Updated on 2024/10/04

Information

 

写真a

 
CAAVEIRO JOSE
 
Organization
Faculty of Pharmaceutical Sciences Department of Pharmaceutical Health Care and Sciences Professor
School of Pharmaceutical Sciences Department of Clinical Pharmacy（Concurrent）
Graduate School of Pharmaceutical Sciences Department of Medicinal Sciences（Concurrent）
School of Interdisciplinary Science and Innovation Department of Interdisciplinary Science and Innovation（Concurrent）
Title
Professor
Contact information
メールアドレス
Tel
0926426662
Profile
Global relations office, Student affairs committee, International education navigation center, Internationalization WG, International course, Strategic International Advisory Group (SIAG), Structural drug discovery center via Green-Pharma, Executive member of ACE-Japan, SCARDA, BINDS.
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Degree

  • Ph.D. ( 2000   UPV/EHU (SPAIN) )

Research History

  • Kyushu University Faculty of Pharmaceutical Sciences Department of Pharmaceutical Health Care and Sciences  Professor

    2017.2 - Present

  • Brandeis University Rosenstiel Basic Medical Sciences Research Center Postdoctoral Associate

    2002.7 - 2007.6

    　 More details

    Country：United States

  • Massachussetts Institute of Technology Chemistry Postdoctoral fellow

    2000.7 - 2002.6

Research Interests・Research Keywords

  • Research theme：Norovirus vaccine ノロウイルスワクチン

    Keyword：Vaccine ワクチン

    Research period： 2022.12 - 2027.3

  • Research theme：Preparation and optimization of immunotoxins 免疫毒素の調製と最適化

    Keyword：Immunotoxin 免疫毒素

    Research period： 2022.4 - 2027.3

  • Research theme：Protein X-ray crystallography analysis 蛋白質X線結晶構造解析

    Keyword：X-ray crystallography X線結晶構造

    Research period： 2017.2 - 2034.5

  • Research theme：Structural and thermodynamic understanding of life 生命の構造的および熱力学的理解

    Keyword：Protein thermodynamics タンパク質の熱力学

    Research period： 2017.2 - 2027.12

  • Research theme：New modality antibodies 新しいモダリティ抗体

    Keyword：Antibodies 抗体

    Research period： 2017.2 - 2026.5

  • Research theme：Biophysical characterization and drug discovery of P2X4, a target for chronic pain 神経因性疼痛の標的である P2X4 の生物物理学的特性評価と創薬。

    Keyword：P2X4, neuropathic pain, P2X4, 神経因性疼痛

    Research period： 2017.2 - 2024.6

  • Research theme：Nanodiscs as a tool in drug discovery of membrane proteins 膜タンパク質の創薬ツールとしてのナノディスク

    Keyword：Nanodiscs ナノディスク

    Research period： 2017.2 - 2024.5

  • Research theme：Structural biology of membrane proteins 膜タンパク質の構造生物学

    Keyword：Membrane protein 膜タンパク質

    Research period： 2017.2 - 2024.5

Awards

  • JB award (reviewer)

    2022.11  

  • JB award (reviewer)

    2021.11  

  • JB award (best paper)

    2019.11  

Papers

▼display all

Books

  • Lipid-Protein Interactions: Strategies of Permeabilization of Biological Membranes.

    Jose Caaveiro（ Role： Sole author）

    Spain  2001.1 

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    Language：Others   Book type：Scholarly book

    Interacciones lipido-proteina: estrategias de permeabilizacion de membranas. Lipid-Protein Interactions: Strategies of Permeabilization of Biological Membranes.

Presentations

  • New antibody modalities for infectious diseases Invited International conference

    Caaveiro, J.M.M.

    39th International Annual Meeting in Pharmaceutical Sciences (IAMPS39)  2024.3 

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    Event date： 2024.3

    Language：English  

    Country：Thailand  

  • 膜孔形成毒素 FraCの免疫毒素への応用

    ＃安田　智徳、妹尾暁暢、谷中冴子、中木戸誠、津本浩平、Caaveiro Jose

    第１１回TR推進合同フォーラム・ライフサイエンス技術交流会  2024.1 

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    Event date： 2024.1

    Language：Japanese   Presentation type：Oral presentation (general)  

