Computational modeling studies reveal the origin of the binding preference of 3‐(3,4‐di hydroisoquinolin‐2( <scp>1H</scp> )‐ylsulfonyl)benzoic acids for <scp>AKR1C3</scp> over its isoforms-Reference-Cited by-同舟云学术

Computational modeling studies reveal the origin of the binding preference of 3‐(3,4‐di hydroisoquinolin‐2( 1H )‐ylsulfonyl)benzoic acids for AKR1C3 over its isoforms

Published:2022-11-22 Issue:12 Volume:31 Page:
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Kong Xiaotian¹^ORCID,Xing Enming²,Wu Sijin³,Zhuang Tony⁴,Li Pui‐Kai²,Li Chunhua¹,Cheng Xiaolin²

Affiliation:

1. College of Life Science and Bioengineering, Faculty of Environment and Life Beijing University of Technology; Beijing International Science and Technology Cooperation Base for Intelligent Physiological Measurement and Clinical Transformation Beijing China

2. Division of Medicinal Chemistry & Pharmacognosy, College of Pharmacy The Ohio State University Columbus Ohio USA

3. Dalian Institute of Chemical Physics, Chinese Academy of Sciences Dalian China

4. J. Willis Hurst Internal Medicine Program, Department of Medicine Emory University Woodruff Georgia USA

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4499

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3. AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders

4. Overview of AKR1C3: Inhibitor Achievements and Disease Insights

5. Aldo-keto Reductase Family 1 Member C3 (AKR1C3) Is a Biomarker and Therapeutic Target for Castration-Resistant Prostate Cancer

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