Phosphoserine modification of the enteropathogenic Escherichia coli Tir molecule is required to trigger conformational changes in Tir and efficient pedestal elongation.
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Cytosolic extract induces Tir translocation and pedestals in EPEC-infected red blood cellsThe enteropathogenic E. coli (EPEC) Tir effector inhibits NF-κB activity by targeting TNFα receptor-associated factorsNck adaptors, besides promoting N-WASP mediated actin-nucleation activity at pedestals, influence the cellular levels of enteropathogenic Escherichia coli Tir effector.Effect of protein kinase A-mediated phosphorylation on the structure and association properties of the enteropathogenic Escherichia coli Tir virulence protein.Involvement of the intermediate filament protein cytokeratin-18 in actin pedestal formation during EPEC infection.The EHEC type III effector NleL is an E3 ubiquitin ligase that modulates pedestal formation.Analysis of the function of enteropathogenic Escherichia coli EspB by random mutagenesis.Contribution of Crk adaptor proteins to host cell and bacteria interactions.Change is good: variations in common biological mechanisms in the epsilonproteobacterial genera Campylobacter and HelicobacterAdhesion of enteropathogenic Escherichia coli to host cells.Virulence of enteropathogenic Escherichia coli, a global pathogenEnteropathogenic and enterohemorrhagic Escherichia coli infections: translocation, translocation, translocation.Comparative analysis of the locus of enterocyte effacement and its flanking regions.Sticky situation: localized adherence of enteropathogenic Escherichia coli to the small intestine epithelium.Type III Secreted Virulence Factors Manipulating Signaling to Actin Dynamics.Enhanced Actin Pedestal Formation by Enterohemorrhagic Escherichia coli O157:H7 Adapted to the Mammalian HostAmino acid residues within enterohemorrhagic Escherichia coli O157:H7 Tir involved in phosphorylation, alpha-actinin recruitment, and Nck-independent pedestal formation.Enteropathogenic Escherichia coli, Samonella, Shigella and Yersinia: cellular aspects of host-bacteria interactions in enteric diseases.Conformation of the EPEC Tir protein in solution: investigating the impact of serine phosphorylation at positions 434/463.PKA-mediated phosphorylation of EPEC-Tir at serine residues 434 and 463: A novel pathway in regulating Rac1 GTPase functionHost protein interactions with enteropathogenic Escherichia coli (EPEC): 14-3-3tau binds Tir and has a role in EPEC-induced actin polymerization.Host-mediated phosphorylation of type III effector AvrPto promotes Pseudomonas virulence and avirulence in tomato.Co-ordinate regulation of distinct host cell signalling pathways by multifunctional enteropathogenic Escherichia coli effector molecules.Enterohaemorrhagic Escherichia coli Tir requires a C-terminal 12-residue peptide to initiate EspF-mediated actin assembly and harbours N-terminal sequences that influence pedestal length.
P2860
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P2860
Phosphoserine modification of the enteropathogenic Escherichia coli Tir molecule is required to trigger conformational changes in Tir and efficient pedestal elongation.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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2001年学术文章
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name
Phosphoserine modification of ...... efficient pedestal elongation.
@en
Phosphoserine modification of ...... efficient pedestal elongation.
@nl
type
label
Phosphoserine modification of ...... efficient pedestal elongation.
@en
Phosphoserine modification of ...... efficient pedestal elongation.
@nl
prefLabel
Phosphoserine modification of ...... efficient pedestal elongation.
@en
Phosphoserine modification of ...... efficient pedestal elongation.
@nl
P2860
P1476
Phosphoserine modification of ...... efficient pedestal elongation.
@en
P2093
P2860
P304
P356
10.1046/J.1365-2958.2001.02693.X
P407
P577
2001-12-01T00:00:00Z