P
Paul Matsudaira
Researcher at National University of Singapore
Publications - 230
Citations - 21743
Paul Matsudaira is an academic researcher from National University of Singapore. The author has contributed to research in topics: Actin & Villin. The author has an hindex of 68, co-authored 229 publications receiving 21008 citations. Previous affiliations of Paul Matsudaira include Singapore–MIT alliance & Brigham and Women's Hospital.
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Journal ArticleDOI
Three-dimensional network photonic crystals via cyclic size reduction/ infiltration of sea urchin exoskeleton
Yung-Hoon Ha,Richard A. Vaia,William F. Lynn,Joseph P. Costantino,Jennifer Hyunjong Shin,Andrew B. Smith,Paul Matsudaira,Edwin L. Thomas +7 more
TL;DR: In this article, a cyclic, sizereduction and infiltration scheme was applied to a sea urchin exoskeleton to fabricate a high-dielectric contrast, 3D photonic crystal exhibiting a stop band in the mid-IR range.
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Fimbrin localized to an insoluble cytoskeletal fraction is constitutively phosphorylated on its headpiece domain in adherent macrophages.
TL;DR: Limited trypsin digestion and phosphoamino acid analysis demonstrated that phosphorylation occurs specifically on serine residues within the 10kD headpiece domain of fimbrin, which could regulate the actin binding and bundling properties of fImbrin or regulate the interaction of fIMbrin with other proteins.
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Total serum protein N-glycome profiling on a capillary electrophoresis-microfluidics platform.
Nico Callewaert,Roland Contreras,Luba Mitnik-Gankin,Loucinda Carey,Paul Matsudaira,Daniel J. Ehrlich +5 more
TL;DR: 8‐aminopyrene‐1,3,6‐trisulfonic acid‐labeled asparagine‐linked glycan (N‐glycan) profiling on a microfluidic electrophoresis platform suggests a practical clinical application for high‐speed compact analyzers which might be uniquely based on microfluidity devices.
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Effect of deuteration on the amide proton relaxation rates in proteins. Heteronuclear NMR experiments on villin 14T.
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A gelsolin-like Ca2+-dependent actin-binding domain in villin.
TL;DR: The purification and preliminary characterization of a 44,000-Mr fragment of villin reveals homology with a 16-residue region near the amino terminus6 of gelsolin, an actin-severing protein found in many cells7–9 and sera10–12, which suggests a common structural basis for the calcium-regulated actin