Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity-Reference-Cited by-同舟云学术

Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity

Published:2016-05-19 Issue:21 Volume:55 Page:2944-2959
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Byeon In-Ja L.,Byeon Chang-Hyeock,Wu Tiyun¹,Mitra Mithun¹,Singer Dustin¹,Levin Judith G.¹,Gronenborn Angela M.

Affiliation:

1. Section on Viral Gene Regulation, Program in Genomics of Differentiation, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, United States

Funder

National Institutes of Health

National Institute of General Medical Sciences

Eunice Kennedy Shriver National Institute of Child Health and Human Development

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00382

Reference138 articles.

1. RNA Editing Enzyme APOBEC1 and Some of Its Homologs Can Act as DNA Mutators

2. DNA Deamination Mediates Innate Immunity to Retroviral Infection

3. Hypermutation of HIV-1 DNA in the Absence of the Vif Protein

4. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA

5. Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome

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