Hideaki Fujitani
University of Tokyo
14 Papers
81 Citations
Hideaki Fujitani is an academic researcher from University of Tokyo. The author has contributed to research in topics: Molecular dynamics & Lipid bilayer. The author has an hindex of 8, co-authored 14 publications.
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Papers
On accurate calculation of the potential of mean force between antigen and antibody: A case of the HyHEL-10-hen egg white lysozyme system
TL;DR: The dissociation free energy calculated along the mTMD diss association pathway is significantly lower than that along the dissociation pathway determined by the steered molecular dynamics (SMD) method, indicating that SMD leads to a meta-stable dissociation state.
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Structural features of interfacial tyrosine residue in ROBO1 fibronectin domain-antibody complex: Crystallographic, thermodynamic, and molecular dynamic analyses.
Taisuke Nakayama,Eiichi Mizohata,Takefumi Yamashita,Satoru Nagatoishi,Makoto Nakakido,Hiroko Iwanari,Yasuhiro Mochizuki,Yuji Kado,Yuki Yokota,Reiko Satoh,Kouhei Tsumoto,Hideaki Fujitani,Tatsuhiko Kodama,Takao Hamakubo,Tsuyoshi Inoue +14 more
TL;DR: Results suggest that mutation analysis considering the binding entropy as well as the binding enthalpy will aid in the development of novel antibody drugs for hepatocellular carcinoma.
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Epiregulin Recognition Mechanisms by Anti-epiregulin Antibody 9E5: STRUCTURAL, FUNCTIONAL, AND MOLECULAR DYNAMICS SIMULATION ANALYSES
Yuji Kado,Eiichi Mizohata,Satoru Nagatoishi,Mariko Iijima,Keiko Shinoda,Takamitsu Miyafusa,Taisuke Nakayama,Takuma Yoshizumi,Akira Sugiyama,Takeshi Kawamura,Young-Hun Lee,Hiroyoshi Matsumura,Hirofumi Doi,Hideaki Fujitani,Tatsuhiko Kodama,Yoshikazu Shibasaki,Kouhei Tsumoto,Tsuyoshi Inoue +17 more
TL;DR: The superimposed structure of 9E5(Fab)·EPR on the known complex structure of EGF·EGFR showed that the 9E 5( Fab) paratope overlaps with Domains I and III on the EGFR, which reveals that the EPR complex could not bind to the EGfr.
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Initiation of prolyl cis-trans isomerisation in the CDR-H3 loop of an antibody in response to antigen binding
Keiko Shinoda,Hideaki Fujitani +1 more
TL;DR: It is found that Asp102, which is immediately adjacent to Pro103, rotates while changing its interacting partner residues in the light chain of 9E5, and at the same time EPR polar residues help to stabilise the intermediate states in the isomerisation process by interacting strongly with Asp 102.
Molecular dynamics simulation-based evaluation of the binding free energies of computationally designed drug candidates: importance of the dynamical effects.
Takefumi Yamashita,Akihiko Ueda,Takashi Mitsui,Takashi Mitsui,Atsushi Tomonaga,Shunji Matsumoto,Tatsuhiko Kodama,Hideaki Fujitani +7 more
TL;DR: The purpose of this work is to yield physical insight into the approximate evaluation method in comparison with an exact molecular dynamics simulation-based method (named MP-CAFEE), which can predict binding free energies accurately.
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