RSC, an essential, abundant chromatin-remodeling complex
about
SS18 together with animal-specific factors defines human BAF-type SWI/SNF complexesCyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest.Chromatin dynamics at DNA replication, transcription and repaircAMP response element-binding protein-binding protein binds to human papillomavirus E2 protein and activates E2-dependent transcriptionA human homologue of yeast anti-silencing factor has histone chaperone activityThe human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomesSYT associates with human SNF/SWI complexes and the C-terminal region of its fusion partner SSX1 targets histonesPBAF chromatin-remodeling complex requires a novel specificity subunit, BAF200, to regulate expression of selective interferon-responsive genes.Identification of a polymorphic, neuron-specific chromatin remodeling complexArchitectural DNA binding by a high-mobility-group/kinesin-like subunit in mammalian SWI/SNF-related complexesThe Cohesin loading factor NIPBL recruits histone deacetylases to mediate local chromatin modificationsReversible disruption of mSWI/SNF (BAF) complexes by the SS18-SSX oncogenic fusion in synovial sarcomaTIP49b, a regulator of activating transcription factor 2 response to stress and DNA damageRepression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complexA human RNA polymerase II complex containing factors that modify chromatin structureA core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genesCockayne syndrome: defective repair of transcription?Molecular analysis of mutations in the CSB (ERCC6) gene in patients with Cockayne syndromeA specificity and targeting subunit of a human SWI/SNF family-related chromatin-remodeling complexMitotic inactivation of a human SWI/SNF chromatin remodeling complexRoles of inositol phosphates and inositol pyrophosphates in development, cell signaling and nuclear processesDirect observation of DNA distortion by the RSC complexDifferential targeting of two distinct SWI/SNF-related Drosophila chromatin-remodeling complexesThe protein encoded by the proto-oncogene DEK changes the topology of chromatin and reduces the efficiency of DNA replication in a chromatin-specific mannerA family of chromatin remodeling factors related to Williams syndrome transcription factorModular decomposition of protein-protein interaction networksThe SWIRM domain: a conserved module found in chromosomal proteins points to novel chromatin-modifying activities.Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic insights gained from human genomicsPost-translational modifications of histones that influence nucleosome dynamicsSWI/SNF chromatin-remodeling factors: multiscale analyses and diverse functionsAutoregulation of the Rsc4 Tandem Bromodomain by Gcn5 AcetylationThe BAH domain of Rsc2 is a histone H3 binding domainTranscriptional repression of the yeast CHA1 gene requires the chromatin-remodeling complex RSC.A UV-induced genetic network links the RSC complex to nucleotide excision repair and shows dose-dependent rewiring.The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex.Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction.The ctf13-30/CTF13 genomic haploinsufficiency modifier screen identifies the yeast chromatin remodeling complex RSC, which is required for the establishment of sister chromatid cohesionThe nuclear actin-related proteins Arp7 and Arp9: a dimeric module that cooperates with architectural proteins for chromatin remodeling.Multiple bromodomain genes are involved in restricting the spread of heterochromatic silencing at the Saccharomyces cerevisiae HMR-tRNA boundary.Direct interaction between Rsc6 and Rsc8/Swh3,two proteins that are conserved in SWI/SNF-related complexes.
