Identification of histone demethylases in Saccharomyces cerevisiae. - Wikidata - thesis-toulmin - TriplyDB

Identification of histone demethylases in Saccharomyces cerevisiae.

Identification of histone demethylases in Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q27939452

about

Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins Rph1/KDM4 mediates nutrient-limitation signaling that leads to the transcriptional induction of autophagy Progress in epigenetic histone modification analysis by mass spectrometry for clinical investigations Crystal structure of the catalytic core of Saccharomyces cerevesiae histone demethylase Rph1: insights into the substrate specificity and catalytic mechanism The histone H3K36 demethylase Rph1/KDM4 regulates the expression of the photoreactivation gene PHR1 Two Saccharomyces cerevisiae JmjC domain proteins demethylate histone H3 Lys36 in transcribed regions to promote elongation.Counteracting H3K4 methylation modulators Set1 and Jhd2 co-regulate chromatin dynamics and gene transcription.Yeast histone H3 lysine 4 demethylase Jhd2 regulates mitotic rDNA condensation Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression Saccharomyces cerevisiae Forms D-2-Hydroxyglutarate and Couples Its Degradation to D-Lactate Formation via a Cytosolic Transhydrogenase.Histone H3K4 demethylases are essential in development and differentiation An high-throughput in vivo screening system to select H3K4-specific histone demethylase inhibitors The histone demethylase activity of Rph1 is not essential for its role in the transcriptional response to nutrient signaling A barcode screen for epigenetic regulators reveals a role for the NuB4/HAT-B histone acetyltransferase complex in histone turnover Oncometabolite D-2-Hydroxyglutarate enhances gene silencing through inhibition of specific H3K36 histone demethylases.Gcn5-mediated Rph1 acetylation regulates its autophagic degradation under DNA damage stress.The JmjN domain of Jhd2 is important for its protein stability, and the plant homeodomain (PHD) finger mediates its chromatin association independent of H3K4 methylation FACT, the Bur kinase pathway, and the histone co-repressor HirC have overlapping nucleosome-related roles in yeast transcription elongation.Gis1 and Rph1 regulate glycerol and acetate metabolism in glucose depleted yeast cells.Distribution and maintenance of histone H3 lysine 36 trimethylation in transcribed locus Interaction of the Jhd2 Histone H3 Lys-4 Demethylase with Chromatin Is Controlled by Histone H2A Surfaces and Restricted by H2B Ubiquitination Histone H3K4 demethylation is negatively regulated by histone H3 acetylation in Saccharomyces cerevisiae The control of elongation by the yeast Ccr4-not complex Histone H3K36 methylation regulates pre-mRNA splicing in Saccharomyces cerevisiae Riches of phenotype computationally extracted from microbial colonies.Epigenetic silencing mediates mitochondria stress-induced longevity.Heterochromatin protein 1a stimulates histone H3 lysine 36 demethylation by the Drosophila KDM4A demethylase.Dissociation of the H3K36 demethylase Rph1 from chromatin mediates derepression of environmental stress-response genes under genotoxic stress in Saccharomyces cerevisiae.The establishment of gene silencing at single-cell resolution.Unambiguous determination of isobaric histone modifications by reversed-phase retention time and high-mass accuracy.KDM5 lysine demethylases are involved in maintenance of 3'UTR length.The histone methyltransferase Dot1/DOT1L as a critical regulator of the cell cycle.Histone modifications as regulators of life and death in Saccharomyces cerevisiae Transcription-associated histone modifications and cryptic transcription.Histone lysine demethylase (KDM) subfamily 4: structures, functions and therapeutic potential.Progressive methylation of ageing histones by Dot1 functions as a timer.The impact of cruciferous vegetable isothiocyanates on histone acetylation and histone phosphorylation in bladder cancer.Inhibitors of enzymes catalyzing modifications to histone lysine residues: structure, function and activity.Choose Your Own Adventure: The Role of Histone Modifications in Yeast Cell Fate.Shaping the cellular landscape with Set2/SETD2 methylation.

