| Title |
Primary Structure of the γ Subunit of the DHP-Sensitive Calcium Channel from Skeletal Muscle
|
|---|---|
| Published in |
Science, April 1990
|
| DOI | 10.1126/science.2158672 |
| Pubmed ID | |
| Authors | |
| Abstract |
Affinity-purified, polyclonal antibodies to the gamma subunit of the dihydropyridine (DHP)-sensitive, voltage-dependent calcium channel have been used to isolate complementary DNAs to the rabbit skeletal muscle protein from an expression library. The deduced primary structure indicates that the gamma subunit is a 25,058-dalton protein that contains four transmembrane domains and two N-linked glycosylation sites, consistent with biochemical analyses showing that the gamma subunit is a glycosylated hydrophobic protein. Nucleic acid hybridization studies indicate that there is a 1200-nucleotide transcript in skeletal muscle but not in brain or heart. The gamma subunit may play a role in assembly, modulation, or the structure of the skeletal muscle calcium channel. |
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Mendeley demographics
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 1 | 2% |
| Unknown | 47 | 98% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Bachelor | 8 | 17% |
| Professor | 8 | 17% |
| Student > Ph. D. Student | 6 | 13% |
| Researcher | 6 | 13% |
| Student > Master | 4 | 8% |
| Other | 7 | 15% |
| Unknown | 9 | 19% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 11 | 23% |
| Biochemistry, Genetics and Molecular Biology | 10 | 21% |
| Neuroscience | 8 | 17% |
| Medicine and Dentistry | 3 | 6% |
| Pharmacology, Toxicology and Pharmaceutical Science | 2 | 4% |
| Other | 3 | 6% |
| Unknown | 11 | 23% |