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

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

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

http://www.wikidata.org/entity/Q24615413

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Structure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activities Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all 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 Analysis of a single-stranded DNA-scanning process in which activation-induced deoxycytidine deaminase (AID) deaminates C to U haphazardly and inefficiently to ensure mutational diversity Nanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.AID and Apobec3G haphazard deamination and mutational diversity Atomic force microscopy studies of APOBEC3G oligomerization and dynamics.Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity.Rationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulations GANP interacts with APOBEC3G and facilitates its encapsidation into the virions to reduce HIV-1 infectivity Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulation APOBEC3G inhibits HIV-1 RNA elongation by inactivating the viral trans-activation response element.Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain.Retroviral restriction factor APOBEC3G delays the initiation of DNA synthesis by HIV-1 reverse transcriptase.APOBEC3G: a double agent in defense Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA.Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity.Catalytic analysis of APOBEC3G involving real-time NMR spectroscopy reveals nucleic acid determinants for deamination.Characterization of the Catalytic Domain of Human APOBEC3B and the Critical Structural Role for a Conserved Methionine.APOBEC2 is a monomer in solution: implications for APOBEC3G models Single-stranded DNA scanning and deamination by APOBEC3G cytidine deaminase at single molecule resolution.Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 Family.APOBEC3G Interacts with ssDNA by Two Modes: AFM Studies.Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.Natural Polymorphisms and Oligomerization of Human APOBEC3H Contribute to Single-stranded DNA Scanning Ability.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 The ssDNA Mutator APOBEC3A Is Regulated by Cooperative Dimerization Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.Binding of RNA by APOBEC3G controls deamination-independent restriction of retroviruses Crystal structures of APOBEC3G N-domain alone and its complex with DNA.The DNA cytosine deaminase APOBEC3H haplotype I likely contributes to breast and lung cancer mutagenesis.

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

http://www.wikidata.org/entity/Q24615413

description

2010 nî lūn-bûn

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2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մայիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

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Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

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Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

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type

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Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

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Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

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Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

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prefLabel

Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

@ast

Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

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Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

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Journal of Biological Chemistry

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Structural model for deoxycyti ...... 1 inactivation enzyme APOBEC3G

@en

P2093

Courtney Prochnow

http://www.w3.org/2001/XMLSchema#string

Dorothy A Erie

http://www.w3.org/2001/XMLSchema#string

Linda Chelico

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Myron F Goodman

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Xiaojiang S Chen

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P2860

APOBEC3G encapsidation into HIV-1 virions: which RNA is it?

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

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

HIV-1 Vif, APOBEC, and intrinsic immunity

Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G

Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation

7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G

The APOBEC-2 crystal structure and functional implications for the deaminase AID

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

Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein

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16195-205

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scholarly article

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3430149

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10.1074/JBC.M110.107987

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21

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285

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20212048

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2871487

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