Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.
about
Suppression of APOBEC3-mediated restriction of HIV-1 by VifNMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificityAPOBEC3A and APOBEC3B Preferentially Deaminate the Lagging Strand Template during DNA ReplicationA DNA sequence recognition loop on APOBEC3A controls substrate specificityInteraction 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 mechanismsTransient overexpression of exogenous APOBEC3A causes C-to-U RNA editing of thousands of genes.Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.Clustered and genome-wide transient mutagenesis in human cancers: Hypermutation without permanent mutators or loss of fitnessHuman APOBEC3A isoforms translocate to the nucleus and induce DNA double strand breaks leading to cell stress and death.APOBEC3A functions as a restriction factor of human papillomavirusSequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities.DNA cytosine and methylcytosine deamination by APOBEC3B: enhancing methylcytosine deamination by engineering APOBEC3B.Natural Polymorphisms and Oligomerization of Human APOBEC3H Contribute to Single-stranded DNA Scanning Ability.The ssDNA Mutator APOBEC3A Is Regulated by Cooperative DimerizationAPOBEC3A damages the cellular genome during DNA replicationStructural analysis of the activation-induced deoxycytidine deaminase required in immunoglobulin diversificationSingle-Molecule Force Spectroscopy Studies of APOBEC3A-Single-Stranded DNA Complexes.Nuclear Magnetic Resonance Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.A biochemical analysis linking APOBEC3A to disparate HIV-1 restriction and skin cancerStructural determinants of human APOBEC3A enzymatic and nucleic acid binding properties.Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.Risks at the DNA Replication Fork: Effects upon Carcinogenesis and Tumor HeterogeneityA Novel Regulator of Activation-Induced Cytidine Deaminase/APOBECs in Immunity and Cancer: Schrödinger's CATalytic Pocket.Role of the single deaminase domain APOBEC3A in virus restriction, retrotransposition, DNA damage and cancer.Possible footprints of APOBEC3F and/or other APOBEC3 deaminases, but not APOBEC3G, on HIV-1 from patients with acute/early and chronic infections.Determinants of efficient degradation of APOBEC3 restriction factors by HIV-1 Vif.D316 is critical for the enzymatic activity and HIV-1 restriction potential of human and rhesus APOBEC3B.Roles of APOBEC3A and APOBEC3B in Human Papillomavirus Infection and Disease Progression.NMR-based method of small changes reveals how DNA mutator APOBEC3A interacts with its single-stranded DNA substrate.Deamination-independent restriction of LINE-1 retrotransposition by APOBEC3HEnzyme cycling contributes to efficient induction of genome mutagenesis by the cytidine deaminase APOBEC3B.Substrate sequence selectivity of APOBEC3A implicates intra-DNA interactions.
P2860
Q27025150-F9198A91-E329-417F-BB2D-60007C8AC257Q27678249-C6C5DBDA-CC74-400E-B228-E1B8223FB9B1Q28272805-F114B2AB-ED63-4CBC-BCE4-67FAA7CEEAD5Q28538801-2613D202-424A-4BC5-B17B-E322DA00B62DQ28539478-3687EAD4-4AE9-47DC-8692-7D4E9E33EC0FQ28541264-15826652-62DC-4EAD-8BDB-4C09AE82ED9DQ30853937-62C08D0F-A13A-47E4-BDE9-5C97114F343CQ33558327-AC2A77AD-8469-4706-9514-259EB6101D86Q34090613-B56A73E2-FA54-4094-B3AE-C6C2D27BF9C8Q34974240-C6BBCB9C-A982-4698-9E6A-9C59B30C78C2Q34992751-72E6A189-43AD-411A-B663-D4D6EE6628FFQ35068754-9671A151-3B43-4867-9BA7-F927C2F0D0ACQ36184715-BBB7DAA5-498B-48BE-9B9D-BE8F20138907Q36283884-CA881B3F-DA70-4420-BF4F-9DCC0573D41EQ36921174-6EA9D173-12AB-40C9-A71E-9132D5CE8D13Q36956935-5AB63316-F74D-4481-AB52-19BAD16051E8Q37029712-BCC5AFDC-41C8-49E3-932E-15894FACC5D2Q37064877-51D67452-B238-4E37-8CB9-26ED86D7C68EQ37091342-2307FC65-883A-41B3-989A-FC19E0D39BD5Q37226085-9FCF1A79-52D1-4683-9C9C-F4F5A1B36B46Q37518666-0174FDF6-2D13-48C1-9465-90713A8C4B79Q37593180-663A2471-7ECB-4877-904E-E38B3A96F829Q37628288-A44679D7-1143-48A1-9CF2-E16E3CE7E62AQ37739072-A98429D9-8F95-4D1A-A331-5ED56CBCD8D9Q38613375-AF975B18-7708-40AB-936F-69F0345CAF4DQ38879828-18F7BE8D-4D88-4F15-A4E5-660F2E4E8DE0Q38951329-78C7A8E5-F181-49F5-A274-A041D6F377CEQ39173531-F48EDB8D-D652-4D4C-A20E-7839C5DC412BQ40076776-E8AFFEF8-BC7D-4896-9A3A-72F395F12092Q40261713-08E63CF1-DAC7-40B1-A865-D78EB6650761Q41539251-EE835706-B367-40F2-8346-E955B85895A3Q47152216-807AF7F6-F06A-47EF-A430-F922316E3E66Q55312858-0DB77A82-4920-428C-92C6-FE85B2E7139A
P2860
Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.
@ast
Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.
@en
type
label
Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.
@ast
Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.
@en
prefLabel
Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.
@ast
Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A.
@en
P2860
P356
P1476
Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A
@en
P2093
P2860
P304
30812-30822
P356
10.1074/JBC.M112.393181
P407
P577
2012-07-20T00:00:00Z