Impact of phosphorylation and phosphorylation-null mutants on the activity and deamination specificity of activation-induced cytidine deaminase.
about
Disruption of Transcriptional Coactivator Sub1 Leads to Genome-Wide Re-distribution of Clustered Mutations Induced by APOBEC in Active Yeast GenesEvolution of phosphorylation-dependent regulation of activation-induced cytidine deaminase.Two forms of activation-induced cytidine deaminase differing in their ability to bind agarose.Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization.Mutations in human AID differentially affect its ability to deaminate cytidine and 5-methylcytidine in ssDNA substrates in vitroReplication protein A (RPA) hampers the processive action of APOBEC3G cytosine deaminase on single-stranded DNARegulation of immunoglobulin class-switch recombination: choreography of noncoding transcription, targeted DNA deamination, and long-range DNA repair.A Proteome-wide Domain-centric Perspective on Protein Phosphorylation.Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain.APOBEC deaminases-mutases with defensive roles for immunity.Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein.A structural basis for the biochemical behavior of activation-induced deoxycytidine deaminase class-switch recombination-defective hyper-IgM-2 mutantsEfficient deamination of 5-methylcytosines in DNA by human APOBEC3A, but not by AID or APOBEC3G.Combinatorial mechanisms regulating AID-dependent DNA deamination: interacting proteins and post-translational modifications.Regulation of activation-induced cytidine deaminase DNA deamination activity in B-cells by Ser38 phosphorylation.Regulation of class switch recombination and somatic mutation by AID phosphorylationDissociation of in vitro DNA deamination activity and physiological functions of AID mutants.Stochastic properties of processive cytidine DNA deaminases AID and APOBEC3G.V-region mutation in vitro, in vivo, and in silico reveal the importance of the enzymatic properties of AID and the sequence environmentThe activation-induced cytidine deaminase (AID) efficiently targets DNA in nucleosomes but only during transcription.Post-translational regulation of activation-induced cytidine deaminase.Restricting activation-induced cytidine deaminase tumorigenic activity in B lymphocytes.Biochemical basis of immunological and retroviral responses to DNA-targeted cytosine deamination by activation-induced cytidine deaminase and APOBEC3G.Modulation of mutagenesis in eukaryotes by DNA replication fork dynamics and quality of nucleotide pools.Activation-induced cytidine deaminase in antibody diversification and chromosome translocation.Altering the spectrum of immunoglobulin V gene somatic hypermutation by modifying the active site of AID.Amino-terminal phosphorylation of activation-induced cytidine deaminase suppresses c-myc/IgH translocation.Hypermutation at A/T sites during G.U mismatch repair in vitro by human B-cell lysates.Enzyme cycling contributes to efficient induction of genome mutagenesis by the cytidine deaminase APOBEC3B.
P2860
Q28547015-5FFAE656-566A-4ADA-8ADE-0EDB3A0E49CFQ33379345-D8A80766-07D3-4929-A2BA-5A9EC8FF48CEQ33527420-856E4987-C38F-48AB-B469-28D2C2655C95Q33558327-22981066-FEC6-4DAC-B33A-4FD5B60686AEQ33819022-E550A603-EF6F-47F8-B46F-10F5A68B68FFQ34026341-17DADDF7-706E-4947-A9B1-6080B0829F85Q34115234-7C9665EC-586E-4513-A099-63332472F5A0Q34157631-F5F337BC-3834-440D-B316-7F65989A7CD6Q34719668-5467A7AB-B9A2-4307-9EE5-E8E4D29460C1Q35012747-4EE3466F-BADB-4743-B845-8936F39B2F93Q35128214-0991CB6E-14C6-4F7E-B095-D15B3E4C7990Q36201805-D74663B6-3EFA-4B11-BCED-21AE36D48655Q36305701-93269ADE-5E8E-40BD-9966-EF909145BE1CQ36316915-CC06F412-BBE8-4CB5-A119-3A42E958D8A6Q36519034-5403CECC-1B97-4E27-89F2-4F035BDBB255Q36946561-9E10A066-15FA-42BD-AD55-025A71088E88Q36949101-8D5108F2-DA44-45E1-9AA9-54F5025F722AQ37140478-5E2AB7DC-14BA-4243-AFCE-ECBD764EDF82Q37193388-CB5BD72D-9C4C-4329-A51A-DB7109523729Q37273144-1E6C0D63-E407-45CD-A3C3-4A3D7D37CE92Q37326092-11F06024-B279-4CEB-9668-7593C1A20C31Q37419452-2BA97879-12F6-4CA2-81E1-2803C60689B1Q37459803-D4117468-1CBA-42A4-B035-DAEC846A6C32Q37483304-7EB9D217-DAF1-412D-B578-38F7DB786A35Q37994933-44721439-054C-411D-86EA-BE75D7E360A8Q39756116-AA1C1896-3A8B-481C-8D9F-1D4124DB12FFQ42582794-2598C22D-AE25-47BA-8A54-260C757C5BFBQ43244319-F8CA3BF9-308E-46CA-847A-4B82FCEE3EBCQ47152216-F05F5FC4-A009-4C60-A240-D92F4E24F19F
P2860
Impact of phosphorylation and phosphorylation-null mutants on the activity and deamination specificity of activation-induced cytidine deaminase.
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
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
name
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@ast
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@en
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@nl
type
label
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@ast
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@en
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@nl
prefLabel
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@ast
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@en
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@nl
P2093
P2860
P356
P1476
Impact of phosphorylation and ...... on-induced cytidine deaminase.
@en
P2093
Alice Landolph
Marcus B Smolka
Myron F Goodman
Peter Calabrese
Phuong Pham
P2860
P304
17428-17439
P356
10.1074/JBC.M802121200
P407
P50
P577
2008-04-16T00:00:00Z