Kouhei Tsumoto
University of Tokyo
462 Papers
2.3K Citations
Kouhei Tsumoto is an academic researcher from University of Tokyo. The author has contributed to research in topics: Chemistry & Antibody. The author has an hindex of 53, co-authored 397 publications. Previous affiliations of Kouhei Tsumoto include Hoffmann-La Roche & National Institute of Advanced Industrial Science and Technology.
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Papers
Repertoire analysis of antibody CDR-H3 loops suggests affinity maturation does not typically result in rigidification
Jeliazko R. Jeliazkov,Adnan Sljoka,Daisuke Kuroda,Nobuyuki Tsuchimura,Naoki Katoh,Kouhei Tsumoto,Jeffrey J. Gray +6 more
TL;DR: The structural flexibility of the CDR-H3 loop for thousands of recently-determined homology models of the human peripheral blood cell antibody repertoire is determined using rigidity theory and results suggest that rigidification may be just one of many biophysical mechanisms for increasing affinity.
Effects of salts on protein-surface interactions: applications for column chromatography.
TL;DR: This review attempts to summarize the mechanism of the salt effects on binding affinity and capacity for various column chromatographies and on nonspecific protein-protein or protein-surface interactions.
Mutations for decreasing the immunogenicity and maintaining the function of core streptavidin.
Kyohei Yumura,Mihoko Ui,Hirofumi Doi,Takao Hamakubo,Tatsuhiko Kodama,Kouhei Tsumoto,Akira Sugiyama +6 more
TL;DR: The results indicated that the hypoimmunogenic muteins retained the biotin‐binding function and the tetramer structure of WT cSA, and the potential mechanisms underlying the success of these mutations in achieving both immune evasion and retention of function are discussed.
Electron microscopy and computational studies of Ebh, a giant cell-wall-associated protein from Staphylococcus aureus.
Sou Sakamoto,Yoshikazu Tanaka,Yoshikazu Tanaka,Isao Tanaka,Toshiaki Takei,Jian Yu,Makoto Kuroda,Min Yao,Toshiko Ohta,Kouhei Tsumoto +9 more
TL;DR: The highly repetitive structure and the associated unique structural flexibility of Ebh support the proposed function of this protein, i.e. binding to sugars in the cell wall, which might result in intra-cell-wall cross-linking that contributes to the rigidity of bacterial cells.
Affinity Improvement of a Cancer-Targeted Antibody through Alanine-Induced Adjustment of Antigen-Antibody Interface.
Takefumi Yamashita,Eiichi Mizohata,Satoru Nagatoishi,Takahiro Watanabe,Makoto Nakakido,Hiroko Iwanari,Yasuhiro Mochizuki,Taisuke Nakayama,Yuji Kado,Yuki Yokota,Hiroyoshi Matsumura,Takeshi Kawamura,Tatsuhiko Kodama,Takao Hamakubo,Tsuyoshi Inoue,Hideaki Fujitani,Kouhei Tsumoto +16 more
TL;DR: Alanine (Ala) mutagenesis scanning of the interfacial residues of a cancer-targeted antibody was performed based on X-ray crystallography analysis, and two substitutions were shown to significantly enhance the binding affinity for the antigen, by up to 30-fold.