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Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP functionStructural and Functional Characterization of Rv2966c Protein Reveals an RsmD-like Methyltransferase from Mycobacterium tuberculosis and the Role of Its N-terminal Domain in Target RecognitionThe human Dnmt2 has residual DNA-(cytosine-C5) methyltransferase activity.Beyond Watson and Crick: DNA methylation and molecular enzymology of DNA methyltransferases.Diversity of DNA methyltransferases that recognize asymmetric target sequences.DNA methyltransferases: mechanistic models derived from kinetic analysis.Biotin-avidin microplate assay for the quantitative analysis of enzymatic methylation of DNA by DNA methyltransferases.A potent cell-active allosteric inhibitor of murine DNA cytosine C5 methyltransferase.Helicobacter pylori DNA methyltransferases and the epigenetic field effect in cancerizationMechanisms and Biological Roles of DNA Methyltransferases and DNA Methylation: From Past Achievements to Future Challenges.Novel m4C modification in type I restriction-modification systems.The cytosine N4-methyltransferase M.PvuII also modifies adenine residues.N(6)-Adenine DNA-methyltransferase in wheat seedlings.Undetectable levels of N6-methyl adenine in mouse DNA: Cloning and analysis of PRED28, a gene coding for a putative mammalian DNA adenine methyltransferase
P2860
Q24555212-D8C2C272-5082-4AA8-9D69-906962AEB64CQ27667462-0EAAB9DE-F482-4DD0-B80D-0AF43617AD96Q34204135-78DF9212-4E61-4C32-87F9-2DB8D784CF3BQ34587622-4C0F0433-EBC9-419A-88F4-D98577EF7268Q37698622-53B8A44A-0A68-4779-897E-E9BFF3A5D66EQ37977119-0B9CCB03-CA20-4D49-8F72-6692C5070ACCQ38312858-05273FB1-18C4-438E-AC27-C3B38133620BQ38359862-0CAD37C1-77C8-4939-B0EC-66B821721D7CQ38587023-FF35B34D-0700-4AF1-8A51-282B13D114CEQ38797211-C67E40DF-A7AF-44E2-9212-CACCBDBA4C77Q42372152-234741CF-302E-45EB-9732-03DCA0CC8E94Q43639216-2F72C700-3485-499B-9A54-B9DA92304A2FQ43953831-79C78AA0-3FCA-4CE6-A073-3D656BBF3E82Q56656183-97055E36-41A0-4794-89C7-544B500735B2
P2860
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im Juli 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в липні 1999
@uk
name
On the Substrate Specificity of DNA Methyltransferases
@en
On the Substrate Specificity of DNA Methyltransferases
@nl
type
label
On the Substrate Specificity of DNA Methyltransferases
@en
On the Substrate Specificity of DNA Methyltransferases
@nl
prefLabel
On the Substrate Specificity of DNA Methyltransferases
@en
On the Substrate Specificity of DNA Methyltransferases
@nl
P2093
P2860
P356
P1476
On the substrate specificity o ...... tosine residues at position N4
@en
P2093
P2860
P304
19538-19544
P356
10.1074/JBC.274.28.19538
P407
P577
1999-07-01T00:00:00Z