SET domain protein lysine methyltransferases: Structure, specificity and catalysis.
about
Sinefungin derivatives as inhibitors and structure probes of protein lysine methyltransferase SETD2Dimerization of a viral SET protein endows its functionEpigenetic transcriptional repression of cellular genes by a viral SET proteinIdentification of a novel gene, CIA6, required for normal pyrenoid formation in Chlamydomonas reinhardtiiEpigenetic Mechanisms in Developmental Alcohol-Induced Neurobehavioral DeficitsHistone methyltransferases: novel targets for tumor and developmental defectsThe functional diversity of protein lysine methylationSMYD proteins: key regulators in skeletal and cardiac muscle development and functionTubulin tyrosine ligase like 12, a TTLL family member with SET- and TTL-like domains and roles in histone and tubulin modifications and mitosisThe Identification and Structure of an N-Terminal PR Domain Show that FOG1 Is a Member of the PRDM Family of ProteinsStructural Biology of Human H3K9 MethyltransferasesStructural and Functional Profiling of the Human Histone Methyltransferase SMYD3Structure of Human SMYD2 Protein Reveals the Basis of p53 Tumor Suppressor MethylationMultivalent Interactions by the Set8 Histone Methyltransferase With Its Nucleosome SubstrateIdentification of two SET domain proteins required for methylation of lysine residues in yeast ribosomal protein Rpl42ab.KDM1 class flavin-dependent protein lysine demethylasesDiscovery of the β-barrel-type RNA methyltransferase responsible for N6-methylation of N6-threonylcarbamoyladenosine in tRNAsmiR-24 regulates menin in the endocrine pancreasGenome-wide analysis of the SET DOMAIN GROUP family in grapevine.Chromatin signaling to kinetochores: transregulation of Dam1 methylation by histone H2B ubiquitinationComparative Analysis of Ralstonia solanacearum MethylomesEZH2: not EZHY (easy) to deal.Histone methylation by NUE, a novel nuclear effector of the intracellular pathogen Chlamydia trachomatisBioinformatic Identification of Novel MethyltransferasesViral-encoded enzymes that target host chromatin functions.Phylogenetic analysis and classification of the Brassica rapa SET-domain protein family.Cancer stem cells generated by alcohol, diabetes, and hepatitis C virus.Current limitations and future opportunities for epigenetic therapies.Substrate and product specificities of SET domain methyltransferasesA molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36.Uncovering the human methyltransferasome.Dynamics of histone lysine methylation: structures of methyl writers and erasersA cytoplasm-specific activity encoded by the Trithorax-like ATX1 geneStructural insights into binding of small molecule inhibitors to Enhancer of Zeste Homolog 2.Lysine methyltransferase G9a methylates the transcription factor MyoD and regulates skeletal muscle differentiationTwo SET domain containing genes link epigenetic changes and aging in Caenorhabditis elegansDifferentially expressed genes distributed over chromosomes and implicated in certain biological processes for site insertion genetically modified rice KemingdaoA direct label-free MALDI-TOF mass spectrometry based assay for the characterization of inhibitors of protein lysine methyltransferases.Epigenetic regulation of oogenesis and germ stem cell maintenance by the Drosophila histone methyltransferase Eggless/dSetDB1.Di- and tri- but not monomethylation on histone H3 lysine 36 marks active transcription of genes involved in flowering time regulation and other processes in Arabidopsis thaliana.
P2860
Q24300459-FBC7AF42-9264-4339-96FF-C6711B29BCF5Q24615662-49420698-07C5-47F6-887E-D296B37DF890Q24618421-3D5F5DDF-482B-44F9-8502-30FFD33221AEQ24635898-C9F43CCB-224D-480A-A279-DA026D66A4E3Q26748876-60206592-12D9-43F5-9FDE-8ECE3D1A14C9Q26775027-8B455337-BED4-4D32-B0F6-F1F0A7F54FF9Q26853164-56022546-38F6-48B3-92B4-D560430A35A3Q26865167-5BEA7571-1572-4AFD-A738-64D15187FCA9Q27332007-459656DA-57CD-4A4D-95C6-DD672DE1437AQ27640551-C125A657-5925-4F87-8C40-4A788484D131Q27659033-311B5CCE-68D9-4A33-B2CA-8B69CACC536EQ27670941-040B9721-574D-415E-9586-E5D4B5E72B31Q27672574-2234DE2D-F6B5-4B00-A52F-2F3AAE84AF3BQ27704231-69EEBA9F-492C-4089-B2A5-57C3C910E9F2Q27931911-986C50A9-9783-4D23-85B6-2152449E6036Q28084876-8E8CC499-5F70-4354-8BB4-A3FBCEABEE36Q28117728-32EFF151-2213-400B-829B-A52C27576D26Q28593937-DE4A0EFF-7069-475D-9283-E3F730498AF3Q30062213-27554EF6-70B5-4CCC-ADD4-6066057A81B3Q33285644-30C5DD00-83AE-44C1-B24D-FDA8910B6976Q33559429-0BFAB957-F582-4E84-A5AA-97B23AE55120Q33610902-250C161A-F14E-4C70-9B70-2498C9252643Q33640286-2D48302E-8A40-4F5B-8B69-1ADE0E0211CAQ33938689-0F3C8C41-FCF1-4338-BAA9-7450320913C6Q34073129-67947384-C9B4-443A-9C2A-A8B9BA5D7F16Q34101030-E9687DD9-6705-40C2-8EB5-569441148025Q34155181-17FA0B24-F19D-41A0-A92F-71B76DC0CF6AQ34195077-7161119E-B8F8-4467-812E-C28401174BA2Q34208487-BC7C3744-E6C7-4288-AEAB-06F0AD1927D5Q34342916-2B61569C-659A-46AF-BE8C-881A19CE933AQ34454874-D3F7418D-2618-4604-9B60-A2547EAA0AABQ34620820-5A0A6527-3721-4F67-AF96-CCF4C4A01DAAQ35040912-D889C54C-6E6F-4037-862F-B5F507AD9034Q35228394-A2F2B3D7-F0E9-4C49-9746-0B8E47174C01Q35735009-42FC0AD2-FF68-4DC0-B986-9A6C6C0867F7Q35836441-84239AD0-0FF2-4E26-80CA-96882E8ECDF7Q36101965-F74651DC-BD91-4BF6-9A3C-ECE6C719889DQ36340686-0DD0BF17-7DA2-4703-ABDF-AE090C405566Q36398891-E4F25386-CE66-4C9C-8AB5-0717205B5649Q36483376-5CC8EF38-2DCA-45B2-B0B1-B95E8CB0A4E9
P2860
SET domain protein lysine methyltransferases: Structure, specificity and catalysis.
description
2006 nî lūn-bûn
@nan
2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի դեկտեմբերին 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
SET domain protein lysine methyltransferases: Structure, specificity and catalysis.
@ast
SET domain protein lysine methyltransferases: Structure, specificity and catalysis.
@en
type
label
SET domain protein lysine methyltransferases: Structure, specificity and catalysis.
@ast
SET domain protein lysine methyltransferases: Structure, specificity and catalysis.
@en
prefLabel
SET domain protein lysine methyltransferases: Structure, specificity and catalysis.
@ast
SET domain protein lysine methyltransferases: Structure, specificity and catalysis.
@en
P1476
SET domain protein lysine methyltransferases: Structure, specificity and catalysis
@en
P2093
P2888
P304
P356
10.1007/S00018-006-6274-5
P577
2006-12-01T00:00:00Z