D.E. Dollins

Duke University — United States

Biochemistry, Genetics and Molecular Biology · Life Sciences

11h-index1.6kcitations25works0.02yr avg
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Research Topics

Endoplasmic Reticulum Stress and Disease(8), Heat shock proteins research(6), Phytase and its Applications(6), Protein Kinase Regulation and GTPase Signaling(4), Cellular transport and secretion(4)

Publications25 total

A structural basis for lithium and substrate binding of an inositide phosphatase
Journal of Biological Chemistry·2020· 14 citedOpen Access
Crystal structure of inositol polyphosphate 1-phosphatase (INPP1) D54A mutant
2020
Crystal structure of inositol polyphosphate 1-phosphatase (INPP1) D54A mutant in complex with inositol (1,4)-bisphosphate
2020
CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE INPP1 IN COMPLEX GADOLINIUM AFTER ADDITION OF INOSITOL 1,3,4-TRISPHOSPHATE AT 2.5 ANGSTROM RESOLUTION
2020
CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE INPP1 IN COMPLEX GADOLINIUM BUT NO LITHIUM AT 3 ANGSTROM RESOLUTION
2020
Vip1 is a kinase and pyrophosphatase switch that regulates inositol diphosphate signaling
Proceedings of the National Academy of Sciences·2020· 71 citedOpen Access
SMOC can act as both an antagonist and an expander of BMP signaling
eLife·2017· 36 citedOpen Access
Author response: SMOC can act as both an antagonist and an expander of BMP signaling
2017Open Access
The NatA Acetyltransferase Complex Bound To ppGpp
2012
Different Poses for Ligand and Chaperone in Inhibitor-Bound Hsp90 and GRP94: Implications for Paralog-Specific Drug Design
Journal of Molecular Biology·2009· 66 citedOpen Access
Characterization of a Selective Inhibitor of Inositol Hexakisphosphate Kinases
Journal of Biological Chemistry·2009· 119 citedOpen Access
Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones
Molecular Cell·2007· 283 citedOpen Access
Cloning and Characterization of Two Human VIP1-like Inositol Hexakisphosphate and Diphosphoinositol Pentakisphosphate Kinases
Journal of Biological Chemistry·2007· 133 citedOpen Access
A Conserved Family of Enzymes That Phosphorylate Inositol Hexakisphosphate
Science·2007· 284 cited
Structure of full length GRP94 with AMP-PNP bound
2006
Structure of Middle plus C-terminal domains (M+C) of GRP94
2006
Structure of N-terminal plus middle domains (N+M) of GRP94
2006
Structure of Unliganded GRP94, the Endoplasmic Reticulum Hsp90
Journal of Biological Chemistry·2005· 75 citedOpen Access
Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL
2005
Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH NECA
2005
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Frequent Co-authors

D.T. Gewirth(13), Robert M. Immormino(12), John D. York(9), P.L. Shaffer(5), Peter C. Fridy(4), Stuart Endo-Streeter(4), James Otto(3), Karen Soldano(3), Jeffrey J. Warren(3), Yuanlin Ren(3), Arif Jivan(2), Frank Claessens(2), Wenli Bai(2), Julie Neubauer(2), J. Terrig Thomas(2), Kristin Andrykovich(2), Tehyen Chu(2), Brian G. Stultz(2), Deborah A. Hursh(2), Malcolm Moos(2)