Substrate and product specificities of SET domain methyltransferases - Wikidata - wikimedia - TriplyDB

Substrate and product specificities of SET domain methyltransferases

Substrate and product specificities of SET domain methyltransferases

http://www.wikidata.org/entity/Q34208487

about

Human METTL20 is a mitochondrial lysine methyltransferase that targets the β subunit of electron transfer flavoprotein (ETFβ) and modulates its activity Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation Histone methyltransferases: novel targets for tumor and developmental defects Transcriptional regulation by the Set7 lysine methyltransferase Protein methylation at the surface and buried deep: thinking outside the histone box Crystal Structure and Functional Analysis of JMJD5 Indicate an Alternate Specificity and Function Multivalent Interactions by the Set8 Histone Methyltransferase With Its Nucleosome Substrate Catalytic and functional roles of conserved amino acids in the SET domain of the S. cerevisiae lysine methyltransferase Set1 A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation.Neuronal Kmt2a/Mll1 histone methyltransferase is essential for prefrontal synaptic plasticity and working memory ETO family protein Mtgr1 mediates Prdm14 functions in stem cell maintenance and primordial germ cell formation Cell signaling, post-translational protein modifications and NMR spectroscopy Rapid changes in histone deacetylases and inflammatory gene expression in expert meditators.Setd5 is essential for mammalian development and the co-transcriptional regulation of histone acetylation.Regulation of histone H3K4 methylation in brain development and disease.Mapping of Post-translational Modifications of Transition Proteins, TP1 and TP2, and Identification of Protein Arginine Methyltransferase 4 and Lysine Methyltransferase 7 as Methyltransferase for TP2.Saccharomyces cerevisiae Eukaryotic Elongation Factor 1A (eEF1A) Is Methylated at Lys-390 by a METTL21-Like Methyltransferase.Proper Activity of Histone H3 Lysine 4 (H3K4) Methyltransferase Is Required for Morphogenesis during Zebrafish Cardiogenesis Engineering of Methylation State Specific 3xMBT Domain Using ELISA Screening.A direct label-free MALDI-TOF mass spectrometry based assay for the characterization of inhibitors of protein lysine methyltransferases.A continuous kinetic assay for protein and DNA methyltransferase enzymatic activities.Differential mRNA expression levels of human histone-modifying enzymes in normal karyotype B cell pediatric acute lymphoblastic leukemia.SET for life: biochemical activities and biological functions of SET domain-containing proteins Purification, crystallization and X-ray crystallographic studies on a putative methyltransferase, YtqB, from Bacillus subtilis.Histone lysine methylation dynamics: establishment, regulation, and biological impact Epigenetic Regulation.Histone Modifications in Major Depressive Disorder and Related Rodent Models.SETD4 Regulates Cell Quiescence and Catalyzes the Trimethylation of H4K20 during Diapause Formation in Artemia.MLL5 (KMT2E): structure, function, and clinical relevance.Orchestration of H3K27 methylation: mechanisms and therapeutic implication.The HIV-1 Tat Protein Is Monomethylated at Lysine 71 by the Lysine Methyltransferase KMT7 Opposite Effects of SET7/9 on Apoptosis of Human Acute Myeloid Leukemia Cells and Lung Cancer Cells.Identification of functionally relevant lysine residues that modulate human farnesoid X receptor activation.Lysine Possesses the Optimal Chain Length for Histone Lysine Methyltransferase Catalysis.Bivalent Epigenetic Control of Oncofetal Gene Expression in Cancer.Neuronal Deletion of Kmt2a/Mll1 Histone Methyltransferase in Ventral Striatum is Associated with Defective Spike-Timing-Dependent Striatal Synaptic Plasticity, Altered Response to Dopaminergic Drugs, and Increased Anxiety.Emerging Roles for Epigenetic Programming in the Control of Inflammatory Signaling Integration in Heath and Disease.Inhibition of Methyltransferase Setd7 Allows the In Vitro Expansion of Myogenic Stem Cells with Improved Therapeutic Potential.SET7/9 promotes hepatocellular carcinoma progression through regulation of E2F1

