Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G.
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Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminaseStructure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activitiesCrystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfacesStructural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3GAn extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme modelTurning up the volume on mutational pressure: is more of a good thing always better? (A case study of HIV-1 Vif and APOBEC3)Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implicationsBase damage within single-strand DNA underlies in vivo hypermutability induced by a ubiquitous environmental agentTwo regions within the amino-terminal half of APOBEC3G cooperate to determine cytoplasmic localization.AID and Apobec3G haphazard deamination and mutational diversityThe artiodactyl APOBEC3 innate immune repertoire shows evidence for a multi-functional domain organization that existed in the ancestor of placental mammals.Adaptive evolution of Mus Apobec3 includes retroviral insertion and positive selection at two clusters of residues flanking the substrate groove.Deficiency in APOBEC2 leads to a shift in muscle fiber type, diminished body mass, and myopathy.Determinants of sequence-specificity within human AID and APOBEC3GIdentification of a single amino acid required for APOBEC3 antiretroviral cytidine deaminase activity.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 complexesStructure of the Vif-binding domain of the antiviral enzyme APOBEC3GAPOBEC2 is a monomer in solution: implications for APOBEC3G modelsA structural basis for the biochemical behavior of activation-induced deoxycytidine deaminase class-switch recombination-defective hyper-IgM-2 mutantsThe DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction.Reverse transcriptase- and RNA packaging signal-dependent incorporation of APOBEC3G into hepatitis B virus nucleocapsids.A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.APOBEC3G subunits self-associate via the C-terminal deaminase domain.Dissecting APOBEC3G substrate specificity by nucleoside analog interference.The choice of nucleotide inserted opposite abasic sites formed within chromosomal DNA reveals the polymerase activities participating in translesion DNA synthesis.Epigenetic reprogramming: is deamination key to active DNA demethylation?A hydrodynamic analysis of APOBEC3G reveals a monomer-dimer-tetramer self-association that has implications for anti-HIV function.Functional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition.Biochemical basis of immunological and retroviral responses to DNA-targeted cytosine deamination by activation-induced cytidine deaminase and APOBEC3G.Mutator effects and mutation signatures of editing deaminases produced in bacteria and yeast.A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIVStructural and functional assessment of APOBEC3G macromolecular complexes.Zinc enhancement of cytidine deaminase activity highlights a potential allosteric role of loop-3 in regulating APOBEC3 enzymes.RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Scoring function to predict solubility mutagenesisInsights into DNA substrate selection by APOBEC3G from structural, biochemical, and functional studies.
P2860
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P2860
Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Extensive mutagenesis experime ...... deaminase domain of APOBEC3G.
@en
type
label
Extensive mutagenesis experime ...... deaminase domain of APOBEC3G.
@en
prefLabel
Extensive mutagenesis experime ...... deaminase domain of APOBEC3G.
@en
P2093
P2860
P1433
P1476
Extensive mutagenesis experime ...... deaminase domain of APOBEC3G.
@en
P2093
Hiroshi Matsuo
Keisuke Shindo
Kuan-Ming Chen
Natalia Martemyanova
Yongjian Lu
P2860
P304
P356
10.1016/J.FEBSLET.2007.08.076
P407
P577
2007-09-07T00:00:00Z