R
Ronald A. Milligan
Researcher at Scripps Research Institute
Publications - 118
Citations - 18633
Ronald A. Milligan is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Microtubule & Kinesin. The author has an hindex of 59, co-authored 118 publications receiving 17651 citations. Previous affiliations of Ronald A. Milligan include University of California, San Francisco & University of Washington.
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Journal ArticleDOI
Structure of the actin-myosin complex and its implications for muscle contraction.
Ivan Rayment,Hazel M. Holden,Michael Whittaker,Christopher B. Yohn,Michael Lorenz,Kenneth C. Holmes,Ronald A. Milligan +6 more
TL;DR: The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.
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Self-assembling organic nanotubes based on a cyclic peptide architecture
TL;DR: The design, synthesis and characterization of a new class of organic nanotubes based on rationally designed cyclic polypeptides are reported, which may have possible applications in inclusion chemistry, catalysis, molecular electronics and molecular separation technology.
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The Way Things Move: Looking Under the Hood of Molecular Motor Proteins
TL;DR: The microtubule-based kinesin motors and actin-based myosin motors generate motions associated with intracellular trafficking, cell division, and muscle contraction using a common core structure and convert energy from adenosine triphosphate into protein motion using a similar conformational change strategy.
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High-resolution model of the microtubule.
TL;DR: A high-resolution model of the microtubule has been obtained by docking the crystal structure of tubulin into a 20 A map of themicrotubule, and the excellent fit indicates the similarity of the tubulin conformation in both polymers and defines the orientation of the Tubulin structure within the micro Tubule.
Journal ArticleDOI
A structural change in the kinesin motor protein that drives motility
Sarah E. Rice,Abel W. Lin,Daniel Safer,Cynthia L. Hart,Nariman Naber,Bridget Carragher,Shane M. Cain,Elena Pechatnikova,Elizabeth M. Wilson-Kubalek,Michael Whittaker,Edward Pate,Roger Cooke,Edwin W. Taylor,Ronald A. Milligan,Ronald D. Vale +14 more
TL;DR: A large conformational change of a ∼15-amino-acid region (the neck linker) in kinesin is detected and visualized using electron paramagnetic resonance, fluorescence resonance energy transfer, pre-steady state kinetics and cryo-electron microscopy.