P2860

04bf862c03c6160a63bb3b78f42d788f0cb530e8 277d9fce65e21aed649d0ba261da27ccd641c352 440da0030010f6db718c16f97ae60e4064f8f3fd ab099660decc31b80a519ed4d81d4a832fa17d03 bcc7745132a5e3d75499501b20f78d7892e8dc0c dc84ebc469733be6655a3d55decd5fc5a8f38c8f df62156c2861bdbffe5ae894ddf52221bc97a108 e97bd1a424718e26dad6e884da101ce2e1e7fd7e

P248

Q21263183-960161F4-E812-4739-ADBF-A2928405919D Q24318081-2F2D0293-4040-43D4-AF9A-2F054CD7572A Q26781745-DCD4FD7F-CB1C-420C-B210-859B88685BE7 Q27665733-FB1E435F-7CA9-47DA-ADB1-C3A9458A8BF7 Q27930846-1396F94E-3929-465D-9947-FB53A2D5EDEB Q27933649-ECCCDEBC-6E7E-4386-84C4-AD9894F4ADDC Q27934039-700021A3-D316-48A2-8D75-2A76900A3FBF Q27935114-C9DC4186-B33F-4EBA-9539-99DDADAF4527 Q27937740-C92BD0C6-33AB-43BB-822B-EABFD016347B Q27938700-CF3E0AF5-1449-461B-B69A-FF51D3758A7C Q28241709-B7BD6543-B60F-4694-9504-9F9EDD163313 Q28539276-C00AA6BD-ED2A-4A79-9D0E-5851712D2961 Q28656049-1F80B2D2-2707-4F93-ABDA-F89FB7FAD270 Q31036616-CD4120E5-C722-44F2-816B-319BC13633C9 Q33554577-C4865BA5-5278-4DFD-98CE-24DEF0A4C292 Q33701454-EDD99D40-FDF6-49E0-BB0B-56A50DAC9F89 Q34042577-EF2D16B6-48B5-4EEF-87D7-7351B178ABFE Q34055678-1FD7889B-18C2-43A8-A369-4338B17E2FAE Q34171125-19262EA6-40F3-4629-A714-F0BFE1B17662 Q35577929-57F53547-C4EA-4D7F-807B-0C2099ECBA1B Q36323434-E83D279A-C41C-433F-813F-35B7639EA8D9 Q36389626-13F321F1-C3E3-4348-A586-0E9E8E919B6C Q36532642-E0D9999D-E57C-461E-8D03-F9FC6D3BA391 Q36827115-C60C8EA0-81F9-452F-8864-2C061D11F491 Q36931115-64573376-E961-40C4-9D2A-AB19088539D1 Q36960145-F3D3A888-0267-44E1-8D21-5C7FAAA44860 Q37097790-1ACA19CD-C6A7-4C3A-A4FE-57A801D3C690 Q37251269-F2105F61-E690-41D0-8AD5-722A514BD25F Q37337415-9612E1F6-349E-421C-AE0C-EDE4BC9A0D52 Q37456238-C97539DA-67D9-44F3-9639-69409B646800 Q37603840-B3A2CEEC-647E-480C-A46D-1984D020BC19 Q37692579-0F558C31-B64B-4D2B-8913-67ACE4997A58 Q37705706-55F03B09-53E1-4016-AC41-08EDFF0E1385 Q38043829-86DBCECF-E8DF-4836-8BB6-C03C62299B73 Q38172162-7697D661-BA12-42DC-BF1D-EF1A2DA7B387 Q38296266-C561127B-13B3-4887-880D-27277A7426F6 Q38764605-F6541E31-55A1-4013-AD01-051340C144A7 Q38833038-0F46E169-7A7C-4C27-9D08-3585A9017250 Q38987852-1761E8F4-9898-402D-882C-274B3D4973CC Q39225775-A0BCBD37-003D-463B-A982-9974EA81DA27

P2860

Identification of histone demethylases in Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q27939452

description

2007 nî lūn-bûn

@nan

2007 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Identification of histone demethylases in Saccharomyces cerevisiae.

@ast

Identification of histone demethylases in Saccharomyces cerevisiae.

@en

Identification of histone demethylases in Saccharomyces cerevisiae.

@nl

type

label

Identification of histone demethylases in Saccharomyces cerevisiae.

@ast

Identification of histone demethylases in Saccharomyces cerevisiae.

@en

Identification of histone demethylases in Saccharomyces cerevisiae.

@nl

prefLabel

Identification of histone demethylases in Saccharomyces cerevisiae.

@ast

Identification of histone demethylases in Saccharomyces cerevisiae.

