Transition State Analogues Enhanced by Fragment-Based Structural Analysis: Bacterial Methylthioadenosine Nucleosidases-Reference-Cited by-同舟云学术

Transition State Analogues Enhanced by Fragment-Based Structural Analysis: Bacterial Methylthioadenosine Nucleosidases

Published:2020-02-05 Issue:7 Volume:59 Page:831-835
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Zhang Di¹²,Burdette Brandon E.²,Wang Zhengyu³,Karn Kumari²,Li Hong-yu³^ORCID,Schramm Vern L.⁴^ORCID,Tyler Peter C.⁵^ORCID,Evans Gary B.⁵,Wang Shanzhi²^ORCID

Affiliation:

1. College of Animal Science and Technology, Jilin Agricultural University, Changchun 130118, China

2. Department of Chemistry, University of Arkansas at Little Rock, Little Rock, Arkansas 72204, United States

3. Department of Pharmaceutical Sciences, University of Arkansas for Medical Science, Little Rock, Arkansas 72205, United States

4. Department of Biochemistry, Albert Einstein College of Medicine, New York, New York 10461, United States

5. Ferrier Research Institute, Victoria University of Wellington, Wellington 5040, New Zealand

Funder

National Cancer Institute

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.9b01092

Reference27 articles.

1. Transition State Analogues for Enzyme Catalysis

2. TRANSITION STATE ANALOG INHIBITORS AND ENZYME CATALYSIS

3. Enzymatic transition states: thermodynamics, dynamics and analogue design

4. Enzymatic transition states and transition state analogues

5. Enzymatic Transition States, Transition-State Analogs, Dynamics, Thermodynamics, and Lifetimes

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