The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis.
about
OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of human LL-37Proteolytic inactivation of tissue factor pathway inhibitor by bacterial omptinsSubstrate specificity of the Escherichia coli outer membrane protease OmpPEnterohemorrhagic and enteropathogenic Escherichia coli evolved different strategies to resist antimicrobial peptidesYersinia infection tools-characterization of structure and function of adhesinsStructural Basis for Activation of an Integral Membrane Protease by LipopolysaccharideMolecular adaptation of a plant-bacterium outer membrane protease towards plague virulence factor PlaTemperature-induced changes in the lipopolysaccharide of Yersinia pestis affect plasminogen activation by the pla surface proteaseThe single substitution I259T, conserved in the plasminogen activator Pla of pandemic Yersinia pestis branches, enhances fibrinolytic activity.Invited review: Breaking barriers--attack on innate immune defences by omptin surface proteases of enterobacterial pathogens.Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membraneOmptin proteins: an expanding family of outer membrane proteases in Gram-negative Enterobacteriaceae.Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity.Highly active and selective endopeptidases with programmed substrate specificitiesProteomic characterization of Yersinia pestis virulence.Multifunctional role of choline binding protein G in pneumococcal pathogenesis.Yersinia pestis kills Caenorhabditis elegans by a biofilm-independent process that involves novel virulence factors.Activation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin.Mechanisms of Antimicrobial Peptide Resistance in Gram-Negative Bacteria.Initial steps of colicin E1 import across the outer membrane of Escherichia coliDissociation of Tissue Destruction and Bacterial Expansion during Bubonic Plague.A surface-focused biotinylation procedure identifies the Yersinia pestis catalase KatY as a membrane-associated but non-surface-located protein.Relative immunogenicity and protection potential of candidate Yersinia Pestis antigens against lethal mucosal plague challenge in Balb/C mice.Evaluation of protective potential of Yersinia pestis outer membrane protein antigens as possible candidates for a new-generation recombinant plague vaccine.Bacterial strategies of resistance to antimicrobial peptides.VirB alleviates H-NS repression of the icsP promoter in Shigella flexneri from sites more than one kilobase upstream of the transcription start siteYersinia pestis: mechanisms of entry into and resistance to the host cell.Prospects for new plague vaccines.Moraxella catarrhalis: from interactions with the host immune system to vaccine development.Coregulation of host-adapted metabolism and virulence by pathogenic yersiniaeNon-proteolytic functions of microbial proteases increase pathological complexity.Escherichia coli outer membrane protease OmpT confers resistance to urinary cationic peptides.Virulence of Erwinia amylovora, a prevalent apple pathogen: Outer membrane proteins and type III secreted effectors increase fitness and compromise plant defenses.Enterohaemorrhagic Escherichia coli produces outer membrane vesicles as an active defence system against antimicrobial peptide LL-37.Antimicrobial Peptide Conformation as a Structural Determinant of Omptin Protease SpecificityInhibition of outer membrane proteases of the omptin family by aprotinin.Mechanisms of resistance to linalool in Salmonella Senftenberg and their role in survival on basil.Capsular antigen fraction 1 and Pla modulate the susceptibility of Yersinia pestis to pulmonary antimicrobial peptides such as cathelicidin.Characterization of putative virulence genes on the related RepFIB plasmids harbored by Cronobacter sppCpa, the outer membrane protease of Cronobacter sakazakii, activates plasminogen and mediates resistance to serum bactericidal activity.
P2860
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P2860
The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The omptin family of enterobac ...... mic spread of Yersinia pestis.
@ast
The omptin family of enterobac ...... mic spread of Yersinia pestis.
@en
type
label
The omptin family of enterobac ...... mic spread of Yersinia pestis.
@ast
The omptin family of enterobac ...... mic spread of Yersinia pestis.
@en
prefLabel
The omptin family of enterobac ...... mic spread of Yersinia pestis.
@ast
The omptin family of enterobac ...... mic spread of Yersinia pestis.
@en
P1476
The omptin family of enterobac ...... mic spread of Yersinia pestis.
@en
P2093
Maini Kukkonen
Timo K Korhonen
P356
10.1016/J.IJMM.2004.01.003
P577
2004-07-01T00:00:00Z