Sentence examples for tnc i from inspiring English sources

A high number of c-fos capsaicin-induced immunoreactive cells in TNC I and II layers in pinealectomized rats was found.

In the TNC dataset, properties that were fully donated to TNC (i.e. acquisition cost = USD $0.00) accounted for over 645 thousand acres of habitat or 12% of the total area protected as fee simple.

We obtain a Kd in the nanomolar range for binding of F2 TnC to TnH 30−61) that reveals a somewhat tighter interaction compared to that observed for vertebrate skeletal TnC, i.e., 8 nM compared to 48 nM in the presence of Ca2+(28).

According to Kemper [32], the number of c-fos immunoreactive cells in TNC I/II is capsaicin dose-dependent and indicates a direct and specific relationship between c-fos expression and the capsaicin concentration used.

All three branches carry fibers that innervate the meninges and meningeal vasculature [33], which were demonstrated in the present study by the increased c-fos expression in all dorsoventral parts of the TNC I/II after the intracranial capsaicin administration.

In this study, we have found a great number of c-fos immunoreactive cells capsaicin induced in TNC I/II layers in pinealectomized rats, when compared with the control group, indicating that pineal gland may be potentially involved in the pathophysiology of neurovascular headaches.

Moreover, the levels of other sarcomeric proteins closely associated with cTnT, namely troponin C (TnC), troponin I (cTnI), tropomyosin, actin, and α myosin heavy chain (MHC) were unchanged in Tnnt2+/− mice.

Relative to wildtype hearts, no changes in levels of troponin C (TnC), troponin I (cTnI), actin, tropomyosin, or β-myosin heavy chain (MHC) were detected in Tnnt2+/− hearts by immunoblot (Figure 2D).

Each tropomyosin interacts with seven actin monomers and binds one troponin complex, consisting of one copy each of troponin C (TnC), troponin I (TnI) and troponin T (TnT).

The thin filament also includes the troponin complex which is composed of three different subunits, troponin C (TnC), troponin I (TnI) and the troponin T (TnT).

Therefore, the increased rate constant of the slow phase that we observed when cTn was incorporated into the myofibrils seems to be most likely due to a slight weakening of TnC-TnI interactions when the cTn complex is bound to actin in the myofibrils.