Results 31 to 40 of about 6,764,388 (368)

Proteins of the Troponin Complex

open access: yesLaboratory Medicine, 1992
The troponin complex is a group of three protein subunits located on the thin filament of the contractile apparatus. These three subunits—troponin T, troponin I, and troponin C—different in genetic and protein structure, act together to regulate muscle contraction.
H. Katus   +3 more
semanticscholar   +2 more sources

Protein kinase C phosphomimetics alter thin filament Ca2+ binding properties. [PDF]

open access: yesPLoS ONE, 2014
Adrenergic stimulation modulates cardiac function by altering the phosphorylation status of several cardiac proteins. The Troponin complex, which is the Ca(2+) sensor for cardiac contraction, is a hot spot for adrenergic phosphorylation. While the effect
Bin Liu   +3 more
doaj   +1 more source

Hypertrophic Cardiomyopathy Mutations of Troponin Reveal Details of Striated Muscle Regulation

open access: yesFrontiers in Physiology, 2022
Striated muscle contraction is inhibited by the actin associated proteins tropomyosin, troponin T, troponin I and troponin C. Binding of Ca2+ to troponin C relieves this inhibition by changing contacts among the regulatory components and ultimately ...
J. M. Chalovich, L. Zhu, D. Johnson
doaj   +1 more source

Small Molecule RPI-194 Stabilizes Activated Troponin to Increase the Calcium Sensitivity of Striated Muscle Contraction

open access: yesFrontiers in Physiology, 2022
Small molecule cardiac troponin activators could potentially enhance cardiac muscle contraction in the treatment of systolic heart failure. We designed a small molecule, RPI-194, to bind cardiac/slow skeletal muscle troponin (Cardiac muscle and slow ...
Zabed Mahmud   +13 more
doaj   +1 more source

NMR analysis of cardiac troponin C‐troponin I complexes: effects of phosphorylation [PDF]

open access: yesFEBS Letters, 1999
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 troponin I(1–80), cardiac troponin I(1–80)DD and cardiac troponin I(1–80)pp, phosphorylated by protein ...
Finley, Natosha   +10 more
openaire   +3 more sources

Monoclonal Antibodies as Probes to Study Ligand-Induced Conformations of Troponin Subunits

open access: yesFrontiers in Physiology, 2022
Striated muscle contraction and relaxation is regulated by Ca2+ at the myofilament level via conformational modulations of the troponin complex. To understand the structure–function relationship of troponin in normal muscle and in myopathies, it is ...
Monica Rasmussen   +2 more
doaj   +1 more source

Discovery of novel cardiac troponin activators using fluorescence polarization-based high throughput screening assays

open access: yesScientific Reports, 2023
The large unmet demand for new heart failure therapeutics is widely acknowledged. Over the last decades the contractile myofilaments themselves have emerged as an attractive target for the development of new therapeutics for both systolic and diastolic ...
Priyanka Parijat   +6 more
doaj   +1 more source

Association of Serum Osteoprotegerin Level With Myocardial Injury and Cardiovascular Calcification in Chronic Kidney Disease Patients

open access: yesFrontiers in Medicine, 2022
BackgroundChronic kidney disease has emerged as a significant independent risk factor for cardiovascular disease. Cardiovascular calcification is an active process involving a complex interaction of inducers and inhibitors.
Kamal M. Okasha   +17 more
doaj   +1 more source

The Solution Structure of a Cardiac Troponin C−Troponin I−Troponin T Complex Shows a Somewhat Compact Troponin C Interacting with an Extended Troponin I−Troponin T Component [PDF]

open access: yesBiochemistry, 2002
We have investigated the structure of the cTnC-cTnI-cTnT(198-298) calcium-saturated, ternary cardiac troponin complex by small-angle scattering with contrast variation. Shape restoration was also applied to the scattering information resulting from the deuterated cTnC subunit, the unlabeled cTnI-cTnT(198-298) subunits, and the entire complex.
William T, Heller   +4 more
openaire   +2 more sources

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