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Lázaro JM

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Publications:

Title Authors Year Journal
Dual Role of φ29 DNA Polymerase Lys529 in Stabilisation of the DNA Priming-Terminus and the Terminal Protein-Priming Residue at the Polymerisation Site. Lázaro JM 2013 PloS one
Active DNA unwinding dynamics during processive DNA replication. Lázaro JM 2012 Proceedings of the National Academy of Sciences of the United States of America
phi29 DNA polymerase active site: role of residue Val250 as metal-dNTP complex ligand and in protein-primed initiation. Lázaro JM 2010 Journal of molecular biology
Improvement of phi29 DNA polymerase amplification performance by fusion of DNA binding motifs. Lázaro JM 2010 Proceedings of the National Academy of Sciences of the United States of America
Proofreading dynamics of a processive DNA polymerase. Lázaro JM 2009 The EMBO journal
Functional importance of bacteriophage phi29 DNA polymerase residue Tyr148 in primer-terminus stabilisation at the 3'-5' exonuclease active site. Lázaro JM 2009 Journal of molecular biology
Involvement of the TPR2 subdomain movement in the activities of phi29 DNA polymerase. Lázaro JM 2009 Nucleic acids research
Editing of misaligned 3'-termini by an intrinsic 3'-5' exonuclease activity residing in the PHP domain of a family X DNA polymerase. Lázaro JM 2008 Nucleic acids research
Characterization of a Bacillus subtilis 64-kDa DNA polymerase X potentially involved in DNA repair. Lázaro JM 2008 Journal of molecular biology
The bacteriophage phi29 DNA polymerase. Lázaro JM 2008 IUBMB Life
Phage phi29 and Nf terminal protein-priming domain specifies the internal template nucleotide to initiate DNA replication. Lázaro JM 2008 Proceedings of the National Academy of Sciences of the United States of America
Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases. Lázaro JM 2007 The EMBO journal
Involvement of phage phi29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication. Lázaro JM 2007 Nucleic acids research
Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity. Lázaro JM 2006 Nucleic acids research
The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transition. Lázaro JM 2006 The EMBO journal
Involvement of phi29 DNA polymerase thumb subdomain in the proper coordination of synthesis and degradation during DNA replication. Lázaro JM 2006 Nucleic acids research
Involvement of the "linker" region between the exonuclease and polymerization domains of phi29 DNA polymerase in DNA and TP binding. Lázaro JM 2005 Gene
A specific subdomain in phi29 DNA polymerase confers both processivity and strand-displacement capacity. Lázaro JM 2005 Proceedings of the National Academy of Sciences of the United States of America
Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage phi29. Lázaro JM 2004 Molecular cell
Two positively charged residues of phi29 DNA polymerase, conserved in protein-primed DNA polymerases, are involved in stabilisation of the incoming nucleotide. Lázaro JM 2004 Journal of molecular biology
Function of the C-terminus of phi29 DNA polymerase in DNA and terminal protein binding. Lázaro JM 2004 Nucleic acids research
phi29 DNA polymerase-terminal protein interaction. Involvement of residues specifically conserved among protein-primed DNA polymerases. Lázaro JM 2004 Journal of molecular biology
phi 29 DNA polymerase residue Leu384, highly conserved in motif B of eukaryotic type DNA replicases, is involved in nucleotide insertion fidelity. Lázaro JM 2003 The Journal of biological chemistry
phi29 DNA polymerase residue Phe128 of the highly conserved (S/T)Lx(2)h motif is required for a stable and functional interaction with the terminal protein. Lázaro JM 2003 Journal of molecular biology
A conserved insertion in protein-primed DNA polymerases is involved in primer terminus stabilisation. Lázaro JM 2003 Journal of molecular biology
Phi29 DNA polymerase residues Tyr59, His61 and Phe69 of the highly conserved ExoII motif are essential for interaction with the terminal protein. Lázaro JM 2002 Nucleic acids research
Importance of the N-terminal region of the phage GA-1 single-stranded DNA-binding protein for its self-interaction ability and functionality. Lázaro JM 2002 The Journal of biological chemistry
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. Lázaro JM 2002 Nucleic acids research
A highly conserved lysine residue in phi29 DNA polymerase is important for correct binding of the templating nucleotide during initiation of phi29 DNA replication. Lázaro JM 2002 Journal of molecular biology
Specific recognition of parental terminal protein by DNA polymerase for initiation of protein-primed DNA replication. Lázaro JM 2000 The Journal of biological chemistry
