Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Ekram Abusamhadneh"'
Publikováno v:
Journal of Biological Chemistry. 277:38565-38570
Cardiac troponin C (TnC) is composed of two globular domains connected by a flexible linker. In solution, linker flexibility results in an ill defined orientation of the two globular domains relative to one another. We have previously shown a decreas
Autor:
Natosha Finley, R. John Solaro, Alex Dvoretsky, Vadim Gaponenko, Ekram Abusamhadneh, M. Bret Abbott, Mark Rance, Paul R. Rosevear, Ge Li
Publikováno v:
Journal of Biological Chemistry. 275:20610-20617
Previously, we utilized (15)N transverse relaxation rates to demonstrate significant mobility in the linker region and conformational exchange in the regulatory domain of Ca(2+)-saturated cardiac troponin C bound to the isolated N-domain of cardiac t
Publikováno v:
Plant Science. 153:25-32
Adenosine nucleosidase from yellow lupin (Lupinus luteus) seeds has been purified to homogeneity. The enzyme catalyzes the hydrolysis of purine nucleosides to the base and the sugar. The enzyme was purified 146-fold to yield a specific activity of 6.
Autor:
Ekram Abusamhadneh, M. Bret Abbott, Natosha Finley, R. John Solaro, Genevieve Gasmi-Seabrook, Mark Rance, Vadim Gaponenko, Paul R. Rosevear
Publikováno v:
Journal of Biological Chemistry. 274:16681-16684
Conformational exchange has been demonstrated within the regulatory domain of calcium-saturated cardiac troponin C when bound to the NH2-terminal domain of cardiac troponin I-(1-80), and cardiac troponin I-(1-80)DD, having serine residues 23 and 24 m
Autor:
Paul R. Rosevear, Natosha Finley, Soumya Sasi, Ekram Abusamhadneh, Alex Dvoretsky, M. Bret Abbott
Publikováno v:
FEBS letters. 506(1)
We have investigated the binding of bepridil to calcium-saturated cardiac troponin C in a cardiac troponin C/troponin I complex. Nuclear magnetic resonance spectroscopy and [(15)N,(2)H]cardiac troponin C permitted the mapping of bepridil-induced amid
Autor:
Torbjörn Drakenberg, Ritva Serimaa, Ekram Abusamhadneh, Arto Annila, M. Bret Abbott, Piero Pollesello, Tia Sorsa, Ilkka Kilpeläinen, Tero Laakso, Carola Tilgmann, Sami Heikkinen, Paul R. Rosevear
Publikováno v:
Sorsa, T, Heikkinen, S, Abbott, M B, Abusamhadneh, E, Laakso, T, Tilgmann, C, Serimaa, R, Annila, A, Rosevear, P, Drakenberg, T, Pollesello, P & Kilpeläinen, I 2001, ' Binding of levosimendan, a calcium sensitizer, to cardiac troponin C ', Journal of Biological Chemistry, vol. 276, no. 12, pp. 9337-9343 . https://doi.org/10.1074/jbc.M007484200
Levosimendan is an inodilatory drug that mediates its cardiac effect by the calcium sensitization of contractile proteins. The target protein of levosimendan is cardiac troponin C (cTnC). In the current work, we have studied the interaction of levosi
Autor:
Genevieve Gasmi-Seabrook, Rui M. M. Brito, Ross J. Solaro, Ekram Abusamhadneh, Natosha Finley, Vadim Gaponenko, Jack W. Howarth, Paul R. Rosevear
Publikováno v:
CIÊNCIAVITAE
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
The N-terminal domain of cardiac troponin I (cTnI) comprising residues 33−80 and lacking the cardiac-specific amino terminus forms a stable binary complex with the C-terminal domain of cardiac troponin C (cTnC) comprising residues 81−161. We have
Autor:
Ekram Abusamhadneh, M. Bret Abbott, R. John Solaro, Vadim Gaponenko, Wen-Ji Dong, Herbert C. Cheung, Genevieve Gasmi-Seabrook, Mark Rance, Paul R. Rosevear, Natosha Finley, Jack W. Howarth
Publikováno v:
FEBS Letters. (1-2):107-112
Phosphorylation of the cardiac specific amino-terminus of troponin I has been demonstrated to reduce the Ca2+ affinity of the cardiac troponin C regulatory site. Recombinant N-terminal cardiac troponin I proteins, cardiac troponin I(33–80), cardiac