Multivalent recognition of histone tails by the PHD fingers of CHD5 - Wikidata - awgldk - TriplyDB

Multivalent recognition of histone tails by the PHD fingers of CHD5

Multivalent recognition of histone tails by the PHD fingers of CHD5

http://www.wikidata.org/entity/Q34352597

about

Role of CHD5 in human cancers: 10 years later Structural basis for histone mimicry and hijacking of host proteins by influenza virus protein NS1 Chd5 requires PHD-mediated histone 3 binding for tumor suppression Application of the protein semisynthesis strategy to the generation of modified chromatin Differential expression and sex chromosome association of CHD3/4 and CHD5 during spermatogenesis The tumor suppressor chromodomain helicase DNA-binding protein 5 (CHD5) remodels nucleosomes by unwrapping.Chd5 orchestrates chromatin remodelling during sperm development.Architects of the genome: CHD dysfunction in cancer, developmental disorders and neurological syndromes A phylogenetic study of SPBP and RAI1: evolutionary conservation of chromatin binding modules.Histones: at the crossroads of peptide and protein chemistry.The chromatin remodeling factor CHD5 is a transcriptional repressor of WEE1.The chromatin remodeler chd5 is necessary for proper head development during embryogenesis of Danio rerio.Reading between the Lines: "ADD"-ing Histone and DNA Methylation Marks toward a New Epigenetic "Sum".Multivalent histone engagement by the linked tandem Tudor and PHD domains of UHRF1 is required for the epigenetic inheritance of DNA methylation.The epigenetic modifier CHD5 functions as a novel tumor suppressor for renal cell carcinoma and is predominantly inactivated by promoter CpG methylation.Reader domain specificity and lysine demethylase-4 family function.Epigenetic silencing of CHD5, a novel tumor-suppressor gene, occurs in early colorectal cancer stages.The Chromodomain Helicase DNA-Binding Chromatin Remodelers: Family Traits that Protect from and Promote Cancer.Deciphering post-translational modification codes.Mind the methyl: methyllysine binding proteins in epigenetic regulation.Interpreting the language of histone and DNA modifications.Structural biology-based insights into combinatorial readout and crosstalk among epigenetic marks.A brief histone in time: understanding the combinatorial functions of histone PTMs in the nucleosome context.Structural aspects of small-molecule inhibition of methyllysine reader proteins.Chd5 Regulates MuERV-L/MERVL Expression in Mouse Embryonic Stem Cells Via H3K27me3 Modification and Histone H3.1/H3.2.The tumor suppressor Chd5 is induced during neuronal differentiation in the developing mouse brain.Covalent Modifications of Histone H3K9 Promote Binding of CHD3.Dysregulation of Sirtuin 2 (SIRT2) and histone H3K18 acetylation pathways associates with adverse prostate cancer outcomes.Heritable Sperm Chromatin Epigenetics: A Break to Remember.

P2860

Q27006929-B66524E7-CFD6-4CF0-ADC7-7B4FBF99C521 Q27690279-9E924BBD-598A-42A8-816B-2A4B74CDAB2F Q28593132-98277927-2782-4926-AC8B-03FAAEAEF2DE Q28831322-D3A022A1-019D-4591-878F-44A7865C9AB9 Q33646049-0CA29CEF-9534-4619-8BB2-366330BDD66A Q33947091-F72C55FF-D69A-4CF2-A654-FBD6A5D07AD9 Q34117192-52EBC5CC-C771-4DFA-87B7-F66DA73E4421 Q34520690-D1B76DAB-D0C2-4526-A946-BA43296CD8B3 Q35036841-6E593202-DD74-4338-AF12-DCEFC4F16D0A Q35229609-B7B84FB9-2292-40EB-8D94-AADF1D200170 Q35270535-C9390754-8075-44B4-A309-CB526AEB756C Q35982052-F92B0E90-1807-45A1-8679-CFEB404E513C Q36703430-AF8F401C-F2F4-498C-BEA3-9E11652DFDE0 Q36948989-DECF8B29-67AB-4518-AAF0-A6F941F0CC71 Q37225359-5D0080AC-4A94-406C-B763-EDE519E007A1 Q37421645-2382F264-0449-46A0-84D5-C14B74B735FF Q37626242-C8A558CA-D074-405C-861A-EEC1AAA20491 Q37735355-E2A58E60-A061-4328-AEEB-FA4F531DBF97 Q38080975-5523AEF7-CC4C-42A1-8D3C-42E6D0DC0520 Q38180674-33BFEF71-7BDE-4ECE-B8F4-630DCC6CABCD Q38196193-6B0FDDBE-A7DE-4132-8FBB-173E28973779 Q38205661-E943FE0B-811A-429A-9233-09CA20E12A01 Q38551630-57D98A8F-7B1D-4A89-B586-CB4720AEFDD1 Q38826160-7D29C953-64C4-4059-AF00-A16D0A822E18 Q41374920-74284BAB-A1CB-477C-AF30-406C1D864B9A Q41786481-FFB0432D-9F13-4564-BF60-F063F8548B39 Q42381392-4FB09E7A-3F71-4D17-A642-21977598E47D Q47144438-1E4F5310-1625-429D-BD81-CCCD5433B9C4 Q47445113-E4F722C8-8129-485D-963C-D0FD3302154F

