Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin. - Wikidata - wikimedia - TriplyDB

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

http://www.wikidata.org/entity/Q37233602

about

KSHV reactivation and novel implications of protein isomerization on lytic switch control NF-κB transcriptional activity is modulated by FK506-binding proteins FKBP51 and FKBP52: a role for peptidyl-prolyl isomerase activity.Prolyl isomerases in gene transcription A brief review of nucleosome structure The role of dietary histone deacetylases (HDACs) inhibitors in health and disease.Post-translational modifications of the intrinsically disordered terminal domains of histone H1: effects on secondary structure and chromatin dynamics.Linker Histone in Diseases.Identification of a novel cAMP dependent protein kinase A phosphorylation site on the human cardiac calcium channel.

P2860

Q28080937-9A53D6B8-0CF4-457D-8C63-8BFAAD36FD12 Q34249196-BD7D7F1E-8EC9-4CE3-872A-16DF7731A338 Q35561852-1060447C-41AD-4792-B107-03B1399F4FDC Q36137489-FFD68893-079A-49AE-89D8-AB0AB7D9EF49 Q38260795-EAA002D9-DD0A-4F76-9962-E662E37A9455 Q38813372-9B3631DB-8077-4655-ABAA-EA813610D2DA Q41036058-FC001F7C-EE8B-4533-9B29-29AAF25722B0 Q46264447-B01093F0-7E08-4099-B04E-6AD6255F8E17

P2860

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

http://www.wikidata.org/entity/Q37233602

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 07 October 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

@en

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

@nl

type

label

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

@en

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

@nl

prefLabel

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

@en

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

@nl

P1433

Q37233602-7FB3CBE6-9F1F-483B-9703-B457FC2E5D74

P1476

Q37233602-2637181A-41A0-4C82-AC3D-A7831D3FB5D1

P2093

Q37233602-0BEA6617-F3D4-491C-A078-9459FB307444

Q37233602-22CBBB54-EA53-44BB-AA47-58E3364BCCE2

Q37233602-6B2A61A8-A04A-40C4-945E-D59012F99521

Q37233602-7A8C9329-86C6-470F-B4B3-EAECB9FD60C6

Q37233602-B2ECADEE-BC9F-4F59-B3D2-11F92143B2C3

Q37233602-B7F65692-1C07-4CCE-9DCA-CCCA2673FD92

Q37233602-E52F6E3B-86A7-4707-A4A9-EAA7F4DF8F09

Q37233602-FDEFE387-4028-4C27-93BB-2C1C9ED0189E

P2860

Q37233602-04BECD16-4981-4A95-ABFB-4217E68CF078

Q37233602-06999358-1C31-4E00-8AA5-3EB5CAA0EAE8

Q37233602-06A3E0D8-B1AD-4688-9FF6-48C624DA1441

Q37233602-0ADED436-1B8A-495C-9DA9-86D2B5967EB5

Q37233602-0EF224F7-115E-4AE7-B280-8251C7080C0F

Q37233602-1674B9D7-E22E-4E4F-8E3A-FEA9ACDD6146

Q37233602-19B93CBF-AB07-49F5-AF84-FA5570D5FB45

Q37233602-1CB0B302-0355-4166-8DA2-1A60DCC59C70

Q37233602-218916B7-C37F-4048-ABBD-E6BB94B0BF62

Q37233602-2302E79B-052F-4398-AE3B-C248F060E5AE

P304

Q37233602-238FCA88-21B7-4693-9BC2-288210C0BBE2

P31

Q37233602-C1038DD4-AA60-40A2-9612-77BE1018E3FB

P356

Q37233602-D4E70A45-C628-4B2D-B4D6-49E8E1969933

P407

Q37233602-9BCB4506-2378-4EAB-8B2F-853579CFA538

P433

Q37233602-9BE75E7B-6627-43D1-8A28-F4DB225CE47A

P478

Q37233602-BD322718-DB23-48F2-96A5-F6A8208D4CCC

P50

Q37233602-35ABBEF9-44D8-41EC-95F0-64AA8D0B7677

P577

Q37233602-683A5EA4-4864-460C-AFB9-82F9A1078732

P5875

Q37233602-F102B86D-3F80-4A9A-BBA6-3E03CB008808

P698

Q37233602-E149FE7E-5463-4EA7-9E97-AC23DC088C80

P932

Q37233602-2F79F850-CDA4-49E0-8695-855ADCF7A797

P356

P1433

Journal of Cell Biology

P1476

Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.

@en

P2093

Craig Mizzen

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

Darin McDonald

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

He Fang

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

Hilmar Strickfaden

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

Jeffrey J Hayes

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

John Th'ng

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

Kylie Williams

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

Nikhil Raghuram

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

P2860

Function of WW domains as phosphoserine- or phosphothreonine-binding modules

H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain

Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin

Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin

Single cell analysis of transcriptional activation dynamics

A human peptidyl-prolyl isomerase essential for regulation of mitosis

A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1

Rapid exchange of histone H1.1 on chromatin in living human cells

Dynamic binding of histone H1 to chromatin in living cells

Signaling to chromatin through histone modifications

P304

57-71

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

P31

scholarly article

P356

10.1083/JCB.201305159

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

P407

P433

1

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

P478

203

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

P50

Michael J. Hendzel

P577

2013-10-07T00:00:00Z

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

P5875

257530141

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

P698

24100296

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

P932

3798258

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