Molecular properties of mammalian proteins that interact with cGMP: Protein kinases, cation channels, phosphodiesterases, and multi-drug anion transporters

Frontiers in Bioscience

Volumn 10, Issue SUPPL. 1, 2005, Pages 2097-2117

  Francis, Sharron H ^a   Blount, Mitsi A ^a   Zoraghi, Roya ^a   Corbin, Jackie D ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

cAMP; Cation channel; cGMP; CNG; Cyclic nucleotide signaling; HCN; Kinase; MRP; Multi drug anion transporters; PDE; Phosphodiesterase; PKG; Review

Indexed keywords

ANION; ANION TRANSPORT PROTEIN; CARBON MONOXIDE; CELL PROTEIN; CYCLIC GMP; CYCLIC NUCLEOTIDE; CYCLIC NUCLEOTIDE DEPENDENT PROTEIN KINASE; DIPYRIDAMOLE; GUANOSINE PHOSPHATE; GUANYLIN; HORMONE; ISOBUTYLMETHYLXANTHINE; NATRIURETIC FACTOR; NITRIC OXIDE; NUCLEOTIDE; PHOSPHODIESTERASE; PHOSPHODIESTERASE INHIBITOR; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN KINASE; SILDENAFIL; TREQUINSIN; ZAPRINAST;

ARTICLE; BINDING AFFINITY; BINDING SITE; BIOLOGICAL PHENOMENA AND FUNCTIONS CONCERNING THE ENTIRE ORGANISM; CATALYSIS; CATION CHANNEL; CELL FUNCTION; CELL TYPE; HUMAN; ION TRANSPORT; LIGAND BINDING; MAMMAL; MAMMAL CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SECOND MESSENGER; STIMULUS;

MAMMALIA;

EID: 21344459311     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1684     Document Type: Article

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