A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin

Proceedings of the National Academy of Sciences of the United States of America

Volumn 101, Issue 27, 2004, Pages 10166-10171

  Clifton, D R ^a   Fields, K A ^a   Grieshaber, S S ^a   Dooley, C A ^a   Fischer, E R ^a   Mead, D J ^a   Carabeo, R A ^a   Hackstadt, T ^a,b  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BACTERIAL PROTEIN; CHLAMYDIA PROTEIN; PHOSPHOPROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM ADHERENCE; CELL MEMBRANE; CHLAMYDIA; CHLAMYDIA TRACHOMATIS; ELECTRICITY; HUMAN; HUMAN CELL; IMMUNOELECTRON MICROSCOPY; IMMUNOPRECIPITATION; INTERNALIZATION; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; YERSINIA;

ACTINS; AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; CHLAMYDIA; COS CELLS; HELA CELLS; HUMANS; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN TRANSPORT; TRANSFECTION; TYROSINE;

BACTERIA (MICROORGANISMS); CHLAMYDIA TRACHOMATIS; CHLAMYDIAE; RICKETTSIALES; YERSINIA;

EID: 3042707297     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0402829101     Document Type: Article

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