The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association. - Wikidata - awgldk - TriplyDB

The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association.

The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association.

http://www.wikidata.org/entity/Q42701117

about

New insights into nucleosome and chromatin structure: an ordered state or a disordered affair?Structural dynamics of nucleosomes at single-molecule resolution Toward convergence of experimental studies and theoretical modeling of the chromatin fiber An advanced coarse-grained nucleosome core particle model for computer simulations of nucleosome-nucleosome interactions under varying ionic conditions Active chromatin and transcription play a key role in chromosome partitioning into topologically associating domains.Structure and organization of chromatin fiber in the nucleus Chemical and biological tools for the preparation of modified histone proteins Application of the protein semisynthesis strategy to the generation of modified chromatin Nucleosome Histone Tail Conformation and Dynamics: Impacts of Lysine Acetylation and a Nearby Minor Groove Benzo[a]pyrene-Derived Lesion Mof-associated complexes have overlapping and unique roles in regulating pluripotency in embryonic stem cells and during differentiation.A distinct switch in interactions of the histone H4 tail domain upon salt-dependent folding of nucleosome arrays Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions.The role of histone tails in the nucleosome: a computational study.Modulation of Higher Order Chromatin Conformation in Mammalian Cell Nuclei Can Be Mediated by Polyamines and Divalent Cations.Mechanisms of x chromosome dosage compensation.ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.Transcriptional control of a whole chromosome: emerging models for dosage compensation.Histones: at the crossroads of peptide and protein chemistry.Dosage compensation in Drosophila.Histone H4 acetylation required for chromatin decompaction during DNA replication.Finding a balance: how diverse dosage compensation strategies modify histone h4 to regulate transcription Histone H4 K16Q mutation, an acetylation mimic, causes structural disorder of its N-terminal basic patch in the nucleosome.A brief review of nucleosome structure Intra- and inter-nucleosomal interactions of the histone H4 tail revealed with a human nucleosome core particle with genetically-incorporated H4 tetra-acetylation Deacetylation of H4-K16Ac and heterochromatin assembly in senescence.Regulation of the H4 tail binding and folding landscapes via Lys-16 acetylation.Distinct contributions of MSL complex subunits to the transcriptional enhancement responsible for dosage compensation in Drosophila.The Influence of Ionic Environment and Histone Tails on Columnar Order of Nucleosome Core Particles Expression, purification and proteomic analysis of recombinant histone H4 acetylated at lysine 16.Histone acetylation dependent energy landscapes in tri-nucleosome revealed by residue-resolved molecular simulations Acetylation Mimics Within a Single Nucleosome Alter Local DNA Accessibility In Compacted Nucleosome Arrays.An H4K16 histone acetyltransferase mediates decondensation of the X chromosome in C. elegans males.H4K16 acetylation marks active genes and enhancers of embryonic stem cells, but does not alter chromatin compaction.Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions Uncovering the forces between nucleosomes using DNA origami.Intra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure.Structure and function of active chromatin and DNase I hypersensitive sites.Mapping physical interactions within chromatin by proteomic approaches.The role of the nucleosome acidic patch in modulating higher order chromatin structure.Establishing epigenetic domains via chromatin-bound histone modifiers.

P2860

Q24626585-CA70C664-F45F-4C81-AAA6-D0352E5B8E67 Q26822880-F90CDC46-9B91-4538-96B5-4810424AB168 Q26852454-F8EAE4A6-F53C-4D34-9AE7-F32A05941C17 Q27319987-FF9A95E0-5C85-4E70-B9C7-63BB26D2E1B9 Q27321750-4D92560F-1518-4CC9-8141-29F444925455 Q28080958-D920E9BE-E909-4A3D-A097-0DEAE7AFCBA4 Q28829535-8D163DEA-8E7A-4AEF-9C80-2D6CF8E441E6 Q28831322-69AC86CA-7E1B-4F6A-9DA5-A0CEAE9111F8 Q30855026-6A26AB42-E04C-4B75-ABDA-B24B0DF13725 Q33764210-BD3BA7CA-BDB0-4E22-A357-73771B9B31B6 Q34245171-2328E306-D596-4FAD-B0D7-8724D7173211 Q34634124-8D7A8673-1035-4C2D-889E-413BA3694ACE Q34727591-B336D14D-403A-4FF6-97AA-A9019DBCF2AF Q34807927-B364B9E8-98C5-4492-81FF-DC695D5A6E34 Q35002469-506A497D-BAA2-4A80-B09D-AC841DA6E10E Q35091749-D0B3984E-B1BD-442C-BECB-3C74A32FFA92 Q35125239-4FE457BE-EE16-4532-B3F0-54061976C27E Q35229609-50A0E905-A7C3-43FC-B24C-4A5778222148 Q35663949-B8CB44D2-D8F1-4ABD-B39F-8FA6287EA4C9 Q35902773-1E3CE4F1-392D-4C2E-8F6B-3CB9E89D0994 Q35910252-9F59E02B-76A6-49B4-82F9-58DCD81A8E53 Q36084173-A3AC8AC5-BD0F-44FD-8B8F-14D400CC0720 Q36137489-7BBFAB96-03D4-4F99-835B-6C8FBB8BDCE8 Q36320931-6A03D9F3-C22D-4285-83BD-82AC6286B049 Q36367732-BC31460E-2763-4C9D-8474-6E90DE53064B Q36397739-27B617A9-8B9C-4A4E-ACC7-377B5943909A Q36478118-8844CFB4-6256-40FD-81FD-3D016AF28E05 Q36850214-4142274D-1789-480D-BC9E-3724B82CB5CA Q37166317-02B9BAC1-5078-4C76-A39C-A6F2CF794AE9 Q37307109-DCE53557-BE93-4B47-B944-D1960D7EF221 Q37314859-F9C45B24-A204-419E-A3C2-87E8E7233202 Q37349779-188D54BB-4C9F-45FE-9CFD-92E1A31673DE Q37358012-843B28C4-F142-4EDF-8970-C4907530A82C Q37415617-4DBE1363-4DC1-46F7-B1AF-0EC3F96A5696 Q37603851-2AE9B1CC-548A-431D-B377-8FD129E993D7 Q37610823-7FFD466E-8786-4F1C-B65E-EF990937BB21 Q37866375-20052702-6953-482D-936B-9B62A5C08987 Q38011665-9F8C8F9D-3E10-43E3-AC32-28B8A0F1C4F5 Q38085143-D1E736A8-8DD7-412F-B0C1-DC593A9540A8 Q38137246-21913CDF-6DEE-4F0C-B0EE-51B4F5BEFDDA

