Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development. - Wikidata - wikimedia - TriplyDB

Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development.

Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development.

http://www.wikidata.org/entity/Q37145387

about

Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage response The ATAC acetyl transferase complex controls mitotic progression by targeting non-histone substrates.PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression SET8 promotes epithelial-mesenchymal transition and confers TWIST dual transcriptional activities Regulation of chromatin by histone modifications Synthesis of lysine methyltransferase inhibitors PR-Set7 and H4K20me1: at the crossroads of genome integrity, cell cycle, chromosome condensation, and transcription Sirtuin-dependent epigenetic regulation in the maintenance of genome integrity MLL2 is required in oocytes for bulk histone 3 lysine 4 trimethylation and transcriptional silencing H4K20me1 contributes to downregulation of X-linked genes for C. elegans dosage compensation Impact of histone H4 lysine 20 methylation on 53BP1 responses to chromosomal double strand breaks Solution structure of the Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNA The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier–Gorlin syndrome A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases Multivalent Interactions by the Set8 Histone Methyltransferase With Its Nucleosome Substrate The emerging role of lysine methyltransferase SETD8 in human diseases Distinct and overlapping functions of the cullin E3 ligase scaffolding proteins CUL4A and CUL4B The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation SET8 is degraded via PCNA-coupled CRL4(CDT2) ubiquitylation in S phase and after UV irradiation 14-3-3 proteins play a role in the cell cycle by shielding cdt2 from ubiquitin-mediated degradation Regulation of TGF-β signaling, exit from the cell cycle, and cellular migration through cullin cross-regulation: SCF-FBXO11 turns off CRL4-Cdt2.Setd5 is essential for mammalian development and the co-transcriptional regulation of histone acetylation.The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate.Relationship between epigenetic changes in Wnt antagonists and acute leukemia Regulation of the histone H4 monomethylase PR-Set7 by CRL4(Cdt2)-mediated PCNA-dependent degradation during DNA damage.Comparative analyses of SUV420H1 isoforms and SUV420H2 reveal differences in their cellular localization and effects on myogenic differentiation.Evolutionarily conserved replication timing profiles predict long-range chromatin interactions and distinguish closely related cell types.Looking at plant cell cycle from the chromatin window.The UBC9 E2 SUMO conjugating enzyme binds the PR-Set7 histone methyltransferase to facilitate target gene repression.MicroRNA binding site polymorphisms as biomarkers in cancer management and research.Fluorescence-based methods for screening writers and readers of histone methyl marks.Polycomb group proteins: multi-faceted regulators of somatic stem cells and cancer.CRL4(Cdt2)-mediated destruction of the histone methyltransferase Set8 prevents premature chromatin compaction in S phase.The histone H4 lysine 20 monomethyl mark, set by PR-Set7 and stabilized by L(3)mbt, is necessary for proper interphase chromatin organization.L3MBTL1 polycomb protein, a candidate tumor suppressor in del(20q12) myeloid disorders, is essential for genome stability.The C. elegans dosage compensation complex mediates interphase X chromosome compaction H4K20 monomethylation faces the WNT Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity.Defining the replication program through the chromatin landscape

P2860

Q24321615-BDCA3696-1D9B-46C8-94F4-D39FADBCB082 Q24323889-E0B73FD4-30CA-4FFD-BA3A-8A9CBCAEDC34 Q24323898-AE74860E-3BEB-4F43-ABD1-26D8E9009976 Q24338563-64C14684-E4BF-4950-9B38-E3A8BD10F5AA Q24339520-2293C9BA-5917-42A4-B2E3-398FCA117EB2 Q24635070-96781780-DD1C-4C07-A6B5-B981F0D41812 Q26799953-48CCF892-738D-4237-9336-96C20039B1E1 Q26823191-6A20ECC6-2CA4-47DD-A3DC-5766001651B5 Q27026871-BD8F6B2E-0059-484E-8687-49971185EDB0 Q27323960-D7B72468-D66B-4664-AD61-1A26B13A5449 Q27331824-58E41228-35C3-4984-B77D-45F8B16045C5 Q27337186-44B742E0-6CFF-4855-9158-D33D648C4C22 Q27676028-40F66A2A-6179-4E84-B0CC-B2EC20A6AA03 Q27677935-7D9854C6-7D71-4CBD-863D-949E31B6D20A Q27679986-016213A0-47F5-44E7-9C38-7AE84028E1CA Q27704231-8151030B-512A-421C-B990-041414B9747A Q28079964-75E9974B-F4DD-4FC9-BA75-7ED3973B01E8 Q28086765-93124FF4-0F50-4001-B827-73B736062604 Q28286787-0ED7C421-7289-4316-ABF3-C555AB5053C8 Q28302907-3D4B2FA0-773F-4D7C-B2C8-900C667DBB5B Q30405556-1E8EA6C7-7ECF-4CA4-984D-F78925BFD351 Q30411902-1FFDC713-ED7B-431C-BE65-E54C70DB3454 Q32874823-E2DB6842-960E-470A-9317-0FC48A4C6BDF Q33553524-F2A64F30-3084-4FD6-9DA1-520CDA25C4B2 Q33671191-F803F728-6A5C-4DA9-A1AA-83165E40209D Q33733896-F4C0BF0C-F2A9-42F3-AC66-384140FA3C1B Q33785780-0E369FD5-DF77-4835-AB67-0D28F5D6C2D0 Q33881351-3194062E-356D-40D3-8F8A-EE5CD1AA2A42 Q33948565-A4FA2081-61D8-412F-863F-BA8480859093 Q33987877-A1FD4FAC-C180-4B33-9991-43E5C01FD934 Q34019040-C28E0568-C1AD-40FB-88AA-FE7A3481AB33 Q34040118-D3E0D857-6E73-4736-BFD1-C6BE331354B0 Q34134903-1F854DB4-275A-4270-857E-7851CED220A6 Q34215301-CFF80263-2EB9-4074-9C40-33CE001DA7DB Q34425328-403505B6-D75C-4DD2-8D21-B2AC4F751AA7 Q34450058-4341A5C3-5DE7-442D-B73B-D7084CCF02F6 Q34515312-8D99CA05-5257-4FF6-B1B4-62CA565F5E70 Q34602378-AA9F1B2B-D5F1-4E77-81FC-DE28D3D06384 Q34647591-D061DD34-69EE-4225-9F7D-4A4319318B6C Q34780596-9BFADF15-4CB0-418D-9C02-FA563AC004B1

