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Person
ISNI: 
0000 0001 2450 3145
Name: 
Hubbard, R. E.
Hubbard, Roderick E.
Creation class: 
article
Text
txt
Creation role: 
author
Related names: 
University of York
Titles: 
4,5-diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer.
Adenine derived inhibitors of the molecular chaperone HSP90-SAR explained through multiple X-ray structures.
Combining hit identification strategies: fragment-based and in silico approaches to orally active 2-aminothieno[2,3-d]pyrimidine inhibitors of the Hsp90 molecular chaperone.
Delineation of a unique protein-protein interaction site on the surface of the estrogen receptor.
Design and characterization of libraries of molecular fragments for use in NMR screening against protein targets.
Discovery of a potent CDK2 inhibitor with a novel binding mode, using virtual screening and initial, structure-guided lead scoping
Experimental and computational mapping of the binding surface of a crystalline protein.
Fluorescence studies of membrane
Fragment approaches in structure-based drug discovery.
Informatics and modeling challenges in fragment-based drug discovery.
Inhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues
Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha.
Making decisions for structural genomics
Novel, potent small-molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design.
NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis.
Recent progress in fragment-based lead discovery
SeeDs approach: integrating fragments into drug discovery., The
sgTarget: a target selection resource for structural genomics.
Structural aspects of agonism and antagonism in the oestrogen receptor
Structural insights into the mechanisms of agonism and antagonism in oestrogen receptor isoforms.
Structural insights into the mode of action of a pure antiestrogen.
Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms.
Structure and mechanism of the oestrogen receptor.
Structure-based discovery of a new class of Hsp90 inhibitors.
Structure of a Cys25-->Ser mutant of human cathepsin S.
Understanding the Mechanism of Ice Binding by Type III Antifreeze Proteins
Contributed to or performed: 
BIOCHEMICAL SOCIETY TRANSACTIONS
Notes: 
Sources: 
JNAM
ZETO