Phosphorylation of histone H3 Thr-45 is linked to apoptosis - Wikidata - awgldk - TriplyDB

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

http://www.wikidata.org/entity/Q34975324

about

PKC-Theta in Regulatory and Effector T-cell Functions Nutrition, epigenetics, and metabolic syndrome Post-translational modifications of histones that influence nucleosome dynamics A peek into the complex realm of histone phosphorylation Proteomics in epigenetics: new perspectives for cancer research Computer-aided Molecular Design of Compounds Targeting Histone Modifying Enzymes Protein kinase C in the immune system: from signalling to chromatin regulation Lestaurtinib inhibits histone phosphorylation and androgen-dependent gene expression in prostate cancer cells Chemical and biological tools for the preparation of modified histone proteins Quantitative proteomic analysis of histone modifications Histone H3 Thr 45 phosphorylation is a replication-associated post-translational modification in S. cerevisiae.Histone H3 serine 57 and lysine 56 interplay in transcription elongation and recovery from S-phase stress Reciprocal epigenetic modification of histone H2B occurs in chromatin during apoptosis in vitro and in vivo Charge state of the globular histone core controls stability of the nucleosome Histone phosphorylation: a chromatin modification involved in diverse nuclear events.Scratching the (lateral) surface of chromatin regulation by histone modifications.Histone H3 phosphorylation in GBM: a new rational to guide the use of kinase inhibitors in anti-GBM therapy.Phosphorylation of histone H2B serine 32 is linked to cell transformation.Histone modifiers in cancer: friends or foes?Regulation by polycomb and trithorax group proteins in Arabidopsis.Breaking the histone code with quantitative mass spectrometry.AKT phosphorylates H3-threonine 45 to facilitate termination of gene transcription in response to DNA damage.Using DNA methylation to understand biological consequences of genetic variability.Histone H3 Ser57 and Thr58 phosphorylation in the brain of 5XFAD mice.Histone core phosphorylation regulates DNA accessibility.Mutation of histone H3 serine 86 disrupts GATA factor Ams2 expression and precise chromosome segregation in fission yeast.Histone H3 phosphorylation - a versatile chromatin modification for different occasions.Regulation of the nucleosome unwrapping rate controls DNA accessibility.Wedelolactone, a medicinal plant-derived coumestan, induces caspase-dependent apoptosis in prostate cancer cells via downregulation of PKCε without inhibiting Akt.Regulation of GTP-binding protein (Gαs) expression in human myometrial cells: a role for tumor necrosis factor in modulating Gαs promoter acetylation by transcriptional complexes.Monitoring Cellular Phosphorylation Signaling Pathways into Chromatin and Down to the Gene Level.Proteomic characterization of novel histone post-translational modifications.Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.Epigenetic targets in human neoplasms.Posttranslational modifications of human histone H3: an update.Mitotic phosphorylation of histone H3 threonine 80.DYRK1A phoshorylates histone H3 to differentially regulate the binding of HP1 isoforms and antagonize HP1-mediated transcriptional repression.Comprehensive Catalog of Currently Documented Histone Modifications.Beyond transcription factors: how oncogenic signalling reshapes the epigenetic landscape.S6 kinase 2 is bound to chromatin-nuclear matrix cellular fractions and is able to phosphorylate histone H3 at threonine 45 in vitro and in vivo.

P2860

Q26777188-3D00472E-DE1D-4D7B-B552-882A3FA071AC Q26829684-AB33290E-EEDC-4D47-A2B9-90145BB81263 Q26852536-AD4E555B-0C5E-4275-ABEF-7501212D00C9 Q26992357-D45A58F6-39F1-4C5B-9487-A6B5AEAB2319 Q27014943-ACBA0E98-6C99-4510-836B-BC2065631969 Q28083849-7AB2228B-4130-4583-BDF0-518DFBD2388D Q28084032-B6D53A16-1B0A-4547-9760-9530D1E4AE20 Q28482432-006FB79D-B2E6-4302-9719-8214F5E1EABA Q28829535-FBBC3EFD-D8C3-44FE-988C-6DC870182A88 Q30375585-E59B26E8-7604-44F2-A8D7-44D3C16E3B4B Q30436419-496C44B9-CD52-4573-B543-178ABB587F1E Q33592954-AE55A7D4-F955-4DC1-94B4-46295FB800E0 Q33838462-6280E5EF-E3DB-41CB-B56B-1ADA911999EF Q34099086-546A0624-422F-45B3-97BB-D7EDB74F1692 Q34297533-25A0E2FE-9571-4173-9115-12D325C52AD6 Q34348859-B419C47D-26BB-4BA8-8187-0148497A5588 Q34698607-D8D7A6F4-4113-47CC-8276-CDF605393E1B Q35128231-8215F247-AF22-42B6-961F-15F19F8EF4B2 Q35216079-8234FBDD-F483-40FD-8EE1-0B74AF3B1EAD Q35630571-DFF3BD5D-9E1A-4AE0-9413-5AEEF344EA24 Q35645008-D5E21822-6472-43C5-A96F-7D8C5050AC9E Q35786083-B92D597F-5938-42BD-BF49-00B5B668F1F0 Q35832672-9B813014-82DC-4D4A-949B-1FA0DB1F443F Q35864785-859A68F4-8F64-4158-A56A-CAEA5D9E685E Q36049970-89CDFA3B-3166-40F9-9896-1516BF5044CA Q36060610-DB7920F3-96CE-47E2-8C28-A93C062EEAA2 Q36345651-B93E5803-3770-42A9-930B-AADE40717D04 Q36368740-B07A5EE5-2E44-4B5F-BF99-C630F35C4E7C Q36521016-CDC0A58C-8849-4926-944C-2AAE1BC2BD7F Q36647410-A07A1B65-36B6-4843-911D-E54D41E21D5D Q36745147-84A611FC-0C88-45B7-A5C6-A1CF4AF9CD62 Q37079424-32EBA119-3450-4FD4-A494-8AF807CB6332 Q37734360-C911B80A-EAF7-4388-B827-9233FD209A29 Q37961723-2CCD6C70-D0B0-43D4-B4FD-7BFF251F09BA Q38232008-4E69EC1A-E570-468B-AC2C-183292C36D4B Q38298173-E85E4C29-EB51-4DE7-8772-BE8BF17B454E Q38307139-82C5023F-5DCE-4E19-BE74-642A5E4893D6 Q38578748-AF3F55D9-70B7-430A-8DF5-E430365298BB Q38843250-445DBEBA-390D-42E0-B5C7-13D3424527AA Q39169842-1C51E8F9-272A-4BCF-8257-ECBE7C272FFF

