scholarly article | Q13442814 |
P2093 | author name string | Walter J | |
Blumenthal RM | |||
Tao T | |||
Brennan KJ | |||
Cotterman MM | |||
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The tac promoter: a functional hybrid derived from the trp and lac promoters | Q24602390 | ||
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 | Q25938983 | ||
Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors | Q26778475 | ||
Buffer gradient gels and 35S label as an aid to rapid DNA sequence determination | Q27860827 | ||
Cloning and sequencing of a cDNA encoding DNA methyltransferase of mouse cells. The carboxyl-terminal domain of the mammalian enzymes is related to bacterial restriction methyltransferases | Q28292993 | ||
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis | Q29053311 | ||
Cloning and sequencing of a cDNA encoding DNA methyltransferase of mouse cells | Q29399636 | ||
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Dideoxy sequencing method using denatured plasmid templates | Q29620525 | ||
N4-methylcytosine as a minor base in bacterial DNA. | Q34048673 | ||
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Sequence motifs specific for cytosine methyltransferases | Q34170996 | ||
Calcium-dependent bacteriophage DNA infection | Q34223120 | ||
The organization and complete nucleotide sequence of the PstI restriction-modification system | Q34255892 | ||
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Cytosine modification in DNA by BcnI methylase yields N4-methylcytosine | Q34272641 | ||
Regulation of transcription factor rho and the alpha subunit of RNA polymerase in Escherichia coli B/r | Q35009023 | ||
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Sequence-specific recognition of double helical nucleic acids by proteins | Q35987597 | ||
Cloning of a restriction-modification system from Proteus vulgaris and its use in analyzing a methylase-sensitive phenotype in Escherichia coli | Q36278645 | ||
Common evolutionary origin of the phage T4 dam and host Escherichia coli dam DNA-adenine methyltransferase genes | Q36279937 | ||
Relaxed sequence specificities of Eco RI endonuclease and methylase: mechanisms, possible practical applications, and uses in defining protein-nucleic acid recognition mechanisms. | Q40256388 | ||
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Sequential order of target-recognizing domains in multispecific DNA-methyltransferases | Q41107194 | ||
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Direct role of the himA gene product in phage λ integration | Q54536631 | ||
The GATATC-modification enzyme EcoRV is closely related to the GATC-recognizing methyltransferases DpnII and dam from E. coli and phage T4. | Q54762518 | ||
Escherichia coli integration host factor binds specifically to the ends of the insertion sequence IS1 and to its major insertion hot-spot in pBR322. | Q54764890 | ||
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From primeval message to present-day gene | Q70262224 | ||
T antigen binding and the control of SV40 gene expression | Q72919984 | ||
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P433 | issue | 11 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | cytosine | Q178425 |
P304 | page(s) | 4161-4175 | |
P577 | publication date | 1989-06-01 | |
P1433 | published in | Nucleic Acids Research | Q135122 |
P1476 | title | Sequence, internal homology and high-level expression of the gene for a DNA-(cytosine N4)-methyltransferase, M.Pvu II. | |
P478 | volume | 17 |
Q36130467 | A family of regulatory genes associated with type II restriction-modification systems |
Q24634671 | Biology of DNA restriction |
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Q24633048 | Characterization of the cloned BamHI restriction modification system: its nucleotide sequence, properties of the methylase, and expression in heterologous hosts |
Q42635400 | Cloning and characterization of two tandemly arranged DNA methyltransferase genes of Neisseria lactamica: an adenine-specific M.NlaIII and a cytosine-type methylase |
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Q40525786 | Complete nucleotide sequence of the PvuII restriction enzyme gene from Proteus vulgaris. |
Q37977119 | DNA methyltransferases: mechanistic models derived from kinetic analysis |
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Q36149422 | In vivo genetic exchange of a functional domain from a type II A methylase between lactococcal plasmid pTR2030 and a virulent bacteriophage |
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Q28776309 | Purification, cloning and sequence analysis of RsrI DNA methyltransferase: lack of homology between two enzymes, RsrI and EcoRI, that methylate the same nucleotide in identical recognition sequences |
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