| The Actin Binding Protein Fesselin is a Member of the Synaptopodin Family |
2011 |
688479 |
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 |
688479 |
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 |
688479 |
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 |
688479 |
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 |
688479 |
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 |
688479 |
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 |
688479 |
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 |
688479 |
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 |
688479 |
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 |
688479 |
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... |