@en

Identification of histone demethylases in Saccharomyces cerevisiae.

@nl

P1433

Q27939452-2F2EDB32-2D17-468C-AB66-9DF71E787CB7

P1476

Q27939452-EB009DDD-7DA0-4788-BE88-67B48B8685B3

P2093

Q27939452-07ABD59F-6917-4EAA-9DB1-B32A0AD90455

Q27939452-233888C0-EDF1-45C9-9C27-4B7E4329F85D

Q27939452-3E5FA2C3-E629-4C23-BCCB-DC1E7B4FE53C

Q27939452-555870E3-F116-4AC7-82B9-287248633C9E

Q27939452-63BA3F9B-13F6-4B08-803E-3CC7D9C54B65

Q27939452-684F21B0-4160-4D38-BB9F-5E9A67246FE4

Q27939452-763415BE-FF91-4F2D-AEA7-625B634985CD

Q27939452-CACE6B1D-0C25-4534-A2D7-24CB19D1025F

P2860

Q27939452-007A6F0E-842C-448F-84FE-D3F0696E0C9B

Q27939452-0A1B961E-6400-4F4C-8050-411049FD70C4

Q27939452-10F0CEDD-EE2B-47E0-9F01-77D8B1E1D614

Q27939452-1419CF12-7FD1-411C-B5F1-390B92862D0C

Q27939452-15B105E9-8FD9-47B2-A9AA-788399374886

Q27939452-1DE6D47E-9A17-48A7-BC95-E8DD57E9AF8A

Q27939452-1E0D69AA-1E2E-4C8B-BBAB-FAFA43569BF7

Q27939452-22795961-247A-4F14-AFE5-0F1B96FFC395

Q27939452-233BFEE7-6B2C-4343-BBA9-BF50ADF030D2

Q27939452-26420E72-DF28-4BF4-8B05-177F4CF62DFF

P304

Q27939452-22271A16-D8EC-4440-9E52-4DEEEE52A88A

P31

Q27939452-3D9D982E-CC3D-4A8C-9553-17D9AA7286AC

P3181

Q27939452-D2073B63-CFA1-4FF9-BBC9-2233E70BD65F

P356

Q27939452-7C24EE43-D9CC-4A92-BBD4-7C2CEA074E1B

P407

Q27939452-65274850-1DDA-4B28-9C17-65ED92EEA51F

P433

Q27939452-79AA75EA-4597-4336-A634-76AE54466946

P478

Q27939452-BBBFB644-FEC2-4E46-AADD-0134FE1683A7

P50

Q27939452-2662A192-7F4E-401E-9178-877672DD74C0

Q27939452-65D0B0F8-8E7D-40F9-A8E6-5491187CA461

Q27939452-A74A9719-82BB-40ED-B13B-823BB70D49DC

Q27939452-F7E29E5A-E658-46BE-82CF-1200A1CB6504

P577

Q27939452-B143930F-A23A-46EF-84CB-26AD52D9D9EA

P5875

Q27939452-0CF024F9-4252-4671-B373-9949F839201A

P698

Q27939452-4C0A1D70-003C-4076-B484-BDBFB18E677D

P921

Q27939452-596CADEC-4934-493B-9FB2-87186CC25C31

Q27939452-FABD5326-B258-49D9-B9C4-E74CD428CF30

P932

Q27939452-766922D6-56BA-4B7B-9BB3-0D3330CA893E

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Identification of histone demethylases in Saccharomyces cerevisiae

@en

P2093

Chein-Hung Chen

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

Chen Ren

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

Chung-Lin Liao

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

Esther M M Bulloch

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

Hui-Ming Yu

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

Lanhao Yang

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

Wan-Sheng Lo

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

Wei-Chieh Huang

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

P2860

Translating the Histone Code

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

Characterization of the retinoblastoma binding proteins RBP1 and RBP2

Histone demethylation mediated by the nuclear amine oxidase homolog LSD1

ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression.

Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association

Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis

P304

14262-14271

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

P31

scholarly article

P3181

631540

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

P356

10.1074/JBC.M609900200

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

P407

P433

19

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

P478

282

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

P50

Michael A. Freitas

P577

2007-03-16T00:00:00Z

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

P5875

6438704

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

P698

17369256

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

P921

Saccharomyces cerevisiae

P932

2855503

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