Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Suzanne M. Curtis"'
Publikováno v:
Journal of Biological Chemistry. 279:11853-11862
Imperatoxin A is a high affinity activator of ryanodine receptors. The toxin contains a positively charged surface structure similar to that of the A fragment of skeletal dihydropyridine receptors (peptide A), suggesting that the toxin and peptide co
Publikováno v:
Biophysical Journal. 80(4):1769-1782
The effect of peptides, corresponding to sequences in the skeletal muscle dihydropyridine receptor II-III loop, on Ca(2+) release from sarcoplasmic reticulum (SR) and on ryanodine receptor (RyR) calcium release channels have been compared in preparat
Publikováno v:
Journal of Biological Chemistry. 276:3319-3323
The ubiquitous glutathione transferases (GSTs) catalyze glutathione conjugation to many compounds and have other diverse functions that continue to be discovered. We noticed sequence similarities between Omega class GSTs and a nuclear chloride channe
Autor:
Suzy M. Pace, Marco G. Casarotto, Esther M. Gallant, Derek R. Laver, Angela F. Dulhunty, Suzanne M. Curtis
Publikováno v:
Biophysical Journal. 77(1):189-203
Peptides, corresponding to sequences in the N-terminal region of the skeletal muscle dihydropyridine receptor (DHPR) II-III loop, have been tested on sarcoplasmic reticulum (SR) Ca2+ release and ryanodine receptor (RyR) activity. The peptides were: A
Autor:
Jorgen Mould, Suzanne M. Curtis, Gerard P. Ahern, Suzy M. Pace, Angela F. Dulhunty, Pauline R. Junankar
Publikováno v:
The Journal of Physiology. 514:313-326
1. Ryanodine receptor (RyR) Ca2+ channels in the sarcoplasmic reticulum (SR) of skeletal muscle are regulated by the 12 kDa FK506- (or rapamycin-) binding protein (FKBP12). Rapamycin can also activate RyR channels with FKBP12 removed, suggesting that
Autor:
Suzanne M. Curtis, Esther M. Gallant, Angela F. Dulhunty, Pierre Pouliquin, Suzy M. Pace, Peta J. Harvey, Marco G. Casarotto, Francesco Zorzato
Publikováno v:
The international journal of biochemistrycell biology. 38(10)
We have determined the structure of a domain peptide corresponding to the extreme 19 C-terminal residues of the ryanodine receptor Ca2+ release channel. We examined functional interactions between the peptide and the channel, in the absence and in th
Autor:
Ester Gallant, James David Swarbrick, Suzanne M. Curtis, Martin J. Scanlon, Angela F. Dulhunty, Gerard M. Gibbs, Moira K O'Bryan
Publikováno v:
The Journal of biological chemistry. 281(7)
The cysteine-rich secretory proteins (Crisp) are predominantly found in the mammalian male reproductive tract as well as in the venom of reptiles. Crisps are two domain proteins with a structurally similar yet evolutionary diverse N-terminal domain a
Autor:
Yamuna Karunasekara, Marco G. Casarotto, Suzanne M. Curtis, Angela F. Dulhunty, Philip G. Board, Peta J. Harvey
Publikováno v:
The Biochemical journal. 385(Pt 3)
A physical association between the II–III loop of the DHPR (dihydropryidine receptor) and the RyR (ryanodine receptor) is essential for excitation–contraction coupling in skeletal, but not cardiac, muscle. However, peptides corresponding to a par
Publikováno v:
The Journal of biological chemistry. 279(12)
Imperatoxin A is a high affinity activator of ryanodine receptors. The toxin contains a positively charged surface structure similar to that of the A fragment of skeletal dihydropyridine receptors (peptide A), suggesting that the toxin and peptide co
Autor:
Angela F. Dulhunty, Marco G. Casarotto, Magdalena M. Sakowska, Louise Cengia, Suzanne M. Curtis
Publikováno v:
The Biochemical journal. 379(Pt 1)
We show that peptide fragments of the dihydropyridine receptor II–III loop alter cardiac RyR (ryanodine receptor) channel activity in a cytoplasmic Ca2+-dependent manner. The peptides were AC (Thr-793–Ala-812 of the cardiac dihydropyridine recept