Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G
about
First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3GMultiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them allThe APOBEC3 family of retroelement restriction factorsSuppression of APOBEC3-mediated restriction of HIV-1 by VifA conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damageInhibition of a NEDD8 Cascade Restores Restriction of HIV by APOBEC3GInteraction of APOBEC3A with DNA assessed by atomic force microscopyDifferent mutagenic potential of HIV-1 restriction factors APOBEC3G and APOBEC3F is determined by distinct single-stranded DNA scanning mechanismsNanoscale structure and dynamics of ABOBEC3G complexes with single-stranded DNA.Atomic force microscopy studies of APOBEC3G oligomerization and dynamics.Specificity of binding of single-stranded DNA-binding protein to its target.APOBEC3G inhibits HIV-1 RNA elongation by inactivating the viral trans-activation response element.Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein.Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexesDirect evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity.SAMHD1 is a single-stranded nucleic acid binding protein with no active site-associated nuclease activityAntiviral 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.Functional requirements of AID's higher order structures and their interaction with RNA-binding proteinsA 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 APOBEC3GThe ssDNA Mutator APOBEC3A Is Regulated by Cooperative DimerizationImaging of DNA and Protein-DNA Complexes with Atomic Force Microscopy.Single-Molecule Force Spectroscopy Studies of APOBEC3A-Single-Stranded DNA Complexes.Mica functionalization for imaging of DNA and protein-DNA complexes with atomic force microscopy.Structural determinants of human APOBEC3A enzymatic and nucleic acid binding properties.APOBEC3B is an enzymatic source of mutation in breast cancer.DNA substrate preparation for atomic force microscopy studies of protein-DNA interactions.The multifaceted roles of RNA binding in APOBEC cytidine deaminase functions.Development of nanotoxicology: implications for drug delivery and medical devices.APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells.Studying protein-DNA interactions using atomic force microscopy.DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315.Structural and functional assessment of APOBEC3G macromolecular complexes.The APOBEC Protein Family: United by Structure, Divergent in Function.
P2860
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P2860
Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G
description
2010 nî lūn-bûn
@nan
2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@ast
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@en
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@nl
type
label
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@ast
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@en
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@nl
prefLabel
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@ast
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@en
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@nl
P2093
P2860
P356
P1476
Atomic force microscopy studie ...... IV restriction factor APOBEC3G
@en
P2093
Alexander Y Lushnikov
Luda S Shlyakhtenko
Yuri L Lyubchenko
P2860
P304
P356
10.1074/JBC.M110.195685
P407
P577
2010-12-01T00:00:00Z