The sortase SrtA of Listeria monocytogenes is involved in processing of internalin and in virulence.
about
Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal diseaseSortases and the art of anchoring proteins to the envelopes of gram-positive bacteriaHousekeeping sortase facilitates the cell wall anchoring of pilus polymers in Corynebacterium diphtheriaeSec-secretion and sortase-mediated anchoring of proteins in Gram-positive bacteriaCrystal structure of Streptococcus pyogenes sortase A: implications for sortase mechanism.Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site.How Listeria monocytogenes organizes its surface for virulenceThe SrtA Sortase of Streptococcus agalactiae is required for cell wall anchoring of proteins containing the LPXTG motif, for adhesion to epithelial cells, and for colonization of the mouse intestine.Gp96 is a receptor for a novel Listeria monocytogenes virulence factor, Vip, a surface protein.Discovery and structure-activity relationship analysis of Staphylococcus aureus sortase A inhibitorsLPXTG protein InlJ, a newly identified internalin involved in Listeria monocytogenes virulence.Sortase A induces Th17-mediated and antibody-independent immunity to heterologous serotypes of group A streptococci.Sortase B, a new class of sortase in Listeria monocytogenes.Pilus biogenesis in Lactococcus lactis: molecular characterization and role in aggregation and biofilm formation.Roles of sortase in surface expression of the major protein adhesin P1, saliva-induced aggregation and adherence, and cariogenicity of Streptococcus mutans.Identification of a point mutation resulting in loss of cell wall anchoring activity of SrtA of Streptococcus mutans NG5Virulence as a target for antimicrobial chemotherapy.A homolog of Bacillus subtilis trigger factor in Listeria monocytogenes is involved in stress tolerance and bacterial virulence.Identification of the agr locus of Listeria monocytogenes: role in bacterial virulenceClostridium difficile has a single sortase, SrtB, that can be inhibited by small-molecule inhibitors.Structural aspects of adhesion to and invasion of host cells by the human pathogen Listeria monocytogenes.Streptococcus pyogenes Sortase Mutants Are Highly Susceptible to Killing by Host Factors Due to Aberrant Envelope PhysiologyListeria monocytogenes surface proteins: from genome predictions to function.The Listeria monocytogenes virulence factor InlJ is specifically expressed in vivo and behaves as an adhesin.Molecular docking based virtual screening of compounds for inhibiting sortase A in L.monocytogenes.Discerning the catalytic mechanism of Staphylococcus aureus sortase A with QM/MM free energy calculations.Dual role for pilus in adherence to epithelial cells and biofilm formation in Streptococcus agalactiae.A comparative genome analysis identifies distinct sorting pathways in gram-positive bacteriaA novel sortase, SrtC2, from Streptococcus pyogenes anchors a surface protein containing a QVPTGV motif to the cell wall.Relevance and application of sortase and sortase-dependent proteins in lactic acid bacteria.Staphylococcus aureus Sortase A transpeptidase. Calcium promotes sorting signal binding by altering the mobility and structure of an active site loop.Mutagenesis studies of substrate recognition and catalysis in the sortase A transpeptidase from Staphylococcus aureus.Directed evolution provides insight into conformational substrate sampling by SrtA.Chinese herb medicine against Sortase A catalyzed transformations, a key role in gram-positive bacterial infection progress.Equilibrium of sortase A dimerization on Staphylococcus aureus cell surface mediates its cell wall sorting activity.Disparate subcellular location of putative sortase substrates in Clostridium difficile.Inactivation of the srtA gene affects localization of surface proteins and decreases adhesion of Streptococcus pneumoniae to human pharyngeal cells in vitro.Synthesis and structure activity relationship studies of novel Staphylococcus aureus Sortase A inhibitors.RrgA and RrgB are components of a multisubunit pilus encoded by the Streptococcus pneumoniae rlrA pathogenicity islet.Home Alone: Elimination of All but One Alternative Sigma Factor in Listeria monocytogenes Allows Prediction of New Roles for σB.
P2860
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P2860
The sortase SrtA of Listeria monocytogenes is involved in processing of internalin and in virulence.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մարտին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
name
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@ast
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@en
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@nl
type
label
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@ast
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@en
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@nl
prefLabel
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@ast
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@en
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@nl
P2093
P2860
P50
P1476
The sortase SrtA of Listeria m ...... f internalin and in virulence.
@en
P2093
Caroline Garandeau
Iharilalao Dubail
Jean-Luc Beretti
P2860
P304
P356
10.1128/IAI.70.3.1382-1390.2002
P407
P577
2002-03-01T00:00:00Z