Zobrazeno 1 - 10
of 123
pro vyhledávání: '"Lawrence B. Smillie"'
Autor:
Richard Sandford, Yan Liu, Lawrence B. Smillie, Xiao-Qing Dai, Xing-Zhen Chen, Qiang Li, Patrick Y. Shen, Shaohua Wang
Publikováno v:
Biochemistry. 42:7618-7625
Polycystin-L (PCL) is an isoform of polycystin-2, the product of the second gene associated with autosomal dominant polycystic kidney disease, and functions as a Ca(2+)-regulated nonselective cation channel. We recently demonstrated that polycystin-2
Publikováno v:
Journal of Biological Chemistry. 275:35106-35115
To investigate the roles of site I and II invariant Glu residues 41 and 77 in the functional properties and calcium-induced structural opening of skeletal muscle troponin C (TnC) regulatory domain, we have replaced them by Ala in intact F29W TnC and
Publikováno v:
Biochemistry. 38:5478-5489
The kinetics and energetics of the binding of three troponin-I peptides, corresponding to regions 96-131 (TnI96-131), 96-139 (TnI96-139), and 96-148 (TnI96-148), to skeletal chicken troponin-C were investigated using multinuclear, multidimensional NM
Autor:
J J Rodrigues, Marisa C. Suarez, Lawrence B. Smillie, Claudio Clemente Faria Barbosa, Martha M. Sorenson, Debora Foguel, Jerson L. Silva
Publikováno v:
Proceedings of the National Academy of Sciences. 93:10642-10646
Calcium binding to the N-domain of troponin C initiates a series of conformational changes that lead to muscle contraction. Calcium binding provides the free energy for a hydrophobic region in the core of N-domain to assume a more open configuration.
Publikováno v:
Nature Structural & Molecular Biology. 2:784-789
Regulation of contraction in skeletal muscle occurs through calcium binding to the protein troponin C. The solution structures of the regulatory domain of apo and calcium-loaded troponin C have been determined by multinuclear, multidimensional nuclea
Publikováno v:
Protein Science. 4:1279-1290
The solution secondary structure of calcium-saturated skeletal troponin C (TnC) in the presence of 15% (v/v) trifluoroethanol (TFE), which has been shown to exist predominantly as a monomer (Slupsky CM, Kay CM, Reinach FC, Smillie LB, Sykes BD, 1995,
Autor:
Joyce R. Pearlstone, T Borgford, E F da Silva, M M Sorenson, Lawrence B. Smillie, Cyril M. Kay, B E Nash, J A Ferro, Murali Chandra
Publikováno v:
Journal of Biological Chemistry. 269:14988-14994
To assess the structural and functional significance of the N helix (residues 3-13) of avian recombinant troponin C (rTnC), we have constructed NHdel, in which residues 1-11 have been deleted, both in rTnC and in the spectral probe mutant F29W (Pearl
Autor:
Joyce R. Pearlstone, Genny Trigo-Gonzalez, Murali Chandra, Thor J. Borgford, Monica X. Li, Kathleen I. Racher, Lawrence B. Smillie, Cyril M. Kay
Publikováno v:
Biochemistry. 33:917-925
The two globular N and C domains of chicken troponin C (TnC) are connected by an exposed alpha-helix (designated D/E; residues 86-94). Recombinant N (residues 1-90) and C (residues 88-162) domains containing either F29 or W29 and F105 or W105 have be
Publikováno v:
Journal of Biological Chemistry. 268:26220-26225
Troponin C can replace calmodulin in the activation of the Ca(2+)-ATPase of pig erythrocytes provided that the reaction medium contains relatively high free Ca2+ concentrations (> 0.5 microM). In the presence of 10 microM free Ca2+, the troponin C-ac