P2860

Multivalent recognition of histone tails by the PHD fingers of CHD5

http://www.wikidata.org/entity/Q34352597

description

2012 nî lūn-bûn

@nan

2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Multivalent recognition of histone tails by the PHD fingers of CHD5

@ast

Multivalent recognition of histone tails by the PHD fingers of CHD5

@en

Multivalent recognition of histone tails by the PHD fingers of CHD5

@nl

type

label

Multivalent recognition of histone tails by the PHD fingers of CHD5

@ast

Multivalent recognition of histone tails by the PHD fingers of CHD5

@en

Multivalent recognition of histone tails by the PHD fingers of CHD5

@nl

prefLabel

Multivalent recognition of histone tails by the PHD fingers of CHD5

@ast

Multivalent recognition of histone tails by the PHD fingers of CHD5

@en

Multivalent recognition of histone tails by the PHD fingers of CHD5

@nl

P1433

Q34352597-8030889B-7790-4025-AB81-3E4530367BCB

P1476

Q34352597-D31FB905-889B-4F29-A35C-89AC2B614537

P2093

Q34352597-2B8CD109-06BB-4A9C-B698-6DF799473276

Q34352597-6F2EC3F0-D226-4483-9AFC-5EEF76DCBE12

Q34352597-89E20AA4-E753-4243-9282-5430DD0E08B6

Q34352597-F4988F76-DDEE-46EF-8B8F-73FFEFBD52DF

P2860

Q34352597-03DE57EA-E3C3-4EAB-AFCE-9E634F56B80A

Q34352597-046DCE9E-9A4B-4265-AE23-9F624B9BE846

Q34352597-05320FD4-EBF3-4B62-AEED-6C65F6DD8385

Q34352597-0A890523-923D-4257-AC60-72FC7A300EE3

Q34352597-0E14589B-DA46-488A-A815-5E9471AFFA16

Q34352597-1DB17796-2D20-4B61-A680-16402358A554

Q34352597-213A4AF2-654D-457D-B764-3EFFDBDB051D

Q34352597-2309841A-4B8A-44C0-B923-57A5BA4145AB

Q34352597-26229E72-5EE8-4C5B-9001-8A241F32595A

Q34352597-27933D70-7C3C-4C55-93F2-E900294EB678

P304

Q34352597-4013C754-979B-469E-9453-DEA16E39FF81

P31

Q34352597-10CDDE52-5CDE-47EF-B76A-63DE10CA4948

P356

Q34352597-F5EDFA55-317B-41C8-B663-CA3129C25B67

P407

Q34352597-62052EAE-259B-40A0-8420-4CFA0F2240C3

P433

Q34352597-32FC4C66-1562-4F6F-8D5D-C649124BAD1B

P478

Q34352597-1296A4CD-E54D-4212-85BA-DDBBCE0FC870

P50

Q34352597-444520F0-9A9A-4614-8F30-718122D29442

Q34352597-7C9E95F4-1344-4BDD-964B-2CB9F2545315

P577

Q34352597-78CD88EF-AA65-4A00-B909-90FD7FA7EA0D

P698

Q34352597-FCF87515-3456-4777-8DBE-0A136A9E2876

P932

Q34352597-3CF73A63-B986-4F2C-AC3B-6D506EF5A144

P356

P1433

P1476

Multivalent recognition of histone tails by the PHD fingers of CHD5

@en

P2093

John M Denu

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

Rajini Srinivasan

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

Samuel S Oliver

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

Tatiana G Kutateladze

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

P2860

Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions

TRIM24 links a non-canonical histone signature to breast cancer

CHD5, a brain-specific paralog of Mi2 chromatin remodeling enzymes, regulates expression of neuronal genes

Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b

The genomic complexity of primary human prostate cancer

Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation.

Yng1 PHD Finger Binding to H3 Trimethylated at K4 Promotes NuA3 HAT Activity at K14 of H3 and Transcription at a Subset of Targeted ORFs

Engineering a protein scaffold from a PHD finger

Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression

Plant Homeodomain (PHD) Fingers of CHD4 Are Histone H3-binding Modules with Preference for Unmodified H3K4 and Methylated H3K9

P304

6534-6544

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

P31

scholarly article

P356

10.1021/BI3006972

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

P407

P433

33

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

P478

51

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

P50

Catherine Musselman

P577

2012-08-08T00:00:00Z

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

P698

22834704

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

P932

3518043

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