Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding. - Wikidata - wikimedia - TriplyDB

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

http://www.wikidata.org/entity/Q37358082

about

Accessing DNA damage in chromatin: Preparing the chromatin landscape for base excision repair Post-translational modifications of histones that influence nucleosome dynamics Mechanisms of Histone Deacetylase Inhibitor-Regulated Gene Expression in Cancer Cells The CENP-A nucleosome: a battle between Dr Jekyll and Mr Hyde Structural characterization of H3K56Q nucleosomes and nucleosomal arrays Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes Structure and organization of chromatin fiber in the nucleus Chromatin-to-nucleoprotamine transition is controlled by the histone H2B variant TH2B Chemical and biological tools for the preparation of modified histone proteins Application of the protein semisynthesis strategy to the generation of modified chromatin Chemical and semisynthesis of posttranslationally modified proteins.Internal modifications in the CENP-A nucleosome modulate centromeric dynamics.Synthesis of histone H3 proteins by a thioacid capture ligation strategy.Acetylation-deacetylation of the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its transcriptional activity and nucleocytoplasmic localization Preparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes.Chemical and biochemical approaches in the study of histone methylation and demethylation A structural perspective on the where, how, why, and what of nucleosome positioning.Scratching the (lateral) surface of chromatin regulation by histone modifications.Local geometry and elasticity in compact chromatin structure.Differential contributions of histone H3 and H4 residues to heterochromatin structure.Histone fold modifications control nucleosome unwrapping and disassembly.Histones: at the crossroads of peptide and protein chemistry.A quantitative model of nucleosome dynamics.Histone core phosphorylation regulates DNA accessibility.Histone Acetylation near the Nucleosome Dyad Axis Enhances Nucleosome Disassembly by RSC and SWI/SNF.Autoacetylation of the MYST lysine acetyltransferase MOF protein Regulation of the nucleosome unwrapping rate controls DNA accessibility.Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamics Divergent Residues Within Histone H3 Dictate a Unique Chromatin Structure in Saccharomyces cerevisiae A reversible protection strategy to improve Fmoc-SPPS of peptide thioesters by the N-Acylurea approach.Site-specific acetylation of the proteasome activator REGγ directs its heptameric structure and functions.ATP-dependent nucleosome unwrapping catalyzed by human RAD51 Histone tails: ideal motifs for probing epigenetics through chemical biology approaches.Dynamics of histone H3 acetylation in the nucleosome core during mouse pre-implantation development.Mechanism(s) of SWI/SNF-induced nucleosome mobilization Sequence-dependent thymine dimer formation and photoreversal rates in double-stranded DNA Evidence that nucleosomes inhibit mismatch repair in eukaryotic cells Chemical approaches for studying histone modifications.Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.Spreading chromatin into chemical biology.

P2860

Q26828361-8B8DAF49-5840-4D25-95D2-2B4D096B90FD Q26852536-5E1006C2-832C-4E61-A58B-8839D98CAB52 Q27015931-B9C9026F-34B5-428A-8033-0206C447748C Q27022631-BC7688BA-1C3B-4FA1-8EC2-5876291E4683 Q27659174-3E3ADD1B-4C83-45F1-814A-A12A14403A3B Q27676304-568A5536-07AC-443A-9D09-A762A2AB2A6F Q28080958-133C8458-6EC1-4772-90F7-8F9F33C52596 Q28505400-1B11B53F-632A-44A8-9F0C-F7DE739C8F33 Q28829535-EEF7F0F2-C0BF-4904-840B-E0581A626983 Q28831322-E3A4B1A0-764D-4CBD-8591-847A1BBA0AFF Q30415911-C15E398F-53C5-4B67-90F9-CEBFDB66D1E3 Q30843972-BA963B2E-EF25-4994-94BD-A040A08981FD Q33758293-783DBBDC-4F16-4D14-AA08-7E21C5AFF0BA Q33783238-283F545B-7E78-4BB0-BB80-84E1BE2FEE59 Q33817639-EF5EB27B-34DB-40DF-B93C-40A9777DF82F Q34030702-8B36017F-FD29-47D2-B7A5-CC7AAD13D864 Q34104251-09AA957E-497A-4255-851B-9F28A99362B6 Q34348859-D4164053-6F5B-47D3-90AD-2B8DB67B237B Q34398588-847F8A43-8F48-46C6-BA79-55512A698E2F Q35065523-D2876EEE-C286-4ECE-8853-DF50F20C5251 Q35149617-C50FF16A-F6F5-4947-97C8-E569D14227AC Q35229609-99E1ED98-9980-4F41-B991-DD10AFDA00D8 Q35447437-10864057-234F-4796-A941-9627C9EBA2DD Q36049970-450FB0A6-802E-4A75-82D5-AB74BCC21D7F Q36234274-CD62DB41-3750-419A-A7E5-0B31B7CDD92D Q36318753-7C18474A-174F-48DC-AFC6-D963B011815B Q36368740-4663ADFE-CF00-4C1F-9342-D7F71638BEA0 Q36379445-F0D84505-5E1B-4A55-AA23-5EB310B5807E Q36429828-7ECC400F-4032-4142-8DC1-39735F431CF6 Q36571620-BDDF060D-5A55-4723-91EE-02A445D786B5 Q36910088-DF030E93-D3B4-4BA4-855F-7BD83805F3D4 Q37122015-8673686B-229F-47B6-A117-C8F319E4D8B3 Q37139778-FEA9A865-AB62-42A5-8458-04C1473B1420 Q37187442-ED8345A0-E3CF-4028-A208-C5D5F4EE73F7 Q37208541-83390EC8-AFBE-4F18-8FB5-5C98077445BA Q37274414-A199BA53-0C34-49F6-BFC6-65362FCC4D9F Q37446019-BDCC93E0-B461-43AB-A0CF-F50A13656469 Q37690523-F7C4FE1D-F332-4F48-8F02-8F3160BF4BFD Q37734360-9FB33F71-B074-4BFA-8B68-B8C781784BB4 Q37829703-4A52D20B-C658-46BE-AE91-352CABD75D2F

