SCOPUS 정보 검색 플랫폼

Volumn 276, Issue 1, 2001, Pages 348-354

Acylation of lysine 983 is sufficient for toxin activity of Bordetella pertussis adenylate cyclase. Substitutions of alanine 140 modulate acylation site selectivity of the toxin acyltransferase CyaC

(5) Basar, Tümay a Havlíček, Vladimír a,b Bezoušková, Silvia a Hackett, Murray b Šebo, Peter a

a INSTITUTE OF MICROBIOLOGY (Czech Republic)

b UNIVERSITY OF WASHINGTON (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ADENYLATE CYCLASE; BACTERIAL ENZYME; BACTERIAL TOXIN; DNA; LYSINE; PERTUSSIS TOXIN;

ACYLATION; AMINO ACID SUBSTITUTION; ARTICLE; BORDETELLA PERTUSSIS; ENZYME ACTIVITY; MASS SPECTROMETRY; NONHUMAN; PERTUSSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; TOXIN ANALYSIS; TWO DIMENSIONAL GEL ELECTROPHORESIS;

ACYLATION; ACYLTRANSFERASES; ADENYLATE CYCLASE TOXIN; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; BORDETELLA PERTUSSIS; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ERYTHROCYTES; HEMOLYSIS; HISTIDINE; LYSINE; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; MUTATION; PALMITIC ACID; PEPTIDE FRAGMENTS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SEQUENCE ALIGNMENT; SERINE; SHEEP; SUBSTRATE SPECIFICITY; VIRULENCE FACTORS, BORDETELLA;

BACTERIA (MICROORGANISMS); BORDETELLA PERTUSSIS;

EID: 0035808430 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M006463200 Document Type: Article

Times cited : (53)

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