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Shigeru Endo

Researcher at Kitasato University

Publications -  27
Citations -  440

Shigeru Endo is an academic researcher from Kitasato University. The author has contributed to research in topics: Crystal & Protein structure. The author has an hindex of 11, co-authored 27 publications receiving 384 citations.

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New tools and functions in data‐out activities at Protein Data Bank Japan (PDBj)

TL;DR: The new RDB PDBj Mine 2, the WebGL molecular viewer Molmil, the ProMode‐Elastic server for normal mode analysis, a virtual reality system for the eF‐site protein electrostatic molecular surfaces, the extensions of the Omokage search for molecular shape similarity, and the integration of PDBJ and BMRB searches are reported.
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ProMode: a database of normal mode analyses on protein molecules with a full-atom model

TL;DR: ProMode, a database collecting NMA results on protein molecules, was constructed and it is hoped that realistic animations of the protein dynamics can be observed easily without expensive software and hardware, and that the dynamic properties for various proteins can be compared with each other.
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Normal mode analysis as a method to derive protein dynamics information from the Protein Data Bank

TL;DR: An elastic network model-based NMA program using dihedral angles as independent variables is developed, focusing on the conformational change upon cAMP and DNA binding, and on the communication between their binding sites remotely located from each other.
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Fabrication and Control of Two-Dimensional Crystalline Arrays of Protein Molecules.

TL;DR: In this paper, a spreading wetting process is used to produce 2D arrays of protein particles. But the key innovation in this fabrication is the spreading wetter process which uses the deformable substrate surface such as mercury surface (mercury method) or the air-water interface (subphase method), where protein solution spread to yield a thin liquid film.
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Ligand-induced conformational change of a protein reproduced by a linear combination of displacement vectors obtained from normal mode analysis.

TL;DR: The results presented herein suggest that some proteins that only undergo significant conformational changes around active sites have a relatively high probability of being involved in an actual conformational change and may help solve the flexible-docking problem of a protein with another molecule.