Small Angle Neutron Scattering Studies of R67 Dihydrofolate Reductase, a Tetrameric Protein with Intrinsically Disordered N-Termini-Reference-Cited by-同舟云学术

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Small Angle Neutron Scattering Studies of R67 Dihydrofolate Reductase, a Tetrameric Protein with Intrinsically Disordered N-Termini

Published:2017-10-11 Issue:44 Volume:56 Page:5886-5899
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Bhojane Purva P.¹,Duff Michael R.¹,Bafna Khushboo²,Agarwal Pratul³^ORCID,Stanley Christopher⁴^ORCID,Howell Elizabeth E.¹²^ORCID

Affiliation:

1. Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996-0840, United States

2. Genome Science and Technology Program, University of Tennessee, Knoxville, Tennessee 37996-0840, United States

3. Computer Science and Mathematics Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, United States

4. Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00822

Reference73 articles.

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

2. Fragment-Based Design of Symmetrical Bis-benzimidazoles as Selective Inhibitors of the Trimethoprim-Resistant, Type II R67 Dihydrofolate Reductase

3. Investigation of Classical Organic and Ionic Liquid Cosolvents for Early-Stage Screening in Fragment-Based Inhibitor Design with Unrelated Bacterial and Human Dihydrofolate Reductases

4. A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site

5. Radical Redesign of a Tandem Array of Four R67 Dihydrofolate Reductase Genes Yields a Functional, Folded Protein Possessing 45 Substitutions

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1. From a binding module to essential catalytic activity: how nature stumbled on a good thing;Chemical Communications;2023

2. Research progress and the application of near-infrared spectroscopy in protein structure and molecular interaction analysis;Vibrational Spectroscopy;2022-07

3. The Bacterial Genomic Context of Highly Trimethoprim-Resistant DfrB Dihydrofolate Reductases Highlights an Emerging Threat to Public Health;Antibiotics;2021-04-13

4. Differentiation of the binding of two ligands to a tetrameric protein with a single symmetric active site by 19 F NMR;Protein Science;2020-12-11

5. Crowders Steal Dihydrofolate Reductase Ligands through Quinary Interactions;Biochemistry;2019-02-06

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