An alternative assay to discover potential calmodulin inhibitors using a human fluorophore-labeled CaM protein

Analytical Biochemistry

Volumn 387, Issue 1, 2009, Pages 64-70

  González Andrade, Martín ^a   Figueroa, Mario ^b   Rodríguez Sotres, Rogelio ^b   Mata, Rachel ^b   Sosa Peinado, Alejandro ^a  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b Universidad Nacional Autonoma de Mexico Facultad de Quimica   (Mexico)

Author keywords

Calmodulin; CaM inhibitors; Fluorescence assay; Fluorophore labeled CaM protein

Indexed keywords

AMINO ACIDS; BROMINE COMPOUNDS; CALCIUM COMPOUNDS; CAMS; FLUORESCENCE; FLUOROPHORES;

BIOTECHNOLOGY INDUSTRY; CALMODULIN-INHIBITORS; CHEMICALLY MODIFIED; FLUORESCENCE ASSAY; FLUORESCENCE BIOSENSORS; HIGH THROUGHPUT SCREENING; INHIBITOR CONCENTRATION; WILD-TYPE PROTEINS;

CALMODULIN;

AMIDE; BROMOBIMANE; CALMODULIN; CALMODULIN INHIBITOR; CHLORPROMAZINE; CYCLIC AMP PHOSPHODIESTERASE; CYSTEINE; MALBRANCHEAMIDE; MUTANT PROTEIN; PHOSPHODIESTERASE; TAJIXANTHONE HYDRATE; UNCLASSIFIED DRUG; XANTHONE DERIVATIVE; BICYCLO COMPOUND; FLUORESCENT DYE; INDOLE ALKALOID;

ARTICLE; BIOSENSOR; BIOTECHNOLOGY; CHEMICAL LABELING; COMPARATIVE STUDY; CONCENTRATION PROCESS; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG DETERMINATION; DRUG INDUSTRY; ENZYME ACTIVATION; FLUORESCENCE; FLUORESCENCE ANALYSIS; HIGH THROUGHPUT SCREENING; IC 50; OXYGEN SATURATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN PURIFICATION; PROTEIN STABILITY; SENSITIVITY ANALYSIS; SPECTRUM; WILD TYPE; ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; GENETIC PROCEDURES; GENETICS; HUMAN; IC50; METABOLISM; SITE DIRECTED MUTAGENESIS; SPECTROFLUOROMETRY;

BICYCLO COMPOUNDS; BIOSENSING TECHNIQUES; CALMODULIN; CIRCULAR DICHROISM; FLUORESCENT DYES; HUMANS; INDOLE ALKALOIDS; INHIBITORY CONCENTRATION 50; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHORIC DIESTER HYDROLASES; SPECTROMETRY, FLUORESCENCE;

EID: 60549110632     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.01.002     Document Type: Article

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