about
Optimal functional levels of activation-induced deaminase specifically require the Hsp40 DnaJa1SMUG1 is able to excise uracil from immunoglobulin genes: insight into mutation versus repairMutations, kataegis and translocations in B cells: understanding AID promiscuous activityImmunity through DNA deaminationMismatch recognition and uracil excision provide complementary paths to both Ig switching and the A/T-focused phase of somatic mutationAltering the pathway of immunoglobulin hypermutation by inhibiting uracil-DNA glycosylase.Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90.Trypanosoma cruzi clonal diversity and the epidemiology of Chagas' disease.Consecutive interactions with HSP90 and eEF1A underlie a functional maturation and storage pathway of AID in the cytoplasm.Evaluation of a recombinant Trypanosoma cruzi mucin-like antigen for serodiagnosis of Chagas' disease.HSP90 inhibitors decrease AID levels and activity in mice and in human cells.Roles for APRIN (PDS5B) in homologous recombination and in ovarian cancer prediction.Dependence of antibody gene diversification on uracil excision.A Trypanosoma cruzi small surface molecule provides the first immunological evidence that Chagas' disease is due to a single parasite lineageTrypanosoma cruzi surface mucins: host-dependent coat diversity.Molecular mechanisms of antibody somatic hypermutation.Activation-induced cytidine deaminase (AID) is necessary for the epithelial-mesenchymal transition in mammary epithelial cells.UNG protects B cells from AID-induced telomere loss.Tumor suppressor and deubiquitinase BAP1 promotes DNA double-strand break repair.Activation induced deaminase C-terminal domain links DNA breaks to end protection and repair during class switch recombinationActivation-induced cytidine deaminase targets SUV4-20-mediated histone H4K20 trimethylation to class-switch recombination sites.Immunoglobulin gene conversion in chicken DT40 cells largely proceeds through an abasic site intermediate generated by excision of the uracil produced by AID-mediated deoxycytidine deamination.Autoimmunity and antibody affinity maturation are modulated by genetic variants on mouse chromosome 12.Active nuclear import and cytoplasmic retention of activation-induced deaminase.Differential accumulation of mutations localized in particular domains of the mucin genes expressed in the vertebrate host stage of Trypanosoma cruzi.Pharmacological manipulation of AID.Somatic hypermutation at A.T pairs: polymerase error versus dUTP incorporation.The Trypanosoma cruzi mucin family is transcribed from hundreds of genes having hypervariable regions.High diversity in mucin genes and mucin molecules in Trypanosoma cruzi.A licensing step links AID to transcription elongation for mutagenesis in B cells.Alternative end-joining and classical nonhomologous end-joining pathways repair different types of double-strand breaks during class-switch recombination.A Combined Nuclear and Nucleolar Localization Motif in Activation-Induced Cytidine Deaminase (AID) Controls Immunoglobulin Class SwitchingPRMT5 is essential for B cell development and germinal center dynamicsUnequal opportunity during class switchingTrypanosoma cruzi surface mucin TcMuc-e2 expressed on higher eukaryotic cells induces human T cell anergy, which is reversibleIbrutinib therapy downregulates AID enzyme and proliferative fractions in chronic lymphocytic leukemia
P50
Q24297481-66C92263-2481-46CD-8BB5-4AC71166A0D7Q24541386-878225A6-3FD7-4FCC-99BC-33DE36F25380Q26768663-F9BAC11A-8B53-4415-95D8-41746BB74E16Q28182160-89A7097E-9BDF-4A0A-AC44-114CC409DE0AQ28586304-78F00D4B-7913-4DC3-868B-C84B96D5A015Q34147986-9B144BEC-E9C6-46E8-B714-ACD1A9A06742Q34340626-D289EAAB-BBC4-457B-89AA-D80EFE016CCCQ35124025-CCBBAF97-F8C4-4CAD-B0BE-D865884E21A3Q35289306-17661317-27A8-4CDF-870C-B502A3611583Q35530282-79C592BA-100E-494A-98F3-2AE68B9C592BQ35952172-5E825915-AF65-4CC2-9F77-ED0038AA5371Q36214613-9A83D0FE-A67B-4957-BB3B-97DE8FDA848CQ36294382-1F419596-6D57-47C1-923B-6DDA3382968AQ36369928-5FEAB5C1-0379-48DC-9F3B-4FB8111893C2Q36401388-C20FE5EF-34A6-46A6-B61E-5BA316B0F27EQ36747477-7836B41D-6E20-4998-9557-48D869FBFFF3Q37088708-A1881DFB-4EFA-47C9-B624-D640D7BB2FD8Q37346703-65FC0F98-57C6-4E90-99CA-3D7188F949A1Q37474898-670352C7-C46C-44A3-AA6D-F759310C37F1Q37659903-D9CE5FCE-546A-4D06-9E40-B59C2E76C52DQ40090064-8122D052-DA31-4C26-8C91-F97DAF06051EQ40591358-82B633A7-6F80-4ED3-A857-0328D445E1DAQ41521075-B1680FBB-8518-4E9D-A4B9-49ED562AB64FQ41792388-65B5E8A8-59F6-4ABC-A333-9CD5C9270747Q42615265-79F922EF-243F-49D9-8B76-749FB13D12BCQ43112311-E3993C20-DCB2-4DF2-9C55-2876E2E48CD9Q45248977-EDEA57E1-4656-4256-B519-2CB90D6E4DD8Q48037712-C57B01E2-898D-4DE3-A596-BBDEE4A24A40Q48056761-03D74BCD-A5D8-4E0A-980F-AF169B848548Q52723490-A56C5871-D23A-4D1D-9C8A-BE7EC562D504Q53085728-C6FE954A-9756-48AD-8C6D-8F353B952781Q57942383-7DEBEEED-2C76-412A-892B-DBD03A754826Q60921863-FA70ECD6-9268-4E8C-BB45-48ADE50567D9Q74441764-ECAF5564-52FA-48DD-B228-3F977E45F79BQ77590319-C370B28A-4A74-456C-B863-9C7976B4511AQ91982768-A446A1C0-9E35-4E1D-8396-5EBD185E2942
P50
description
onderzoeker
@nl
researcher, ORCID id # 0000-0003-2896-0321
@en
name
Javier M Di Noia
@ast
Javier M Di Noia
@en
Javier M Di Noia
@es
Javier M Di Noia
@nl
type
label
Javier M Di Noia
@ast
Javier M Di Noia
@en
Javier M Di Noia
@es
Javier M Di Noia
@nl
prefLabel
Javier M Di Noia
@ast
Javier M Di Noia
@en
Javier M Di Noia
@es
Javier M Di Noia
@nl
P106
P1153
6603704827
P21
P31
P496
0000-0003-2896-0321