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Function of the C-terminus of phi29 DNA polymerase in DNA and terminal protein binding.
Truniger V, Lázaro JM, Salas M. Truniger V, et al. Nucleic Acids Res. 2004 Jan 16;32(1):361-70. doi: 10.1093/nar/gkh184. Print 2004. Nucleic Acids Res. 2004. PMID: 14729920 Free PMC article.
The (I/Y)XGG motif of adenovirus DNA polymerase affects template DNA binding and the transition from initiation to elongation.
Brenkman AB, Heideman MR, Truniger V, Salas M, van der Vliet PC. Brenkman AB, et al. Among authors: truniger v. J Biol Chem. 2001 Aug 10;276(32):29846-53. doi: 10.1074/jbc.M103159200. Epub 2001 Jun 4. J Biol Chem. 2001. PMID: 11390396
Analysis of O29 DNA polymerase by partial proteolysis: binding of terminal protein in the double-stranded DNA channel.
Truniger V, Blanco L, Salas M. Truniger V, et al. J Mol Biol. 2000 Jan 21;295(3):441-53. doi: 10.1006/jmbi.1999.3370. J Mol Biol. 2000. PMID: 10623537
Role of the "YxGG/A" motif of Phi29 DNA polymerase in protein-primed replication.
Truniger V, Blanco L, Salas M. Truniger V, et al. J Mol Biol. 1999 Feb 12;286(1):57-69. doi: 10.1006/jmbi.1998.2477. J Mol Biol. 1999. PMID: 9931249
A DNA binding motif coordinating synthesis and degradation in proofreading DNA polymerases.
Truniger V, Lázaro JM, Salas M, Blanco L. Truniger V, et al. EMBO J. 1996 Jul 1;15(13):3430-41. EMBO J. 1996. PMID: 8670845 Free PMC article.
Phi 29 DNA polymerase requires the N-terminal domain to bind terminal protein and DNA primer substrates.
Truniger V, Lázaro JM, Salas M, Blanco L. Truniger V, et al. J Mol Biol. 1998 May 15;278(4):741-55. doi: 10.1006/jmbi.1998.1724. J Mol Biol. 1998. PMID: 9614939
Involvement of the "linker" region between the exonuclease and polymerization domains of phi29 DNA polymerase in DNA and TP binding.
Truniger V, Bonnin A, Lázaro JM, de Vega M, Salas M. Truniger V, et al. Gene. 2005 Mar 28;348:89-99. doi: 10.1016/j.gene.2004.12.041. Gene. 2005. PMID: 15777661
Two positively charged residues of phi29 DNA polymerase, conserved in protein-primed DNA polymerases, are involved in stabilisation of the incoming nucleotide.
Truniger V, Lázaro JM, Salas M. Truniger V, et al. J Mol Biol. 2004 Jan 9;335(2):481-94. doi: 10.1016/j.jmb.2003.10.024. J Mol Biol. 2004. PMID: 14672657
phi 29 DNA polymerase residue Leu384, highly conserved in motif B of eukaryotic type DNA replicases, is involved in nucleotide insertion fidelity.
Truniger V, Lázaro JM, de Vega M, Blanco L, Salas M. Truniger V, et al. J Biol Chem. 2003 Aug 29;278(35):33482-91. doi: 10.1074/jbc.M303052200. Epub 2003 Jun 12. J Biol Chem. 2003. PMID: 12805385
A positively charged residue of phi29 DNA polymerase, highly conserved in DNA polymerases from families A and B, is involved in binding the incoming nucleotide.
Truniger V, Lázaro JM, Esteban FJ, Blanco L, Salas M. Truniger V, et al. Nucleic Acids Res. 2002 Apr 1;30(7):1483-92. doi: 10.1093/nar/30.7.1483. Nucleic Acids Res. 2002. PMID: 11917008 Free PMC article.
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