Phosphorylation of tyrosine 474 of the enteropathogenic Escherichia coli (EPEC) Tir receptor molecule is essential for actin nucleating activity and is preceded by additional host modifications

Molecular Microbiology

Volumn 31, Issue 4, 1999, Pages 1229-1241

  Kenny, Brendan ^a  

^a SCHOOL OF MEDICAL SCIENCES   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ANTIBODY; BACTERIAL PROTEIN; INTEGRIN; OUTER MEMBRANE PROTEIN; RECEPTOR; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; CYTOPLASM; ENTEROPATHY; ESCHERICHIA COLI; GASTROINTESTINAL HEMORRHAGE; GENE DELETION; HOST CELL; MOLECULAR RECOGNITION; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PATHOGENICITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; TARGET CELL;

ACTINS; ADHESINS, BACTERIAL; AMINO ACID SEQUENCE; BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL PROTEINS; BINDING SITES; CARRIER PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI O157; ESCHERICHIA COLI PROTEINS; HELA CELLS; HUMANS; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; RECEPTORS, CELL SURFACE; TYROSINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0033002855     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01265.x     Document Type: Article

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