about
Mutations, kataegis and translocations in B cells: understanding AID promiscuous activityTranscriptional stalling in B-lymphocytes: a mechanism for antibody diversification and maintenance of genomic integrityThe AID-induced DNA damage response in chromatin.Overlapping hotspots in CDRs are critical sites for V region diversificationConsecutive interactions with HSP90 and eEF1A underlie a functional maturation and storage pathway of AID in the cytoplasm.Parp3 negatively regulates immunoglobulin class switch recombination.Cell Cycle Regulates Nuclear Stability of AID and Determines the Cellular Response to AID.Mutagenesis by AID: Being in the Right Place at the Right Time.HSP90 inhibitors decrease AID levels and activity in mice and in human cells.The preferred nucleotide contexts of the AID/APOBEC cytidine deaminases have differential effects when mutating retrotransposon and virus sequences compared to host genesRegulation of AID, the B-cell genome mutator.PARP activation promotes nuclear AID accumulation in lymphoma cellsActivation-induced cytidine deaminase (AID) is necessary for the epithelial-mesenchymal transition in mammary epithelial cells.AIDing Chromatin and Transcription-Coupled Orchestration of Immunoglobulin Class-Switch Recombination.Hormones and AID: balancing immunity and autoimmunity.Control of Transposon-Mediated Directed Mutation by the Escherichia coli Phosphoenolpyruvate:Sugar Phosphotransferase System.Complex downstream effects of nuclear export inhibition in B-cell lymphomas: a possible role for activation-induced cytidine deaminase (AID).Predicting AID off-targets: A step forward.Investigation of AID, Dicer, and Drosha Expressions in Patients with Chronic Lymphocytic Leukemia.A licensing step links AID to transcription elongation for mutagenesis in B cells.
P2860
Q26768663-CD3B4CBB-7EF4-44B3-BF65-DC27727EAAAFQ26862917-C452FE0B-E438-45A8-9BA3-E0D659F490EBQ34715036-ADEFA4CC-DBD0-49D9-9B35-E75899474A84Q35128767-1C35622C-8B4E-488A-8D4A-2A1B192FA4FAQ35289306-54E271CD-BAEE-4F7F-8BEC-C57B100F02DFQ35637214-06E63397-22E6-4619-9652-12D40E7EAE60Q35768862-BD0EA843-BB52-4FCE-B4C7-84A19FB7E4D0Q35768901-F4240015-EACF-464F-89DA-A39012069DB2Q35952172-A56D3762-B972-4769-AFD5-0A6FDAACD139Q36330081-FC62757E-94FE-4203-9E41-946BB63CB84DQ36557058-AFC9C5DD-2622-4E33-9FA2-47C9D867233CQ37022423-87BC8CF7-24B5-4080-B30C-A9B738911A14Q37088708-584BAA70-AB47-4746-9EF5-7695D750CA2EQ37683558-B310F63D-E26B-492B-A08C-1964C0C6732BQ38062548-1BE83DC2-3227-4EA7-B9E4-9BC16B7CFF48Q38544467-BEE4D396-1478-47F6-BEE9-3BA06D0ED830Q42583771-66C78DDD-EE5D-4E57-A979-5EB38C3129ABQ49960852-171B3A61-D149-4547-9F21-0F805370CA72Q51067407-9D609A1D-4ACB-451F-A9D6-0EC2DE413755Q52723490-AA8CF768-A32C-4102-93FA-A46321DEE6B0
P2860
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Activation induced deaminase: how much and where?
@en
type
label
Activation induced deaminase: how much and where?
@en
prefLabel
Activation induced deaminase: how much and where?
@en
P1476
Activation induced deaminase: how much and where?
@en
P2093
Alexandre Orthwein
Javier M Di Noia
P304
P356
10.1016/J.SMIM.2012.05.001
P577
2012-06-09T00:00:00Z