M Salas

Characterization and purification of a phage phi 29-encoded DNA polymerase required for the initiation of replication.

L. Blanco, M. Salas, L Blanco, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Fidelity of phi 29 DNA polymerase. Comparison between protein-primed initiation and DNA polymerization.

L. Blanco, J. Esteban, M. Salas, 1993, The Journal of biological chemistry.

Resolution of head‐on collisions between the transcription machinery and bacteriophage Φ29 DNA polymerase is dependent on RNA polymerase translocation

M. Salas, M Salas, M Elías-Arnanz, 1999, The EMBO journal.

Structural and functional relationships between prokaryotic and eukaryotic DNA polymerases.

L. Blanco, A. Bernad, Á. Zaballos, 1987, The EMBO journal.

Protein-priming of DNA replication.

M. Salas, M Salas, Margarita Salas, 1991, Annual review of biochemistry.

Highly efficient DNA synthesis by the phage phi 29 DNA polymerase

C Garmendia, L. Blanco, A. Bernad, 1989 .

Phi 29 DNA polymerase active site. Residue ASP249 of conserved amino acid motif "Dx2SLYP" is critical for synthetic activities.

M. Blasco, L. Blanco, M. Salas, 1993, The Journal of biological chemistry.

Phi 29 DNA polymerase requires the N-terminal domain to bind terminal protein and DNA primer substrates.

L. Blanco, M. Salas, L Blanco, 1998, Journal of molecular biology.

A Novel Kinetic Analysis to Calculate Nucleotide Affinity of Proofreading DNA Polymerases:

L. Blanco, J. Esteban, M. Salas, 1995, The Journal of Biological Chemistry.

The bacteriophage phi 29 DNA polymerase, a proofreading enzyme.

C Garmendia, L. Blanco, A. Bernad, 1992, The Journal of biological chemistry.