Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain - Wikidata - awgldk - TriplyDB

Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain

Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain

http://www.wikidata.org/entity/Q27678049

about

ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression Histone methyltransferases: novel targets for tumor and developmental defects The interplay of histone modifications - writers that read Crystal structure of human BS69 Bromo-ZnF-PWWP reveals its role in H3K36me3 nucleosome binding A new class of multimerization selective inhibitors of HIV-1 integrase Retroviral integration: Site matters: Mechanisms and consequences of retroviral integration site selection Retroviral DNA Integration Multivalent 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 replication A 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 Selectivity Host 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 enzymes A 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 accessibility PWWP 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-3F0A40AC88CB Q26775027-BD137FE8-248F-4970-8E17-A76F8BC0DDFF Q26782196-94D34A84-A6B0-4B19-B317-C87EFAC028B2 Q27682593-2BA9788C-5574-4B5C-8E3D-F3B0EFA7966D Q27683994-0FBA8092-F551-4204-B3EF-DB8B4CCC5FC8 Q28088514-C1F72D47-94A0-4BA2-AC4A-5CD010E9D092 Q28596842-37F3B7EB-76EE-4B86-9C57-EE6FFB360231 Q31139142-14C4D7BC-D026-40A0-BDF2-5C3B636CF1C0 Q33905467-734FD41B-FC49-4B33-B811-BDA99C070417 Q34249653-6351E2B3-2CAA-4FA1-9DED-7300259BE9A6 Q34430521-40736A87-38E2-4165-AEB3-9F7A04993DB5 Q34611548-300B58DD-68C2-4555-B042-D4EC1FDD8610 Q35060475-0B1D45A7-4B25-4AD8-A9A2-B5B0B5BC06EE Q35066149-847AF24B-6421-479D-AE51-E2F7071AFDE9 Q35146397-77B690A3-F558-4FD5-8943-831867B3A582 Q35229609-7E245E36-C8DA-465F-865A-98F369205C6D Q35557387-DF6934D7-C2FA-4AF6-BD33-C18F9D389C8E Q35663664-62018893-D269-4851-9733-20058ACE7B25 Q35916677-398F3649-28E3-449D-8733-AB80A92369AE Q36176014-DEF52B83-F108-4D14-A615-DF82B5228960 Q36805622-8B6617C9-50BA-4161-B7BE-43D660549126 Q36884617-345D4E3E-FDB2-48B7-8AFF-DEA3A7428FFB Q36922166-E0714F2B-542A-413D-B846-3A9DDD9B4F27 Q37336436-F4C24516-C15B-499C-A9AB-3E38056070A5 Q38180674-83B7A31A-AFA0-405A-92EF-DF2D1FA88FEB Q38199193-60BD9970-4507-4252-90E0-D79C91A939B2 Q38212003-E7A167F1-45B3-43DB-B439-98CF2867CB79 Q38264568-D0952F0F-0E24-4302-A134-5837B2A25F77 Q38494694-441B7D7C-2D6D-41DA-8205-C6D9DA5E5F17 Q38926847-5BACAC07-86EB-41BE-AADE-9E5A3F22C6CD Q38983286-C0A14B28-8890-4920-8B04-48698A69FF90 Q39003524-93018CE6-2978-40E5-A34F-8D2AE3850360 Q39138694-DB7B9EBB-B896-4373-9340-D221ADC5FF91 Q39310736-7A5E3F69-8CDE-4C2B-8E76-E9609AAED841 Q39923243-269226EE-164B-4F0C-92C0-A33E875AF50C Q41077356-403A545A-CEC1-4B47-8A2E-C2479DA3D5A8 Q41830627-3C7DF4E4-3994-4C8D-ADFA-0B61EC297CF0 Q43573529-E206FA67-99E9-41F7-BF60-C0E0E437167B Q45874795-083EC9A6-2023-4370-973E-82FB712E1950 Q46266907-ED4AE550-0EB7-4A9D-B17A-C5A33A63471F

