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The Transient Receptor Potential Channels TRPP2 and TRPC1 Form a Heterotetramer with a 2:2 Stoichiometry and an Alternating Subunit Arrangement

There is functional evidence that polycystin-2 (TRPP2) interacts with other members of the transient receptor potential family, including TRPC1 and TRPV4. Here we have used atomic force microscopy to study the structure of the TRPP2 homomer and the interaction between TRPP2 and TRPC1. The molecular...

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Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς: Kobori, Toshiro, Smith, Graham D., Sandford, Richard, Edwardson, J. Michael
Μορφή: Artigo
Γλώσσα:Inglês
Έκδοση: American Society for Biochemistry and Molecular Biology 2009
Θέματα:
Διαθέσιμο Online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2790980/
https://ncbi.nlm.nih.gov/pubmed/19850920
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.060228
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