scholarly article | Q13442814 |
P356 | DOI | 10.1126/SCIENCE.7892605 |
P698 | PubMed publication ID | 7892605 |
P2093 | author name string | K Jo | |
M D Topal | |||
P433 | issue | 5205 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 1817-1820 | |
P577 | publication date | 1995-03-01 | |
P1433 | published in | Science | Q192864 |
P1476 | title | DNA topoisomerase and recombinase activities in Nae I restriction endonuclease | |
P478 | volume | 267 |
Q39798515 | A new Thermus sp. class-IIS enzyme sub-family: isolation of a 'twin' endonuclease TspDTI with a novel specificity 5'-ATGAA(N(11/9))-3', related to TspGWI, TaqII and Tth111II. |
Q43048971 | A view of consecutive binding events from structures of tetrameric endonuclease SfiI bound to DNA. |
Q44273168 | Amino acid substitutions at position 43 of NaeI endonuclease. Evidence for changes in NaeI structure |
Q37243964 | An EM view of the FokI synaptic complex by single particle analysis |
Q31037795 | Asymmetric photocross-linking pattern of restriction endonuclease EcoRII to the DNA recognition sequence |
Q42587210 | Bacteriophage T4 endonuclease II, a promiscuous GIY-YIG nuclease, binds as a tetramer to two DNA substrates |
Q41755822 | Conserved themes but novel activities in recombinases and topoisomerases |
Q52995430 | Cooperative binding properties of restriction endonuclease EcoRII with DNA recognition sites. |
Q27624935 | Crystal structure of NaeI--an evolutionary bridge between DNA endonuclease and topoisomerase |
Q71726932 | Different enzymes with similar structures involved in Mg(2+)-mediated polynucleotidyl transfer |
Q40240500 | Diversity of type II restriction endonucleases that require two DNA recognition sites |
Q38362416 | EcoRII: a restriction enzyme evolving recombination functions? |
Q34616052 | 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 |
Q77521029 | Flp ribonuclease activities. Mechanistic similarities and contrasts to site-specific DNA recombination |
Q33910413 | Imaging DNA loops induced by restriction endonuclease EcoRII. A single amino acid substitution uncouples target recognition from cooperative DNA interaction and cleavage |
Q40015527 | Nick sensing by vaccinia virus DNA ligase requires a 5' phosphate at the nick and occupancy of the adenylate binding site on the enzyme. |
Q34604464 | Phylogenomics of DNA topoisomerases: their origin and putative roles in the emergence of modern organisms |
Q47858291 | Polynucleotide ligase activity of eukaryotic topoisomerase I. |
Q33184404 | PrfA protein of Bacillus species: prediction and demonstration of endonuclease activity on DNA |
Q41064313 | Recombination by resolvase to analyse DNA communications by the SfiI restriction endonuclease |
Q34187086 | Restriction endonucleases: classification, properties, and applications |
Q34008473 | Self-generated DNA termini relax the specificity of SgrAI restriction endonuclease |
Q34652687 | Similarities and differences among 105 members of the Int family of site-specific recombinases |
Q34666242 | Step-wise DNA relaxation and decatenation by NaeI-43K. |
Q24555230 | Structure and function of type II restriction endonucleases |
Q73849348 | Structure-based sequence alignment of type-II restriction endonucleases |
Q44004427 | The N-terminus of m5C-DNA methyltransferase MspI is involved in its topoisomerase activity |
Q36003818 | The domain organization of NaeI endonuclease: separation of binding and catalysis |
Q40789437 | The nucleotide mapping of DNA double-strand breaks at the CYS3 initiation site of meiotic recombination in Saccharomyces cerevisiae |
Q32030823 | Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins |
Q33843093 | Type II restriction endonucleases--a historical perspective and more |
Q35627759 | Visual analysis of concerted cleavage by type IIF restriction enzyme SfiI in subsecond time region |
Q42535945 | in-silico analysis suggests alterations in the function of XisA protein as a possible mechanism of butachlor toxicity in the nitrogen fixing cyanobacterium Anabaena sp. PCC 7120. |
Search more.