Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin.

scientific article published on July 1997

Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.272.29.18125
P698PubMed publication ID9218446

P50authorVsevolod V. GurevichQ42173663
P2093author name stringJ L Benovic
J G Krupnick
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Kinetics, binding constant, and activation energy of the 48-kDa protein-rhodopsin complex by extra-metarhodopsin II.Q52538921
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Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segmentsQ24632640
Desensitization of the isolated beta 2-adrenergic receptor by beta-adrenergic receptor kinase, cAMP-dependent protein kinase, and protein kinase C occurs via distinct molecular mechanismsQ28181949
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Primary and secondary structure of bovine retinal S antigen (48-kDa protein).Q34351336
Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein)Q34376629
Effects of carboxyl-terminal truncation on the stability and G protein-coupling activity of bovine rhodopsinQ41460708
A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activationQ41473791
P433issue29
P407language of work or nameEnglishQ1860
P304page(s)18125-18131
P577publication date1997-07-01
P1433published inJournal of Biological ChemistryQ867727
P1476titleMechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin
P478volume272

Reverse relations

cites work (P2860)
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