Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Jayant James Jayasundar"'
Publikováno v:
PLoS ONE, Vol 9, Iss 2, p e87135 (2014)
Cardiac troponin (cTn) is the Ca(2+)-sensitive molecular switch that controls cardiac muscle activation and relaxation. However, the molecular detail of the switching mechanism and how the Ca(2+) signal received at cardiac troponin C (cTnC) is commun
Externí odkaz:
https://doaj.org/article/c066a69b554b4ac9b5a5965bcaee941d
Publikováno v:
Journal of Molecular Biology. 400:1036-1045
Residue Ser151 of cardiac troponin I (cTnI) is known to be phosphorylated by p21-activated kinase 3 (PAK3). It has been found that PAK3-mediated phosphorylation of cTnI induces an increase in the sensitivity of myofilament to Ca(2+), but the detailed
Publikováno v:
Journal of Biological Chemistry. 284:16432-16441
Cardiac thin filament deactivation is initiated by Ca2+ dissociation from troponin C (cTnC), followed by multiple structural changes of thin filament proteins. These structural transitions are the molecular basis underlying the thin filament regulati
Dynamic Effects of Tropomyosin D230N Mutation and Fetal Troponin T on the Tropomyosin Overlap Region
Autor:
Mark T. McConnell, Jayant James Jayasundar, Jil C. Tardiff, Lauren Grinspan, Benjamin A. Schwartz, Ofer Fass
Publikováno v:
Biophysical Journal. 106(2)
Introduction: Mutations in the cardiac thin filament cause changes in protein structure and dynamics. These alterations result in the complex tissue remodeling seen in patients with hypertrophic and dilated cardiomyopathies. Our group is investigatin
Autor:
Mark T. McConnell, Benjamin J. Schwartz, Lauren Grinspan, Ofer Fass, Jayant James Jayasundar, Jil C. Tardiff
Publikováno v:
Biophysical Journal. 110:464a
Cardiac thin filament protein mutants cause changes in protein structure and dynamics. This results in the pathological tissue remodeling seen in patients with hypertrophic (HCM) and dilated (DCM) cardiomyopathies. We propose that two mutations, alph
Autor:
Flora Meilleur, Jeong Ho Ju, Dazhi Liu, David J.E. Callaway, Jinkui Zhao, Lilin He, Zimei Bu, Jayant James Jayasundar
Ezrin is a member of the ezrin-radixin-moesin family (ERM) of adapter proteins that are localized at the interface between the cell membrane and the cortical actin cytoskeleton, and they regulate a variety of cellular functions. The structure represe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77b82225b6d7244443a3b004030bb4c0
https://europepmc.org/articles/PMC3481312/
https://europepmc.org/articles/PMC3481312/
Publikováno v:
Biochemistry. 46(34)
Regulation of cardiac muscle function is initiated by binding of Ca2+ to troponin C (cTnC) which induces a series of structural changes in cTnC and other thin filament proteins. These structural changes are further modulated by crossbridge formation
Publikováno v:
PLoS ONE, Vol 9, Iss 2, p e87135 (2014)
PLoS ONE
PLoS ONE
Cardiac troponin (cTn) is the Ca(2+)-sensitive molecular switch that controls cardiac muscle activation and relaxation. However, the molecular detail of the switching mechanism and how the Ca(2+) signal received at cardiac troponin C (cTnC) is commun
Autor:
Kenneth Scott Brooks, Sarah J. Lehman, Jil C. Tardiff, Jayant James Jayasundar, Michael R. Williams
Publikováno v:
Biophysical Journal. 106:348a
Mutations in cardiac troponin T (cTnT) have been linked to hypertrophic cardiomyopathy (HCM). Previous experiments in our lab utilizing a novel cTnT R92L transgenic mouse model revealed an allosterically mediated decrease in the PKA phosphorylation p
Publikováno v:
Biophysical Journal. (3):6a
Cardiac troponin regulates the functioning of the heart. Ca2+binding to cTnC and PKA-phosphorylation of the unique N-extension (Nxt) of cTnI play critical roles in regulation. However details of the Ca2+ and PKA phosphorylation signal transduction is