Primary structure of the beta subunit of the DHP-sensitive calcium channel from skeletal muscle. 1989

P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
Institut für Physiologische Chemie, Medizinische Fakultät, Homburg/Saar, Federal Republic of Germany.

Complementary DNAs for the beta subunit of the dihydropyridine-sensitive calcium channel of rabbit skeletal muscle were isolated on the basis of peptide sequences derived from the purified protein. The deduced primary structure is without homology to other known protein sequences and is consistent with the beta subunit being a peripheral membrane protein associated with the cytoplasmic aspect of the sarcolemma. The protein contains sites that might be expected to be preferentially phosphorylated by protein kinase C and guanosine 3',5'-monophosphate-dependent protein kinase. A messenger RNA for this protein appears to be expressed in brain.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D011978 Receptors, Nicotinic One of the two major classes of cholinergic receptors. Nicotinic receptors were originally distinguished by their preference for NICOTINE over MUSCARINE. They are generally divided into muscle-type and neuronal-type (previously ganglionic) based on pharmacology, and subunit composition of the receptors. Nicotinic Acetylcholine Receptors,Nicotinic Receptors,Nicotinic Acetylcholine Receptor,Nicotinic Receptor,Acetylcholine Receptor, Nicotinic,Acetylcholine Receptors, Nicotinic,Receptor, Nicotinic,Receptor, Nicotinic Acetylcholine,Receptors, Nicotinic Acetylcholine
D002121 Calcium Channel Blockers A class of drugs that act by selective inhibition of calcium influx through cellular membranes. Calcium Antagonists, Exogenous,Calcium Blockaders, Exogenous,Calcium Channel Antagonist,Calcium Channel Blocker,Calcium Channel Blocking Drug,Calcium Inhibitors, Exogenous,Channel Blockers, Calcium,Exogenous Calcium Blockader,Exogenous Calcium Inhibitor,Calcium Channel Antagonists,Calcium Channel Blocking Drugs,Exogenous Calcium Antagonists,Exogenous Calcium Blockaders,Exogenous Calcium Inhibitors,Antagonist, Calcium Channel,Antagonists, Calcium Channel,Antagonists, Exogenous Calcium,Blockader, Exogenous Calcium,Blocker, Calcium Channel,Blockers, Calcium Channel,Calcium Blockader, Exogenous,Calcium Inhibitor, Exogenous,Channel Antagonist, Calcium,Channel Blocker, Calcium,Inhibitor, Exogenous Calcium
D004095 Dihydropyridines Pyridine moieties which are partially saturated by the addition of two hydrogen atoms in any position.
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
April 1990, Science (New York, N.Y.),
P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
August 1987, Proceedings of the National Academy of Sciences of the United States of America,
P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
January 1987, Nature,
P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
August 1990, General physiology and biophysics,
P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
December 1988, European journal of biochemistry,
P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
July 1991, Nature,
P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
January 1993, Genomics,
P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
February 1996, Genomics,
P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
January 2006, Journal of muscle research and cell motility,
P Ruth, and A Röhrkasten, and M Biel, and E Bosse, and S Regulla, and H E Meyer, and V Flockerzi, and F Hofmann
June 1986, Biochemistry,
Copied contents to your clipboard!