Bacillus thuringiensis Cry4Ba toxin employs two receptor-binding loops for synergistic interactions with Cyt2Aa2

Biochemical and Biophysical Research Communications

Volumn 435, Issue 2, 2013, Pages 216-221

  Lailak, Chitsirin ^a   Khaokhiew, Tararat ^a   Promptmas, Chamras ^a   Promdonkoy, Boonhiang ^b   Pootanakit, Kusol ^a   Angsuthanasombat, Chanan ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

^b NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

Author keywords

Bacillus thuringiensis; Cry toxins; Cyt toxins; Larvicidal restoration; Quartz crystal microbalance; Receptor binding loops; Synergism

Indexed keywords

BACTERIAL TOXIN; CRY4BA TOXIN; CYT2AA2 TOXIN; PHENYLALANINE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS THURINGIENSIS; BIOLOGICAL ACTIVITY; CONTROLLED STUDY; GENE MUTATION; MOLECULAR INTERACTION; MUTANT; NONHUMAN; PRIORITY JOURNAL; QUARTZ CRYSTAL MICROBALANCE; RECEPTOR BINDING;

BACILLUS THURINGIENSIS; BACTERIAL PROTEINS; BACTERIAL TOXINS; BINDING SITES; ENDOTOXINS; HEMOLYSIN PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION;

BACILLUS THURINGIENSIS; BACILLUS THURINGIENSIS SEROVAR ISRAELENSIS; ESCHERICHIA COLI;

EID: 84878427784     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.04.078     Document Type: Article

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