P2860
1a6540b7cbc3ee1568df49c0c464661cbcdc1b13299698fc10218ec724f608873c7937b657823c132a69d580d053657e04df1fa524e08bfe4bbe2580457d0decf1be7cdafb46cd9e07803c23e0020859715b5535384044e1f027ff62bd03a9c12e5e59f977707deddda9a7a9059d0daad57dbb3128157703842c111b8ace948700d5691cbccdc019e2b66a7f90d632d3d45df743806309b472c5acd3981cd53a919013ba5544c4d61ababf4c197b6a374aa86d1aa186f23a9da51d6c367046c515cfc4730446312ba989b79fb739ed6aea63743ac9f116b14c271b92ef172a3adea24b597bb699e6578f3c81c88daa6f
P248
Q21134718-A521D2DE-EFCF-4CC5-BDDF-90869FCE0690Q22008677-C28881CF-83FE-4DDC-8091-12A6A8668F60Q22065678-CC87CAC8-618F-4EF6-BC03-D696E621D726Q22253278-5780EFB0-00FD-41A7-876E-592053235867Q22253863-69CFF6CB-ED32-43BA-B749-6CE5A94A9295Q24290517-97A50CAB-18F5-4C42-AB8C-6C85DA9A9379Q24291965-55C9035D-201B-43E2-ACF6-57EABE1C7433Q24306301-D0C26000-58DC-4910-B73C-A20A16A9326FQ24309294-695F0BAB-7160-4C40-8D68-AF00A79FF67FQ24321741-5850D8F5-74C9-4B2F-94A9-DEF6FC95FFDCQ24322682-A1271343-85EC-48CF-9001-1D9EBE3BA576Q24337483-52CF7CE0-F2AB-4647-978B-81266C6A40B5Q24514481-750928A6-ABA1-4CB7-9A6E-9B7AA28A24AAQ24522344-2CF20261-F558-4F25-9F82-6A10F23BAD38Q24522669-B8B14115-6D5A-49F1-8552-846497A91A8FQ24530537-9EAF154F-E7CF-4190-928A-9DF420A1DFA2Q24532391-5100F7E1-D322-40DE-BDA7-4A837A100A3BQ24538671-32664AD2-2374-4E8E-8DF6-5EFB727B6FC9Q24551058-27F6A29F-6505-4C40-8ADA-D7FF0E790A42Q24596960-D777D489-75A2-4C51-94FD-0C1B0D311C37Q24599387-78AA8204-B61A-414A-9815-5F1F21E520D9Q24599789-1AB2B596-4A8B-446A-BBFA-E59A0172A15DQ24602965-4378565C-AEA7-48F7-A12A-237A61709159Q24605064-D3801A1A-45A8-429D-B894-A45865C3B1CEQ24673669-C5552B1C-7D19-4CC4-A3A6-FE0E3A21CF6AQ24797641-C7D455F0-BA73-46A5-A47B-1B67047D5C79Q24802519-7ABB5E62-31D4-4256-819E-FD2E0E1AD7BAQ26776098-9DFF71F0-E0C7-4612-A487-2D66DCD315CEQ26852536-3783D056-D941-4E5F-9A49-D9518C6C1711Q27009284-1EFABC50-F4E7-4532-8281-FDD53B758FC8Q27647842-CD4D0CED-CB63-4E36-A181-542D7832A56BQ27679325-A3824994-C66F-4C1D-AE01-86C04B0386E2Q27929875-24CC6218-E718-44FC-AE38-08583A3406EEQ27930598-E6998BF5-818D-4120-A7E5-5AE32FEFF356Q27930726-637000EC-E755-4F9E-BC70-C8914241D094Q27930736-AB66018A-DF5B-4B15-8D1E-9A025649905EQ27930793-EA2E861C-839D-4547-9B8F-17D184FBA432Q27930895-5A0B73E6-D049-44DD-9608-F9EB551A56A5Q27931849-2A08565E-B8EA-4333-AEFC-9518CE99F934Q27932111-6B452018-EFBD-4964-A4A8-E90C9065810A
P2860
RSC, an essential, abundant chromatin-remodeling complex
description
1996 nî lūn-bûn
@nan
1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
RSC, an essential, abundant chromatin-remodeling complex
@ast
RSC, an essential, abundant chromatin-remodeling complex
@en
RSC, an essential, abundant chromatin-remodeling complex
@nl
type
label
RSC, an essential, abundant chromatin-remodeling complex
@ast
RSC, an essential, abundant chromatin-remodeling complex
@en
RSC, an essential, abundant chromatin-remodeling complex
@nl
prefLabel
RSC, an essential, abundant chromatin-remodeling complex
@ast
RSC, an essential, abundant chromatin-remodeling complex
@en
RSC, an essential, abundant chromatin-remodeling complex
@nl
P2093
P3181
P1433
P1476
RSC, an essential, abundant chromatin-remodeling complex.
@en
P2093
B R Cairns
R D Kornberg
P304
P3181
P356
10.1016/S0092-8674(00)81820-6
P407
P577
1996-12-27T00:00:00Z