Dimeric c-di-GMP is required for post-translational regulation of alginate production in pseudomonas aeruginosa

Journal of Biological Chemistry

Volumn 290, Issue 20, 2015, Pages 12451-12462

  Whitney, John C ^a,b,e   Whitfield, Gregory B ^a,b   Marmont, Lindsey S ^a,b   Yip, Patrick ^a   Neculai, A Mirela ^a   Lobsanov, Yuri D ^a   Robinson, Howard ^c   Ohman, Dennis E ^d   Howell, P Lynne ^a,b  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c BROOKHAVEN NATIONAL LABORATORY   (United States)

^d VETERANS AFFAIRS MEDICAL CENTER   (United States)

^e UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALGINATE; BACTERIA; BIOLOGICAL MEMBRANES; PHYSIOLOGY; PROTEINS; PULMONARY DISEASES;

BINDING ACTIVITIES; CHRONIC OBSTRUCTIVE PULMONARY DISEASE; CYTOPLASMIC REGIONS; EXOPOLYSACCHARIDES; MUTATIONAL ANALYSIS; PSEUDOMONAS AERUGINOSA; SIGNALING MOLECULES; TRANSLATIONAL REGULATION;

CRYSTAL STRUCTURE;

ALGINIC ACID; ARGININE; CYCLIC DIMERIC GUANOSINE MONOPHOSPHATE; CYCLIC GMP; UNCLASSIFIED DRUG; ALG44 PROTEIN, PSEUDOMONAS AERUGINOSA; BACTERIAL PROTEIN; BIS(3',5')-CYCLIC DIGUANYLIC ACID; GLUCURONIC ACID; HEXURONIC ACID; MEMBRANE PROTEIN; VIRULENCE FACTOR;

ALLELE; ARTICLE; BACTERIAL CHROMOSOME; CARBOHYDRATE SYNTHESIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOPLASM; DIMERIZATION; IN VITRO STUDY; IN VIVO STUDY; MUTATION; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN PROCESSING; PSEUDOMONAS AERUGINOSA; SIGNAL TRANSDUCTION; STOICHIOMETRY; ANALOGS AND DERIVATIVES; BINDING SITE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PATHOGENICITY; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; SECRETION (PROCESS); X RAY CRYSTALLOGRAPHY;

PSEUDOMONAS AERUGINOSA;

ALGINATES; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYCLIC GMP; GLUCURONIC ACID; HEXURONIC ACIDS; HUMANS; MEMBRANE PROTEINS; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PSEUDOMONAS AERUGINOSA; VIRULENCE FACTORS;

EID: 84929378451     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.645051     Document Type: Article

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