 Chris Berger
The primary goal of my research program is to understand how key structural components of the motor protein myosin function to produce force and motion during muscle contraction. To directly address these important and unresolved questions, conformational changes within smooth muscle myosin are examined at critical steps of the contractile cycle using intrinsic and extrinsic fluorescent probes.
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 Joe Haeberle
My laboratory is interested in the regulation of smooth muscle contraction and nonmuscle motility. Earlier studies centered on the role of the phosphorylatable regulatory light chain subunit of myosin in the activation of contraction. More recently, our focus has shifted to the actin thin filament and the associated regulatory proteins including tropomyosin, caldesmon, calponin and calmodulin. The goal is to not only determine how thin filament proteins control contraction, but also to determine how thin filament linked regulation is coordinated with myosin phosphorylation to govern the overall contractile properties of cells.
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 Bob Low
My more recent research has involved regulation of the smooth muscle myosin heavy chain gene. This single gene codes for at least four heavy chain isoforms, the expression of which is considered to indicate the most advanced degrees of smooth muscle differentiation. Identification of the promoter regulatory elements responsible for the expression of this gene and the factors responsible for determining the differential splicing necessary to allow the subsequent expression of each isoform are the central goals of this research.
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 Susan Lowey
My laboratory studies the role of myosin in muscle contraction. Many aspects of the interaction between myosin and actin have been elaborated since the sliding filament theory of contraction was originally proposed in the 1950's, but a detailed mechanism of how ATP hydrolysis is coupled to force generation is still not available. Current structural models have focused on conformational changes occurring at the interface between the catalytic domain and the light chain-binding domain in myosin.
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 David Maughan
We are interested in the molecular basis of muscle contraction. Using recombinant DNA technology and advanced engineering techniques, my colleagues and I examine the relationship between the structure and function of muscle proteins. We study insect flight muscle and mouse cardiac muscle as well as human cardiac muscle obtained from patients with normal or failing hearts. Our long-range goal is to apply our knowledge of muscle function to the diagnosis and treatment of muscle disease.
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 Lou Mulieri
My research is directed at bridging the gap between clinically measured parameters of normal and abnormal left ventricular function and their corresponding, in vitro parameters at the tissue and cellular level. The object is to identify the key cellular and subcellular processes that bear a causal relation to clinically abnormal parameters (e.g. one success has been the discovery that the force-frequency relation in the isolated myocardial strip preparation which is removed from all acute cardiovascular systemic neurological and hormonal inputs, mirrors the heart rate-dependence of in vivo left ventricular function in both non-failing and failing human hearts).
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 Joe Patlak
I have been active in the field of single molecule measurement and kinetic analysis since 1977. Originally my emphasis was the study of single ion channels in muscle membrane. During the past two decades my work focused on developing single channel measurements of Na+ channel conductance and kinetic properties, primarily in skeletal muscle.
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 Mark Rould
One of Dr. Rould's primary convictions is to make x-ray crystallography more accessible to a wider biological community, to allow biochemists and biologists to add high resolution structural characterization to their repertoire of techniques available for the study of macromolecules and their interactions.
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 Art Rovner
My two major interest areas both involve understanding how structural variation in the smooth muscle myosin molecule impacts upon its function, and thus upon smooth muscle contraction. Much of my experimentation is based upon the ability to express homogeneous preparations of mutated or naturally-occurring recombinant myosin or actin molecules in the baculovirus system.
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 Kathy Trybus
A major aim of my research program is to understand how molecular motors work: how the activity of various myosins is regulated, as well as how they move actin and produce force. One motor we have particularly focused on is smooth muscle myosin, which has several unique features: its activity is regulated by light chain phosphorylation, it moves actin at a slower rate than does skeletal muscle myosin, and it has several isoforms that modulate contractile activity.
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 Peter VanBuren
Myosin cross-bridges projecting from the thick filament interact with the actin-containing thin filament in a cyclical fashion to give rise to muscle contraction. The interaction of myosin with actin is modulated by the actin-associated regulatory proteins, troponin (Tn) and tropomyosin (Tm). In relaxed muscle, these regulatory proteins block myosin binding to actin. Muscle is activated through the binding of calcium to Tn, which ultimately results in a shift of the Tm molecule on the actin filament. With this Tm shift, the myosin binding site on actin is exposed, allowing actin and myosin to interact.
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 David Warshaw
The Warshaw Molecular Motors Group focuses on the structure and function of the contractile proteins associated with muscle contraction. Specifically, how the myosin molecular motor interacts with actin to convert the energy from ATP hydrolysis into mechanical work. We take a comparative approach by using the various muscle types in both normal and disease states as model systems for providing myosin motors that differ substantially in both their structure and functional capacities.
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