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Robert Robinson

Researcher at Okayama University

Publications -  552
Citations -  10609

Robert Robinson is an academic researcher from Okayama University. The author has contributed to research in topics: Brucine & Actin. The author has an hindex of 44, co-authored 552 publications receiving 9683 citations. Previous affiliations of Robert Robinson include Uppsala University & Salk Institute for Biological Studies.

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Crystal Structure of Arp2/3 Complex

TL;DR: A crystal structure of bovine Arp2/3 complex, an assembly of seven proteins that initiates actin polymerization in eukaryotic cells, is determined at 2.0 angstrom resolution and it is predicted that WASp/Scar proteins activate Arp 2-3 complex by bringing Arp1 into proximity with Arp3 for nucleation of a branch on the side of a preexisting actin filament.
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A survey of anthocyanins. I.

TL;DR: The anthocyanins have been identified in the flowers, fruits or leaves of approximately 200 species of plants as mentioned in this paper, and the results have been combined with earlier data, to ascertain the frequency with which derivatives of the three main Anthocyanidin types occur as flower pigments among the species so far examined.
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The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation.

TL;DR: It is proposed that binding Ca2+ can release the connections that join the N- and C-terminal halves of gelsolin, enabling each half to bind actin relatively independently.
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Crystal structure of the N-terminal domain of sialoadhesin in complex with 3' sialyllactose at 1.85 A resolution.

TL;DR: The structure of the functional N-terminal domain from the extracellular region of the cell surface receptor sialoadhesin has been determined in complex with the oligosaccharide 3' sialyllactose and provides structural information for the siglec family of proteins.
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The evolution of compositionally and functionally distinct actin filaments

TL;DR: It is proposed that different mechanisms were selected in bacteria, plants and metazoa, which achieved actin filament compositional variation leading to the expansion of their functional diversity.