A positively charged residue of 29 DNA polymerase, highly conserved in DNA polymerases from families A and B, is involved in binding the incoming nucleotide

By Truniger V.   Lázaro J.M.   Esteban F.J.   Blanco L.   Salas M.  

Nucleic Acids Research, Vol. 30, Iss. 7, 2002-04 ,pp. : 1483-1492

Oxford University Press

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Role of the “YxGG/A” Motif of Ø29 DNA Polymerase in Protein-primed Replication

By Truniger V.   Blanco L.   Salas M.  

Journal of Molecular Biology, Vol. 286, Iss. 1, 1999-02 ,pp. : 57-69

Academic Press

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Phage ø29 DNA Polymerase Residues Involved in the Proper Stabilisation of the Primer-terminus at the 3′-5′ Exonuclease Active Site

By de Vega M.   Lázaro J.M.   Salas M.  

Journal of Molecular Biology, Vol. 304, Iss. 1, 2000-11 ,pp. : 1-9

Academic Press

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Φ29 DNA polymerase residues Tyr59, His61 and Phe69 of the highly conserved ExoII motif are essential for interaction with the terminal protein

By Eisenbrandt R.   Lázaro J.M.   Salas M.   Vega M.d.  

Nucleic Acids Research, Vol. 30, Iss. 6, 2002-03 ,pp. : 1379-1386

Oxford University Press

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Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity

By Longás Elisa   de Vega Miguel   Lázaro José M.   Salas Margarita  

Nucleic Acids Research, Vol. 34, Iss. 20, 2006-11 ,pp. : 6051-6063

Oxford University Press

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