Ca2+ dependent calmodulin binding to cardiac ryanodine receptor (RyR2) calmodulin-binding domains

Autor: Michael Toft Overgaard, Sui Rong Wayne Chen, Mads Toft Søndergaard, Filip Van Petegem, Malene Brohus

Publikováno v: Brohus, M, Søndergaard, M T, Chen, W S R, Van Petegem, F & Overgaard, M T 2019, ' Ca 2+ dependent calmodulin binding to cardiac ryanodine receptor (RyR2) calmodulin-binding domains ', Biochemical Journal, vol. 476, no. 2, pp. 193-209 . https://doi.org/10.1042/BCJ20180545

The Ca 2+ sensor calmodulin (CaM) regulates cardiac ryanodine receptor (RyR2)-mediated Ca 2+ release from the sarcoplasmic reticulum. CaM inhibits RyR2 in a Ca 2+ -dependent manner and aberrant CaM-dependent inhibition results in life-threatening car

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6822e3c075b96269c1195cc06af787fc
https://vbn.aau.dk/ws/files/295146658/193.full.pdf

Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca 2+ release channel/ryanodine receptors

Autor: M. De Waard, Jean-Marc Sabatier, Isaac N. Pessah, Paul D. Allen, C. Lecomte, Lili Chen, E. Di Luccio, Delphine Bichet, Ziad Fajloun, R. Kharrat, Hervé Rochat, M. El Ayeb

Publikováno v: FEBS Letters
FEBS Letters, 2000, 469 (2-3), pp.179-185. ⟨10.1016/S0014-5793(00)01239-4⟩
FEBS Letters, Wiley, 2000, 469 (2-3), pp.179-185. ⟨10.1016/S0014-5793(00)01239-4⟩

International audience; Maurocalcine is a novel toxin isolated from the venom of the chactid scorpion Scorpio maurus palmatus. It is a 33‐mer basic peptide cross‐linked by three disulfide bridges, which shares 82% sequence identity with imperatox

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0e37e030d848ab228688e67d72a2a96
https://hal-riip.archives-ouvertes.fr/pasteur-02018803