“Organization and sequence of the hsd genes of Escherichia coli K-12”. Journal of Molecular Biology198 (2): 159–70. (November 1987). doi:10.1016/0022-2836(87)90303-2. PMID3323532.
“The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases”. Gene74 (1): 253–9. (December 1988). doi:10.1016/0378-1119(88)90298-3. PMID3248728.
“Evolution of type II DNA methyltransferases. A gene duplication model”. Journal of Molecular Biology206 (2): 313–21. (March 1989). doi:10.1016/0022-2836(89)90481-6. PMID2541254.
“Sequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferases”. Gene157 (1–2): 3–11. (May 1995). doi:10.1016/0378-1119(94)00783-O. PMID7607512.
“Mutations that confer de novo activity upon a maintenance methyltransferase”. Journal of Molecular Biology221 (2): 431–40. (September 1991). doi:10.1016/0022-2836(91)80064-2. PMID1833555.
Chahar, Sanjay; Elsawy, Hany; Ragozin, Sergey; Jeltsch, Albert (January 2010). “Changing the DNA Recognition Specificity of the EcoDam DNA-(Adenine-N6)-Methyltransferase by Directed Evolution”. Journal of Molecular Biology395 (1): 79–88. doi:10.1016/j.jmb.2009.09.027. PMID19766657.
Maier, Johannes A. H.; Albu, Razvan F.; Jurkowski, Tomasz P.; Jeltsch, Albert (2015-12-01). “Investigation of the C-terminal domain of the bacterial DNA-(adenine N6)-methyltransferase CcrM”. Biochimie119: 60–67. doi:10.1016/j.biochi.2015.10.011. ISSN0300-9084. PMID26475175.
“Cytosine-specific type II DNA methyltransferases. A conserved enzyme core with variable target-recognizing domains”. J. Mol. Biol.206 (2): 305–12. (March 1989). doi:10.1016/0022-2836(89)90480-4. PMID2716049.
“Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine”. Cell74 (2): 299–307. (July 1993). doi:10.1016/0092-8674(93)90421-L. PMID8343957.
“Stalling of Human DNA (Cytosine-5) Methyltransferase at Single Strand Conformers form a Site of Dynamic Mutation”. Journal of Molecular Biology275 (1): 67–79. (1998). doi:10.1006/jmbi.1997.1430. PMID9451440.
“Differential Requirement for DNA Methyltransferse 1 In Maintaining Cancer Cell Gene Promoter Hypermethylation”. Cancer Research66 (2): 729–735. (2006). doi:10.1158/0008-5472.CAN-05-1537. PMID16424002.
“Organization and sequence of the hsd genes of Escherichia coli K-12”. Journal of Molecular Biology198 (2): 159–70. (November 1987). doi:10.1016/0022-2836(87)90303-2. PMID3323532.
“The amino acid sequence of the eukaryotic DNA [N6-adenine]methyltransferase, M.CviBIII, has regions of similarity with the prokaryotic isoschizomer M.TaqI and other DNA [N6-adenine] methyltransferases”. Gene74 (1): 253–9. (December 1988). doi:10.1016/0378-1119(88)90298-3. PMID3248728.
“Evolution of type II DNA methyltransferases. A gene duplication model”. Journal of Molecular Biology206 (2): 313–21. (March 1989). doi:10.1016/0022-2836(89)90481-6. PMID2541254.
“Sequence motifs characteristic for DNA [cytosine-N4] and DNA [adenine-N6] methyltransferases. Classification of all DNA methyltransferases”. Gene157 (1–2): 3–11. (May 1995). doi:10.1016/0378-1119(94)00783-O. PMID7607512.
“Mutations that confer de novo activity upon a maintenance methyltransferase”. Journal of Molecular Biology221 (2): 431–40. (September 1991). doi:10.1016/0022-2836(91)80064-2. PMID1833555.
Chahar, Sanjay; Elsawy, Hany; Ragozin, Sergey; Jeltsch, Albert (January 2010). “Changing the DNA Recognition Specificity of the EcoDam DNA-(Adenine-N6)-Methyltransferase by Directed Evolution”. Journal of Molecular Biology395 (1): 79–88. doi:10.1016/j.jmb.2009.09.027. PMID19766657.
Maier, Johannes A. H.; Albu, Razvan F.; Jurkowski, Tomasz P.; Jeltsch, Albert (2015-12-01). “Investigation of the C-terminal domain of the bacterial DNA-(adenine N6)-methyltransferase CcrM”. Biochimie119: 60–67. doi:10.1016/j.biochi.2015.10.011. ISSN0300-9084. PMID26475175.
“Cytosine-specific type II DNA methyltransferases. A conserved enzyme core with variable target-recognizing domains”. J. Mol. Biol.206 (2): 305–12. (March 1989). doi:10.1016/0022-2836(89)90480-4. PMID2716049.
“Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine”. Cell74 (2): 299–307. (July 1993). doi:10.1016/0092-8674(93)90421-L. PMID8343957.
“Stalling of Human DNA (Cytosine-5) Methyltransferase at Single Strand Conformers form a Site of Dynamic Mutation”. Journal of Molecular Biology275 (1): 67–79. (1998). doi:10.1006/jmbi.1997.1430. PMID9451440.
“Differential Requirement for DNA Methyltransferse 1 In Maintaining Cancer Cell Gene Promoter Hypermethylation”. Cancer Research66 (2): 729–735. (2006). doi:10.1158/0008-5472.CAN-05-1537. PMID16424002.
Maier, Johannes A. H.; Albu, Razvan F.; Jurkowski, Tomasz P.; Jeltsch, Albert (2015-12-01). “Investigation of the C-terminal domain of the bacterial DNA-(adenine N6)-methyltransferase CcrM”. Biochimie119: 60–67. doi:10.1016/j.biochi.2015.10.011. ISSN0300-9084. PMID26475175.