Department of Global Healthcare
Associate Professor: Jose M.M. Caaveiro, Ph.D.
Assistant Professor: Tomohiro Yamashita, Ph.D.
In the laboratory of Global Healthcare we address topics relevant to universal public health. (1) We seek to elucidate the molecular
basis of diseases of global reach such as cancer, infectious diseases (AIDS, Influenza, and MRSA) and neurodegenerative diseases.
(2) We apply state of the art screening technologies to find novel compounds to fight disease, and also to ameliorate people suffering
from chronic and neuropathic pain. And (3) we develop technologies for a more efficient use of antibodies and their cellular
Fcg receptors by employing rational design methodologies. With strong support from the recently created Green-Pharma Research
Center, and relying on a large network of collaborators in academia and industry, we aim to make decisive contributions to improve
human well-being. We also seek to augment the international presence of the School of Pharmaceutical Sciences, and to catalyze
the emergence of leadership students with a deeper understanding of global issues.
Department of Global Healthcare
Graduate School of Pharmaceutical Sciences
3-1-1 Maidashi, Higashi-ku, Fukuoka-shi, 812-8582
- Tashima, et al. (2018) Weak electrostatic interactions between collagen and monomeric SLRP osteomodulin govern the shape of type I collagen fibrils. Commun. Biol. 1:33.
- Miyanabe et al. (2018) Intramolecular H-bonds govern the recognition of a flexible peptide by an antibody. J. Biochem. DOI:10.1093/jb/mvy032
- Kiyoshi et al. (2018) Assessing the heterogeneity of the Fc-glycan of a therapeutic antibody using an engineered FcγReceptor IIIa-immobilized column. Sci. Rep. 8:3955.
- Kiyoshi et al. (2017) Glycosylation of IgG-Fc: a molecular perspective. Int. Immunol. 29:311-317.
- Tanaka et al. (2017) Haemolytic actinoporins interact with carbohydrates using their lipid-binding module. Philos. Trans. R. Soc. Lond. B Biol. Sci., 372: 20160216.
- Rujas et al. (2017) Functional contacts between MPER and the anti-HIV-1 broadly neutralizing antibody 4E10 extend into the core of the membrane. J. Mol. Biol., 429:1213–1226.
- Rujas, et al. (2017) Peripheral membrane interactions boost the engagement by an anti HIV-1 broadly neutralizing antibody. J. Biol. Chem. 292:5571–5583.
- Kudo et al (2017) Disruption of cell adhesion by an antibody targeting the cell-adhesive intermediate (X-dimer) of human P-cadherin. Sci. Rep. 7:39518.
- Yamashita et al. (2016) Duloxetine inhibits microglial P2X4 receptor function and alleviates neuropathic pain after peripheral nerve injury. PLoS One, 11: e0165189.
- Rujas et al. (2016) Structural basis for broad neutralization of HIV-1 through the molecular recognition of 10E8 helical epitope at the membrane interface. Sci. Rep. 6:38177.
- Kudo et al. (2016) Adhesive dimerization of human P-cadherin catalyzed by a chaperone-like mechanism. Structure, 24:1523-1536.
- Matsumura et al. (2016) A novel P2X4 receptor-selective antagonist produces anti-allodynic effect in a mouse model of herpetic pain. Sci Rep. 6:32461.
- Morante et al. (2016) Identification of a membrane-bound prepore species clarifies the lytic mechanism of actinoporins. J. Biol. Chem. 291:19210-19219.
- Caaveiro et al. (2015) Structural analysis of Fc/FcγR complexes: a blueprint for antibody design. Immunol. Rev. 268:201-221.
- Kiyoshi et al. (2015) Structural basis for binding of human IgG1 to its high-affinity human receptor FcγRI. Nat. Commun. 6:6866.
- Tanaka et al. (2015) Structural basis for self-assembly of a cytolytic pore lined by protein and lipid. Nat. Commun. 6:6337.