Radlinska M - Search Results

1

Polyphyletic evolution of type II restriction enzymes revisited: two independent sources of second-hand folds revealed.

Bujnicki JM, Radlinska M, Rychlewski L. Bujnicki JM, et al. Among authors: radlinska m. Trends Biochem Sci. 2001 Jan;26(1):9-11. doi: 10.1016/s0968-0004(00)01690-x. Trends Biochem Sci. 2001. PMID: 11165501

2

Molecular phylogenetics of DNA 5mC-methyltransferases.

Bujnicki JM, Radlinska M. Bujnicki JM, et al. Among authors: radlinska m. Acta Microbiol Pol. 1999;48(1):19-30. Acta Microbiol Pol. 1999. PMID: 10467693

3

Molecular evolution of DNA-(cytosine-N4) methyltransferases: evidence for their polyphyletic origin.

Bujnicki JM, Radlinska M. Bujnicki JM, et al. Among authors: radlinska m. Nucleic Acids Res. 1999 Nov 15;27(22):4501-9. doi: 10.1093/nar/27.22.4501. Nucleic Acids Res. 1999. PMID: 10536161 Free PMC article.

4

Structural characterization of two tandemly arranged DNA methyltransferase genes from Neisseria gonorrhoeae MS11: N4-cytosine specific M.NgoMXV and nonfunctional 5-cytosine-type M.NgoMorf2P.

Radlinska M, Bujnicki JM, Piekarowicz A. Radlinska M, et al. Proteins. 1999 Dec 1;37(4):717-28. doi: 10.1002/(sici)1097-0134(19991201)37:4<717::aid-prot20>3.0.co;2-p. Proteins. 1999. PMID: 10651285

5

Is the HemK family of putative S-adenosylmethionine-dependent methyltransferases a "missing" zeta subfamily of adenine methyltransferases? A hypothesis.

Bujnicki JM, Radlinska M. Bujnicki JM, et al. Among authors: radlinska m. IUBMB Life. 1999 Sep;48(3):247-9. doi: 10.1080/713803519. IUBMB Life. 1999. PMID: 10690633 Free article.

6

Atomic model of the 5-methylcytosine-specific restriction enzyme McrA reveals an atypical zinc finger and structural similarity to betabetaalphaMe endonucleases.

Bujnicki JM, Radlinska M, Rychlewski L. Bujnicki JM, et al. Among authors: radlinska m. Mol Microbiol. 2000 Sep;37(5):1280-1. doi: 10.1046/j.1365-2958.2000.02010.x. Mol Microbiol. 2000. PMID: 10972843 Free article. No abstract available.

7

mRNA:guanine-N7 cap methyltransferases: identification of novel members of the family, evolutionary analysis, homology modeling, and analysis of sequence-structure-function relationships.

Bujnicki JM, Feder M, Radlinska M, Rychlewski L. Bujnicki JM, et al. Among authors: radlinska m. BMC Bioinformatics. 2001;2:2. doi: 10.1186/1471-2105-2-2. Epub 2001 Jun 22. BMC Bioinformatics. 2001. PMID: 11472630 Free PMC article.

8

Cloning and characterization of M.LmoA118I, a novel DNA:m4C methyltransferase from the Listeria monocytogenes phage A118, a close homolog of M.NgoMXV.

Bujnicki JM, Radlinska M. Bujnicki JM, et al. Among authors: radlinska m. Acta Microbiol Pol. 2001;50(2):155-60. Acta Microbiol Pol. 2001. PMID: 11720310

9

Cloning of enterohemorrhagic Escherichia coli phage VT-2 dam methyltransferase.

Radlinska M, Bujnicki JM. Radlinska M, et al. Acta Microbiol Pol. 2001;50(2):161-7. Acta Microbiol Pol. 2001. PMID: 11720311

10

Site-directed mutagenesis defines the catalytic aspartate in the active site of the atypical DNA: m4C methyltransferase M.NgoMXV.

Radlinska M, Bujnicki JM. Radlinska M, et al. Acta Microbiol Pol. 2001;50(2):97-105. Acta Microbiol Pol. 2001. PMID: 11720315

M.NgoMXV is one of the few atypical DNA:m4C methyltransferases that does not possess a serine residue in its predicted active site. We previously reported a homology model of M.NgoMXV and argued that the aspartate side chain at a corresponding position, similarly to …

M.NgoMXV is one of the few atypical DNA:m4C methyltransferases that does not possess a serine residue in its predicted active site. W …

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