Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
about
Structural implications for K5/K12-di-acetylated histone H4 recognition by the second bromodomain of BRD2Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7The role of human bromodomains in chromatin biology and gene transcriptionLysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein associationAutoregulation of the Rsc4 Tandem Bromodomain by Gcn5 AcetylationStructures of the Dual Bromodomains of the P-TEFb-activating Protein Brd4 at Atomic ResolutionStructural Basis for Acetylated Histone H4 Recognition by the Human BRD2 BromodomainDifferent orientations of low-molecular-weight fragments in the binding pocket of a BRD4 bromodomainNuA4-directed chromatin transactions throughout the Saccharomyces cerevisiae genome.Multiple bromodomain genes are involved in restricting the spread of heterochromatic silencing at the Saccharomyces cerevisiae HMR-tRNA boundary.The Yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone H3.Interdependent recruitment of SAGA and Srb mediator by transcriptional activator Gcn4p.Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.Bromodomain: an acetyl-lysine binding domainThe histone H3 acetylase dGcn5 is a key player in Drosophila melanogaster metamorphosis.The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosisSpecificity of the HP1 chromo domain for the methylated N-terminus of histone H3.GCN5 is a required cofactor for a ubiquitin ligase that targets NF-kappaB/RelAMulti-tasking on chromatin with the SAGA coactivator complexes.Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectivesSolution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tailsThermodynamic analysis of acetylation-dependent Pb1 bromodomain-histone H3 interactionsTargeted recruitment of Rpd3 histone deacetylase represses transcription by inhibiting recruitment of Swi/Snf, SAGA, and TATA binding proteinKeeping it in the family: diverse histone recognition by conserved structural foldsHuman THAP7 is a chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressor.The bromodomain of Gcn5 regulates site specificity of lysine acetylation on histone H3DNA-binding properties of the recombinant high-mobility-group-like AT-hook-containing region from human BRG1 protein.Mouse BRWD1 is critical for spermatid postmeiotic transcription and female meiotic chromosome stability.3,5-dimethylisoxazoles act as acetyl-lysine-mimetic bromodomain ligands.The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases.PfGCN5-mediated histone H3 acetylation plays a key role in gene expression in Plasmodium falciparum.Nucleosome competition reveals processive acetylation by the SAGA HAT module.Role of histone acetylation in the control of gene expression.Eaf3 regulates the global pattern of histone acetylation in Saccharomyces cerevisiae.Mechanisms of ATP dependent chromatin remodeling.Kinetic analysis of acetylation-dependent Pb1 bromodomain-histone interactions.Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation.Structure and acetyl-lysine recognition of the bromodomain.Chromatin Central: towards the comparative proteome by accurate mapping of the yeast proteomic environment.Polybromo-1: the chromatin targeting subunit of the PBAF complex.
P2860
Q24295275-177AD29C-C1A6-4731-8901-7BCF6060BA2DQ24337326-C5235C78-08BC-4F79-99B7-8AE091840E47Q24631840-A4073EF7-520C-49FC-AB5E-375596A1A2B3Q24675122-485D30D3-78A2-4EAE-9EC7-FEDA067F7641Q27647842-4B5AAC71-C472-40C1-ADD3-BFB9D0E666D1Q27657784-41A893E3-5F49-480E-AD73-6017C17D4B82Q27658848-8EDD1BC4-5BBE-48B4-B03A-9FDC299A64FEQ27687015-3186B0D3-20C0-4AA5-86E2-47DD9EA19975Q27930805-5601AFA2-DCFD-4E9E-B023-3BC60AFA6725Q27931849-87592F0D-3F16-41B1-BB31-F9107A5575D8Q27935044-7D83DAE0-6015-4E6F-9973-BB4535A8C3FEQ27939381-5995C181-0C55-49F7-A66B-91B91B151CE9Q27939462-E0325F13-2EC9-4030-8768-A830F3145010Q28209708-DE5E6B69-6036-4425-A4CC-F86AAE14714BQ28769333-EBA59765-4B3F-4A10-A8C6-A97BDCE55206Q29618035-8D5D35E8-2113-4701-B797-07B3B0810B80Q30307942-AACC464F-85D5-448C-A601-272C8DD60580Q30438310-758D462E-530C-4500-A4E8-7EA6AB5E4AABQ30443104-9BB14DB6-5860-4A0A-B9D9-5AB41B2B1FB5Q30570945-CE5AE6AE-E7A9-4550-89E6-4CF95A387498Q33298555-292FDA3F-90DE-4F02-996A-F96D85311263Q33314479-0896C3F5-C0A8-4F76-8D06-F51498D39698Q34324720-82AC1B71-4684-4ECC-A907-0FDD6AA0B1BEQ34336457-6DF72BB5-C423-46A2-AA6A-F6453D469560Q34370639-4D4E10F8-76D9-4BED-BDF6-FF8486CC0328Q34468312-D294A45A-BE56-4120-99A6-20FE910E0DA4Q34578743-5ECB13D6-D3A9-41C0-B8E5-CF0CA9EA05A1Q34825937-6F20B2B0-39F6-448A-9D55-E970E4C0901AQ35280915-C2388820-6824-463E-A998-59FC446462C9Q35666251-F908D56C-62B7-435C-B920-C25D54F60823Q35947048-A320131C-FA00-4BA6-ABFF-46A3584E0A66Q36155203-B0D1B4AE-6522-41B7-8BEE-525E1ACD07F6Q36164767-B8BE635D-8CB4-42DD-8D6B-40B643CA5BFBQ36222165-1DED569F-B3EF-43AF-969D-2E62B07FFD70Q36738573-54F02D5F-707B-4BC1-A780-D1496BF54967Q36844745-D950AE04-BCDA-4FE0-B0D6-8632EFACD91DQ36908396-E4E0E223-D866-45CE-AA39-95DF42625B4CQ36908432-0DCC9408-73CC-406E-AC72-3FFA39D88C54Q37038553-01C645B3-2D7F-41BF-B2FE-2066CD1B9B89Q37107294-C78C46E5-6CDC-477B-AC81-D4956EC84B88
P2860
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@ast
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@en
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@nl
type
label
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@ast
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@en
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@nl
prefLabel
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@ast
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@en
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@nl
P356
P1476
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
@en
P2093
Martinez-Yamout MA
P304
P356
10.1006/JMBI.2000.4207
P407
P577
2000-12-01T00:00:00Z