P2860

Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain

http://www.wikidata.org/entity/Q27678049

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

P1433

Q27678049-AD3F799A-517F-496B-B947-21F11C209955

P1476

Q27678049-01E14EE5-7443-4FB4-8033-A79D8CDC52AE

P2093

Q27678049-786696F9-9D49-413C-8E07-59436B43FF30

Q27678049-8FBAB15B-E14F-49B1-AB51-1A070CAAACCD

Q27678049-B4552BCE-2B1F-4F6E-A8E1-E323162A66A5

P2860

Q27678049-048F823C-D8EF-4101-BDF6-5E61545251A8

Q27678049-076CEBBD-2BB5-4CAE-B5C6-B59F34182460

Q27678049-09E890D3-0ACF-4074-93F4-2E61EE26D58E

Q27678049-13EA5D24-4C1B-4FE8-B833-E9349DE9DF11

Q27678049-1962EDB1-B558-411D-98D1-1EFC9819D5D7

Q27678049-1FCC8B6E-BE94-4B90-B14D-46EF0E069915

Q27678049-2E12EFF0-018A-4656-978F-18175437DCE7

Q27678049-3030015A-5C4C-4583-B08F-57F71DE6A592

Q27678049-319A8612-382F-4EAD-B848-7A1A795AC574

Q27678049-33554CB2-87E8-4947-B26B-88F12FAF04B6

P2888

Q27678049-563FD1FE-FB65-41FA-A872-4C028BE6EC6E

P304

Q27678049-6D2A8EBA-0487-4FB1-8335-AC572D8B9F53

P31

Q27678049-2F4DFD70-D4C0-4B00-BA97-F2A37238979F

P3181

Q27678049-DD91C2AB-B95B-4A7D-83A9-1D9055340E8D

P356

Q27678049-E0208E14-6F44-44A8-B057-871DC08F106B

P433

Q27678049-536B3A58-BCA5-4C92-9946-615094F685DD

P478

Q27678049-C5FC7236-6534-43D2-B318-3FEE82E4F3C9

P50

Q27678049-1F301178-3CE2-42A5-9E7E-0C48BE4DD999

Q27678049-23B64DD9-AA5C-49D5-81C9-87BCA45659A0

Q27678049-915FC38A-3150-415B-84E1-6F25A2208171

Q27678049-DB748EBD-4847-42FA-B3D1-6558D0275980

Q27678049-F3B37F47-11DB-484B-9B99-EFA4D1AE8080

P577

Q27678049-F9A10CA6-A27B-4288-9965-3B98017721CC

P5875

Q27678049-F08BB5C1-B3A6-4CEE-B4FE-82A6CC99B825

P6179

Q27678049-864C272F-4514-44B2-A08C-484CE82508FC

P698

Q27678049-CC7ABDE6-0211-4D37-AF50-E7C1C4EA2F53

P932

Q27678049-CDF9B8A7-FC2D-4082-9BBA-785349DF30A2

P3181

P356

P1433

Epigenetics & Chromatin

P1476

Nucleosomal DNA binding drives ...... somes by the PSIP1-PWWP domain

@en

P2093

Frederik Ma van Schaik

http://www.w3.org/2001/XMLSchema#string

Ht Marc Timmers

http://www.w3.org/2001/XMLSchema#string

Rick van Nuland

http://www.w3.org/2001/XMLSchema#string

P2860

Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation

Crystal structure of the nucleosome core particle at 2.8 A resolution

Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.

Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4

Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers

The transcriptional co-activator LEDGF/p75 displays a dynamic scan-and-lock mechanism for chromatin tethering

Electrostatics of nanosystems: application to microtubules and the ribosome

On the attribution and additivity of binding energies

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Fast and accurate short read alignment with Burrows-Wheeler transform

P2888

P304

12

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2776910

http://www.w3.org/2001/XMLSchema#string

P356

10.1186/1756-8935-6-12

http://www.w3.org/2001/XMLSchema#string

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

6

http://www.w3.org/2001/XMLSchema#string

P50

Marieke Simonis

Sebastiaan van Heesch

P577

2013-05-08T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

236665036

http://www.w3.org/2001/XMLSchema#string

P6179

1008960468

http://www.w3.org/2001/XMLSchema#string

P698

23656834

http://www.w3.org/2001/XMLSchema#string

P932

3663649

http://www.w3.org/2001/XMLSchema#string