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The APOBEC Protein Family: United by Structure, Divergent in Function

Trends in biochemical sciences (Amsterdam. Regular ed.), 2016-07, Vol.41 (7), p.578-594

2016

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Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands

Trends in biochemical sciences (Amsterdam. Regular ed.), 2018-08, Vol.43 (8), p.606-622

2018

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Functions and regulation of the APOBEC family of proteins

Seminars in cell & developmental biology, 2012-05, Vol.23 (3), p.258-268

2012

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Structural insights for HIV-1 therapeutic strategies targeting Vif

Trends in biochemical sciences (Amsterdam. Regular ed.), 2014-09, Vol.39 (9), p.373-380

2014

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RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates

Nucleic acids research, 2015-10, Vol.43 (19), p.9434-9445

2015

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Deaminase Activity on Single-stranded DNA (ssDNA) Occurs in Vitro when APOBEC3G Cytidine Deaminase Forms Homotetramers and Higher-order Complexes

The Journal of biological chemistry, 2011-09, Vol.286 (35), p.30655-30661

2011

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A Novel Ebola Virus VP40 Matrix Protein-Based Screening for Identification of Novel Candidate Medical Countermeasures

Viruses, 2020-12, Vol.13 (1), p.52

2020

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RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing

RNA biology, 2017-09, Vol.14 (9), p.1153-1165

Smith, Harold C.

2017

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The multifaceted roles of RNA binding in APOBEC cytidine deaminase functions

Wiley interdisciplinary reviews. RNA, 2014-07, Vol.5 (4), p.493-508

2014

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Sangivamycin is highly effective against SARS-CoV-2 in vitro and has favorable drug properties

JCI insight, 2022-01, Vol.7 (1)

2022

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APOBEC3G Subunits Self-associate via the C-terminal Deaminase Domain

The Journal of biological chemistry, 2008-11, Vol.283 (48), p.33329-33336

2008

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Nanostructures of APOBEC3G Support a Hierarchical Assembly Model of High Molecular Mass Ribonucleoprotein Particles from Dimeric Subunits

The Journal of biological chemistry, 2006-12, Vol.281 (50), p.38122-38126

2006

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The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G

Retrovirology, 2007-11, Vol.4 (1), p.81-81, Article 81

2007

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Measuring Editing Activity and Identifying Cytidine-to-Uridine mRNA Editing Factors in Cells and Biochemical Isolates

Methods in Enzymology, 2007, Vol.424, p.389-416

Smith, Harold C.

2007

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Nuclear Exclusion of the HIV-1 Host Defense Factor APOBEC3G Requires a Novel Cytoplasmic Retention Signal and Is Not Dependent on RNA Binding

The Journal of biological chemistry, 2008-03, Vol.283 (12), p.7320-7327

2008

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APOBEC3G: a double agent in defense

Trends in biochemical sciences (Amsterdam. Regular ed.), 2011-05, Vol.36 (5), p.239-244

Smith, Harold C.

2011

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Sangivamycin is preferentially incorporated into viral RNA by the SARS-CoV-2 polymerase

Antiviral research, 2023-10, Vol.218, p.105716-105716, Article 105716

2023

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A New Class of Antiretroviral Enabling Innate Immunity by Protecting APOBEC3 from HIV Vif-Dependent Degradation

Trends in molecular medicine, 2018-05, Vol.24 (5), p.507-520

2018

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Cyclic peptides with a distinct arginine-fork motif recognize the HIV trans-activation response RNA in vitro and in cells

The Journal of biological chemistry, 2021-12, Vol.297 (6), p.101390-101390, Article 101390

2021

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structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1

Proceedings of the National Academy of Sciences - PNAS, 2004-05, Vol.101 (21), p.8114-8119

2004

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Corrigendum to “Sangivamycin is preferentially incorporated into viral RNA by the SARS-CoV-2 polymerase” [Antivir. Res. 218 (2023) 105716–105728, doi: 10.1016/j.antiviral.2023.105716]

Antiviral research, 2023-11, Vol.219, p.105729-105729, Article 105729

2023

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Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity

Biochemical and biophysical research communications, 2011-09, Vol.412 (4), p.612-617

2011

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High-Affinity Recognition of HIV‑1 Frameshift-Stimulating RNA Alters Frameshifting in Vitro and Interferes with HIV‑1 Infectivity

Journal of medicinal chemistry, 2014-02, Vol.57 (3), p.723-732

2014

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HIV‑1 Frameshift RNA-Targeted Triazoles Inhibit Propagation of Replication-Competent and Multi-Drug-Resistant HIV in Human Cells

ACS chemical biology, 2017-06, Vol.12 (6), p.1674-1682

2017

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Increasing the yield of soluble recombinant protein expressed in E. coli by induction during late log phase

BioTechniques, 2003-03, Vol.34 (3), p.524-530

2003

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The APOBEC Protein Family: United by Structure, Divergent in Function

Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands

Functions and regulation of the APOBEC family of proteins

Structural insights for HIV-1 therapeutic strategies targeting Vif

RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates

Deaminase Activity on Single-stranded DNA (ssDNA) Occurs in Vitro when APOBEC3G Cytidine Deaminase Forms Homotetramers and Higher-order Complexes

A Novel Ebola Virus VP40 Matrix Protein-Based Screening for Identification of Novel Candidate Medical Countermeasures

RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing

The multifaceted roles of RNA binding in APOBEC cytidine deaminase functions

Sangivamycin is highly effective against SARS-CoV-2 in vitro and has favorable drug properties

APOBEC3G Subunits Self-associate via the C-terminal Deaminase Domain

Nanostructures of APOBEC3G Support a Hierarchical Assembly Model of High Molecular Mass Ribonucleoprotein Particles from Dimeric Subunits

The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G

Measuring Editing Activity and Identifying Cytidine-to-Uridine mRNA Editing Factors in Cells and Biochemical Isolates

Nuclear Exclusion of the HIV-1 Host Defense Factor APOBEC3G Requires a Novel Cytoplasmic Retention Signal and Is Not Dependent on RNA Binding

APOBEC3G: a double agent in defense

Sangivamycin is preferentially incorporated into viral RNA by the SARS-CoV-2 polymerase

A New Class of Antiretroviral Enabling Innate Immunity by Protecting APOBEC3 from HIV Vif-Dependent Degradation

Cyclic peptides with a distinct arginine-fork motif recognize the HIV trans-activation response RNA in vitro and in cells

structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1

Corrigendum to “Sangivamycin is preferentially incorporated into viral RNA by the SARS-CoV-2 polymerase” [Antivir. Res. 218 (2023) 105716–105728, doi: 10.1016/j.antiviral.2023.105716]

Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity

High-Affinity Recognition of HIV‑1 Frameshift-Stimulating RNA Alters Frameshifting in Vitro and Interferes with HIV‑1 Infectivity

HIV‑1 Frameshift RNA-Targeted Triazoles Inhibit Propagation of Replication-Competent and Multi-Drug-Resistant HIV in Human Cells

Increasing the yield of soluble recombinant protein expressed in E. coli by induction during late log phase

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