Assays for the determination of structure and dynamics of the interaction of the chromodomain with histone peptides.
about
Specificity of the chromodomain Y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifsMolecular recognition of histone lysine methylation by the Polycomb group repressor dSfmbtTRIM24 links a non-canonical histone signature to breast cancerHistone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patternsDirect interaction between DNMT1 and G9a coordinates DNA and histone methylation during replicationEpigenetic virtues of chromodomainsMolecular implications of evolutionary differences in CHD double chromodomains.The plant homeodomain finger of RAG2 recognizes histone H3 methylated at both lysine-4 and arginine-2The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners.A stable transcription factor complex nucleated by oligomeric AML1–ETO controls leukaemogenesisHP1 recruits activity-dependent neuroprotective protein to H3K9me3 marked pericentromeric heterochromatin for silencing of major satellite repeatsChd5 requires PHD-mediated histone 3 binding for tumor suppressionDouble chromodomains cooperate to recognize the methylated histone H3 tailA homogeneous method for investigation of methylation-dependent protein-protein interactions in epigeneticsEpigenetics. Restricted epigenetic inheritance of H3K9 methylation.Specificity, propagation, and memory of pericentric heterochromatin.14-3-3 proteins recognize a histone code at histone H3 and are required for transcriptional activationHeterochromatin protein 1 forms distinct complexes to direct histone deacetylation and DNA methylationHeterochromatin Protein 1a (HP1a) partner specificity is determined by critical amino acids in the chromo shadow domain and C-terminal extensionMultimerization and H3K9me3 binding are required for CDYL1b heterochromatin associationDual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3.Systematic analysis of histone modification readout.Quantitative assessment of protein interaction with methyl-lysine analogues by hybrid computational and experimental approaches.Methods to identify and functionally analyze factors that specifically recognize histone lysine methylation.Epigenetics: Tools and Technologies.A Polycomb group protein complex with sequence-specific DNA-binding and selective methyl-lysine-binding activities.Methylation of lysine 9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1β with the nucleosome.Multimerization of Drosophila sperm protein Mst77F causes a unique condensed chromatin structure.
P2860
Q24308689-2D691272-8BE8-43C3-9723-77A8D0FC04E0Q24316968-97012217-043C-4F96-99DE-94A2204C034CQ24317243-C990585C-40F2-486B-9A2D-7B61F606FDEBQ24320777-852782B9-0A45-4433-A21A-8AEF08058278Q24322623-BBFD5740-A11B-40ED-9E52-D0D4EE330FABQ24675218-D6DDE70B-5C20-4B25-B8EC-0424E991AA48Q27016161-6AB224CE-7BB2-493A-93DF-EA0C5B46ACF5Q27644441-0C8E04BB-4CF4-4D13-86EC-ED228FF475C5Q27649107-B7720A73-B4BC-41A2-8009-E5434990E01EQ27667453-889065D3-44E3-4045-986B-FDA5CAD528D4Q27678844-2A8747B5-3983-43D4-A527-89932AE8D379Q28476760-51C7D5CC-9A49-4F0C-8B13-81D2FB103E96Q28593132-49C0DC78-C169-4CE4-8D56-EEBD32531DF7Q29614522-C8E72DDA-84D0-45DD-8A55-92B4D55A0042Q33608860-C919ABA6-88D7-4964-A562-1C7F02151870Q34470100-2CF8D324-7199-43B6-962B-91FFCB0B72ECQ34986658-9AF06C81-7A71-47F5-9E58-5E8CF505ED18Q36392006-3FD9FF50-A74F-4176-B8A9-2A7FC2F839D4Q37119648-01026E45-CEB0-4C1B-AAB4-73BF3FE75F78Q37311851-81F3DAE7-656B-4B41-B668-F8743875383BQ37454345-A7060D6E-421E-497F-BBCF-999A42C42773Q37592817-FE3F06C2-08B9-427C-A295-E1AEAEA88D8CQ38065114-5B5A9DCD-67CB-4F51-B808-ED2F67C10240Q40628134-6A74FF02-926E-4DE1-996C-0E152E461026Q41886987-1C1D94A7-8221-4E26-AA4B-556629CA0515Q42030420-30287637-49DA-41ED-B509-78F0A6CF7AEAQ42424377-408BB68E-8F5E-48DA-A985-077613FED4A0Q42564984-1BA435AB-0833-4D23-AD1F-56D97AC530F0Q42658978-59667FE6-6428-456B-940C-F7C44DD52153
P2860
Assays for the determination of structure and dynamics of the interaction of the chromodomain with histone peptides.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Assays for the determination o ...... odomain with histone peptides.
@ast
Assays for the determination o ...... odomain with histone peptides.
@en
type
label
Assays for the determination o ...... odomain with histone peptides.
@ast
Assays for the determination o ...... odomain with histone peptides.
@en
prefLabel
Assays for the determination o ...... odomain with histone peptides.
@ast
Assays for the determination o ...... odomain with histone peptides.
@en
P2093
P1476
Assays for the determination o ...... odomain with histone peptides.
@en
P2093
Sepideh Khorasanizadeh
Steven A Jacobs
Wolfgang Fischle
P304
P356
10.1016/S0076-6879(03)76009-1
P407
P577
2004-01-01T00:00:00Z