P2860

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

http://www.wikidata.org/entity/Q34975324

description

2009 nî lūn-bûn

@nan

2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@ast

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@en

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@nl

type

label

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@ast

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@en

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@nl

prefLabel

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@ast

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@en

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@nl

P1433

Q34975324-9D4DDF11-9F29-4269-90BB-2EF2733E5108

P1476

Q34975324-FEEA6668-D9A0-4889-B04C-3BCED3264907

P2093

Q34975324-4917FD8F-135C-43CD-88AE-D4299DF4EE30

Q34975324-68B74B50-6855-4749-AB07-6760936B3FBC

Q34975324-6D5C58A0-0DB6-442F-8139-2DEEF2AC5E79

Q34975324-9AE3C7F0-A4FB-451C-8A88-D8E293AF13E6

Q34975324-BE463248-17BF-4368-A15D-8FC2CA5ED085

P2860

Q34975324-08CC58E6-9AF2-4E65-B1BF-E11208EC5B38

Q34975324-0C5D202F-D2F5-4355-86E5-B91263698554

Q34975324-230F41C2-15E1-43C7-AF7B-5CE62F0FD439

Q34975324-27F106F8-9EB7-4BAA-9BF6-98FC8518D875

Q34975324-295EE364-2937-448D-8933-7EBBFA8A9739

Q34975324-2C7B92CC-0E0F-435E-B1E7-96DC57E0149F

Q34975324-3887D4DC-73E8-4BDC-8A74-4983B3DA2058

Q34975324-38F6E0B6-DEAD-453B-8D00-F306F0022AF9

Q34975324-45542B6A-FA7E-45AB-BBE3-D51BA36F2EBC

Q34975324-5151C5CB-A549-4D04-BD98-EA4E0F29AEFA

P304

Q34975324-041E7D86-66E5-4398-A9B8-4248B58AD67A

P31

Q34975324-47F6C923-2602-4E70-B329-B4B187008452

P356

Q34975324-A5B7B7CE-D5D3-48DD-853E-DE323C105D3C

P407

Q34975324-AFD0E06A-7FC9-4E48-8F99-28772680E384

P433

Q34975324-6EA7C595-2650-4A3B-BD0D-88C62C051EE5

P478

Q34975324-C1D5B2FD-7424-415E-AA06-A577EDF272BE

P50

Q34975324-190A28DD-CA5E-444C-B8FC-DF49E3AD1A60

Q34975324-4F3DCEE9-CD7E-498A-B228-4CD8F7431588

Q34975324-63B04407-62B7-4350-8790-F1CE8A5A9966

Q34975324-B2E07D76-CEEE-4B9F-AAA1-5ABAF77CC98D

Q34975324-B962FAFC-EB6D-4B6C-8228-5FE632DA54F4

Q34975324-CB6B43C3-DB4A-4973-93EF-08F04A421AC7

Q34975324-F8E6D4E4-621A-4906-AF07-F86B7B4DED9E

P577

Q34975324-A33572C7-01D1-459D-9D9E-63AE78B34591

P698

Q34975324-FB323428-CF19-42AA-8A5E-786AA0018334

P921

Q34975324-D1364334-9927-490A-B0F4-23DE4E6C84B9

P932

Q34975324-0EF93BDA-6DB7-41C9-8700-4EFD3ECF698C

P356

JBC.M109.005421

P1433

Journal of Biological Chemistry

P1476

Phosphorylation of histone H3 Thr-45 is linked to apoptosis

@en

P2093

Heba Ismail

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

Ivan Gout

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

Joanna Somers

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

Karen Halls

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

Matthias Mann

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

P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Regulation of chromatin structure by site-specific histone H3 methyltransferases

Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

The language of covalent histone modifications

Chromatin modifications and their function

Up-regulation of steroid sulphatase activity in HL60 promyelocytic cells by retinoids and 1alpha,25-dihydroxyvitamin D3

Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap

P304

16575-16583

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

P31

scholarly article

P356

10.1074/JBC.M109.005421

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

P407

P433

24

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

P478

284

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

P50

Tony Kouzarides

Michiel Vermeulen

Jesper V. Olsen

Tom Owen-Hughes

P577

2009-04-10T00:00:00Z

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

P698

19363025

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

P921

phosphorylation

P932

2713519

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