scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.M307053200 |
P698 | PubMed publication ID | 12917398 |
P50 | author | Pradeep Bist | Q118395419 |
P2093 | author name string | Desirazu N Rao | |
P2860 | cites work | Structure and function of type II restriction endonucleases | Q24555230 |
The DNA (cytosine-5) methyltransferases | Q24614934 | ||
Purification and characterisation of a novel DNA methyltransferase, M.AhdI | Q24671538 | ||
A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes | Q24684053 | ||
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 | Q25938983 | ||
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding | Q25938984 | ||
The role of metals in catalysis by the restriction endonuclease BamHI | Q27765729 | ||
Rapid and efficient site-specific mutagenesis without phenotypic selection | Q27860608 | ||
The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif | Q28214697 | ||
Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase | Q28510756 | ||
Characterization of AloI, a restriction-modification system of a new type | Q34102760 | ||
M.EcoPl5 methylates the second adenine in its recognition sequence | Q35772916 | ||
DNA binding and recognition by the IIs restriction endonuclease MboII. | Q38295631 | ||
Interaction of EcoP15I DNA methyltransferase with oligonucleotides containing the asymmetric sequence 5'-CAGCAG-3'. | Q38304144 | ||
Binding of EcoP15I DNA methyltransferase to DNA reveals a large structural distortion within the recognition sequence | Q38312746 | ||
Identification of TaqI endonuclease active site residues by Fe2+-mediated oxidative cleavage | Q38330980 | ||
Functional analysis of conserved motifs in EcoP15I DNA methyltransferase | Q38356849 | ||
The metal-independent type IIs restriction enzyme BfiI is a dimer that binds two DNA sites but has only one catalytic centre | Q38357645 | ||
Substrate DNA and cofactor regulate the activities of a multi-functional restriction-modification enzyme, BcgI. | Q39721172 | ||
Functional cooperation between exonucleases and endonucleases--basis for the evolution of restriction enzymes | Q39744399 | ||
Structure and Function of DNA Methyltransferases | Q40475987 | ||
Purification and properties of the Eco57I restriction endonuclease and methylase--prototypes of a new class (type IV) | Q40535626 | ||
Chemistry and biology of DNA methyltransferases | Q41311755 | ||
Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes | Q48069333 | ||
Calcium-proton and calcium-magnesium antagonisms in calmodulin: microcalorimetric and potentiometric analyses | Q48289010 | ||
Type III DNA restriction and modification systems EcoP1 and EcoP15. Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1 mod mutants | Q48327658 | ||
Specific DNA recognition by EcoRV restriction endonuclease induced by calcium ions. | Q54618527 | ||
BASE FLIPPING | Q56256582 | ||
LXXIII.—Oxidation of tartaric acid in presence of iron | Q60304014 | ||
DNA restriction--modification enzymes of phage P1 and plasmid p15B. Subunit functions and structural homologies | Q67286996 | ||
Cloning, over-expression and the catalytic properties of the EcoP15 modification methylase from Escherichia coli | Q69387013 | ||
Characterization of a new sarcoplasmic calcium-binding protein with magnesium-induced cooperativity in the binding of calcium | Q70967977 | ||
Quantitative evaluation of metal ion binding to PvuII restriction endonuclease | Q73345804 | ||
Identification of the metal-binding sites of restriction endonucleases by Fe2+-mediated oxidative cleavage | Q73543792 | ||
FokI requires two specific DNA sites for cleavage | Q74326486 | ||
Probing the role of cysteine residues in the EcoP15I DNA methyltransferase | Q77195407 | ||
Two intertwined methylation activities of the MmeI restriction-modification class-IIS system from Methylophilus methylotrophus | Q77702970 | ||
P433 | issue | 43 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | mutational analysis | Q1955810 |
P304 | page(s) | 41837-41848 | |
P577 | publication date | 2003-08-12 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Identification and mutational analysis of Mg2+ binding site in EcoP15I DNA methyltransferase: involvement in target base eversion | |
P478 | volume | 278 |
Q42087303 | A divalent metal ion-dependent N(1)-methyl transfer to G37-tRNA. |
Q36868466 | DNA base flipping by both members of the PspGI restriction-modification system |
Q37698622 | Diversity of DNA methyltransferases that recognize asymmetric target sequences |
Q28477117 | Functional analysis of an acid adaptive DNA adenine methyltransferase from Helicobacter pylori 26695 |
Q42399985 | Kinetics of Methylation by EcoP1I DNA Methyltransferase |
Q99240507 | Mg2+-Dependent Methyl Transfer by a Knotted Protein: A Molecular Dynamics Simulation and Quantum Mechanics Study |
Q36598928 | Structure, function and mechanism of exocyclic DNA methyltransferases |
Q33831806 | The impact of the C-terminal domain on the interaction of human DNA topoisomerase II α and β with DNA. |
Q46353173 | TrmD: A Methyl Transferase for tRNA Methylation With m1G37. |
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