Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA. - Test2 - elhamkhani - TriplyDB

Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

http://www.wikidata.org/entity/Q30525163

about

Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all The APOBEC3 family of retroelement restriction factors Filming biomolecular processes by high-speed atomic force microscopy Suppression of APOBEC3-mediated restriction of HIV-1 by Vif Interaction of APOBEC3A with DNA assessed by atomic force microscopy Different mutagenic potential of HIV-1 restriction factors APOBEC3G and APOBEC3F is determined by distinct single-stranded DNA scanning mechanisms AID and Apobec3G haphazard deamination and mutational diversity Atomic force microscopy studies of APOBEC3G oligomerization and dynamics.APOBEC3G inhibits HIV-1 RNA elongation by inactivating the viral trans-activation response element.Assembly of the SLIP1-SLBP complex on histone mRNA requires heterodimerization and sequential binding of SLBP followed by SLIP1.Genetic analysis of the localization of APOBEC3F to human immunodeficiency virus type 1 virion cores.Catalytic analysis of APOBEC3G involving real-time NMR spectroscopy reveals nucleic acid determinants for deamination.APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.Impact of H216 on the DNA binding and catalytic activities of the HIV restriction factor APOBEC3G Crystal structures of APOBEC3G N-domain alone and its complex with DNA.DNA substrate preparation for atomic force microscopy studies of protein-DNA interactions.Studying protein-DNA interactions using atomic force microscopy.Reassessing APOBEC3G Inhibition by HIV-1 Vif-Derived Peptides.The C-terminal cytidine deaminase domain of APOBEC3G itself undergoes intersegmental transfer for a target search, as revealed by real-time NMR monitoring.Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G.Remodeling of RecG Helicase at the DNA Replication Fork by SSB Protein.Quantitative analysis of location- and sequence-dependent deamination by APOBEC3G using real-time NMR spectroscopy.Visualization of DNA and protein-DNA complexes with atomic force microscopy.

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Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

http://www.wikidata.org/entity/Q30525163

description

2012 nî lūn-bûn

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2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2012年の論文

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2012年論文

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2012年论文

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Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

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Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

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type

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Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

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Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

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Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

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Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

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Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.

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Alexander Y Lushnikov

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Atsushi Miyagi

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Luda S Shlyakhtenko

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Ming Li

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Yuri L Lyubchenko

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P2860

Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1

Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces

Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G

First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G

Mutational processes molding the genomes of 21 breast cancers

An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model

Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications

Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G

DNA deamination mediates innate immunity to retroviral infection

The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain

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6432-6440

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Reuben S Harris

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