Joseph M. Chalovich

There are 10 included publications by Joseph M. Chalovich :

TitleDateViewsBrief Description
The Actin Binding Protein Fesselin is a Member of the Synaptopodin Family 2011 27634 Fesselin is a natively unfolded protein that is abundant in avian smooth muscle. Like many natively nfolded proteins fesselin has multiple binding partners including actin myosin calmodulin and ŽÂ±-actinin. Fesselin accelerates actin polymerization a...
Ca2+ and Ionic Strength Dependencies of S1-ADP Binding to Actin-Tropomyosin-Troponin: Regulatory Implications 2011 27634 Skeletal and cardiac muscle contraction are inhibited by the actin-associated complex of tropomyosin-troponin. Binding of Ca21 to troponin or binding of ATP-free myosin to actin reverses this inhibition. Ca21 and ATP-free myosin stabilize different t...
Calponin interaction with alpha-actinin-actin: evidence for a structural role for calponin. 2011 27634 The purpose of this study was to address the paradox of calponin localization with a-actinin and filamin two proteins with tandem calponin homology (CH) domains by determining the effect of these proteins on the binding of calponin to actin. The resu...
Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution 2011 27634 The myosin 2 family of molecular motors includes isoforms regulated n different ways. Vertebrate smooth-muscle myosin is activated by phosphorylation of the regulatory light chain whereas scallop striated adductor-muscle myosin is activated by direct...
The delta-14 Mutation of Human Cardiac Troponin T Enhances ATPase Activity and Alters the Cooperative Binding of S1-ADP to Regulated Actin 2011 27634 The complex of tropomyosin and troponin binds to actin and inhibits activation of myosin ATPase activity and force production of striated muscles at low free Ca2+ concentrations. Ca2+ stimulates ATP activity and at subsaturating actin concentrations ...
Fesselin a Synaptopodin-like Protein Stimulates Actin Nucleation and Polymerization 2011 27634 Fesselin is a proline-rich actin binding protein that has recently been isolated from smooth muscle [Leinweber B. D. Fredricksen R. S. Hoffman D. R. and Chalovich J. M. (1999) J. Muscle Res. Cell Motil. 20 539–545]. Fesselin is similar to synaptopo...
Franklinization: Early Therapeutic Use of Static Electricity 2012 27634 Laupus Library History Collections & the Department of Bioethics & Interdisciplinary Studies sponsor the History of Medicine Presentations as an educational service for the East Carolina University community. The Library hopes that the speakers and t...
A Long Helix from the Central Region of Smooth Muscle Caldesmon 2011 27634 The central region of smooth muscle caldesmon is predicted to form α-helices on the basis of its primary structure. We have isolated a fragment (CT54) that contains this region. The hydrodynamic roperties and the electron microscopic images suggest ...
Tropomyosin Dynamics in Cardiac Thin Filaments: A Multisite Förster Resonance Energy Transfer and Anisotropy Study 2011 27634 Cryoelectron microscopy studies have identified distinct locations of tropomyosin (Tm) within the Ca21-free Ca21-saturated and myosin-S1-saturated states of the thin filament. On the other hand steady-state Förster resonance energy transfer (FRET) s...
Troponin-tropomyosin: an allosteric switch or a steric blocker? 2011 27634 The interaction of myosin subfragment 1 (S1) with actin-tropomyosin-troponin (regulated actin) is highly nucleotide dependent. The binding of S1 or S1-ADP (but not S1-ATP nor N N - -phenylenedimaleimide-modified S1-ATP) to regulated actin activates A...