scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.M209192200 |
P698 | PubMed publication ID | 12519752 |
P2093 | author name string | Michael D Topal | |
Kevin L Carrick | |||
P2860 | cites work | Mutational analysis of Escherichia coli DNA ligase identifies amino acids required for nick-ligation in vitro and for in vivo complementation of the growth of yeast cells deleted for CDC9 and LIG4 | Q24548868 |
Crystallographic and functional studies of very short patch repair endonuclease | Q27618500 | ||
Structure of the adenylation domain of an NAD+-dependent DNA ligase | Q27618601 | ||
Crystal structure of NAD+-dependent DNA ligase: modular architecture and functional implications | Q27621613 | ||
Crystal structure of NaeI--an evolutionary bridge between DNA endonuclease and topoisomerase | Q27624935 | ||
Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining | Q27628850 | ||
Structure of NaeI-DNA complex reveals dual-mode DNA recognition and complete dimer rearrangement | Q27633648 | ||
Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7 | Q27732795 | ||
RNA capping enzyme and DNA ligase: a superfamily of covalent nucleotidyl transferases | Q28273119 | ||
Type II restriction endonucleases: structural, functional and evolutionary relationships | Q33745019 | ||
Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases | Q33888460 | ||
DNA and spermidine provide a switch mechanism to regulate the activity of restriction enzyme Nae I. | Q34324777 | ||
Effects on NaeI-DNA recognition of the leucine to lysine substitution that transforms restriction endonuclease NaeI to a topoisomerase: a model for restriction endonuclease evolution | Q34616052 | ||
Step-wise DNA relaxation and decatenation by NaeI-43K. | Q34666242 | ||
The domain organization of NaeI endonuclease: separation of binding and catalysis | Q36003818 | ||
Structural similarities between topoisomerases that cleave one or both DNA strands | Q36163323 | ||
Use of specific oligonucleotide duplexes to stimulate cleavage of refractory DNA sites by restriction endonucleases | Q38321306 | ||
NaeI endonuclease binding to pBR322 DNA induces looping | Q38336509 | ||
Role of nucleotidyltransferase motifs I, III and IV in the catalysis of phosphodiester bond formation by Chlorella virus DNA ligase | Q39530871 | ||
Mutational analysis of Chlorella virus DNA ligase: catalytic roles of domain I and motif VI. | Q39725358 | ||
Ability of DNA and spermidine to affect the activity of restriction endonucleases from several bacterial species | Q43886671 | ||
Nonidentical DNA-binding sites of endonuclease NaeI recognize different families of sequences flanking the recognition site | Q44501284 | ||
Effect of single amino acid changes in the region of the adenylylation site of T4 RNA ligase | Q45264522 | ||
Estimation of globular protein secondary structure from circular dichroism. | Q51259487 | ||
Formation of a cleavasome: enhancer DNA-2 stabilizes an active conformation of NaeI dimer. | Q54233463 | ||
Changing a leucine to a lysine residue makes NaeI endonuclease hypersensitive to DNA intercalative drugs | Q71394776 | ||
Cloning and expression of the NaeI restriction endonuclease-encoding gene and sequence analysis of the NaeI restriction-modification system | Q72114927 | ||
DNA topoisomerase and recombinase activities in Nae I restriction endonuclease | Q72635901 | ||
DNA cleavage by NaeI: protein purification, rate-limiting step, and accuracy | Q72891359 | ||
P433 | issue | 11 | |
P407 | language of work or name | English | Q1860 |
P1104 | number of pages | 7 | |
P304 | page(s) | 9733-9739 | |
P577 | publication date | 2003-01-08 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Amino acid substitutions at position 43 of NaeI endonuclease. Evidence for changes in NaeI structure | |
P478 | volume | 278 |
Q40240500 | Diversity of type II restriction endonucleases that require two DNA recognition sites | cites work | P2860 |
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