Troponin is a molecular switch, directly regulating the Ca 2+-dependent activation of
myofilament in striated muscle contraction. Cardiac troponin is subject to covalent and …

Homeostasis of cardiac function requires significant adjustments in sarcomeric protein
phosphorylation. The existence of unique peptides in cardiac sarcomeres, which are …

Cardiac failure is one of the leading causes of mortality in developed countries. As life
expectancies of the populations of these countries grow, the number of patients suffering …

We present here the solution structure for the bisphosphorylated form of the cardiac N-
extension of troponin I (cTnI1-32), a region for which there are no previous high-resolution …

Controversy abounds in the cardiac muscle literature over the rate-limiting steps of cardiac
muscle contraction and relaxation. However, the idea of a single biochemical mechanism …

The cardiac isoform of troponin I (cTnI) has a unique 31-residue N-terminal region that binds
cardiac troponin C (cTnC) to increase the calcium sensitivity of the sarcomere. The …

Besides the core structure conserved in all troponin I isoforms, cardiac troponin I (cTnI) has
an N-terminal extension that contains phosphorylation sites for protein kinase A under β …

The cardiac-specific N-terminus of cardiac troponin I (cTnI) is known to modulate the activity
of troponin upon phosphorylation with protein kinase A (PKA) by decreasing its Ca2+ affinity …

The key events in regulating cardiac muscle contraction involve Ca 2+ binding to and
release from cTnC (troponin C) and structural changes in cTnC and other thin filament …

The first human cardiac troponin I (hcTnI) mutation in the N-terminal 32 residue region,
R21C (arginine residue number 21 mutated to cysteine), which has been linked to …