Functional connection between deimination and deacetylation of histones. - Wikidata - wikimedia - TriplyDB

Functional connection between deimination and deacetylation of histones.

Functional connection between deimination and deacetylation of histones.

http://www.wikidata.org/entity/Q37334003

about

Peptidylarginine deiminases in citrullination, gene regulation, health and pathogenesis Computer-aided Molecular Design of Compounds Targeting Histone Modifying Enzymes The role of epigenetics in resistance to Cisplatin chemotherapy in lung cancer Potential role for PAD2 in gene regulation in breast cancer cells.Probing the Roles of Calcium-Binding Sites during the Folding of Human Peptidylarginine Deiminase 4.Genome-wide analysis reveals PADI4 cooperates with Elk-1 to activate c-Fos expression in breast cancer cells.Citrullination of DNMT3A by PADI4 regulates its stability and controls DNA methylation Citrullination of histone H3 interferes with HP1-mediated transcriptional repression.HDAC1, HDAC4, and HDAC9 Bind to PC3/Tis21/Btg2 and Are Required for Its Inhibition of Cell Cycle Progression and Cyclin D1 Expression.Citrullination of inhibitor of growth 4 (ING4) by peptidylarginine deminase 4 (PAD4) disrupts the interaction between ING4 and p53 Autodeimination of protein arginine deiminase 4 alters protein-protein interactions but not activity.A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.Histone deacetylase inhibitors: clinical implications for hematological malignancies.Conservative Mechanisms of Extracellular Trap Formation by Annelida Eisenia andrei: Serine Protease Activity Requirement.Protein deiminases: new players in the developmentally regulated loss of neural regenerative ability.Protein Arginine Methylation and Citrullination in Epigenetic Regulation Epigenetic regulation of estrogen signaling in breast cancer Epigenetic mechanisms in multiple sclerosis: implications for pathogenesis and treatment The interplay between the lysine demethylase KDM1A and DNA methyltransferases in cancer cells is cell cycle dependent.Molecular Interplay between the Dimer Interface and the Substrate-Binding Site of Human Peptidylarginine Deiminase 4.Effective combination therapies in preclinical endocrine resistant breast cancer models harboring ER mutations.Epigenetics and gene expression.Histone arginine methylation.Epigenetics of estrogen receptor signaling: role in hormonal cancer progression and therapy.Arginine/lysine-methyl/methyl switches: biochemical role of histone arginine methylation in transcriptional regulation.The role of dietary histone deacetylases (HDACs) inhibitors in health and disease.PAD4: pathophysiology, current therapeutics and future perspective in rheumatoid arthritis.Histone Modifications and Cancer.PADI4 acts as a coactivator of Tal1 by counteracting repressive histone arginine methylation.A Critical Reappraisal of Neutrophil Extracellular Traps and NETosis Mimics Based on Differential Requirements for Protein Citrullination.Role of citrullination modification catalyzed by peptidylarginine deiminase 4 in gene transcriptional regulation.Protein arginine deiminase 4: a target for an epigenetic cancer therapy.Structural and Functional Impacts of ER Coactivator Sequential Recruitment.PAD4 regulates proliferation of multipotent haematopoietic cells by controlling c-myc expression Prostate Cancer Patients-Negative Biopsy Controls Discrimination by Untargeted Metabolomics Analysis of Urine by LC-QTOF: Upstream Information on Other Omics Development and use of clickable activity based protein profiling agents for protein arginine deiminase 4.PADI4 rs2240337 G>A polymorphism is associated with susceptibility of esophageal squamous cell carcinoma in a Chinese population.Rheumatoid arthritis and citrullination.Human Deiminases: Isoforms, Substrate Specificities, Kinetics, and Detection.

P2860

Q26991867-050F9B74-6442-4646-8069-8D1EC71FA2C7 Q28083849-FC54CE62-3728-4EBC-AE44-32371411A9A9 Q28387891-EED679FA-9197-4510-83C7-24050AA5D15C Q28728858-A0102FDA-F7BF-41C0-B61B-06F538990104 Q33729177-E75DFE93-59A8-40DB-808E-41B7E4BB5EA7 Q33926858-1C407708-030E-4589-9C05-A48C72C7B555 Q33983526-5D881F83-9A69-457F-A65B-8A339406553E Q34426561-10FB56A9-F622-4617-95E7-74DA037CFEBD Q34531716-F41C3BCC-13B4-4E70-88C5-914269191B40 Q34947947-EBD937CF-0DF8-45E9-9CCB-5E137DFE9F1B Q34969938-57397E26-2A37-484C-8308-D0741A39173C Q34990282-DF8DAABB-7B06-4468-B98E-8FD37B0E7A5F Q36001847-9BEA0EB3-136D-42B5-AB6A-749E2D01427C Q36077806-91504793-391A-4351-86DB-C6694FCC6B07 Q36623411-E1E3CED2-B876-4C24-A36B-5E4C6E19A02E Q36713555-0F146E01-5C25-4580-83D9-9EE13F13F6C3 Q36891892-0D84FDBD-141B-4A54-AF69-B9C44C367C04 Q36948933-472910FF-7058-439A-81E6-256AD359B8AA Q37644797-A1C264C2-EEB3-4DFE-8164-A73712B46E90 Q37648828-6AA124D7-4CBF-4088-8698-0796F74EA37A Q37688020-49029A52-C5A7-4FA6-8CDD-665C0AC98997 Q37749500-A554A751-D4F1-48DA-AFD2-916E7EA026F2 Q37809211-E5F14EDB-7825-4355-93A5-05BED8D0E61C Q37911312-8CD90224-342D-4CC7-9771-9EA5EF8037EC Q37962018-0CD19CF8-A025-4B5F-8B13-51230AD9316E Q38260795-813D946E-0280-45C7-BDD9-80C044437249 Q38747640-1248D309-7A09-4BA2-A292-7B8B673572A0 Q38796064-B8CD9642-316F-4C40-A602-A9461DB55630 Q38990455-B047BF6B-8DA3-4952-9C47-36750CD8245A Q39014892-185C744D-1656-4CA9-9BAC-BD925D754168 Q39283898-78622122-6DBE-40EC-A3E5-FFE2DEB82693 Q39668030-2B4AF90A-2410-479F-8C30-BA8A6CAA52B4 Q41596664-8916C1B8-D7BC-4B8A-AF30-B04DAA7459C5 Q42098686-440862D3-81B0-4C7E-82E2-6276C006842E Q42359959-22149BC1-C986-40EB-AD39-E2053B2CC826 Q42736960-13A2A994-EAF7-4005-8ACE-816F7F35D59B Q47124742-1E758328-54C0-49C0-BA82-AAC4841BBC85 Q47762707-41F1792D-5F4D-4F24-BCFB-4F737AE2B074 Q48005731-336C8B97-F6F0-4BE4-A3E8-5EE5D952B201

