Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Yoko Akazawa-Ogawa"'
Autor:
Tomonari Matsuda, Yoko Akazawa-Ogawa, Lilian-Kaede Komaba, Norihiko Kiyose, Nobuo Miyazaki, Yusaku Mizuguchi, Tetsuo Fukuta, Yuji Ito, Yoshihisa Hagihara
Publikováno v:
Frontiers in Immunology, Vol 14 (2024)
Antibody maturation is the central function of the adaptive immune response. This process is driven by the repetitive selection of mutations that increase the affinity toward antigens. We hypothesized that a precise observation of this process by hig
Externí odkaz:
https://doaj.org/article/223ca25edde843b4b82c917d9040faed
Autor:
Masahiro Noji, Tatsushi Samejima, Keiichi Yamaguchi, Masatomo So, Keisuke Yuzu, Eri Chatani, Yoko Akazawa-Ogawa, Yoshihisa Hagihara, Yasushi Kawata, Kensuke Ikenaka, Hideki Mochizuki, József Kardos, Daniel E. Otzen, Vittorio Bellotti, Johannes Buchner, Yuji Goto
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
Noji et al. test link between protein folding and misfolding upon heating and agitation. They show that folding and amyloid formation are separated by the supersaturation barrier of a protein, breakdown of which shifts the protein to the amyloid path
Externí odkaz:
https://doaj.org/article/ed4d8eeda119466189e820b1da445527
Publikováno v:
Biomolecules, Vol 11, Iss 6, p 810 (2021)
In this study, we assessed the potential of arginine and lysine solubility-enhancing peptide (SEP) tags to control the solubility of a model protein, anti-EGFR VHH-7D12, in a thermally denatured state at a high temperature. We produced VHH-7D12 antib
Externí odkaz:
https://doaj.org/article/b0f3979ea1b249609fe01dc48b89a19e
Publikováno v:
European Journal of Pharmaceutics and Biopharmaceutics. 165:13-21
We previously demonstrated that amorphous aggregates of misfolded VHH-7D12 antibodies (VHH-Mis), a potential anti-EGFR drug, can generate a robust serum IgG response. Here we investigate the immunogenic nature, especially the specificity of the immun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::934a8be9df5657e0591395647ca098ef
https://doi.org/10.1016/j.ejpb.2021.05.004
https://doi.org/10.1016/j.ejpb.2021.05.004
Publikováno v:
European Journal of Pharmaceutics and Biopharmaceutics. 152:164-174
Amorphous aggregates of therapeutic proteins can provoke an unwanted immune response (anti-drug antibodies; ADAs), but counter-examples have led to some controversy. Amorphous aggregates can possess unique biophysical and biochemical attributes depen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ae9527236729421d63961f2bbb66343
https://doi.org/10.1016/j.ejpb.2020.05.006
https://doi.org/10.1016/j.ejpb.2020.05.006
Publikováno v:
The Journal of Biochemistry. 168:63-72
Site-specific conjugation of double-stranded DNA using antibodies enables the development of unique applications for antibody–drug conjugates utilizing recent advances in nucleic acid medicines. Here, we describe a novel method to conjugate a camel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcb99d6775eaf82ba50425767810e062
https://doi.org/10.1093/jb/mvaa029
https://doi.org/10.1093/jb/mvaa029
Autor:
Yuji Ito, Yoshihisa Hagihara, Fukuta Tetsuo, Norihiko Kiyose, Lilian-Kaede Komaba, Miyazaki Nobuo, Mizuguchi Yusaku, Yoko Akazawa-Ogawa, Tomonari Matsuda
Time-resolved antibody repertoire analysis is essential to elucidate the antibody maturation process during immunization. However, most analyses are merely snapshot comparisons of unimmunized and fully immunized animals. In this study, an alpaca was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a4355066f23a8aabd36e9f3b743727d
https://doi.org/10.1101/2021.06.29.449501
https://doi.org/10.1101/2021.06.29.449501
Publikováno v:
Biomolecules
In this study, we assessed the potential of arginine and lysine solubility-enhancing peptide (SEP) tags to control the solubility of a model protein, anti-EGFR VHH-7D12, in a thermally denatured state at a high temperature. We produced VHH-7D12 antib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::09caf5787b165655d63e613a29584488
https://pubmed.ncbi.nlm.nih.gov/34072518
https://pubmed.ncbi.nlm.nih.gov/34072518
Publikováno v:
European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V. 165
We previously demonstrated that amorphous aggregates of misfolded V
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f2ad735a0ec5f2363dc34b11c57a677e
https://pubmed.ncbi.nlm.nih.gov/33971271
https://pubmed.ncbi.nlm.nih.gov/33971271
Publikováno v:
European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V. 152
Amorphous aggregates of therapeutic proteins can provoke an unwanted immune response (anti-drug antibodies; ADAs), but counter-examples have led to some controversy. Amorphous aggregates can possess unique biophysical and biochemical attributes depen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::748b72b7e72ef92d7509ab675551a893
https://pubmed.ncbi.nlm.nih.gov/32416134
https://pubmed.ncbi.nlm.nih.gov/32416134