Interdomain twists of human thymidine phosphorylase and its active–inactive conformations: Binding of 5‐FU and its analogues to human thymidine phosphorylase versus dihydropyrimidine dehydrogenase-Reference-Cited by-同舟云学术

Interdomain twists of human thymidine phosphorylase and its active–inactive conformations: Binding of 5‐FU and its analogues to human thymidine phosphorylase versus dihydropyrimidine dehydrogenase

Published:2019-09-06 Issue:5 Volume:94 Page:1956-1972
ISSN:1747-0277
Container-title:Chemical Biology & Drug Design
language:en
Short-container-title:Chem Biol Drug Des

Author:

Tozer Tiffany¹,Heale Kali¹,Manto Chagas Caroline¹,Barros Andre Luis Branco²,Alisaraie Laleh¹³^ORCID

Affiliation:

1. School of Pharmacy Memorial University of Newfoundland St. John’s Newfoundland Canada

2. Department of Clinical and Toxicological Analysis Universidade Federal de Minas Gerais (UFMG) Belo Horizonte Minas Gerais Brazil

3. Department of Chemistry Memorial University of Newfoundland St. John's Newfoundland Canada

Funder

Memorial University of Newfoundland

Publisher

Wiley

Subject

Molecular Medicine,Biochemistry,Drug Discovery,Pharmacology,Organic Chemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/cbdd.13596

Reference32 articles.

1. Normal Mode Analysis of Biomolecular Structures: Functional Mechanisms of Membrane Proteins

2. Drug metabolites and their effects on the development of adverse reactions: Revisiting Lipinski’s Rule of Five

3. Comparison of Secondary Structure Formation Using 10 Different Force Fields in Microsecond Molecular Dynamics Simulations

4. Particle mesh Ewald: AnN⋅log(N) method for Ewald sums in large systems

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