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.
about
Structure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activitiesHuman LINE-1 restriction by APOBEC3C is deaminase independent and mediated by an ORF1p interaction that affects LINE reverse transcriptase activityPrototype foamy virus Bet impairs the dimerization and cytosolic solubility of human APOBEC3GGuardian of the Human Genome: Host Defense Mechanisms against LINE-1 RetrotranspositionMultiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them allSuppression of APOBEC3-mediated restriction of HIV-1 by VifStructural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3FRationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulationsStructural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulationRandom mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G.Local sequence targeting in the AID/APOBEC family differentially impacts retroviral restriction and antibody diversification.Association of potent human antiviral cytidine deaminases with 7SL RNA and viral RNP in HIV-1 virions.Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain.Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 Family.The RNA Binding Specificity of Human APOBEC3 Proteins Resembles That of HIV-1 NucleocapsidRetroelements versus APOBEC3 family members: No great escape from the magnificent sevenIdentification of the HIV-1 Vif and Human APOBEC3G Protein Interface.HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3GA computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.Determinants of FIV and HIV Vif sensitivity of feline APOBEC3 restriction factors.Binding of RNA by APOBEC3G controls deamination-independent restriction of retrovirusesCrystal structures of APOBEC3G N-domain alone and its complex with DNA.Vif proteins from diverse primate lentiviral lineages use the same binding site in APOBEC3GAPOBEC3G oligomerization is associated with the inhibition of both Alu and LINE-1 retrotranspositionThe double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme.Biochemical and biological studies of mouse APOBEC3.DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315.RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis.Identification and characterization of loop7 motif and its role in regulating biological function of human APOBEC3G through molecular modeling and biological assay.Identification of small molecule compounds targeting the interaction of HIV-1 Vif and human APOBEC3G by virtual screening and biological evaluation.
P2860
Q24310511-8B138A4D-CD69-41E7-BC44-F28C41BAE3E8Q24625056-06304533-12A9-4300-BE7F-DCD53C8B503DQ24629953-5257DA19-C52B-466E-8262-DAC9BDF154D9Q26742086-4BC6C123-B191-44E4-9F7B-E13DA9031E4AQ26823568-F9F7D5F2-2D81-4128-8D2A-CA954C8D7A1AQ27025150-E7E34B1F-381E-4DA5-98E1-D8E080F0E483Q27680506-FE06E36E-8515-49C1-B3CD-D280A68C9E94Q33634092-EB07C4FA-22E5-4565-AF1A-05512B038A74Q33878087-B88A1CD8-8394-40B2-BEA7-89E458710446Q34412223-282011CA-38ED-4262-BB70-F9C34B07F0FAQ34412763-C56874D1-C471-4FAF-BA29-177083F18708Q34416419-51B95068-D30A-4B46-A453-6C7142833CBDQ34719668-E3C35EDE-A266-4509-BB4E-C1BBBE971FC2Q36081987-1567FFAB-B742-44D8-B537-BA37271A327FQ36107814-D235C36C-A3C2-4837-A8B3-B7A370A2A44CQ36162443-763BB945-5C6F-4374-B816-85CE854DFB65Q36348886-D919AEE5-2B8D-43EA-83DC-BB79081625E4Q36647213-6161A639-FD17-4660-AF4E-1BC702A55746Q36871140-2E2590B5-D5C0-41E3-9473-A3A594280679Q37059673-612C7172-C0BB-4881-90F2-5D68881D5D7FQ37122122-F9FA3CCA-1420-4EF9-ADAF-9AC7BA1F625AQ37153949-25C51B0C-A328-4374-8A35-DA53F4DC0B1EQ37252797-B977D873-AED0-4228-8737-CFD7F984B93CQ37404667-E191BBBD-B164-4C15-8E98-F1071CEBA84AQ37504461-0BBDB25F-6CD1-47FA-BF47-65F1CC3067DCQ37713539-CDE79CAE-615C-4923-B5D5-59258811A337Q38708725-BE15C6A8-1FCC-47B6-B492-C71BEE7BFECCQ39015203-AA2E1FA6-8A80-4BA3-BA26-C9573B731E12Q39762406-6DB2EEC1-184A-446B-B9D5-2C615EF1D731Q41229652-3D411DB3-631E-4F8E-A378-E10FEE5A34CFQ55380693-B457C0D6-35EE-44FF-BDBA-9106CE1BAF62
P2860
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.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 23 September 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Functional analysis and struct ...... fection and Alu transposition.
@en
Functional analysis and struct ...... fection and Alu transposition.
@nl
type
label
Functional analysis and struct ...... fection and Alu transposition.
@en
Functional analysis and struct ...... fection and Alu transposition.
@nl
prefLabel
Functional analysis and struct ...... fection and Alu transposition.
@en
Functional analysis and struct ...... fection and Alu transposition.
@nl
P2093
P2860
P356
P1433
P1476
Functional analysis and struct ...... nfection and Alu transposition
@en
P2093
Didier Trono
Olivier Michielin
Priscilla Turelli
Ute F Röhrig
Vincent Zoete
Yannick Bulliard
P2860
P304
12611-12621
P356
10.1128/JVI.01491-09
P407
P577
2009-09-23T00:00:00Z