Isofunctional Clustering and Conformational Analysis of the Arsenate Reductase Superfamily Reveals Nine Distinct Clusters-Reference-Cited by-同舟云学术

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Isofunctional Clustering and Conformational Analysis of the Arsenate Reductase Superfamily Reveals Nine Distinct Clusters

Published:2020-11-02 Issue:44 Volume:59 Page:4262-4284
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Rosen Mikaela R.¹^ORCID,Leuthaeuser Janelle B.¹^ORCID,Parish Carol A.¹^ORCID,Fetrow Jacquelyn S.¹^ORCID

Affiliation:

1. Department of Chemistry, Gottwald Center for the Sciences, University of Richmond, Richmond, Virginia 23713, United States

Funder

American Chemical Society Petroleum Research Fund

National Science Foundation

University of Richmond

Floyd D. and Elisabeth S. Gottwald Endowment

University of Richmond Arts and Sciences Undergraduate Research Committee

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00651

Reference95 articles.

1. Arsenic toxicity and potential mechanisms of action

2. The origami of thioredoxin-like folds

3. Similarities and differences in the thioredoxin superfamily

4. The Thioredoxin Superfamily in Oxidative Protein Folding

5. An Atlas of the Thioredoxin Fold Class Reveals the Complexity of Function-Enabling Adaptations

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1. Structural and functional mapping of ars gene cluster in Deinococcus indicus DR1;Computational and Structural Biotechnology Journal;2023

2. Genome-Resolved Metagenomics and Metatranscriptomics Reveal that Aquificae Dominates Arsenate Reduction in Tengchong Geothermal Springs;Environmental Science & Technology;2022-10-13

3. Proposed mechanism for monomethylarsonate reductase activity of human omega-class glutathione transferase GSTO1-1;Biochemical and Biophysical Research Communications;2022-01

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