P2860

Monomethylation of histone H4-lysine 20 is involved in chromosome structure and stability and is essential for mouse development.

http://www.wikidata.org/entity/Q37145387

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 17 February 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Monomethylation of histone H4- ...... sential for mouse development.

@en

Monomethylation of histone H4- ...... sential for mouse development.

@nl

type

label

Monomethylation of histone H4- ...... sential for mouse development.

@en

Monomethylation of histone H4- ...... sential for mouse development.

@nl

prefLabel

Monomethylation of histone H4- ...... sential for mouse development.

@en

Monomethylation of histone H4- ...... sential for mouse development.

@nl

P1433

Q37145387-4998389D-03FD-4B3A-A827-AFD9DBB40783

P1476

Q37145387-2E72733E-0F24-40BD-AAF3-3D09C6181CD5

P2093

Q37145387-26003765-0463-4145-9D5A-E9B31B81E1A2

Q37145387-718F464C-DF05-441F-A1D7-601577A25864

Q37145387-B61761AE-B29D-45C6-9839-AEB234897C8D

Q37145387-B88CB536-9F35-41D9-8798-0E43B97FB846

Q37145387-C4B46D8E-623A-4504-A475-DC0DE2DB6E7F

Q37145387-CAA76C61-F452-4610-8D16-98DA6D770D94

Q37145387-CD66F3CB-474D-4614-8111-AD46DB696804

Q37145387-EC77F3A0-5968-4DE2-9390-021A662D77F2

P2860

Q37145387-0746092F-010E-4401-A84D-A1D55EE84169

Q37145387-0A26B7D4-1C06-430B-A837-7C1F535195D3

Q37145387-10228977-B823-4FBA-A23A-57BA02189CCA

Q37145387-1191356F-CA3A-40BB-B8F5-6FB213B41E9F

Q37145387-1991DEA3-7904-4028-9521-7F87DF759BD3

Q37145387-1BBE2055-25A0-4A5F-81FB-E4E2DCB1AFD7

Q37145387-1F1025B0-849A-4A84-9F26-6CAE54B821F7

Q37145387-21F807E0-3CBC-406D-9D8C-C3E4774E7FAC

Q37145387-2287BC34-FBFB-492B-87A9-6564FA21D9C7

Q37145387-3C75D1DE-3BFD-4376-AE02-37AB1ABF075D

P304

Q37145387-53720C13-B22C-44C2-BD59-DCA9787F2900

P31

Q37145387-EE7B77B3-725E-4E54-A39A-50864CF5FDA5

P356

Q37145387-9DDD4BC4-E145-4A38-A7DA-861937ED0C42

P407

Q37145387-D3BF0798-E7E5-41D8-B579-4FBF16C4B61B

P433

Q37145387-37F0DEA8-409B-4256-8F88-E56731835649

P478

Q37145387-02B3C51A-55FD-4BB9-A817-82E2F9B86FB3

P50

Q37145387-450EAC4C-FA86-492E-B613-A159B64CBE2F

P577

Q37145387-FE337EAC-B041-4C0A-B91C-1FE45669FA68

P5875

Q37145387-A549C6BC-2453-4CC6-8C49-B38B6D14DF83

P698

Q37145387-8307D7FA-8DCB-4926-A7BC-EDA559B0AEED

P932

Q37145387-D9836723-E968-4A59-ABD3-92013F3556E9

P356

P1433

Molecular and Cellular Biology

P1476

Monomethylation of histone H4- ...... sential for mouse development.

@en

P2093

Edith Heard

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

Hisanobu Oda

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

Ikuhiro Okamoto

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

Jianhua Chu

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

Maria Elena Torres-Padilla

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

Michael M Shen

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

Niall Murphy

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

Sandy M Price

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

P2860

Specificity and mechanism of the histone methyltransferase Pr-Set7.

L3MBTL1, a histone-methylation-dependent chromatin lock

Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1

Modulation of p53 function by SET8-mediated methylation at lysine 382

A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin

Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair

Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes.

A chromosomal memory triggered by Xist regulates histone methylation in X inactivation

High-resolution profiling of histone methylations in the human genome

Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer

P304

2278-2295

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

P31

scholarly article

P356

10.1128/MCB.01768-08

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

P407

P433

8

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

P478

29

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

P50

P577

2009-02-17T00:00:00Z

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

P5875

24021446

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

P698

19223465

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

P932

2663305

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