Cloning and characterization of an extracellular Ca-sensing receptor from bovine parathyroid
Nature, ISSN: 0028-0836, Vol: 366, Issue: 6455, Page: 575-580
1993
- 2,470Citations
- 317Captures
- 3Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations2,470
- Citation Indexes2,465
- 2,465
- CrossRef1,998
- Patent Family Citations3
- Patent Families3
- Policy Citations2
- Policy Citation2
- Captures317
- Readers317
- 317
- Mentions3
- News Mentions2
- News2
- References1
- Wikipedia1
Most Recent News
Promiscuous G-protein activation by the calcium-sensing receptor
Nature, Published online: 17 April 2024; doi:10.1038/s41586-024-07331-1 Structures of the human calcium-sensing receptor can be bound into complex with G proteins from three different Gα subtypes while maintaining G-protein-binding specificity.
Article Description
Maintenance of a stable internal environment within complex organisms requires specialized cells that sense changes in the extracellular concentration of specific ions (such as Ca). Although the molecular nature of such ion sensors is unknown, parathyroid cells possess a cell surface Ca-sensing mechanism that also rec-ognizes trivalent and polyvalent cations (such as neomycin) and couples by changes in phosphoinositide turnover and cytosolic Ca to regulation of parathyroid hormone secretion. The latter restores normocalcaemia by acting on kidney and bone. We now report the cloning of complementary DNA encoding an extracellular Ca -sensing receptor from bovine parathyroid with pharmacological and functional properties nearly identical to those of the native receptor. The novel & sim;120K receptor shares limited similarity with the metabotropic glutamate receptors and features a large extracellular domain, containing clusters of acidic aminoacid residues possibly involved in calcium binding, coupled to a seven-membrane-spanning domain like those in the G-protein-coupled receptor superfamily. © 1993 Nature Publishing Group.
Bibliographic Details
Springer Science and Business Media LLC
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