1997 - Fellow of the American Academy of Arts and Sciences
1991 - Member of the National Academy of Sciences
James A. Spudich focuses on Myosin, Actin, Cell biology, Biochemistry and Biophysics. His Myosin study integrates concerns from other disciplines, such as Dictyostelium discoideum and Dictyostelium. His research integrates issues of Microtubule, Molecular motor, Protein filament and Microfilament in his study of Actin.
His Cell biology research incorporates themes from Chemotaxis, Cell movement, Cytokinesis and Cytoskeleton. In general Biochemistry, his work in Heavy meromyosin, Binding site, Enzyme and Heavy chain is often linked to Lever linking many areas of study. His biological study spans a wide range of topics, including Molecular Motor Proteins, Kinesin, Crystallography, Protein structure and Kinetics.
Myosin, Actin, Cell biology, Biochemistry and Biophysics are his primary areas of study. The various areas that he examines in his Myosin study include Hypertrophic cardiomyopathy, Molecular motor and Dictyostelium. His research investigates the link between Actin and topics such as Microfilament that cross with problems in Arp2/3 complex and Actin remodeling.
Mitosis is closely connected to Cytokinesis in his research, which is encompassed under the umbrella topic of Cell biology. His Skeletal muscle research extends to the thematically linked field of Biochemistry. Many of his research projects under Biophysics are closely connected to Processivity with Processivity, tying the diverse disciplines of science together.
His primary areas of study are Myosin, Actin, Cell biology, Hypertrophic cardiomyopathy and Biophysics. His Myosin research is multidisciplinary, relying on both Cardiomyopathy, Molecular motor and Sarcomere. His study on Actin is covered under Biochemistry.
His study looks at the relationship between Cell biology and fields such as Enzyme, as well as how they intersect with chemical problems. His Biophysics research focuses on Muscle contraction and how it relates to Inhibitory postsynaptic potential. His work in Myosin head addresses subjects such as Microfilament, which are connected to disciplines such as Mitosis and Cytokinesis.
James A. Spudich mainly investigates Myosin, Cell biology, Actin, Myosin head and Hypertrophic cardiomyopathy. Part of his project on Myosin includes research on Biophysics and Biochemistry. His research in Biochemistry intersects with topics in Förster resonance energy transfer and Skeletal muscle.
His research integrates issues of SUPERFAMILY, Microfilament Protein and Contractility in his study of Cell biology. James A. Spudich combines subjects such as Smooth muscle contraction, Methylation, ATP hydrolysis, Mutant and Cytoskeleton with his study of Actin. The study incorporates disciplines such as Myosin ATPase and Microfilament in addition to Myosin head.
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The Regulation of Rabbit Skeletal Muscle Contraction I. BIOCHEMICAL STUDIES OF THE INTERACTION OF THE TROPOMYOSIN-TROPONIN COMPLEX WITH ACTIN AND THE PROTEOLYTIC FRAGMENTS OF MYOSIN
James A. Spudich;Susan Watt.
Journal of Biological Chemistry (1971)
Single myosin molecule mechanics: piconewton forces and nanometre steps
Jeffrey T. Finer;Robert M. Simmons;James A. Spudich.
Purification of muscle actin.
Joel D. Pardee;James A. Spudich.
Methods in Enzymology (1982)
Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination
A De Lozanne;JA Spudich.
Fluorescent actin filaments move on myosin fixed to a glass surface
Stephen J. Kron;James A. Spudich.
Proceedings of the National Academy of Sciences of the United States of America (1986)
Myosin-V is a processive actin-based motor
Amit D. Mehta;Ronald S. Rock;Matthias Rief;James A. Spudich.
Single-molecule biomechanics with optical methods.
Amit D. Mehta;Matthias Rief;James A. Spudich;David A. Smith.
Optimized localization analysis for single-molecule tracking and super-resolution microscopy.
Kim I Mortensen;L Stirling Churchman;James A Spudich;Henrik Flyvbjerg.
Nature Methods (2010)
Quantitative measurements of force and displacement using an optical trap.
Robert M. Simmons;Jeffrey T. Finer;Steven Chu;James A. Spudich.
Biophysical Journal (1996)
Myosin subfragment-1 is sufficient to move actin filaments in vitro.
Yoko Yano Toyoshima;Stephen J. Kron;Elizabeth M. McNally;Kenneth R. Niebling.
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