about
EscA is a crucial component of the type III secretion system of enteropathogenic Escherichia coliA Highly Effective Component Vaccine against Nontyphoidal Salmonella enterica Infections.EscE and EscG are cochaperones for the type III needle protein EscF of enteropathogenic Escherichia coliStructural microengineers: pathogenic Escherichia coli redesigns the actin cytoskeleton in host cells.Transmembrane domains interactions within the membrane milieu: principles, advances and challenges.Two motifs within a transmembrane domain, one for homodimerization and the other for heterodimerization.Quantitative proteomic analysis reveals formation of an EscL-EscQ-EscN type III complex in enteropathogenic Escherichia coli.Translocation of effectors: revisiting the injectosome model.The Ruler Protein EscP of the Enteropathogenic Escherichia coli Type III Secretion System Is Involved in Calcium Sensing and Secretion Hierarchy Regulation by Interacting with the Gatekeeper Protein SepL.Arginine mutations within a transmembrane domain of Tar, an Escherichia coli aspartate receptor, can drive homodimer dissociation and heterodimer association in vivo.Preassembly of membrane-active peptides is an important factor in their selectivity toward target cells.A transferrin-like protein that does not bind iron is induced by iron deficiency in the alga Dunaliella salina.The composition rather than position of polar residues (QxxS) drives aspartate receptor transmembrane domain dimerization in vivo.Structural adaptation of the glycophorin A transmembrane homodimer to D-amino acid modifications.Impairment of innate immune killing mechanisms by bacteriostatic antibiotics.The identification of a minimal dimerization motif QXXS that enables homo- and hetero-association of transmembrane helices in vivo.The role of EscD in supporting EscC polymerization in the type III secretion system of enteropathogenic Escherichia coli.Deciphering the Mechanical Properties of Type III Secretion System EspA Protein by Single Molecule Force Spectroscopy.EscI: a crucial component of the type III secretion system forms the inner rod structure in enteropathogenic Escherichia coli.Specificity in transmembrane helix-helix interactions mediated by aromatic residues.Peer power: A women's peer-mentoring program at the workplace: example from the academiaVibrio cholerae autoinducer-1 enhances the virulence of enteropathogenic Escherichia coliHetero-assembly between all-L- and all-D-amino acid transmembrane domains: forces involved and implication for inactivation of membrane proteinsProline localized to the interaction interface can mediate self-association of transmembrane domainsThe Third Transmembrane Domain of EscR Is Critical for Function of the Enteropathogenic Escherichia coli Type III Secretion System
P50
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P50
description
researcher
@en
wetenschapper
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հետազոտող
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name
Neta Sal-Man
@ast
Neta Sal-Man
@en
Neta Sal-Man
@es
Neta Sal-Man
@nl
Neta Sal-Man
@sl
type
label
Neta Sal-Man
@ast
Neta Sal-Man
@en
Neta Sal-Man
@es
Neta Sal-Man
@nl
Neta Sal-Man
@sl
prefLabel
Neta Sal-Man
@ast
Neta Sal-Man
@en
Neta Sal-Man
@es
Neta Sal-Man
@nl
Neta Sal-Man
@sl
P106
P1153
6603307385
P2798
P31
P496
0000-0002-1109-479X
P569
2000-01-01T00:00:00Z