Crowders Steal Dihydrofolate Reductase Ligands through Quinary Interactions-Reference-Cited by-同舟云学术

Crowders Steal Dihydrofolate Reductase Ligands through Quinary Interactions

Published:2019-02-06 Issue:9 Volume:58 Page:1198-1213
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Duff Michael R.¹,Desai Nidhi¹,Craig Michael A.¹,Agarwal Pratul K.¹^ORCID,Howell Elizabeth E.¹^ORCID

Affiliation:

1. Department of Biochemistry & Cellular and Molecular Biology Department, University of Tennessee-Knoxville, Knoxville, Tennessee 37996, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b01110

Reference100 articles.

1. Preorganization and protein dynamics in enzyme catalysis

2. Structure, Dynamics, and Catalytic Function of Dihydrofolate Reductase

3. Trimethoprim Resistance determined by R Factors

4. Nudeotide sequence analysis of tbe trimethoprim resistant dihydrofolate reductase encoded by R plasmid R751

5. Integron-Associated DfrB4, a Previously Uncharacterized Member of the Trimethoprim-Resistant Dihydrofolate Reductase B Family, Is a Clinically Identified Emergent Source of Antibiotic Resistance

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