Results 1 to 10 of about 6,632,424 (253)
Anti–Cardiac Troponin Autoantibodies Are Specific to the Conformational Epitopes Formed by Cardiac Troponin I and Troponin T in the Ternary Troponin Complex [PDF]
Clinical Chemistry, 2016 Abstract BACKGROUND Autoantibodies to cardiac troponins (TnAAbs) could negatively affect cardiac troponin I (cTnI) measurements by TnAAbs-sensitive immunoassays. We investigated the epitope specificity of TnAAbs and its influence on cTnI immunodetection in patients with acute myocardial infarction ...
Alexandra V Vylegzhanina +7 more
semanticscholar +5 more sources
Calcium-dependent Changes in the Flexibility of the Regulatory Domain of Troponin C in the Troponin Complex [PDF]
Journal of Biological Chemistry, 2005 With the recent advances in structure determination of the troponin complex, it becomes even more important to understand the dynamics of its components and how they are affected by the presence or absence of Ca(2+). We used NMR techniques to study the backbone dynamics of skeletal troponin C (TnC) in the complex.
Tharin M. A. Blumenschein +4 more
semanticscholar +7 more sources
Molecular dynamics simulations of the cardiac troponin complex performed with FRET distances as restraints. [PDF]
PLoS ONE, 2014 Cardiac troponin (cTn) is the Ca(2+)-sensitive molecular switch that controls cardiac muscle activation and relaxation. However, the molecular detail of the switching mechanism and how the Ca(2+) signal received at cardiac troponin C (cTnC) is ...
Jayant James Jayasundar +4 more
doaj +2 more sources
Ca2+-induced PRE-NMR changes in the troponin complex reveal the possessive nature of the cardiac isoform for its regulatory switch. [PDF]
PLoS ONE, 2014 The interaction between myosin and actin in cardiac muscle, modulated by the calcium (Ca2+) sensor Troponin complex (Tn), is a complex process which is yet to be fully resolved at the molecular level. Our understanding of how the binding of Ca2+ triggers
Nicole M Cordina +7 more
doaj +2 more sources
Dynamics of a Troponin Chimera Reproduce the Effects of Calcium on the Troponin Complex [PDF]
Biophysical Journal, 2012 In striated muscle, contraction is regulated in a Ca2+-dependent manner by the three subunits of the troponin complex. Troponin I (TnI) inhibits actomyosin ATPase in the absence of calcium; Ca2+ binding to troponin C (TnC) causes conformational changes that alter the interaction between TnI and TnC, removing the inhibition. These conformational changes
Olivier Julien +5 more
openalex +3 more sources
Phosphorylation of the ‘37000 component’ of the troponin complex (troponin-T) [PDF]
Biochemical Journal, 1973 Most of the phosphorus present in the troponin complex, which on average contains 1 mol of P/80000g, is associated with the ‘37000 component’ (0.6mol of P/mol). The inhibitory protein and particularly the ‘37000 component’, but not the calcium-binding protein, were phosphorylated when incubated with phosphorylase b kinase and [γ-32P]ATP.
H. A. Cole, S. V. Perry
openaire +4 more sources
Order–Disorder Transitions in the Cardiac Troponin Complex [PDF]
Journal of Molecular Biology, 2016 The troponin complex is a molecular switch that ties shifting intracellular calcium concentration to association and dissociation of actin and myosin, effectively allowing excitation-contraction coupling in striated muscle. Although there is a long history of muscle biophysics and structural biology, many of the mechanistic details that enable troponin'
Lauren Ann Metskas, Elizabeth Rhoades
openaire +4 more sources
Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants. [PDF]
Journal of Biological Chemistry, 1994 Ca2+ regulation of vertebrate-striated muscle contraction is initiated by conformational changes in the Ca(2+)-binding protein troponin C (TnC) and subsequent changes in the interaction of TnC with the inhibitory protein TnI. We have constructed mutants of rabbit skeletal muscle TnC in which natural Cys-98 was replaced by Leu, and a single Cys residue ...
Tetsuo Kobayashi +3 more
openalex +3 more sources
NMR analysis of cardiac troponin C‐troponin I complexes: effects of phosphorylation [PDF]
FEBS 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 ...
Natosha L. Finley +10 more
openalex +4 more sources
Frontiers in Cardiovascular Medicine, 2021 Background: The measurement of cardiac troponin I (cTnI) is widely used in the diagnosis of acute myocardial infarction (AMI). Although existing cTnI detection methods measure total cTnI, the significance of undegraded full-size-cTnI levels is still not ...
Biao Huang +13 more
doaj +2 more sources