Beyond Traditional Structure-Based Drug Design: The Role of Iron Complexation, Strain, and Water in the Binding of Inhibitors for Hypoxia-Inducible Factor Prolyl Hydroxylase 2 | Zendy

Scott D. Bembenek | Zendy; Hariharan Venkatesan | Zendy; Hillary M. Peltier | Zendy; Mark D. Rosen | Zendy; Terrance D. Barrett | Zendy; Kimon C. Kanelakis | Zendy; Heather L. Palomino | Zendy; Theresa I. Brondstetter | Zendy; Taraneh Mirzadegan | Zendy; Michael H. Rabinowitz | Zendy

Open Access

Beyond Traditional Structure-Based Drug Design: The Role of Iron Complexation, Strain, and Water in the Binding of Inhibitors for Hypoxia-Inducible Factor Prolyl Hydroxylase 2

Author(s) -

Scott D. Bembenek,

Hariharan Venkatesan,

Hillary M. Peltier,

Mark D. Rosen,

Terrance D. Barrett,

Kimon C. Kanelakis,

Heather L. Palomino,

Theresa I. Brondstetter,

Taraneh Mirzadegan,

Michael H. Rabinowitz

Publication year - 2019

Publication title -

acs omega

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.779

H-Index - 40

ISSN - 2470-1343

DOI - 10.1021/acsomega.9b00199

Subject(s) - benzimidazole , docking (animal) , stereochemistry , chemistry , pyrazole , ligand (biochemistry) , active site , combinatorial chemistry , rational design , bioisostere , binding site , drug discovery , enzyme , biochemistry , chemical synthesis , biology , in vitro , receptor , medicine , organic chemistry , genetics , nursing

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