Interaction of MxiG with the cytosolic complex of the type III secretion system controls Shigella virulence

FASEB Journal

Volumn 26, Issue 4, 2012, Pages 1717-1726

  Barison, Nicola ^a   Lambers, Jutta ^a   Hurwitz, Robert ^a   Kolbe, Michael ^a  

^a MAX PLANCK INSTITUTE FOR INFECTION BIOLOGY   (Germany)

Author keywords

Fha domain; Protein phosphorylation; Protein transport; Spa33

Indexed keywords

BACTERIAL PROTEIN; PHOSPHOPROTEIN; PROTEIN MXIG; PROTEIN SPA33; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL VIRULENCE; BINDING SITE; CELL INVASION; COMPLEX FORMATION; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; HOST CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; SHIGELLA FLEXNERI; SURFACE PLASMON RESONANCE; TYPE III SECRETION SYSTEM;

AMINO ACID SEQUENCE; BACTERIAL OUTER MEMBRANE PROTEINS; CRYSTALLOGRAPHY, X-RAY; CYTOSOL; GENE KNOCKDOWN TECHNIQUES; HELA CELLS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; SECRETORY PATHWAY; SEQUENCE ALIGNMENT; SHIGELLA FLEXNERI;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; SHIGELLA; SHIGELLA FLEXNERI;

EID: 84860914359     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.11-197160     Document Type: Article

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