P2860

The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association.

http://www.wikidata.org/entity/Q42701117

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

The effects of histone H4 tail ...... folding and self-association.

@en

The effects of histone H4 tail ...... folding and self-association.

@nl

type

label

The effects of histone H4 tail ...... folding and self-association.

@en

The effects of histone H4 tail ...... folding and self-association.

@nl

prefLabel

The effects of histone H4 tail ...... folding and self-association.

@en

The effects of histone H4 tail ...... folding and self-association.

@nl

P1433

Q42701117-BCF5105D-9A14-474C-A350-2F37DCE41F89

P1476

Q42701117-EEBC3666-DD37-4F08-8022-BB219429B37E

P2093

Q42701117-03C03030-2FB9-44EF-98F7-C9CFCBC58500

Q42701117-587DBB08-6583-4223-BEAE-2F2C05B8D567

Q42701117-60E0D8B6-14DA-471B-B74D-3008EEA5DCF6

Q42701117-D7EF9D3E-0222-410D-B300-625D1E03F600

Q42701117-DECE61AB-044E-44FD-A2C0-82466C2A213E

Q42701117-FBD8A041-FC74-41D6-986A-AF3A4406EB13

P2860

Q42701117-046E7D93-D343-430B-B4AF-7D20CF46F04C

Q42701117-0563E127-BD71-4ED9-9EDF-207B48BA836F

Q42701117-0F517F00-D7C2-4CC8-9F0F-752B067DD652

Q42701117-114166A3-C7B7-4312-9089-BD5401C618B6

Q42701117-118C0016-920D-4A79-B70A-FAAF73304E32

Q42701117-1997830A-F674-4068-BE19-312DC8A4D057

Q42701117-1F4FEFC8-188F-493B-A437-966F657DF757

Q42701117-20F4BFD8-C202-47B8-A67A-3E1CE8B3F436

Q42701117-2AD6CEB1-B964-47B3-BC73-D368B9F424C5

Q42701117-2DEF1120-3015-4A27-8F90-1625DF011A96

P304

Q42701117-5E4C76B2-F429-4053-AA8E-1F1E2A73FD24

P31

Q42701117-60317104-BCB4-40F7-8BD5-2949D49B1657

P356

Q42701117-7A2276C6-59C6-4F54-91B7-754A2172CF67

P407

Q42701117-DFEF663E-9116-4169-BEFA-B9BCCB287AE9

P433

Q42701117-99461F35-74DE-4153-9197-C220C824010F

P478

Q42701117-7B54BAE4-5302-4E40-A589-4F434E9EE52C

P50

Q42701117-C52554E4-5D24-4735-BE3E-86B5FD3CF776

P577

Q42701117-A110CBE8-EAB0-40D6-A3D4-38A82D30A384

P5875

Q42701117-2381A5D5-B4C6-4C03-91FA-E157E26806EC

P698

Q42701117-537EF2FB-13FD-400A-8BE7-2B81E04BC091

P932

Q42701117-28C78AE4-2FF4-4F64-AB0D-B9782C809E67

P356

P1433

Nucleic Acids Research

P1476

The effects of histone H4 tail ...... n folding and self-association

@en

P2093

Abdollah Allahverdi

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

Curt A Davey

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

Lars Nordenskiöld

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

Nikolay Korolev

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

Renliang Yang

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

Yanping Fan

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

P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

EM measurements define the dimensions of the "30-nm" chromatin fiber: evidence for a compact, interdigitated structure

Asymmetries in the nucleosome core particle at 2.5 A resolution

Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution

Insights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with Inhibitors

Using soft X-rays for a detailed picture of divalent metal binding in the nucleosome

Structural insight into the sequence dependence of nucleosome positioning

Perturbations in nucleosome structure from heavy metal association

UCSF Chimera--a visualization system for exploratory research and analysis

Cracking the enigmatic linker histone code

P304

1680-1691

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

P31

scholarly article

P356

10.1093/NAR/GKQ900

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

P407

P433

5

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

P478

39

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

P50

P577

2010-11-02T00:00:00Z

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

P5875

47675602

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

P698

21047799

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

P932

3061077

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