M.EcoPl5 methylates the second adenine in its recognition sequence

scientific article published on July 25, 1991

M.EcoPl5 methylates the second adenine in its recognition sequence is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1093/NAR/19.14.3997
P953full work available at URLhttp://academic.oup.com/nar/article-pdf/19/14/3997/3308127/19-14-3997.pdf
https://europepmc.org/articles/PMC328496
https://europepmc.org/articles/PMC328496?pdf=render
P932PMC publication ID328496
P698PubMed publication ID1861989

P50authorAndreas MeiselQ42715890
P2093author name stringD. H. Krüger
T. A. Bickle
P2860cites workNucleotide sequence of adenovirus 2 DNA fragment encoding for the carboxylic region of the fiber protein and the entire E4 regionQ35741364
DNA recognition and cleavage by the EcoP15 restriction endonucleaseQ40289784
Effect of site-specific methylation on DNA modification methyltransferases and restriction endonucleasesQ64140382
P433issue14
P407language of work or nameEnglishQ1860
P921main subjectgeneticsQ7162
P304page(s)3997
P577publication date1991-07-01
1991-07-25
P1433published inNucleic Acids ResearchQ135122
P1476titleM.EcoP15 methylates the second adenine in its recognition sequence
M.EcoPl5 methylates the second adenine in its recognition sequence
P478volume19

Reverse relations

cites work (P2860)
Q33851803ATP-dependent restriction enzymes
Q24634671Biology of DNA restriction
Q24816456Characterization of the Type III restriction endonuclease PstII from Providencia stuartii.
Q35259150DNA cleavage site selection by Type III restriction enzymes provides evidence for head-on protein collisions following 1D bidirectional motion.
Q38295255DNA recognition by the EcoP15I and EcoPI modification methyltransferases
Q37698622Diversity of DNA methyltransferases that recognize asymmetric target sequences
Q35921364Effect of site-specific methylation on DNA modification methyltransferases and restriction endonucleases
Q34990892Effect of site-specific methylation on restriction endonucleases and DNA modification methyltransferases
Q39744399Functional cooperation between exonucleases and endonucleases--basis for the evolution of restriction enzymes
Q40855229Genomic structure of the human DNA methyltransferase gene
Q44548818Identification and mutational analysis of Mg2+ binding site in EcoP15I DNA methyltransferase: involvement in target base eversion
Q34598959MmeI: a minimal Type II restriction-modification system that only modifies one DNA strand for host protection
Q36305686Movement of DNA sequence recognition domains between non-orthologous proteins.
Q77195407Probing the role of cysteine residues in the EcoP15I DNA methyltransferase
Q42128175S-adenosyl homocysteine and DNA ends stimulate promiscuous nuclease activities in the Type III restriction endonuclease EcoPI
Q39095250Type III restriction endonucleases are heterotrimeric: comprising one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA.
Q37698719Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysis
Q55043499Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage
Q34358103Type III restriction-modification enzymes: a historical perspective

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