Results 321 to 330 of about 6,764,388 (368)

Biology of the troponin complex in cardiac myocytes

Progress in Cardiovascular Diseases, 2004
Troponin is the regulatory complex of the myofibrillar thin filament that plays a critical role in regulating excitation-contraction coupling in the heart. Troponin is composed of three distinct gene products: troponin C (cTnC), the 18-kD Ca(2+)-binding subunit; troponin I (cTnI), the approximately 23-kD inhibitory subunit that prevents contraction in ...
Michael S, Parmacek, R John, Solaro
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Calcium binding by the troponin complex, and the purification and properties of troponin A

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract The percentage of tropomyosin and troponin in rabbit psoas muscle was estimated to be 4.2% and 5.6% of the myofibrillar protein, respectively. This suggests that on the thin filament there are two molecules of tropomyosin per 390 A, and probably two molecules of the troponin complex.
D J, Hartshorne, H Y, Pyun
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The Troponin Complex: Discriminating the Signal from the Noise

The American Journal of Medicine, 2022
Patients presenting to the emergency department with consideration of an acute coronary syndrome (ACS) are risk-stratified with sensitive troponin assays. Among many patients who present with symptoms other than chest pain, they are admitted for observation if the troponin assay is above the upper reference limit of that specific assay. With the advent
Ion S. Jovin, Edward O. McFalls
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[Distribution of tryptophan groups in molecules of troponin T, troponin I-troponin T complex, and alpha-actinin].

Biofizika, 2001
The method of fluorescence quenching was used to experimentally determine the distribution of tryptophan residues in molecules of troponin T, troponin T-troponin I complexes, and alpha-actinin. Iodide and cesium ions, and acrylamide were used as quenchers.
A G, Gvritishvili, S O, Simonishvili, N I, Butkhuzi, K Sh, Kuridze, M Sh, Simonidze, E V, But, M M, Zaalishvili   +6 more
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Proximity relationships between residue 6 of troponin I and residues in troponin C: further evidence for extended conformation of troponin C in the troponin complex.

Biochemistry, 2000
Skeletal muscle troponin C (TnC) adopts an extended conformation when crystallized alone and a compact one when crystallized with an N-terminal troponin I (TnI) peptide, TnI(1-47) [Vassylyev et al. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 4847-4852]. The N-terminal region of TnI (residues 1-40) was suggested to play a functional role of facilitating ...
Y. Luo, J. Leszyk, B. Li, J. Gergely, T. Tao   +4 more
semanticscholar   +3 more sources

Binding of Troponin I and the Troponin I−Troponin C Complex to Actin−Tropomyosin. Dissociation by Myosin Subfragment 1

Biochemistry, 2000
Troponin I (TnI) is the component of the troponin complex, TnI, TnC, TnT, that is responsible for inhibition of actomyosin ATPase activity. Using the fluorescence of pyrene-labeled tropomyosin (Tm), we probed the interaction of TnI and TnIC with Tm on the reconstituted muscle thin filament.
X, Zhou, E P, Morris, S S, Lehrer
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MOLECULAR MECHANISMS OF TROPONIN COMPLEX AND TROPOMYOSIN INTERACTION

X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023: Cб. тез., 2023
Studies of the molecular mechanisms of muscle contraction are again becoming extremely relevant. The cornerstone of this kind of research is the establishment of a detailed mechanism of molecular rearrangements in the troponin-tropomyosin system underlying the regulation of muscle contraction in norm and pathology. The aim of this work was to establish
V.V. Nefedova, O.I. Kechko, A.M. Matyushenko, D.I. Levitsky   +3 more
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Fluorescence Energy Transfer Study of Troponin C-Melittin Complex

Journal of Biochemistry, 1995
Fluorescence energy transfer study of rabbit skeletal troponin C (TnC), which binds a donor, dansylaziridine, to Met-25 in helix A and an acceptor, 5-(iodoacetamido)eosin, to Cys-98 in helix E revealed (i) the donor-acceptor distance did not change upon Mg2+ and Ca2+ binding to TnC, (ii) melittin binding to Ca(2+)-free TnC induced a remarkable decrease
H, Sano, T, Iio
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Characterization of Cardiac Troponin Fragment Composition Reveals Potential for Differentiating Etiologies of Myocardial Injury.

Clinical Chemistry
BACKGROUND Increased cardiac troponin (cTn) concentrations occur in acute myocardial injury and chronic diseases. Characterization of cTn composition in the circulation may assist in differentiating etiologies of myocardial injury.
Ling Li, Yuqing Liu, I. Katrukha, Litao Zhang, Xin Shu, Ao Xu, Juan Yang, Yu Wu, Yisha Jing, Hui Wang, Tongxin Ni, K. Schulz, A. Bereznikova, A. Katrukha, F. Apple, Yi Zhang, Zhenlu Zhang   +16 more
semanticscholar   +1 more source

Physarum tropomyosin-troponin complex. Isolation and properties.

Journal of biochemistry, 1976
The relaxing protein (TM-TN complex) was isolated from plasmodia of Physarum. SDS-gel electrophoresis revealed that the relaxing protein consists of tropomyosin subunits with a molecular weight of 35,000 troponin subunits with molecular weights of 38,000 (T) and 24,000 (I) and several other components. No component corresponding to muscle troponinC (MW-
T, Kato, Y, Tonomura
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