APOBEC3G subunits self-associate via the C-terminal deaminase domain.
about
Crystal 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 modelRNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1Atomic force microscopy studies of APOBEC3G oligomerization and dynamics.Rationalisation of the differences between APOBEC3G structures from crystallography and NMR studies by molecular dynamics simulationsLeveraging APOBEC3 proteins to alter the HIV mutation rate and combat AIDS.Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulationMicrocrystallography, high-pressure cryocooling and BioSAXS at MacCHESS.NOA36 protein contains a highly conserved nucleolar localization signal capable of directing functional proteins to the nucleolus, in mammalian cellsRetroviral restriction factor APOBEC3G delays the initiation of DNA synthesis by HIV-1 reverse transcriptase.APOBEC deaminases-mutases with defensive roles for immunity.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 complexesDirect evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity.Characterization of the Catalytic Domain of Human APOBEC3B and the Critical Structural Role for a Conserved Methionine.Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 Family.HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3GBinding of RNA by APOBEC3G controls deamination-independent restriction of retrovirusesIntracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA.A hydrodynamic analysis of APOBEC3G reveals a monomer-dimer-tetramer self-association that has implications for anti-HIV function.Biochemical basis of immunological and retroviral responses to DNA-targeted cytosine deamination by activation-induced cytidine deaminase and APOBEC3G.The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme.APOBEC3G-Mediated G-to-A Hypermutation of the HIV-1 Genome: The Missing Link in Antiviral Molecular MechanismsMechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.The multifaceted roles of RNA binding in APOBEC cytidine deaminase functions.Structural and functional assessment of APOBEC3G macromolecular complexes.RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G.Solution structure of extracellular loop of human β4 subunit of BK channel and its biological implication on ChTX sensitivity.Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid Ligands
P2860
Q24599263-7B9670A0-22BA-4B9E-8A03-FC0F576C50E2Q24615413-4EA0E18C-C19C-4191-81E9-181A2074E8B4Q24642268-76FFA335-DF75-4234-807A-5F973C8D7195Q28474904-DDCD762D-3CEB-4B2D-8FDE-BF77A2E9AD38Q30558175-48F3742F-E50A-486F-939A-C43EEB4E4E4EQ33634092-400A8C75-BE98-4A7A-88F6-60B0D052F571Q33654949-DD12EDD0-53DC-4876-81D9-3B60BAC8ADCDQ33878087-A6875FFD-4AE1-4F08-8B9A-B776701AD2BAQ34416246-7B2B2388-5C66-475A-8FA1-78DC156E7E5AQ34630287-6A94BB98-D06F-42D2-9092-7B5B9D094656Q34745411-849F7BD1-413C-4ADC-89CA-D1849C9B824BQ35012747-D9488753-0192-4845-B5ED-5A2BA81093A5Q35080239-40C81ABE-C8D1-4D1C-A2C6-7E0C3C461567Q35182930-F1D4581C-E35D-40F8-8AE8-6350C01D3197Q35209374-D7C1F35E-F12E-4B3D-9641-AA30294D6C76Q35747955-291C8A9E-C38E-46BE-99E6-948D3BEC53CAQ36081987-218DB8EB-B16B-4C1E-8A1A-2C02FA433172Q36647213-CD30E96F-5104-4756-A807-E4C78B1FABEDQ37122122-2D9D600F-39C7-4EAB-8BBE-C492EC741144Q37236852-194E75B7-E2B5-42BC-9467-80FBB5F83469Q37438750-3D7CB054-FFBB-404C-8934-13D241565E39Q37459803-C81BD70E-F20F-4C84-8B60-6BA2A8CCD909Q37504461-931B81AC-E77B-475A-811A-0FE17520EFE2Q37512973-DA371BD3-3D43-4CBB-8C10-52D00F2AB41BQ37593180-6CC3AD8E-F825-42C7-80A9-27DBBBA9D6BAQ38199065-2997E286-E52E-4BA4-AA70-6F56E6B7B47BQ38778847-9A92C061-9937-4194-9014-D17995775E2AQ39015203-00EE06B5-D206-41FA-A012-EFE193203AA4Q40479772-1EA87006-4C7C-4889-B6E9-DD3D4AD066BBQ41701165-86B0B72A-885C-47D6-B112-CCC2FFA6EA7AQ52653223-7634D6D7-4703-41D4-9C25-052AA2764F14Q57173759-A38E9813-09CB-4EF1-B165-44AB64791B6E
P2860
APOBEC3G subunits self-associate via the C-terminal deaminase domain.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
APOBEC3G subunits self-associate via the C-terminal deaminase domain.
@en
type
label
APOBEC3G subunits self-associate via the C-terminal deaminase domain.
@en
prefLabel
APOBEC3G subunits self-associate via the C-terminal deaminase domain.
@en
P2093
P2860
P356
P1476
APOBEC3G subunits self-associate via the C-terminal deaminase domain.
@en
P2093
Jason D Salter
Joseph E Wedekind
Ryan P Bennett
P2860
P304
33329-33336
P356
10.1074/JBC.M803726200
P407
P50
P577
2008-10-08T00:00:00Z