نتایج جستجو برای: cardiac myosin

تعداد نتایج: 295185  

Journal: :The Journal of clinical investigation 1996
C L Pummerer K Luze G Grässl K Bachmaier F Offner S K Burrell D M Lenz T J Zamborelli J M Penninger N Neu

Immunization with cardiac myosin induces T cell-mediated myocarditis in genetically predisposed mice and serves as a model for autoimmune heart disease. This study was undertaken to identify pathogenic epitopes on the myosin molecule. Our approach was based on the comparison of the pathogenicity between cardiac (alpha-)myosin and soleus muscle (beta-)myosin. We show that alpha-myosin is the imm...

Journal: :The Journal of experimental biology 2016
James A Spudich Tural Aksel Sadie R Bartholomew Suman Nag Masataka Kawana Elizabeth Choe Yu Saswata S Sarkar Jongmin Sung Ruth F Sommese Shirley Sutton Carol Cho Arjun S Adhikari Rebecca Taylor Chao Liu Darshan Trivedi Kathleen M Ruppel

Hypertrophic cardiomyopathy is the most frequently occurring inherited cardiovascular disease, with a prevalence of more than one in 500 individuals worldwide. Genetically acquired dilated cardiomyopathy is a related disease that is less prevalent. Both are caused by mutations in the genes encoding the fundamental force-generating protein machinery of the cardiac muscle sarcomere, including hum...

Journal: :Annals of the rheumatic diseases 1995
F J Tinahones F J Soriguer E Collantes G Pérez-Lindón P Sánchez Guijo J A Lillo

1 Khaw B A, Gold H K, Fallon J T, Haber E. Detection of serum cardiac myosin light chains in acute experimental myocardial infarction: radioimmunoassay of cardiac myosin light chains. Circulation 1978; 58: 1130-6. 2 Trahern C A, Gere J B, Krauth G H, Bigham D A. Clinical assessment of serum myosin light chains in the diagnosis of acute myocardial infarction. AmJCardiol 1978; 41: 641-5. 3 Katus ...

Journal: :The Journal of Cell Biology 1987
C A Dechesne P Bouvagnet D Walzthöny J J Léger

Two mAbs, one specific for cardiac alpha-myosin heavy chains (MHC) and the other specific for cardiac beta-MHC, were used to investigate the heavy-chain dimeric organization of rat cardiac ventricular myosin. Epitopes of the two mAbs were mapped on the myosin molecule by electron microscopy of rotary shadowed mAb-myosin complexes. mAbs were clearly identifiable by the different locations of the...

Journal: :Circulation research 2015
Richard L Moss Daniel P Fitzsimons J Carter Ralphe

Cardiac myosin-binding protein-C (cMyBP-C) is a thick filament-associated protein that seems to contribute to the regulation of cardiac contraction through interactions with either myosin or actin or both. Several studies over the past several years have suggested that the interactions of cardiac myosin-binding protein-C with its binding partners vary with its phosphorylation state, binding pre...

2013
Ruth F. Sommese Suman Nag Shirley Sutton Susan M. Miller James A. Spudich Kathleen M. Ruppel

Hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy (DCM) lead to significant cardiovascular morbidity and mortality worldwide. Mutations in the genes encoding the sarcomere, the force-generating unit in the cardiomyocyte, cause familial forms of both HCM and DCM. This study examines two HCM-causing (I79N, E163K) and two DCM-causing (R141W, R173W) mutations in the troponin T subunit of...

Journal: :JACC: Basic to Translational Science 2017

Journal: :The Journal of Cell Biology 1991
E M McNally M M Bravo-Zehnder L A Leinwand

To begin to understand the nature of myosin subunit assembly, we determined the region of a vertebrate sarcomeric myosin heavy chain required for binding of light chain 1. We coexpressed in Escherichia coli segments of the rat alpha cardiac myosin heavy chain which spanned the carboxyl terminus of subfragment 1 and the amino terminus of subfragment 2 with a full-length rat cardiac myosin light ...

Journal: :Circulation research 1982
C Klotz J J Leger M Elzinga

Myosin light chains from normal and hypertrophied human hearts were partially sequenced in order to see whether structural modifications of these light subunits could provide a molecular basis for the changes observed in heart properties and in myosin enzymatic activity. Normal light chains were prepared form hearts taken at autopsy, weighing 350 g or less and apparently devoid of myocardial di...

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