Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A - Wikidata - wikimedia - TriplyDB

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

http://www.wikidata.org/entity/Q29614520

about

Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1 Rapid activation of the bivalent gene Sox21 requires displacement of multiple layers of gene-silencing machinery Structural basis for molecular recognition and presentation of histone H3 by WDR5 Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1 RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.Structural basis of the recognition of a methylated histone tail by JMJD2A Structure and site-specific recognition of histone H3 by the PHD finger of human autoimmune regulator Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2 PHD finger recognition of unmodified histone H3R2 links UHRF1 to regulation of euchromatic gene expression Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1 Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53 Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain Structural insights into human KAP1 PHD finger-bromodomain and its role in gene silencing Regulation of chromatin by histone modifications Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor Role of hPHF1 in H3K27 methylation and Hox gene silencing Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair Epigenetic Mechanisms in Developmental Alcohol-Induced Neurobehavioral Deficits Structural and functional coordination of DNA and histone methylation KDM4/JMJD2 histone demethylases: epigenetic regulators in cancer cells Nucleation and spreading of a heterochromatic domain in fission yeast.Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression Structural and functional analyses of methyl-lysine binding by the malignant brain tumour repeat protein Sex comb on midleg The plant homeodomain finger of RAG2 recognizes histone H3 methylated at both lysine-4 and arginine-2 Structural Basis for Lower Lysine Methylation State-Specific Readout by MBT Repeats of L3MBTL1 and an Engineered PHD Finger Structural Basis for the Recognition of Methylated Histone H3K36 by the Eaf3 Subunit of Histone Deacetylase Complex Rpd3S Role of the polycomb protein EED in the propagation of repressive histone marks Mouse Piwi interactome identifies binding mechanism of Tdrkh Tudor domain to arginine methylated Miwi Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans Structure of an atypical Tudor domain in theDrosophilaPolycomblike protein Structural basis for methylarginine-dependent recognition of Aubergine by Tudor

P2860

Q21263183-250480B4-E142-4530-97B5-504183BCC74B Q24292904-1B3906F9-E4D2-4ACB-B7A7-EA09160E484C Q24298348-BC1861AD-8988-4A9E-90C5-6C5EC0A9B563 Q24299712-34A30A7B-FD17-4C2E-BE6B-4B256518AF0E Q24301141-322163D9-3888-4FA5-BD98-62910FFCF997 Q24301290-C9A6B804-5DCD-4D1C-A93C-AE6C4768D007 Q24301311-DA5A3073-4B1B-40BA-8761-BE1DC09AD17B Q24301878-26A32EA1-ADAE-4C21-81A2-05A4A4C88511 Q24303435-3D599F21-3388-495D-B603-17C07E4E9F8B Q24306486-3FFCF502-1466-48F3-9BC9-DB534B946E16 Q24306793-BFCE9082-1DA2-4BB4-ADDF-B56DDADF3668 Q24310492-86E83376-C820-4E4D-9C78-E3ADE8076DB6 Q24311521-939D9775-DBBB-4893-89A8-154A1770BA62 Q24313233-4C3D6552-ABEF-40BC-A41C-5D30AE73E57A Q24315922-66F1DB0F-0FA1-4AA6-AEB8-68B51C15CDDC Q24320777-152B0D1D-4910-4BA4-B3DB-91B75ABB786C Q24338923-409F74DF-BF70-4229-A3A3-855606591A91 Q24594648-9686A9EE-354B-41E9-8BCF-52009C7C0548 Q24613876-1AE27E58-472F-4156-A53E-4D5994C41A1C Q24615547-A9172DB5-C852-42BC-ACC7-13AB28F35766 Q24634118-C171974E-174E-480C-B499-6163985EA1AB Q24635070-9A3B2FD2-89E9-4A16-AEF5-A270D8516130 Q24648004-A752FC56-EE1D-408C-AA7B-A4201250B56C Q24658072-10B79E3D-5AEE-455C-8EF8-567CBA90569B Q24669691-41ECB29D-70DC-4D63-8B38-F055F2D19169 Q26748876-CA6133D2-D9EC-432B-BDED-B3CFDDE63D81 Q26825534-8E9924EF-8A12-44BE-BEFD-7062A6460AF1 Q27007679-E5DFD4B6-7084-4955-92B7-A15A7A990E9E Q27317215-3B7F78B5-C1B6-4E9F-A398-010963FF81C2 Q27646401-346A70F0-4D47-4B26-BD9B-1A774C644A8F Q27647088-15F6E367-E7D7-43B1-B2E6-4060696FB0BE Q27648759-B15EACD9-937A-403A-BE4B-8BF928D7DA49 Q27649107-2E2311EC-AC0A-4026-A9D2-B581B41DDD3D Q27649150-FBD64838-659F-4375-89B2-B8DB7146DBDC Q27652290-34DBE8A7-C1BD-4172-A4FE-A6089AA10533 Q27657483-CFFFCA4B-616C-457C-99BB-F5B05364A4D0 Q27658209-250ED6E1-C364-4047-A890-2D7C872CD266 Q27662561-B2250339-7450-4975-9F51-61A6B282C1AB Q27663647-9117D967-F603-4180-8BB6-0E85FA44F7B9 Q27664064-C941D8D5-0995-4B12-8E44-5E3B245D963E

P2860

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

http://www.wikidata.org/entity/Q29614520

description

2006 nî lūn-bûn

@nan

2006 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

@ast

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

@en

type

label

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

@ast

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

@en

prefLabel

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

@ast

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

@en

P1433

Q29614520-B80E9874-DD86-4F65-B5A5-55B2DCDE024B

P1476

Q29614520-06AA3ED5-7540-47AC-ADB3-48E89BAE000D

P2093

Q29614520-3E5A64EA-4D0E-466B-B122-0488D8A51DF3

Q29614520-6887B9C7-B9E0-4BAD-B12C-0277A1A9F650

Q29614520-8308C0ED-3ADF-487E-B9F2-ABFEC9078D9A

Q29614520-CEEDFE8C-5822-4B3D-8252-C4B45831F326

Q29614520-ED25FFEC-833C-4D29-A519-845A96927145

P304

Q29614520-F0A1A29B-E9B5-44A0-960A-2B8BC5146375

P31

Q29614520-25E5AD5A-35A3-4A6B-B99E-19384862A297

P3181

Q29614520-EFC36AA4-74B3-4A5E-BDAF-24C11FB303FE

P356

Q29614520-874BCC53-48DC-4584-974A-EA7F6A4EA3F5

P407

Q29614520-1475BDFF-9469-45CC-BF8E-541A4827FD01

P433

Q29614520-3C848169-AA10-40E4-ADD0-C5663B64EE8E

P478

Q29614520-B467B8B2-5862-4590-A09A-BA2F23BD1143

P577

Q29614520-66766E51-3FB2-4BE4-BF0D-58FB9CA392F2

P5875

Q29614520-6B01E38F-B3D8-427E-9D9A-58D162AF9104

P698

Q29614520-FDA220E0-0026-41FA-9D7C-D1BE7AE4168F

P3181

P356

SCIENCE.1125162

P1433

P1476

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A

@en

P2093

Bedford MT

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

Fang J

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

Huang Y

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

Xu RM

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

Zhang Y

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

P304

748-51

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

P31

scholarly article

P3181

1724144

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

P356

10.1126/SCIENCE.1125162

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

P407

P433

5774

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

P478

312

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

P577

2006-05-05T00:00:00Z

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

P5875

7178955

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

P698

16601153

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