D. E. Dollins

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.

R. Immormino, D. E. Dollins, J. J. Warren, 2007, Molecular cell.

Characterization of a Selective Inhibitor of Inositol Hexakisphosphate Kinases

J. York, Peter C. Fridy, C. Downes, 2009, Journal of Biological Chemistry.

Cloning and Characterization of Two Human VIP1-like Inositol Hexakisphosphate and Diphosphoinositol Pentakisphosphate Kinases*

J. Otto, J. York, Peter C. Fridy, 2007, Journal of Biological Chemistry.

Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design.

R. Immormino, B. Blagg, D. E. Dollins, 2009, Journal of molecular biology.

Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone*

R. Immormino, D. E. Dollins, D. Gewirth, 2004, Journal of Biological Chemistry.

Structural basis of androgen receptor binding to selective androgen response elements.

F. Claessens, D. E. Dollins, D. Gewirth, 2004, Proceedings of the National Academy of Sciences of the United States of America.

A Conserved Family of Enzymes That Phosphorylate Inositol Hexakisphosphate

J. Otto, J. York, T. Haystead, 2007, Science.

Structure of Unliganded GRP94, the Endoplasmic Reticulum Hsp90

R. Immormino, D. E. Dollins, D. Gewirth, 2005, Journal of Biological Chemistry.

Vip1 is a kinase and pyrophosphatase switch that regulates inositol diphosphate signaling

J. Otto, J. York, D. E. Dollins, 2020, Proceedings of the National Academy of Sciences.

A structural basis for lithium and substrate binding of an inositide phosphatase

J. Ponder, J. York, J. Xiong, 2020, The Journal of biological chemistry.