P2860

Functional connection between deimination and deacetylation of histones.

http://www.wikidata.org/entity/Q37334003

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 06 July 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Functional connection between deimination and deacetylation of histones.

@en

Functional connection between deimination and deacetylation of histones.

@nl

type

label

Functional connection between deimination and deacetylation of histones.

@en

Functional connection between deimination and deacetylation of histones.

@nl

prefLabel

Functional connection between deimination and deacetylation of histones.

@en

Functional connection between deimination and deacetylation of histones.

@nl

P1433

Q37334003-72086609-2459-4F7C-9010-39AEC38F6470

P1476

Q37334003-F6857C2E-4AA4-47F1-8EEF-23E63DED4343

P2093

Q37334003-0DF3E578-8845-4BDB-B602-59B8EED30B3D

Q37334003-1B586857-3CBC-4C2A-8830-959F1E200EEC

Q37334003-2E6C5403-3CBD-4786-8419-7E609386F037

Q37334003-7653F833-9100-458B-91FC-8992B7F137D3

Q37334003-E6270AE6-6809-43B1-B975-BC54B01718B6

P2860

Q37334003-0BB9FA75-7B9B-4F5C-9B33-B46EBDE8A766

Q37334003-101EED1B-5607-4681-9C11-B53090998404

Q37334003-10BB0419-CDC1-480D-84FE-97D062345D44

Q37334003-14B27467-EB88-4125-B8DA-D3072941B849

Q37334003-25655199-25E6-4237-A386-936B2B92CFAE

Q37334003-34E35857-2C22-4121-9580-A0797CE5E35C

Q37334003-35DCC809-193A-4AB2-B563-BC31EF8809D3

Q37334003-39A079BB-EB98-4FB1-8B76-C262F576775B

Q37334003-39E51BF9-DC86-43B5-8B0B-86C581145F8B

Q37334003-3AC47E38-6FDD-4BA4-ABBE-B753461D9294

P304

Q37334003-AC85ACF1-0F8C-4096-BA51-7658E0543E55

P31

Q37334003-6EF7F33A-E7B4-45B4-9C66-370FD4F50639

P356

Q37334003-9F9B858E-30C8-4AE9-9B69-E348ABD588CD

P407

Q37334003-C3797C26-ECD5-4B96-A16C-28E1E9E405F3

P433

Q37334003-153E59C2-C9C6-4472-9F97-91BDC6EE0B73

P478

Q37334003-D547F7E0-C09E-4D85-8B61-792E7C97DED3

P50

Q37334003-9137F421-BBE1-42E3-9B2C-87286ADA75C0

P577

Q37334003-7455BBE4-6813-4098-BAE9-39E95F21667F

P698

Q37334003-C4A6387A-EC8B-48B6-A998-8A4AB20985B2

P932

Q37334003-1DFEEC62-EF6C-4827-9426-67D289D6098E

P356

P1433

Molecular and Cellular Biology

P1476

Functional connection between deimination and deacetylation of histones.

@en

P2093

François Fuks

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

Hélène Denis

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

Michiyuki Yamada

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

Pascale Putmans

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

Rachel Deplus

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

P2860

Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3)

Regulation of chromatin structure by site-specific histone H3 methyltransferases

Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

JMJD6 is a histone arginine demethylase

The Polycomb group protein EZH2 directly controls DNA methylation

Histone deimination antagonizes arginine methylation

Dnmt3L is a transcriptional repressor that recruits histone deacetylase.

LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription

JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor

Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases

P304

4982-4993

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

P31

scholarly article

P356

10.1128/MCB.00285-09

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

P407

P433

18

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

P478

29

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

P50

Raphaël Métivier

P577

2009-07-06T00:00:00Z

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

P698

19581286

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

P932

2738279

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