Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G - Wikidata - awgldk - TriplyDB

Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G

Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G

http://www.wikidata.org/entity/Q34536866

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First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all The APOBEC3 family of retroelement restriction factors Suppression of APOBEC3-mediated restriction of HIV-1 by Vif A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage Inhibition of a NEDD8 Cascade Restores Restriction of HIV by APOBEC3G 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 Nanoscale 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 complexes Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity.SAMHD1 is a single-stranded nucleic acid binding protein with no active site-associated nuclease activity 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.Functional requirements of AID's higher order structures and their interaction with RNA-binding proteins 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 Imaging 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.

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Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G

http://www.wikidata.org/entity/Q34536866

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

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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

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JBC.M110.195685

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Journal of Biological Chemistry

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Atomic force microscopy studie ...... IV restriction factor APOBEC3G

@en

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Alexander Y Lushnikov

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

Luda S Shlyakhtenko

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

Ming Li

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

Yuri L Lyubchenko

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

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Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies

APOBEC3 proteins mediate the clearance of foreign DNA from human cells

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

Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces

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

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

Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution

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

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3387-3395

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scholarly article

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10.1074/JBC.M110.195685

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5

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286

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Reuben S Harris

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2010-12-01T00:00:00Z

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21123176

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3030345

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