The Relaxation Properties of Myofibrils Are Compromised by Amino Acids that Stabilize α-Tropomyosin.
Scellini, Beatrice; Piroddi, Nicoletta; Matyushenko, Alexander M; Levitsky, Dmitrii I; Poggesi, Corrado; Lehrer, Sherwin S; Tesi, Chiara.
; 112(2): 376-387, 2017 Jan 24.
Artigo em Inglês | MEDLINE | ID: mdl-28122223
Myopathic mutations in the ß-chain of tropomyosin differently affect the structural and functional properties of ßß- and αß-dimers.
Polymorphism in tropomyosin structure and function.
Morphological Modifications in Myofibrils by Suppressing Tropomyosin 4α in Chicken Cardiac Myocytes.
Structural and functional properties of αß-heterodimers of tropomyosin with myopathic mutations Q147P and K49del in the ß-chain.
Transmission of stability information through the N-domain of tropomyosin is interrupted by a stabilizing mutation (A109L) in the hydrophobic core of the stability control region (residues 97-118).
Precise Binding of Tropomyosin on Actin Involves Sequence-Dependent Variance in Coiled-Coil Twisting.
Important announcement: a rational nomenclature for tropomyosin variants.
Hypertrophic cardiomyopathy mutations increase myofilament Ca<sup>2+</sup> buffering, alter intracellular Ca<sup>2+</sup> handling, and stimulate Ca<sup>2+</sup>-dependent signaling.
Structure of the rigor actin-tropomyosin-myosin complex.
Myofilament lattice structure in presence of a skeletal myopathy-related tropomyosin mutation.