P2860

Q24306907-183CE305-0803-45BB-827C-26BFED046E0F Q24315705-F17542FF-AD56-4B70-BACB-035DD6D30011 Q26775027-B17F7ABE-DEE2-4770-A9BF-ED81F9D8B0DB Q27009508-4F9F2E46-3630-477E-85C7-7FBA383DF44D Q27025874-D80195AC-4453-4556-895C-DB30EB0B8391 Q27671023-156EA078-165A-4F4C-9452-E68ECB81E5FF Q27704231-43B9D2D7-3503-4FC7-A67B-1A4DCB35FBB7 Q27935081-270CDAD8-ACCE-4BFC-AE49-287B05B59EF8 Q27939199-15A9D481-697D-4E43-8790-AF6229462008 Q27939383-115BBE1C-892C-400D-B505-FE4EC03D1038 Q28512874-B78CA6B8-623F-4E6D-8E5D-C89A3AB7798B Q28589379-EDB01ADC-E3FE-480E-A861-CCA3757F9BFE Q28830783-65B1A494-37E4-4C98-81E7-0110119654CD Q30579284-89541743-CB2D-4CE3-9D04-4DC1C1FFBB7C Q32874823-FB56FB22-0F6C-4BFD-986C-953A00CB05AC Q34079415-713513B5-B1C6-40A8-9D1D-9E7F279978EB Q35583111-2F642BAB-252A-4816-A1E4-FE79A04001B1 Q35675772-80173C23-84C9-446B-909D-1FA8AA02953D Q35749749-B2EBE8DB-6222-4C65-AAAC-8EDCF457F33B Q35998418-99F83907-CEFC-4E72-9AED-A3BB8A6C1DB2 Q36340686-53EE9965-699F-4798-92B9-24A56700BDED Q36370680-33A392B5-9E08-4286-908A-C1518CF0A9DC Q36656083-FAA574DB-FFE3-4C4C-B4D3-1CDA2A73F0DE Q37615671-FF7FDCDB-9363-459B-8A6A-690DE9E3138E Q37685286-94DF0C24-6236-4B8C-B97A-C2F1CF1081CF Q38064095-378B177E-F4C2-4FD9-AB53-23C739DFBE99 Q38667118-30DEADDA-5F27-4E1C-BBBE-737590418B16 Q38681922-14CCA35A-1739-4908-9131-324A80F28ADC Q38723933-019D796B-2AF7-4C56-A9D3-0DAC7A12C522 Q39131004-73F9D58D-4023-4E96-9719-529385539AA6 Q39440781-51C9A1FB-4866-46D5-845E-29DD38ACBC3A Q40731101-CA908F1D-5AF0-457F-AA64-5FD011DAD771 Q41439912-6CAFF51A-3924-476F-924E-B9D86E748C29 Q41943299-8EA06082-5670-4027-98C9-C6CA746A02DF Q47165835-88846217-66D4-4BAC-BA46-0E7EDC98FF67 Q47295917-A39D779B-96A3-4E7C-B2E6-D5505EFB762F Q47404387-AA91CBEC-C1FB-43D6-AF1E-F2C5AD88B3AC Q50045989-AB1F73AA-4828-45DE-8328-76FDF02D8DD1 Q50209897-BE80E5ED-D087-46E1-AB04-1B29CEE5761A Q58802944-A0AB995C-AE52-4374-A283-014C24153877

P2860

Substrate and product specificities of SET domain methyltransferases

http://www.wikidata.org/entity/Q34208487

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Substrate and product specificities of SET domain methyltransferases

@ast

Substrate and product specificities of SET domain methyltransferases

@en

Substrate and product specificities of SET domain methyltransferases

@nl

type

label

Substrate and product specificities of SET domain methyltransferases

@ast

Substrate and product specificities of SET domain methyltransferases

@en

Substrate and product specificities of SET domain methyltransferases

@nl

prefLabel

Substrate and product specificities of SET domain methyltransferases

@ast

Substrate and product specificities of SET domain methyltransferases

@en

Substrate and product specificities of SET domain methyltransferases

@nl

P1433

Q34208487-AF6B718D-F09F-4E80-B3B4-9BBE230DC39A

P1476

Q34208487-E262F018-80E8-4FA8-8C04-81480E560A93

P2093

Q34208487-914573AC-2EA2-4370-AF1B-81B677918B12

Q34208487-D704342E-DD68-424D-B124-FB8BFE8840E6

P2860

Q34208487-02258581-B161-462B-AD63-61A8ADEAC161

Q34208487-071C6359-7013-474D-B09A-2CDC56B0AF57

Q34208487-076714AC-E2EC-4143-A58B-97AD7094DEE3

Q34208487-0A4C63F3-1F73-4557-86E5-5FE2A3F8FCA1

Q34208487-1017ED9C-E082-4368-9A8B-1548A949B6B0

Q34208487-18C24625-0FB5-4AA2-B45A-6CB1955A32AD

Q34208487-192F2802-E70C-4FF0-893A-4AD13A56F715

Q34208487-198CDBE2-0008-44EA-978E-9A4646D45ABA

Q34208487-1EB9063F-431F-49A2-B9CC-0E36255B9676

Q34208487-2357AB1B-3C25-450A-BDDA-5EF0C89725A0

P304

Q34208487-DF77BB80-616C-4515-B220-BBB1463CAFA5

P31

Q34208487-6BEAA8D3-3DD4-42B3-ACC6-0D0736B31FCC

P356

Q34208487-2820771F-DAE8-4257-8B04-1C8C32CDC585

P433

Q34208487-7CD078C6-4225-40DC-A49A-D95F9BD75804

P478

Q34208487-97032185-6F7D-4720-9A93-80332E6947A4

P577

Q34208487-62666C10-AC6B-4B36-94A3-D7D09F296458

P5875

Q34208487-00264004-FCA7-47FC-B249-9C1CF18AE89E

P698

Q34208487-F7112ADA-F4AB-4D2A-9FF8-49CEF6E3B20B

P932

Q34208487-6D7AB229-BBC8-4B81-A326-E0CADCF14E18

P356

P1433

P1476

Substrate and product specificities of SET domain methyltransferases

@en

P2093

Paul A Del Rizzo

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

Raymond C Trievel

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

P2860

Regulation of chromatin structure by site-specific histone H3 methyltransferases

p53 is regulated by the lysine demethylase LSD1

Structure and catalytic mechanism of the human histone methyltransferase SET7/9

Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation

Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4

G9a and Glp methylate lysine 373 in the tumor suppressor p53

Methylation of the retinoblastoma tumor suppressor by SMYD2

Structural basis for the methylation site specificity of SET7/9

Interplay between lysine methylation and Cdk phosphorylation in growth control by the retinoblastoma protein

Regulation of p53 activity through lysine methylation

P304

1059-1067

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

P31

scholarly article

P356

10.4161/EPI.6.9.16069

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

P433

9

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

P478

6

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

P577

2011-09-01T00:00:00Z

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

P5875

51576441

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

P698

21847010

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

P932

3225744

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