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

Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: American Chemical Society 2019-04-01
Series:ACS Omega
Online Access:http://dx.doi.org/10.1021/acsomega.9b00199
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spelling doaj-2f7bcabc827d4448a44a96c74939a0852020-11-25T03:04:10ZengAmerican Chemical SocietyACS Omega2470-13432019-04-01446703670810.1021/acsomega.9b00199Beyond Traditional Structure-Based Drug Design: The Role of Iron Complexation, Strain, and Water in the Binding of Inhibitors for Hypoxia-Inducible Factor Prolyl Hydroxylase 2Scott D. Bembenek0Hariharan Venkatesan1Hillary M. Peltier2Mark D. Rosen3Terrance D. Barrett4Kimon C. Kanelakis5Heather L. Palomino6Theresa I. Brondstetter7Taraneh Mirzadegan8Michael H. Rabinowitz9†Discovery Sciences, Janssen Research & Development, San Diego, California, United States†Discovery Sciences, Janssen Research & Development, San Diego, California, United StatesJanssen Research & Development, San Diego, California, United StatesJanssen Research & Development, San Diego, California, United States§Cardiovascular Metabolic Therapeutic Area, Janssen Research & Development, San Diego, California, United StatesJanssen Research & Development, San Diego, California, United StatesJanssen Research & Development, San Diego, California, United StatesJanssen Research & Development, San Diego, California, United States†Discovery Sciences, Janssen Research & Development, San Diego, California, United StatesJanssen Research & Development, San Diego, California, United Stateshttp://dx.doi.org/10.1021/acsomega.9b00199
collection DOAJ
language English
format Article
sources DOAJ
author 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
spellingShingle 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
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
ACS Omega
author_facet 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
author_sort Scott D. Bembenek
title 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
title_short 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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_sort 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
publisher American Chemical Society
series ACS Omega
issn 2470-1343
publishDate 2019-04-01
url http://dx.doi.org/10.1021/acsomega.9b00199
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