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The RAG1 N-terminal domain is an E3 ubiquitin ligaseUSP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2AAn ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/BMOZ and MORF, two large MYSTic HATs in normal and cancer stem cellsNp95 is a histone-binding protein endowed with ubiquitin ligase activityRegulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylationEpigenetic regulation of the histone-to-protamine transition during spermiogenesisRad6 plays a role in transcriptional activation through ubiquitylation of histone H2B.Non-traditional functions of ubiquitin and ubiquitin-binding proteinsHDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeuticsDeubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylationRNF8-dependent histone modifications regulate nucleosome removal during spermatogenesisSystematic characterization of the zinc-finger-containing proteins in the mouse transcriptome.Epigenetic mechanisms regulate Mallory Denk body formation in the livers of drug-primed miceThe DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites.Glucocorticoid receptor mutants demonstrate increased motility inside the nucleus of living cells: time of fluorescence recovery after photobleaching (FRAP) is an integrated measure of receptor function.Regulation of histone H2A and H2B deubiquitination and Xenopus development by USP12 and USP46.The elusive structural role of ubiquitinated histones.An increasingly complex code.RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesisAltered testicular gene expression patterns in mice lacking the polyubiquitin gene UbbRemodelling the paternal chromatin at fertilization in mammalsA haploid affair: core histone transitions during spermatogenesis.Histone H2B ubiquitination and beyond: Regulation of nucleosome stability, chromatin dynamics and the trans-histone H3 methylation.Lessons from the genome sequence of Neurospora crassa: tracing the path from genomic blueprint to multicellular organism.Ubiquitylation of histone H2B controls RNA polymerase II transcription elongation independently of histone H3 methylation.The FACT chromatin modulator: genetic and structure/function relationships.Histone ubiquitination and deubiquitination in transcription, DNA damage response, and cancer.Histone deacetylase inhibitors: clinical implications for hematological malignancies.An epigenetic code for DNA damage repair pathways?Histone H2B ubiquitylation and deubiquitylation in genomic regulation.The RAD6 pathway: control of DNA damage bypass and mutagenesis by ubiquitin and SUMO.Impaired V(D)J recombination and lymphocyte development in core RAG1-expressing mice.Putative molecular mechanism underlying sperm chromatin remodelling is regulated by reproductive hormones.RNF111-dependent neddylation activates DNA damage-induced ubiquitination.Epigenetic events in malignant melanoma.Evaluating epigenetic landmarks in the brain of multiple sclerosis patients: a contribution to the current debate on disease pathogenesisTalking to chromatin: post-translational modulation of polycomb group function.Altered histone monoubiquitylation mediated by mutant huntingtin induces transcriptional dysregulation.Telomeres, histone code, and DNA damage response.
P2860
Q24297482-F20EFB8C-E914-4AFB-9570-D1E292795B77Q24311562-0E6EEC31-44AB-4C13-80D3-E6023AB583AEQ24535295-B39C4DDB-659E-4CF1-9D25-11A15741C5E3Q24570117-8F8D175F-94EB-44F2-9AFD-9CAA8CDA8F30Q24629660-96D30D31-A09F-4C23-9FED-E8FC30ACBFEAQ24793292-D8D0D023-1600-493F-A393-D22AD51E7100Q26768549-AC449374-0AF7-4255-9939-65C7D17434FAQ27930655-D8883F1F-029F-4112-BD04-CB0A24B7E3AAQ28187368-1A488386-47E2-4A9A-B671-948FEA110E32Q28290352-AFDD73E0-6101-421F-AA83-9C1DE7F94310Q28585918-DAE0EF7A-090D-4023-95AE-9285245F189FQ28589254-30769721-ACA5-4AB3-895F-FC2C0F729C2FQ30805640-EC1C6830-D025-43EC-BC14-3558E6DFE8D4Q33868680-BECD9DBF-2A79-4C39-8EA2-A70146325280Q34479820-F0592449-A196-4119-9840-05C7FDA8514DQ34521324-9C847BB8-5B5C-41A7-9AB3-5D99E0B82716Q34606198-5AD50296-3000-4824-8C51-740379C3E6B9Q34746899-CB7C9984-978A-4DA7-B372-AD05B4D161E2Q34796349-ABC0B498-BBBD-4089-9BED-12307BAFA5C3Q34829400-1B5E09AC-C17A-426F-A749-08B391AA0044Q35097653-291BAE61-864B-4588-A7CE-196DF059118EQ35114064-68383FC5-3474-4DE7-8E93-5C8611EEA4DEQ35191538-BAA88239-86D4-4C9D-BD9E-6919125289DAQ35592200-85CBAC66-711B-4313-921E-350BCCCEB019Q35684970-CDADD0FC-B91E-4912-8582-59E484663C19Q35720902-C061A377-D120-4E7B-A31A-DD5001F84840Q35851279-815C6232-F5A3-4E4A-9488-38FDF9C1898CQ35971184-ACA1C865-8508-46E2-8D4A-C50D914C880CQ36001847-10978177-6940-4FC1-A032-FFC733FDD2A9Q36164740-C53258CB-27B6-4A20-BE82-C9D87F21710BQ36238608-5557A54A-786D-4E0C-B02B-8AA29D1E9282Q36249152-CBB8A716-0E97-4A49-AEC4-B4504C51F055Q36371862-CC3646D8-A2FE-4FE8-8CB8-E3F7A8DF5598Q36547794-A8DF2585-0F09-4B49-84EF-EAD08BBE86BAQ36677932-C9BAA34E-3344-43F3-9583-7C6EA9B5D651Q36764224-B042604F-9ACA-4D36-81E6-9EB322FC7DB5Q37130888-56EEE39D-430C-4D75-B97E-40E56B9A6FD2Q37350145-13F07706-93AD-4093-A247-351B545F6394Q37352446-A7B73FCA-BB78-4D3D-995C-F6759CD4CEA5Q37384129-337BE651-0E7C-4592-A875-B16566F1C7A1
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Histone ubiquitination: a tagging tail unfolds?
@ast
Histone ubiquitination: a tagging tail unfolds?
@en
Histone ubiquitination: a tagging tail unfolds?
@nl
type
label
Histone ubiquitination: a tagging tail unfolds?
@ast
Histone ubiquitination: a tagging tail unfolds?
@en
Histone ubiquitination: a tagging tail unfolds?
@nl
prefLabel
Histone ubiquitination: a tagging tail unfolds?
@ast
Histone ubiquitination: a tagging tail unfolds?
@en
Histone ubiquitination: a tagging tail unfolds?
@nl
P2093
P2860
P356
P1433
P1476
Histone ubiquitination: a tagging tail unfolds?
@en
P2093
George Lindsey
John D Lewis
Juan Ausió
Laure J M Jason
Susan C Moore
P2860
P304
P356
10.1002/BIES.10038
P407
P577
2002-02-01T00:00:00Z