Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Paul R. Rosevear"'
Publikováno v:
Journal of Biological Chemistry. 287:8254-8262
The structural role of the unique myosin-binding motif (m-domain) of cardiac myosin-binding protein-C remains unclear. Functionally, the m-domain is thought to directly interact with myosin, whereas phosphorylation of the m-domain has been shown to m
Autor:
Paul R. Rosevear, Genevieve Gasmi-Seabrook, Linda Columbus, Jack W. Howarth, Vadim Gaponenko, Wayne L. Hubbell, Jie Yuan
Publikováno v:
Protein Science. 9:302-309
We describe a simple experimental approach for the rapid determination of protein global folds. This strategy utilizes site-directed spin labeling (SDSL) in combination with isotope enrichment to determine long-range distance restraints between amide
Autor:
Natosha L. Finley, Hanna Osinska, Jeffrey Robbins, Paul R. Rosevear, Raisa Klevitsky, Sakthivel Sadayappan, Jack W. Howarth, John N. Lorenz
Publikováno v:
The FASEB Journal. 22:1246-1257
Cardiac troponin I (cTnI) phosphorylation modulates myocardial contractility and relaxation during beta-adrenergic stimulation. cTnI differs from the skeletal isoform in that it has a cardiac specific N' extension of 32 residues (N' extension). The r
Autor:
Paul R. Rosevear, Natosha Finley
Publikováno v:
Journal of Biological Chemistry. 279:54833-54840
Protein kinase C phosphorylation of cardiac troponin, the Ca(2+)-sensing switch in muscle contraction, is capable of modulating the response of cardiac muscle to a Ca(2+) ion concentration. The N-domain of cardiac troponin I contains two protein kina
Publikováno v:
Biochemistry. 43:11371-11379
Cardiac troponin C (cTnC) is the Ca(2+)-binding component of the troponin complex and, as such, is the Ca(2+)-dependent switch in muscle contraction. This protein consists of two globular lobes, each containing a pair of EF-hand metal-binding sites,
Autor:
Paul R. Rosevear, Natosha L. Finley
Publikováno v:
Journal of Molecular and Cellular Cardiology. 35:1011-1015
Autor:
Ronald W. Millard, Paul R. Rosevear
Publikováno v:
Journal of the American College of Cardiology. 59:1642-1644
In this issue of the Journal , Bodi et al. ([1][1]) report the application of nuclear magnetic resonance (NMR) spectroscopic techniques to detect and characterize a predictive cardiac-specific metabolomic (also known as metabonomic) profile on the ba
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:
Herbert C. Cheung, M B Abbott, B DaGue, Richard M. Caprioli, Wen-Ji Dong, A Dvoretsky, Paul R. Rosevear
Publikováno v:
Biochemistry. 40:5992-6001
Multidimensional heteronuclear magnetic resonance studies of the cardiac troponin C/troponin I(1-80)/troponin I(129-166) complex demonstrated that cardiac troponin I(129-166), corresponding to the adjacent inhibitory and regulatory regions, interacts
Publikováno v:
Biochemistry. 39:15217-15224
We introduce a new simple methodology allowing the measurement of (1)H-(15)N residual dipolar couplings, dipolar shifts, and unpaired electron-amide proton distances. This method utilizes a zinc finger tag fused at either the N- or the C-terminus of