhibition of hsp90 Paralogs: Uncovering the Role of Helix 1 in Grp94-Selective Ligand BindingNanette L S Que, Paul M Seidler, Wen J Aw, et al.
Journal of Molecular Biology|September 7, 2014
Characterization of the Grp94/OS-9 chaperone-lectin complexPaul M Seidler, Stephen A Shinsky, Feng Hong, et al.
Proteins|May 30, 2019
Structures of Hsp90α and Hsp90β bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivityJohn D Huck, Nanette L S Que, Sahil Sharma, et al.
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