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Takatoshi Arakawa

Researcher at University of Tokyo

Publications -  56
Citations -  1824

Takatoshi Arakawa is an academic researcher from University of Tokyo. The author has contributed to research in topics: Active site & Glycoside hydrolase. The author has an hindex of 18, co-authored 56 publications receiving 1467 citations. Previous affiliations of Takatoshi Arakawa include Kyoto University & Tokyo University of Agriculture and Technology.

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G-protein-coupled receptor inactivation by an allosteric inverse-agonist antibody

TL;DR: The raising of a mouse monoclonal antibody against human A2AAR that prevents agonist but not antagonist binding to the extracellular ligand-binding pocket is reported and results suggest a new strategy to modulate the activity of G-protein-coupled receptors.
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Crystal structure of the anion exchanger domain of human erythrocyte band 3

TL;DR: The crystal structure of the transmembrane anion exchanger domain of AE1 is reported, which includes 14 trans Membrane helices and provides a basis for understanding the effects of mutations that lead to red blood cell diseases and also gives insight into the mechanism of ion transport.
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Structure and mechanism of the mammalian fructose transporter GLUT5

TL;DR: It is shown that a single point mutation is enough to switch the substrate-binding preference of GLUT5 from fructose to glucose, and local asymmetric rearrangements of carboxy-terminal transmembrane bundle helices TM7 and TM10 underlie a ‘gated-pore’ transport mechanism in such monosaccharide transporters.
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Structures of the 5-HT2A receptor in complex with the antipsychotics risperidone and zotepin

TL;DR: The structures of human 5-HT2AR in complex with the second-generation antipsychotics risperidone and zotepine effectively stabilize the inactive conformation by forming direct contacts with the residues at the bottom of the ligand-binding pocket, the movements of which are important for receptor activation.
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Rho and Anillin-dependent Control of mDia2 Localization and Function in Cytokinesis

TL;DR: Diaphanous-related formin, mDia, is an actin nucleation/polymerization factor functioning downstream of the small GTPase Rho that is required for the localization and function of mDIA2 in cytokinesis.