Differential functional behavior of viral phi29, Nf and GA-1 SSB proteins. Lázaro JM 2000 Nucleic acids research
An aspartic acid residue in TPR-1, a specific region of protein-priming DNA polymerases, is required for the functional interaction with primer terminal protein. Lázaro JM 2000 Journal of molecular biology
Phage phi 29 DNA polymerase residues involved in the proper stabilisation of the primer-terminus at the 3'-5' exonuclease active site. Lázaro JM 2000 Journal of molecular biology
Phage phi29 terminal protein residues Asn80 and Tyr82 are recognition elements of the replication origins. Lázaro JM 1999 The Journal of biological chemistry
A single tyrosine prevents insertion of ribonucleotides in the eukaryotic-type phi29 DNA polymerase. Lázaro JM 1999 Journal of molecular biology
Role of the first aspartate residue of the "YxDTDS" motif of phi29 DNA polymerase as a metal ligand during both TP-primed and DNA-primed DNA synthesis. Lázaro JM 1998 Journal of molecular biology
Mutational analysis of phi29 DNA polymerase residues acting as ssDNA ligands for 3'-5' exonucleolysis. Lázaro JM 1998 Journal of molecular biology
Phi 29 DNA polymerase requires the N-terminal domain to bind terminal protein and DNA primer substrates. Lázaro JM 1998 Journal of molecular biology
Bacteriophage phi29 early protein p17 is conditionally required for the first rounds of viral DNA replication. Lázaro JM 1998 Gene
o29 DNA polymerase residue Lys383, invariant at motif B of DNA-dependent polymerases, is involved in dNTP binding. Lázaro JM 1997 Journal of molecular biology
An invariant lysine residue is involved in catalysis at the 3'-5' exonuclease active site of eukaryotic-type DNA polymerases. Lázaro JM 1997 Journal of molecular biology
A DNA binding motif coordinating synthesis and degradation in proofreading DNA polymerases. Lázaro JM 1996 The EMBO journal
Protein-nucleic acid interactions in bacteriophage phi 29 DNA replication. Lázaro JM 1995 FEMS microbiology reviews
Primer terminus stabilization at the phi 29 DNA polymerase active site. Mutational analysis of conserved motif KXY. Lázaro JM 1995 The Journal of biological chemistry
Purification of bacteriophage phi 29 DNA polymerase. Lázaro JM 1995 Methods in enzymology
Primer-terminus stabilization at the psi 29 DNA polymerase active site. Mutational analysis of conserved motif TX2GR. Lázaro JM 1994 The Journal of biological chemistry
Terminal protein-primed DNA amplification. Lázaro JM 1994 Proceedings of the National Academy of Sciences of the United States of America
Phi 29 DNA polymerase active site. Residue ASP249 of conserved amino acid motif "Dx2SLYP" is critical for synthetic activities. Lázaro JM 1993 The Journal of biological chemistry
Phi 29 DNA polymerase active site. The conserved amino acid motif "Kx3NSxYG" is involved in template-primer binding and dNTP selection. Lázaro JM 1993 The Journal of biological chemistry
Phi 29 DNA polymerase active site. Mutants in conserved residues Tyr254 and Tyr390 are affected in dNTP binding. Lázaro JM 1992 The Journal of biological chemistry
Site-directed mutagenesis at the Exo III motif of phi 29 DNA polymerase; overlapping structural domains for the 3'-5' exonuclease and strand-displacement activities. Lázaro JM 1992 The EMBO journal
The highly conserved amino acid sequence motif Tyr-Gly-Asp-Thr-Asp-Ser in alpha-like DNA polymerases is required by phage phi 29 DNA polymerase for protein-primed initiation and polymerization. Lázaro JM 1990 Proceedings of the National Academy of Sciences of the United States of America
A conserved 3'----5' exonuclease active site in prokaryotic and eukaryotic DNA polymerases. Lázaro JM 1989 Cell
Highly efficient DNA synthesis by the phage phi 29 DNA polymerase. Symmetrical mode of DNA replication. Lázaro JM 1989 The Journal of biological chemistry
Effects of internal deletions on the priming activity of the phage phi 29 terminal protein. Lázaro JM 1989 Gene
Protein-primed replication of bacteriophage phi 29 DNA. Lázaro JM 1988 Biochimica et biophysica acta
Effect of NH4+ ions on phi 29 DNA-protein p3 replication: formation of a complex between the terminal protein and the DNA polymerase. Lázaro JM 1987 J Virol
Replication of phage phi 29 DNA in vitro: role of the viral protein p6 in initiation and elongation. Lázaro JM 1986 Nucleic acids research
Overproduction and purification of protein P6 of Bacillus subtilis phage phi 29: role in the initiation of DNA replication. Lázaro JM 1985 Nucleic acids research
Purification in a functional form of the terminal protein of Bacillus subtilis phage phi 29. Lázaro JM 1984 Proceedings of the National Academy of Sciences of the United States of America
Physical map of bacteriophage phi29 DNA. Lázaro JM 1976 Virology
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