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345 related items for PubMed ID: 11419939
1. S-adenosyl-L-methionine is required for DNA cleavage by type III restriction enzymes. Bist P, Sistla S, Krishnamurthy V, Acharya A, Chandrakala B, Rao DN. J Mol Biol; 2001 Jun 29; 310(1):93-109. PubMed ID: 11419939 [Abstract] [Full Text] [Related]
2. Functional characterization and modulation of the DNA cleavage efficiency of type III restriction endonuclease EcoP15I in its interaction with two sites in the DNA target. Möncke-Buchner E, Rothenberg M, Reich S, Wagenführ K, Matsumura H, Terauchi R, Krüger DH, Reuter M. J Mol Biol; 2009 Apr 17; 387(5):1309-19. PubMed ID: 19250940 [Abstract] [Full Text] [Related]
3. Interaction of EcoP1 modification methylase with S-adenosyl-L-methionine: a UV-crosslinking study. Krishnamurthy V, Rao DN. Biochem Mol Biol Int; 1994 Mar 17; 32(4):623-32. PubMed ID: 8038713 [Abstract] [Full Text] [Related]
4. Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I. Janscak P, Sandmeier U, Szczelkun MD, Bickle TA. J Mol Biol; 2001 Feb 23; 306(3):417-31. PubMed ID: 11178902 [Abstract] [Full Text] [Related]
5. DNA cleavage by type III restriction-modification enzyme EcoP15I is independent of spacer distance between two head to head oriented recognition sites. Mücke M, Reich S, Möncke-Buchner E, Reuter M, Krüger DH. J Mol Biol; 2001 Sep 28; 312(4):687-98. PubMed ID: 11575924 [Abstract] [Full Text] [Related]
6. Interaction of EcoP15I DNA methyltransferase with oligonucleotides containing the asymmetric sequence 5'-CAGCAG-3'. Ahmad I, Rao DN. J Mol Biol; 1994 Sep 30; 242(4):378-88. PubMed ID: 7932697 [Abstract] [Full Text] [Related]
7. Sequence-specific DNA binding by EcoKI, a type IA DNA restriction enzyme. Powell LM, Dryden DT, Murray NE. J Mol Biol; 1998 Nov 13; 283(5):963-76. PubMed ID: 9799636 [Abstract] [Full Text] [Related]
8. Structural domains in the type III restriction endonuclease EcoP15I: characterization by limited proteolysis, mass spectrometry and insertional mutagenesis. Wagenführ K, Pieper S, Mackeldanz P, Linscheid M, Krüger DH, Reuter M. J Mol Biol; 2007 Feb 09; 366(1):93-102. PubMed ID: 17156795 [Abstract] [Full Text] [Related]
12. Functional analysis of conserved motifs in EcoP15I DNA methyltransferase. Ahmad I, Rao DN. J Mol Biol; 1996 Jun 07; 259(2):229-40. PubMed ID: 8656425 [Abstract] [Full Text] [Related]
13. Scanning force microscopy of DNA translocation by the Type III restriction enzyme EcoP15I. Reich S, Gössl I, Reuter M, Rabe JP, Krüger DH. J Mol Biol; 2004 Aug 06; 341(2):337-43. PubMed ID: 15276827 [Abstract] [Full Text] [Related]
14. Functional analysis of conserved motifs in type III restriction-modification enzymes. Saha S, Ahmad I, Reddy YV, Krishnamurthy V, Rao DN. Biol Chem; 1998 Aug 06; 379(4-5):511-7. PubMed ID: 9628345 [Abstract] [Full Text] [Related]
15. Structural change of tRNA (Gm18) methyltransferase by binding of methyl donor analogues. Watanabe K, Nureki O, Fukai S, Endo Y, Hori H. Nucleic Acids Symp Ser (Oxf); 2005 Aug 06; (49):301-2. PubMed ID: 17150753 [Abstract] [Full Text] [Related]
16. Functional consequences of mutating conserved SF2 helicase motifs in the Type III restriction endonuclease EcoP15I translocase domain. Mackeldanz P, Alves J, Möncke-Buchner E, Wyszomirski KH, Krüger DH, Reuter M. Biochimie; 2013 Apr 06; 95(4):817-23. PubMed ID: 23220200 [Abstract] [Full Text] [Related]
18. The type I restriction endonuclease R.EcoR124I: over-production and biochemical properties. Janscak P, Abadjieva A, Firman K. J Mol Biol; 1996 Apr 19; 257(5):977-91. PubMed ID: 8632480 [Abstract] [Full Text] [Related]
19. DNA recognition by the EcoP15I and EcoPI modification methyltransferases. Ahmad I, Krishnamurthy V, Rao DN. Gene; 1995 May 19; 157(1-2):143-7. PubMed ID: 7607479 [Abstract] [Full Text] [Related]
20. A novel mutant of the type I restriction-modification enzyme EcoR124I is altered at a key stage of the subunit assembly pathway. Weiserova M, Dutta CF, Firman K. J Mol Biol; 2000 Dec 01; 304(3):301-10. PubMed ID: 11090275 [Abstract] [Full Text] [Related] Page: [Next] [New Search]