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dc.contributor.advisorAndrade, Rodrigo
dc.contributor.authorOuellette, Andrea
dc.date.accessioned2008-03-10T13:15:47Z
dc.date.available2008-03-10T13:15:47Z
dc.date.copyright2002-01-01
dc.date.issued2002
dc.identifier.urihttp://hdl.handle.net/10920/4354
dc.description1 broadside ; ill.
dc.description.abstractNamed for the transient receptor potential channels in Drosophila visual transduction, TRP channels are ubiquitously expressed in virtually all animals. •TRPs are classified into three subtypes based on sequence homology: short, long, and osm-9-like •TRP proteins assemble into tetrameric cation channels •Activated by the phospholipase C pathway associated with metabotropic receptors •May be gated by depletion of intracellular Ca2+ stores or DAG •Heteromultimeric channels may contribute to the electrophysiological properties and activation mechanism of TRPs •We studied currents from HEK293 cells expressing both human TRP1 and murine TRP4 to determine the effect of heteromer formation.We were hoping to understand how heteromer formation affects the voltage dependence of TRP channels, regardless of a dependence on Ca2+ for activationen
dc.description.tableofcontentsIntroduction -- Materials and methods -- Results -- Conclusions -- Acknowledgments -- Commonly referenced articles
dc.language.isoen_USen
dc.publisherKalamazoo College
dc.subject.lcshTRP channels
dc.titleVoltage Dependence of the Cation-Nonselective TRP Channelsen
dc.typePresentationen


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  • Diebold Symposium Posters and Schedules [320]
    Poster and oral presentations by senior biology majors that include the results of their Senior Individualized Projects (SIPs) at the Diebold Symposium. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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