Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Roque El-Hayek"'
Autor:
Noriaki Ikemoto, Roque El-Hayek
Publikováno v:
FEBS Letters. 394:330-334
We attached the conformational probe methylcoumarin acetate (MCA) specifically to the junctional foot protein (JFP) moiety of triads, and monitored conformational changes in the JFP during polarization and depolarization of the T-tubule moiety. The M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c13649ad688701b05d9bbd44dea5443
https://doi.org/10.1016/0014-5793(96)00973-8
https://doi.org/10.1016/0014-5793(96)00973-8
Publikováno v:
Biochemistry. 34:12584-12589
Perchlorate is one of the most potent activators of skeletal muscle excitation-contraction (E-C) coupling reported in the literature, but the detailed mechanism of its action remains to be elucidated. In an attempt to further resolve the mode of perc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92c3f664279b820d370fef860df6e4a9
https://doi.org/10.1021/bi00039a013
https://doi.org/10.1021/bi00039a013
Autor:
Brian M. Martin, Roque El-Hayek, W.D. Schleuning, Richard L. Moss, Roberto Coronado, J. Mochca-Morales, Jeffery M. Morrissette, Jitandrakumar R. Patel, B. Haendler, J. Krätzschmar
Publikováno v:
Biophysical Journal. 68:2280-2288
Helothermine, a protein from the venom of the Mexican beaded lizard (Heloderma horridum horridum), was found to inhibit [3H]ryanodine binding to cardiac and skeletal sarcoplasmic reticulum, to block cardiac and skeletal ryanodine receptor channels in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc1b2a43b8b8149fe49d7b85f0a0f29a
https://doi.org/10.1016/s0006-3495(95)80410-8
https://doi.org/10.1016/s0006-3495(95)80410-8
Publikováno v:
Journal of Biological Chemistry. 270:15634-15638
We investigated both conformational changes in the junctional foot protein (JFP) and Ca2+ release from sarcoplasmic reticulum (SR) in parallel after stimulation of triadic vesicles by the JFP-specific ligand, polylysine. To monitor protein conformati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b395ced899b49566a18a258041e53eb
https://doi.org/10.1074/jbc.270.26.15634
https://doi.org/10.1074/jbc.270.26.15634
Publikováno v:
Biochemistry. 33:10961-10968
Excitation-Ca2+ release coupling properties in the heavy microsomal fraction of the rabbit skeletal muscle enriched in triads were investigated by following the same type of approach used for the studies of excitation-contraction coupling in the skin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e2932f8d929ebe635a9f1b14238a4bc
https://doi.org/10.1021/bi00202a015
https://doi.org/10.1021/bi00202a015
Publikováno v:
Biophysical Journal. 65:779-789
Studies of [3H]ryanodine binding, 45Ca2+ efflux, and single channel recordings in planar bilayers indicated that the fatty acid metabolite palmitoyl carnitine produced a direct stimulation of the Ca2+ release channel (ryanodine receptor) of rabbit an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::132fec9a4c489b2f6c9de4498e54f102
https://doi.org/10.1016/s0006-3495(93)81101-9
https://doi.org/10.1016/s0006-3495(93)81101-9
Publikováno v:
Biochemical and Biophysical Research Communications. 187:894-900
We tested whether the hydantoin muscle relaxants dantrolene, azumolene, or aminodantrolene could alter the binding of [3H]PN200-110 to transverse tubule dihydropyridine receptors or the binding of [3H]ryanodine to junctional sarcoplasmic reticulum Ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fd1328d823e8c75cc40b0cd2b967e3c
https://doi.org/10.1016/0006-291x(92)91281-t
https://doi.org/10.1016/0006-291x(92)91281-t
Publikováno v:
Journal of Biological Chemistry. 266:19135-19138
We identified a peptide fraction from the venom of the scorpion Buthotus hottentota that stimulated binding of [3H]ryanodine to ryanodine receptors of skeletal and cardiac sarcoplasmic reticulum and brain microsomes in a highly specific manner. Activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77cb106dafaa575bd0c9243ee7a066f7
https://doi.org/10.1016/s0021-9258(18)54969-3
https://doi.org/10.1016/s0021-9258(18)54969-3
Publikováno v:
American journal of physiology. Cell physiology. 279(4)
In skeletal muscle fibers, the intracellular loop between domains II and III of the α1-subunit of the dihydropyridine receptor (DHPR) may directly activate the adjacent Ca2+release channel in the sarcoplasmic reticulum. We examined the effects of sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec88811ee33a31d549247d8f626c0d09
https://pubmed.ncbi.nlm.nih.gov/11003569
https://pubmed.ncbi.nlm.nih.gov/11003569
Publikováno v:
The Journal of biological chemistry. 275(16)
Localized distribution of malignant hyperthermia (MH) and central core disease (CCD) mutations in N-terminal and central domains of the ryanodine receptor suggests that the interaction between these domains may be involved in Ca(2+) channel regulatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce6335667aff3d8a35039a4fd9737320
https://pubmed.ncbi.nlm.nih.gov/10766778
https://pubmed.ncbi.nlm.nih.gov/10766778