about
The ζ toxin induces a set of protective responses and dormancyCrystal structure of the plasmid maintenance system epsilon/zeta: functional mechanism of toxin zeta and inactivation by epsilon 2 zeta 2 complex formationBacillus subtilis RecN binds and protects 3'-single-stranded DNA extensions in the presence of ATP.Bacillus subtilis RecU Holliday-junction resolvase modulates RecA activitiesStructural insight into gene transcriptional regulation and effector binding by the Lrp/AsnC family.Structures of omega repressors bound to direct and inverted DNA repeats explain modulation of transcriptionThe cell pole: the site of cross talk between the DNA uptake and genetic recombination machineryEvidence for different pathways during horizontal gene transfer in competent Bacillus subtilis cellsCrystal structure of omega transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5 A resolutionStructural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39PStreptococcus pyogenes pSM19035 requires dynamic assembly of ATP-bound ParA and ParB on parS DNA during plasmid segregationStructural basis for the nuclease activity of a bacteriophage large terminaseStructural basis for DNA recognition and loading into a viral packaging motorThe 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA bindingGenetic recombination in Bacillus subtilis: a division of labor between two single-strand DNA-binding proteinsRecruitment of Bacillus subtilis RecN to DNA double-strand breaks in the absence of DNA end processingVisualization of DNA double-strand break repair in live bacteria reveals dynamic recruitment of Bacillus subtilis RecF, RecO and RecN proteins to distinct sites on the nucleoidsA novel role for RecA under non-stress: promotion of swarming motility in Escherichia coli K-12.In vitro and in vivo stability of the epsilon2zeta2 protein complex of the broad host-range Streptococcus pyogenes pSM19035 addiction system.Fur activates the expression of Salmonella enterica pathogenicity island 1 by directly interacting with the hilD operator in vivo and in vitroOverexpression of the recA gene decreases oral but not intraperitoneal fitness of Salmonella enterica.The organization of Physcomitrella patensRAD51 genes is unique among eukaryotic organismsBacillus subtilis homologous recombination: genes and products.RecX facilitates homologous recombination by modulating RecA activitiesMolecular anatomy of the Streptococcus pyogenes pSM19035 partition and segrosome complexes.Plasmid copy-number control and better-than-random segregation genes of pSM19035 share a common regulatorParAB Partition Dynamics in Firmicutes: Nucleoid Bound ParA Captures and Tethers ParB-Plasmid Complexes.Bacillus subtilis RecU protein cleaves Holliday junctions and anneals single-stranded DNA.The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage and encapsidation.Bacillus subtilis polynucleotide phosphorylase 3'-to-5' DNase activity is involved in DNA repair.Staphylococcal pathogenicity island DNA packaging system involving cos-site packaging and phage-encoded HNH endonucleases.Plasmid pSM19035, a model to study stable maintenance in Firmicutes.Double-strand break repair in bacteria: a view from Bacillus subtilis.Early steps of double-strand break repair in Bacillus subtilis.Headful DNA packaging: bacteriophage SPP1 as a model system.Bacillus subtilis bacteriophage SPP1-encoded gene 34.1 product is a recombination-dependent DNA replication protein.The Interplay between Different Stability Systems Contributes to Faithful Segregation: Streptococcus pyogenes pSM19035 as a Model.Bacillus subtilis tau subunit of DNA polymerase III interacts with bacteriophage SPP1 replicative DNA helicase G40P.Site-specific recombination by the beta protein from the streptococcal plasmid pSM19035: minimal recombination sequences and crossing over sitePurification and characterization of the RecF protein from Bacillus subtilis 168.
P50
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Juan C. Alonso
@ast
Juan C. Alonso
@en
Juan C. Alonso
@es
Juan C. Alonso
@nl
Juan C. Alonso
@sl
type
label
Juan C. Alonso
@ast
Juan C. Alonso
@en
Juan C. Alonso
@es
Juan C. Alonso
@nl
Juan C. Alonso
@sl
prefLabel
Juan C. Alonso
@ast
Juan C. Alonso
@en
Juan C. Alonso
@es
Juan C. Alonso
@nl
Juan C. Alonso
@sl
P1053
D-2595-2009
P106
P1153
7403482175
P21
P31
P3829
P3835
juan-carlos-alonso8
P496
0000-0002-5178-7179