Results 31 to 40 of about 2,484 (223)
Cytoskeleton, Volume 81, Issue 12, Page 815-831, December 2024.Abstract Familial hypertrophic cardiomyopathy (HCM) affects .2% of the world's population and is inherited in an autosomal dominant manner. Mutations in cardiac α‐actin are the cause in 1%–5% of all observed cases. Here, we describe the recombinant production, purification, and characterization of the HCM‐linked cardiac α‐actin variants p.A21V and p ...
Johannes N. Greve +3 more
wiley +1 more source
Human Tonic and Phasic Smooth Muscle Myosin Isoforms Are Unresponsive to the Loop 1 Insert
International Scholarly Research Notices, Volume 2013, Issue 1, 2013., 2013 Smooth muscle myosin gene products include two isoforms, SMA and SMB, differing by a 7‐residue peptide in loop 1 (i7) at the myosin active site where ATP is hydrolyzed. Using chicken isoforms, previous work indicated that the i7 deletion in SMA prolongs strong actin binding by inhibiting active site ingress and egress of nucleotide when compared to i7 ...
Katalin Ajtai +6 more
wiley +1 more source
Induction of Myocarditis and Valvuluitis in Lewis Rats by Different Epitopes of Cardiac Myosin and its Implications in Rheumatic Carditis [PDF]
, 2002 Immune responses against cardiac myosin and group A streptococcal M protein have been implicated in the pathogenesis of rheumatic heart disease.
Cunningham, Madeleine W. +5 more
core
Small, Volume 20, Issue 51, December 19, 2024.Inherent sensitivity toward external load forms a basis for the myosin motors physiological adaptation. Here, this study shows that the mechanical performance of cardiac and slow skeletal myosin II is determined by the lifetime of force‐producing actin bound myosin states. Load modulates the bound duration, and the steady‐state abundance of actin‐bound
Tianbang Wang +3 more
wiley +1 more source
BioMed Research International, Volume 2012, Issue 1, 2012., 2012 Microfabricated thermoelectric controllers can be employed to investigate mechanisms underlying myosin‐driven sliding of Ca2+‐regulated actin and disease‐associated mutations in myofilament proteins. Specifically, we examined actin filament sliding—with or without human cardiac troponin (Tn) and α‐tropomyosin (Tm)—propelled by rabbit skeletal heavy ...
Nicolas M. Brunet +7 more
wiley +1 more source
The 66 k-Da protein identified as a light meromyosin is involved in the setting of surimi [PDF]
, 1997 The 66 kilo-Dalton (k-Da) protein split off from the cross linked myosin heavy chain (CMHC) formed due to the setting of Alaska pollack surimi, frozen-storage of Pacific cod flesh, and vinegar-curing of Pacific mackerel mince was identified as a light ...
Niwa, E., Nowsad Alam, A.K.M.
core
Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1. [PDF]
, 2006 SSE1 and SSE2 encode the essential yeast members of the Hsp70-related Hsp110 molecular chaperone family. Both mammalian Hsp110 and the Sse proteins functionally interact with cognate cytosolic Hsp70s as nucleotide exchange factors.
Morano, Kevin A +2 more
core +1 more source
Betaine protects urea‐induced denaturation of myosin subfragment‐1 [PDF]
The FEBS Journal, 2008 We have demonstrated previously that urea inhibits the activity and alters the tertiary structure of skeletal muscle myosin in a biphasic manner. This was attributed to differential effects on its globular and filamentous portion. The inhibition of catalytic activity was counteracted by methylamines. With the aim of comprehending the effects of urea on
Susana, Ortiz-Costa +2 more
openaire +2 more sources
Mechanochemical consequences of myopathy‐linked mutations in Tpm2.2 on striated muscle contractility
The FASEB Journal, Volume 38, Issue 1, 15 January 2024.Myopathy‐linked mutations in Tpm2.2, an isoform of striated muscle tropomyosin, can lead to hypercontractile or hypocontractile molecular phenotypes. Depending on the localization of the mutations in Tpm2.2 sequence, they have different impacts on the association of Tpm2.2 with actin and the regulation of the actin–myosin cross‐bridge cycle.
Recep Küçükdogru +6 more
wiley +1 more source
Myosin Binding Protein‐C: A Regulator of Actomyosin Interaction in Striated Muscle
BioMed Research International, Volume 2011, Issue 1, 2011., 2011 Myosin‐Binding protein‐C (MyBP‐C) is a family of accessory proteins of striated muscles that contributes to the assembly and stabilization of thick filaments, and regulates the formation of actomyosin cross‐bridges, via direct interactions with both thick myosin and thin actin filaments.
Maegen A. Ackermann +2 more
wiley +1 more source