P2860

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

http://www.wikidata.org/entity/Q37358082

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 11 June 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

@en

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

@nl

type

label

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

@en

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

@nl

prefLabel

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

@en

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding.

@nl

P1433

Q37358082-9FC48344-6DD2-4A11-965C-352C2BC7355F

P1476

Q37358082-7BD03A3A-EE76-4EB3-A3C5-DEB18505C67A

P2093

Q37358082-3850610B-3497-4F31-8173-0308D57F02E0

Q37358082-46109335-88F5-4641-A62F-CF2C9FE35F71

Q37358082-4ACBA9E1-0882-453E-ACB3-0CD10CAA3F40

Q37358082-5DAD2558-895C-4239-9EDC-086A97E2BD21

Q37358082-951AFF04-96A6-43D8-9E50-14317ED8F30D

Q37358082-9D364497-0B7C-457A-B99F-C920B4A679CB

Q37358082-D44DB98A-BF61-47DB-BF52-34D1EA0068C4

Q37358082-D991825C-170C-4A83-B5A9-AE2B6BD96C64

P2860

Q37358082-01463A45-A437-4806-9CA8-E1A45B3A1186

Q37358082-01A5210B-E784-4551-94EF-D1979B166CA7

Q37358082-025BA58D-058B-42FD-8339-E7DD4B5063DC

Q37358082-0D6DCFA1-E02D-455B-9675-F33FCAC12C3E

Q37358082-11F33A6F-28B9-4640-86B3-8BD392A6DD28

Q37358082-180939EE-C0B1-487A-82F1-EFDF02BD8829

Q37358082-33DF526E-8431-4622-B9C0-1B60E4CDC55C

Q37358082-34777BD6-9EF3-4339-872B-58837B15085C

Q37358082-44914C52-2CEF-4E2B-8611-6F9F93EA10E7

Q37358082-4842B48E-DEAF-45B2-8B12-2D0684B0F87D

P304

Q37358082-19937003-0F55-45B9-9EFA-A46E153F3508

P31

Q37358082-1E8E0C06-451E-4BA0-83F4-4C4C675C52B5

P356

Q37358082-88A7D73E-58AA-455E-980C-4E02C0A44D88

P407

Q37358082-7E71BAE9-C23C-40D8-9B92-4FDBCBC97062

P433

Q37358082-45BB1B92-7AD6-4B9A-BF72-E7805EA6ABCA

P478

Q37358082-6A7F2ABD-ADAA-4B55-80B6-0D4C0097C2A1

P50

Q37358082-BF81A6CE-F0D9-4D15-B9C9-D63FA3D861DF

P577

Q37358082-0CDA7961-0F2D-4E9C-B26D-D2195987F617

P698

Q37358082-607E7A39-62EC-4E56-9FE0-548BB003B9A8

P932

Q37358082-8EE667EF-CB15-4B10-8105-16E900B81E59

P356

JBC.M109.003202

P1433

Journal of Biological Chemistry

P1476

Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding

@en

P2093

Alex M Mooney

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

Annick Edon

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

Jonathan W Picking

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

Justin A North

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

Michael G Poirier

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

Mridula Manohar

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

Richard Fishel

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

Robin J Nakkula

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

P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

A genomic code for nucleosome positioning

Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions

The language of covalent histone modifications

Chromatin modifications and their function

Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms.

Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II.

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers

Histone H4-K16 acetylation controls chromatin structure and protein interactions

Histone and chromatin cross-talk

P304

23312-23321

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

P31

scholarly article

P356

10.1074/JBC.M109.003202

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

P407

P433

35

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

P478

284

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

P50

Jennifer J Ottesen

P577

2009-06-11T00:00:00Z

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

P698

19520870

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

P932

2749105

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