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    Chalovich, Joseph (20)
    Chen, Yi-Der (3)Beall, Brent (2)Brenner, Bernhard (2)Gafurov, Boris (2)Kobayashi, Tomoyoshi (2)Marriott, Gerard (2)Mathur, Mohit C. (2)Schroeter, Mechthild M. (2)Stafford, Walter F. (2)... View MoreSubjectActin (5)Caldesmon (4)Tropomyosin (3)Actin binding (2)Actin polymerization (2)Fesselin (2)S1-ADP (2)Smooth muscle (2)Troponin (2)Actin binding protein (1)... View MoreDate Issued2020 - 2021 (1)2010 - 2019 (1)2000 - 2009 (10)1991 - 1999 (8)Has File(s)true (20)

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    Kinetics of Binding of Caldesmon to Actin 

    Chalovich, Joseph; Chen, Yi-Der; Dudek, Ronald W.; Hai, Luo (East Carolina University, 1995-04-28)
    The time course of interaction of caldesmon with actin may be monitored by fluorescence changes that occur upon the binding of 12-(N-methyl-N-(7-nitrobenz-2-oxa-l,3-diazol-4-yl))-labeled caldesmon to actin or to acrylodan ...
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    Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution 

    Jung, Hyun Suk; Burgess, Stan A.; Billington, Neil; Colegrave, Melanie; Patel, Hitesh; Chalovich, Joseph; Chantler, Peter D.; Knight, Peter J. (East Carolina University, 2008-04-22)
    The myosin 2 family of molecular motors includes isoforms regulated in different ways. Vertebrate smooth-muscle myosin is activated by phosphorylation of the regulatory light chain, whereas scallop striated adductor-muscle ...
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    Troponin-tropomyosin: an allosteric switch or a steric blocker? 

    Resetar, Andrea M.; Stephens, Jacqueline M.; Chalovich, Joseph (East Carolina University, 2002-08)
    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) ...
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    A Long Helix from the Central Region of Smooth Muscle Caldesmon 

    Wang, C.-L. Albert; Chalovich, Joseph; Graceffa, Philip; Lu, Renne C.; Mabuchi, Katsuhide; Stafford, Walter F. (East Carolina University, 1991-07-25)
    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 properties and the electron ...
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    Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin. 

    Velaz, Laly; Chen, Yi-Der; Chalovich, Joseph (East Carolina University, 1993-08)
    The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of myosin*ATP to actin. Afragment isolated from a chymotryptic digest of caldesmon contains features of the intact molecule ...
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    Inhibition of contraction and myosin light chain phosphorylation in guinea-pig smooth muscle by p21-activated kinase 1 

    Wirth, A.; Schroeter, M.; Kock-Hauser, C.; Manser, E.; Chalovich, Joseph; de Lanerolle, P.; Pfitzer, G. (East Carolina University, 2003-06-01)
    The p21-activated protein kinases (PAKs) have been implicated in cytoskeletal rearrangements and modulation of non-muscle contractility. Little, however, is known about the role of the PAK family members in smooth muscle ...
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    The delta-14 Mutation of Human Cardiac Troponin T Enhances ATPase Activity and Alters the Cooperative Binding of S1-ADP to Regulated Actin 

    Gafurov, Boris; Fredricksen, Scott; Cai, Anmei; Brenner, Bernhard; Chase, P. Bryant; Chalovich, Joseph (East Carolina University, 2004-12-07)
    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 ...
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    Equilibration and Exchange of Fluorescently Labeled Molecules in Skeletal Muscle Fibers Studied Using Confocal Microscopy 

    Kraft, T.; Messerli, M.; Rutishauser, B.; Wallimann, T.; Perriard, J.-C.; Chalovich, Joseph; Brenner, Bernhard (East Carolina University, 1995-04)
    Diffusion of molecules into skinned muscle fibers is often necessary when studying muscle contraction and its regulation. Usually, it is assumed that diffusion of molecules is fast also in the structured system of a muscle ...
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    The Interaction of Caldesmon with the COOH Terminus of Actin 

    Crosbie, Rachelle; Adams, Susan; Chalovich, Joseph; Reisler, Emil (East Carolina University, 1991-10-25)
    Caldesmon interacts with the NH2-terminal region of actin. It is now shown in airfuge centrifugation experiments that modification of the penultimate cysteine residue of actin significantly weakens its binding to caldesmon ...
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    Negative Charges at Protein Kinase C Sites of Troponin I Stabilize the Inactive State of Actin 

    Mathur, Mohit C.; Kobayashi, Tomoyoshi; Chalovich, Joseph (East Carolina University, 2008-01-15)
    Alterations in the troponin complex can lead to increases or decreases in contractile activity. Most mutations of troponin that cause hypertrophic cardiomyopathy increase the activity of cardiac muscle fibers. In at least ...
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