Kinetics of Conformational Transitions in Cardiac Troponin Induced by Ca2+ Dissociation Determined by Förster Resonance Energy Transfer
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference24 articles.
1. Structures of the troponin C regulatory domains in the apo and calcium-saturated states
2. Calcium binding to the regulatory domain of skeletal muscle troponin C induces a highly constrained open conformation
3. Binding of Cardiac Troponin-I147-163 Induces a Structural Opening in Human Cardiac Troponin-C,
4. Interaction of the Second Binding Region of Troponin I with the Regulatory Domain of Skeletal Muscle Troponin C as Determined by NMR Spectroscopy
5. Troponin I Inhibitory Peptide (96−115) Has an Extended Conformation When Bound to Skeletal Muscle Troponin C
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1. Molecular dynamics provides new insights into the mechanism of calcium signal transduction and interdomain interactions in cardiac troponin;FEBS Open Bio;2021-06-09
2. The concerted movement of the switch region of Troponin I in cardiac muscle thin filaments as tracked by conventional and pulsed (DEER) EPR;Journal of Structural Biology;2017-12
3. Fluorescence Based Characterization of Calcium Sensitizer Action on the Troponin Complex;Chemical Biology & Drug Design;2015-09-16
4. Ca2+-Induced PRE-NMR Changes in the Troponin Complex Reveal the Possessive Nature of the Cardiac Isoform for Its Regulatory Switch;PLoS ONE;2014-11-13
5. In Situ Time-Resolved FRET Reveals Effects of Sarcomere Length on Cardiac Thin-Filament Activation;Biophysical Journal;2014-08
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