scholarly article | Q13442814 |
P2093 | author name string | I Taylor | |
G Kneale | |||
D Watts | |||
P2860 | cites work | Conservation of complex DNA recognition domains between families of restriction enzymes | Q44918995 |
Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice. | Q52904158 | ||
Complementation analysis of temperature-sensitive host specificity mutations in Escherichia coli | Q53770636 | ||
EcoA and EcoE: alternatives to the EcoK family of type I restriction and modification systems of Escherichia coli. | Q54790634 | ||
High-level expression of the cloned genes encoding the subunits of and intact DNA methyltransferase, M.EcoR124 | Q68079186 | ||
The hsd (host specificity) genes of E. coli K12 | Q72873220 | ||
Mutations the confer de Novo activity upon a maintenance methyltransferase | Q33323418 | ||
Structural homologies among type I restriction-modification systems | Q33927977 | ||
DNA recognition by a new family of type I restriction enzymes: a unique relationship between two different DNA specificities | Q33930317 | ||
Recombination of constant and variable modules alters DNA sequence recognition by type IC restriction-modification enzymes | Q33937287 | ||
The EcoA restriction and modification system of Escherichia coli 15T-: enzyme structure and DNA recognition sequence | Q33939378 | ||
EcoA: the first member of a new family of type I restriction modification systems. Gene organization and enzymatic activities | Q36424348 | ||
EcoR124 and EcoR124/3: the first members of a new family of type I restriction and modification systems | Q36427335 | ||
Restriction and modification systems | Q37041891 | ||
In vitro specificity of EcoRI DNA methyltransferase | Q38326831 | ||
Purification and biochemical characterisation of theEcoR124 type I modification methylase | Q38330901 | ||
Bacterial DNA modification. | Q40141670 | ||
Basis for changes in DNA recognition by the EcoR124 and EcoR124/3 type I DNA restriction and modification enzymes | Q41994610 | ||
P433 | issue | 21 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 4929-4935 | |
P577 | publication date | 1993-10-01 | |
P1433 | published in | Nucleic Acids Research | Q135122 |
P1476 | title | Substrate recognition and selectivity in the type IC DNA modification methylase M.EcoR124I. | |
P478 | volume | 21 |
Q33851803 | ATP-dependent restriction enzymes |
Q33940558 | Characterisation of the structure of ocr, the gene 0.3 protein of bacteriophage T7. |
Q54521339 | Characterization of an EcoR124I restriction-modification enzyme produced from a deleted form of the DNA-binding subunit, which results in a novel DNA specificity. |
Q41300410 | Cleavage of a model DNA replication fork by a Type I restriction endonuclease. |
Q34178514 | Complex restriction enzymes: NTP-driven molecular motors |
Q40794101 | DNA-binding induces a major structural transition in a type I methyltransferase. |
Q40395854 | Dam methylase from Escherichia coli: kinetic studies using modified DNA oligomers: hemimethylated substrates |
Q38346263 | Dam methyltransferase from Escherichia coli: kinetic studies using modified DNA oligomers: nonmethylated substrates |
Q37698622 | Diversity of DNA methyltransferases that recognize asymmetric target sequences |
Q47969980 | Expression and characterisation of the N-terminal fragment of the HsdS subunit of M.EcoR124I. |
Q30662423 | Families of restriction enzymes: an analysis prompted by molecular and genetic data for type ID restriction and modification systems |
Q39718396 | High resolution footprinting of a type I methyltransferase reveals a large structural distortion within the DNA recognition site |
Q38330725 | Interaction of the type I methyltransferase M.EcoR124I with modified DNA substrates: sequence discrimination and base flipping |
Q41609450 | Methods for the analysis of DNA-protein interactions |
Q24555228 | Nucleoside triphosphate-dependent restriction enzymes |
Q38336583 | Protein-protein and protein-DNA interactions in the type I restriction endonuclease R.EcoR124I. |
Q40790792 | Structural and functional analysis of the engineered type I DNA methyltransferase EcoR124I(NT) |
Q34228621 | Structural and functional analysis of the symmetrical Type I restriction endonuclease R.EcoR124I(NT). |
Q24548508 | Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle) |
Q34744985 | Tyrosine 27 of the specificity polypeptide of EcoKI can be UV crosslinked to a bromodeoxyuridine-substituted DNA target sequence |
Search more.