Novel protein-protein interactions of the Yersinia pestis type III secretion system elucidated with a matrix analysis by surface plasmon resonance and mass spectrometry

Journal of Biological Chemistry

Volumn 279, Issue 37, 2004, Pages 38693-38700

  Swietnicki, Wieslaw ^a   O'Brien, Sarah ^a   Holman, Kari ^a   Cherry, Scott ^a   Brueggemann, Ernst ^a   Tropea, Joseph E ^a   Hines, Harry B ^a   Waugh, David S ^a   Ulrich, Robert G ^a,b  

^a NATIONAL CANCER INSTITUTE   (United States)

^b UNITED STATES ARMY MEDICAL RESEARCH INSTITUTE OF INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; DESORPTION; DISEASE CONTROL; LASERS; MASS SPECTROMETRY; SURFACE PLASMON RESONANCE;

BINARY COMPLEXES; LASER DESORPTIONS; PROTEIN-PROTEIN INTERACTIONS; TRANSLOCATION REGULATOR PROTEINS;

PROTEINS;

BACTERIAL PROTEIN; CHAPERONE; PROTEIN LCRH; PROTEIN LCRQ; PROTEIN TYEA; PROTEIN YMOA; PROTEIN YOPH; PROTEIN YOPK; PROTEIN YSC; PROTEIN YSCE; RECOMBINANT PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG; YERSINIA OUTER PROTEIN;

ARTICLE; COMPLEX FORMATION; MAMMAL CELL; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PLAGUE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; SURFACE PLASMON RESONANCE; YERSINIA ENTEROCOLITICA; YERSINIA PESTIS;

BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL PROTEINS; DNA-BINDING PROTEINS; KINETICS; LIGANDS; MASS SPECTROMETRY; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; OPEN READING FRAMES; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN-TYROSINE-PHOSPHATASE; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SURFACE PLASMON RESONANCE; TIME FACTORS; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS; YERSINIA; YERSINIA PESTIS;

BACTERIA (MICROORGANISMS); MAMMALIA; NEGIBACTERIA; YERSINIA; YERSINIA ENTEROCOLITICA; YERSINIA PESTIS;

EID: 4644290877     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M405217200     Document Type: Article

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