id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
work_gpvpq3f5hnenzlbmznoelkycsa	Brett A. Colson	Constitutive Phosphorylation of Cardiac Myosin Binding Protein-C Increases the Probability of Myosin Cross-bridge Interaction with Actin	2009.0	1	.pdf	application/pdf	1677	100	57	In a mouse line with the entire cardiac TnI gene deleted, a partial destruction of the slow TnT gene promoter produces a knockdown effect. The double transgenic mice exhibited decreased expression of slow TnT mRNA and protein in adult diaphragm muscle. As a consequence of slow TnT deficiency, the sTnT-KD diaphragm muscle contained a higher proportion of fast TnT, decreased slow TnI and binds the N-terminal domain of TnI independently of Ca2þ. TnH, and transmitted to the C-lobe of F1, resulting in a change in the interaction of the TnI inhibitory domain and actin. Decreased Fatigue Tolerance In Diaphragm Muscle Of Slow Troponin T Knockdown Mice Tracking of Qdot Conjugated Titin Antibodies in Single Myofibril Stretch Experiments Reveals Ig-domain Unfolding at Physiological Sarcomere Lengths Constitutive Phosphorylation of Cardiac Myosin Binding Protein-C Increases the Probability of Myosin Cross-bridge Interaction with Actin Obscurin Interacts with a Novel Isoform of Myosin Binding Protein C-Slow to Regulate the Assembly of Thick Filaments	./cache/work_gpvpq3f5hnenzlbmznoelkycsa.pdf	./txt/work_gpvpq3f5hnenzlbmznoelkycsa.txt