Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain
about
ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppressionHistone methyltransferases: novel targets for tumor and developmental defectsThe interplay of histone modifications - writers that readCrystal structure of human BS69 Bromo-ZnF-PWWP reveals its role in H3K36me3 nucleosome bindingA new class of multimerization selective inhibitors of HIV-1 integraseRetroviral integration: Site matters: Mechanisms and consequences of retroviral integration site selectionRetroviral DNA IntegrationMultivalent engagement of TFIID to nucleosomes.Histone-binding domains: strategies for discovery and characterization.Molecular mechanisms of retroviral integration site selection.Psip1/Ledgf p75 restrains Hox gene expression by recruiting both trithorax and polycomb group proteins.The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase.TOX4 and NOVA1 proteins are partners of the LEDGF PWWP domain and affect HIV-1 replicationA novel microscopy-based high-throughput screening method to identify proteins that regulate global histone modification levels.Towards understanding methyllysine readout.Histones: at the crossroads of peptide and protein chemistry.Traceless semisynthesis of a set of histone 3 species bearing specific lysine methylation marks.DNA Physical Properties and Nucleosome Positions Are Major Determinants of HIV-1 Integrase SelectivityHost Factors in Retroviral Integration and the Selection of Integration Target Sites.Towards a Safer, More Randomized Lentiviral Vector Integration Profile Exploring Artificial LEDGF Chimeras.Recognition of the nucleosome by chromatin factors and enzymesA PWWP Domain of Histone-Lysine N-Methyltransferase NSD2 Binds to Dimethylated Lys-36 of Histone H3 and Regulates NSD2 Function at Chromatin.The Competitive Interplay between Allosteric HIV-1 Integrase Inhibitor BI/D and LEDGF/p75 during the Early Stage of HIV-1 Replication Adversely Affects Inhibitor Potency.Bromo- and extraterminal domain chromatin regulators serve as cofactors for murine leukemia virus integration.Mind the methyl: methyllysine binding proteins in epigenetic regulation.LEDGINs, non-catalytic site inhibitors of HIV-1 integrase: a patent review (2006 - 2014).Histone target selection within chromatin: an exemplary case of teamwork.Integration site and clonal expansion in human chronic retroviral infection and gene therapy.Touch, act and go: landing and operating on nucleosomes.Allosteric control of mammalian DNA methyltransferases - a new regulatory paradigm.TALEN knockout of the PSIP1 gene in human cells: analyses of HIV-1 replication and allosteric integrase inhibitor mechanism.Enzymology of Mammalian DNA Methyltransferases.Binding of PHF1 Tudor to H3K36me3 enhances nucleosome accessibilityPWWP domains and their modes of sensing DNA and histone methylated lysines.A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT.DNA binding drives the association of BRG1/hBRM bromodomains with nucleosomes.ASH1L Links Histone H3 Lysine 36 Dimethylation to MLL Leukemia.Accessibility of the histone H3 tail in the nucleosome for binding of paired readers.Interactions between Retroviruses and the Host Cell Genome.Quantitative and Structural Assessment of Histone Methyllysine Analogue Engagement by Cognate Binding Proteins Reveals Affinity Decrements Relative to Those of Native Counterparts.
P2860
Q24338606-70F86CB6-4CB8-4030-AFCB-3F0A40AC88CBQ26775027-BD137FE8-248F-4970-8E17-A76F8BC0DDFFQ26782196-94D34A84-A6B0-4B19-B317-C87EFAC028B2Q27682593-2BA9788C-5574-4B5C-8E3D-F3B0EFA7966DQ27683994-0FBA8092-F551-4204-B3EF-DB8B4CCC5FC8Q28088514-C1F72D47-94A0-4BA2-AC4A-5CD010E9D092Q28596842-37F3B7EB-76EE-4B86-9C57-EE6FFB360231Q31139142-14C4D7BC-D026-40A0-BDF2-5C3B636CF1C0Q33905467-734FD41B-FC49-4B33-B811-BDA99C070417Q34249653-6351E2B3-2CAA-4FA1-9DED-7300259BE9A6Q34430521-40736A87-38E2-4165-AEB3-9F7A04993DB5Q34611548-300B58DD-68C2-4555-B042-D4EC1FDD8610Q35060475-0B1D45A7-4B25-4AD8-A9A2-B5B0B5BC06EEQ35066149-847AF24B-6421-479D-AE51-E2F7071AFDE9Q35146397-77B690A3-F558-4FD5-8943-831867B3A582Q35229609-7E245E36-C8DA-465F-865A-98F369205C6DQ35557387-DF6934D7-C2FA-4AF6-BD33-C18F9D389C8EQ35663664-62018893-D269-4851-9733-20058ACE7B25Q35916677-398F3649-28E3-449D-8733-AB80A92369AEQ36176014-DEF52B83-F108-4D14-A615-DF82B5228960Q36805622-8B6617C9-50BA-4161-B7BE-43D660549126Q36884617-345D4E3E-FDB2-48B7-8AFF-DEA3A7428FFBQ36922166-E0714F2B-542A-413D-B846-3A9DDD9B4F27Q37336436-F4C24516-C15B-499C-A9AB-3E38056070A5Q38180674-83B7A31A-AFA0-405A-92EF-DF2D1FA88FEBQ38199193-60BD9970-4507-4252-90E0-D79C91A939B2Q38212003-E7A167F1-45B3-43DB-B439-98CF2867CB79Q38264568-D0952F0F-0E24-4302-A134-5837B2A25F77Q38494694-441B7D7C-2D6D-41DA-8205-C6D9DA5E5F17Q38926847-5BACAC07-86EB-41BE-AADE-9E5A3F22C6CDQ38983286-C0A14B28-8890-4920-8B04-48698A69FF90Q39003524-93018CE6-2978-40E5-A34F-8D2AE3850360Q39138694-DB7B9EBB-B896-4373-9340-D221ADC5FF91Q39310736-7A5E3F69-8CDE-4C2B-8E76-E9609AAED841Q39923243-269226EE-164B-4F0C-92C0-A33E875AF50CQ41077356-403A545A-CEC1-4B47-8A2E-C2479DA3D5A8Q41830627-3C7DF4E4-3994-4C8D-ADFA-0B61EC297CF0Q43573529-E206FA67-99E9-41F7-BF60-C0E0E437167BQ45874795-083EC9A6-2023-4370-973E-82FB712E1950Q46266907-ED4AE550-0EB7-4A9D-B17A-C5A33A63471F
P2860
Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain
description
2013 nî lūn-bûn
@nan
2013 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@ast
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@en
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@nl
type
label
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@ast
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@en
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@nl
prefLabel
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@ast
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@en
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@nl
P2093
P2860
P50
P3181
P356
P1476
Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain
@en
P2093
Frederik Ma van Schaik
Ht Marc Timmers
Rick van Nuland
P2860
P2888
P3181
P356
10.1186/1756-8935-6-12
P577
2013-05-08T00:00:00Z
P5875
P6179
1008960468