Hypermutation by intersegmental transfer of APOBEC3G cytidine deaminase (Q39935230)

15 September 2017

Hypermutation by intersegmental transfer of APOBEC3G cytidine deaminase (English)

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15 September 2017

2

Elena Britan-Rosich

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15 September 2017

Roni Nowarski

1

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PubMed ID

18820687

15 September 2017

Tamar Shiloach

series ordinal

3

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PubMed ID

18820687

15 September 2017

Moshe Kotler

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4

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15 September 2017

28 September 2008

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Nature Structural & Molecular Biology

15 September 2017

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15 September 2017

15

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15 September 2017

10

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15 September 2017

1059-1066

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https://scigraph.springernature.com/pub.10.1038/nsmb.1495

15 September 2017

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Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts

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HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation

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APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses.

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APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast

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High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition

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

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Monomeric APOBEC3G is catalytically active and has antiviral activity.

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Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions

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Cytidine deamination induced HIV-1 drug resistance

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Turning up the volume on mutational pressure: is more of a good thing always better? (A case study of HIV-1 Vif and APOBEC3)

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Unique progressive cleavage mechanism of HIV reverse transcriptase RNase H

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Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities

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31 March 2020

Two are better than one

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A novel zinc-binding motif found in two ubiquitous deaminase families

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31 March 2020

Identifiers

DOI

10.1038/NSMB.1495

1 reference

15 September 2017

1 reference

PubMed ID

18820687