A substrate-inspired probe monitors translocation, activation, and subcellular targeting of bacterial type III effector protease AvrPphB

Chemistry and Biology

Volumn 20, Issue 2, 2013, Pages 168-176

  Lu, Haibin ^a   Wang, Zheming ^a,b   Shabab, Mohammed ^c   Oeljeklaus, Julian ^e   Verhelst, Steven H ^d,f   Kaschani, Farnusch ^a,e   Kaiser, Markus ^b,e   Bogyo, Matthew ^d   Van Der Hoorn, Renier A L ^a,b  

^a MAX PLANCK INSTITUTE FOR PLANT BREEDING RESEARCH   (Germany)

^b CHEMICAL GENOMICS CENTRE OF THE MAX PLANCK SOCIETY   (Germany)

^c MAX PLANCK INSTITUTE FOR CHEMICAL ECOLOGY   (Germany)

^d STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^e UNIVERSITY OF DUISBURG ESSEN   (Germany)

^f TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AVRPPHB PROTEASE; PROTEINASE; UNCLASSIFIED DRUG;

ACYLATION; ARTICLE; CELL DEATH; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME RELEASE; ENZYME SPECIFICITY; HOST CELL; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROCESSING; PROTEIN UNFOLDING; PSEUDOMONAS SYRINGAE;

AMINO ACID SEQUENCE; ARABIDOPSIS; BACTERIAL PROTEINS; HYDROGEN-ION CONCENTRATION; MOLECULAR PROBES; MOLECULAR SEQUENCE DATA; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; PSEUDOMONAS SYRINGAE; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 84874304682     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2012.11.007     Document Type: Article

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