Validation of Alexa-647-ATP as a powerful tool to study P2X receptor ligand binding and desensitization

Biochemical and Biophysical Research Communications

Volumn 438, Issue 2, 2013, Pages 295-300

  Bhargava, Yogesh ^a   Nicke, Annette ^b   Rettinger, Jürgen ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b MAX PLANCK INSTITUTE OF EXPERIMENTAL MEDICINE   (Germany)

Author keywords

Alexa 647 ATP; Allosteric interaction; Binding; Desensitization; Ion channel; P2X1 receptor

Indexed keywords

PURINERGIC P2X RECEPTOR; PURINERGIC P2X1 RECEPTOR;

ANIMAL CELL; ARTICLE; BINDING SITE; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DESENSITIZATION; INTERNALIZATION; LIGAND BINDING; NEUROTRANSMISSION; NONHUMAN; OOCYTE; PRIORITY JOURNAL; RECEPTOR OCCUPANCY; XENOPUS LAEVIS;

ALEXA-647-ATP; ALLOSTERIC INTERACTION; BINDING; DESENSITIZATION; ION CHANNEL; MAGNESIUM OOCYTE RINGER'S SOLUTION; MGORI; OOCYTE RINGER'S SOLUTION; ORI; P2X1 RECEPTOR; PAO; PHENYL ARSINE OXIDE; VCF; VOLTAGE CLAMP FLUOROMETRY;

ADENOSINE TRIPHOSPHATE; ANIMALS; CARBOCYANINES; ENZYME INHIBITORS; FLUORESCENT DYES; OOCYTES; PATCH-CLAMP TECHNIQUES; PROTEIN BINDING; RATS; RECEPTORS, PURINERGIC P2X1; RNA, COMPLEMENTARY; XENOPUS LAEVIS;

ALEXA;

EID: 84882668864     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.07.058     Document Type: Article

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