    Venue：九州大学馬出キャンパス 九州大学医学部百年講堂   Country：Japan  

  • 医薬品開発に向けた化膿連鎖球菌の鉄取り込み蛋白質に関する構造基盤

    ＃塩見敏生、妹尾暁暢、谷中冴子、中木戸誠、津本浩平、Caaveiro Jose

    第１１回TR推進合同フォーラム・ライフサイエンス技術交流会  2024.1 

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    Event date： 2024.1

    Language：Japanese   Presentation type：Oral presentation (general)  

    Venue：九州大学馬出キャンパス 九州大学医学部百年講堂   Country：Japan  

  • ノロウイルス変異株のVLPを用いた抗体の作出と特性評価

    ＃田川純平、谷中冴子、加藤百合、増田亮津、李在萬、妹尾暁暢、 小山浩輔、植田正、西田基宏、日下部宜宏、Caaveiro Jose

    第3回日本抗体学会学術大会懇親会  2023.12 

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    Event date： 2023.12

    Language：Japanese   Presentation type：Oral presentation (general)  

    Venue：ライカ南国ホール（鹿児島中央駅直結）   Country：Japan  

    ノロウイルスは、下痢や嘔吐を伴う胃腸炎を引き起こす非エンベロープ型ウイルスである。ノロウイルスは変異が入りやすく、変異型ノロウイルスに対しては、既存のノロウイルス抗体の親和性が低減する。そのため、変異型ノロウイルスに対する抗体の作成、及びノロウイルス抗体の中和メカニズムの解明が望まれている。そこで我々は、変異型ノロウイルスに対する高い親和性を持つ抗体を創出し、ノロウイルスと抗体の相互作用を理解することを目的とした。
    本研究では、ヒトに感染する主流の変異株のGII.4株と、2014年に流行し始めた新しい変異株のGII.17株のVLPを混合してマウスに免疫し、ハイブリドーマ技術を用いることで、ノロウイルス結合抗体を産生するハイブリドーマ細胞を作成した。ELISAを用いたスクリーニングにより、GII.4株とGII.17にそれぞれ特異的に結合するモノクローナル抗体産生ハイブリドーマ細胞を取得した。ハイブリドーマ細胞の大量培養とProtein Gを用いた精製によりモノクローナル抗体を高収量・高純度で取得した。得られたモノクローナル抗体を用いて結合評価を行なったところ、得られたモノクローナル抗体はGII.4株とGII.17株にそれぞれ特異的に結合するものが多く得られた一方、交差反応性を有する抗体も得られたことが明らとなった。この結果より、動物への免疫により、得られる多くの抗体の認識部位が株間での変異の多い位置を認識している一方、配列保存性の高い領域に対して結合し、多くの変異株に対して結合する抗体も稀に得られる可能性を示している。

  • ヘムと相互作用する化膿レンサ球菌由来鉄獲得蛋白質の構造基盤

    ＃関幹太、妹尾暁暢、谷中冴子、Caaveiro Jose

    第96回日本生化学会大会  2023.11 

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    Event date： 2023.10 - 2023.11

    Language：Japanese   Presentation type：Oral presentation (general)  

    Venue：福岡市福岡国際会議場マリンメッセ福岡B観   Country：Japan  

    化膿連鎖球菌はヒトの皮膚などに存在する常在菌である。毎年推定7億件の感染症が報告されており、咽頭炎や扁桃炎等の軽度なものから致死に至る劇症型侵襲性感染症まで様々な症状を引き起こす。劇症型レンサ球菌感染症の致死率は約30%と非常に高く、優れた抗菌剤の開発が望まれている。現在、第一選択薬は抗生物質であるアンピシリンが広く用いられているが、既存の抗菌剤の乱用によって細菌叢が撹乱され他菌種も含めた耐性菌の出現が問題となっている。そのため、耐性菌の出現リスクを抑えた分子標的薬開発に資する菌種特異的な蛋白質の機能解析が求められる。本研究ではそのような標的として、菌の宿主内での生育に必須な鉄イオンを獲得する機能を果たす蛋白質に着目する。化膿連鎖球菌における鉄獲得は、主にShr(Streptococcal hemoprotein receptor)と呼ばれる蛋白質によって達成されている。Shrは宿主生体由来のヘモグロビンに結合しているヘム分子から鉄を獲得する。本研究ではShrによるヘム結合メカニズムを解明することを目的とした。
    　Shrは全長が1275残基ものアミノ酸から構成される多ドメイン蛋白質である。ヘム結合の分子基盤を解明するため、まずはヘム結合に関与すると考えられているドメインのみを切り出し、大腸菌発現系にて調製した。得られた組換え蛋白質がヘム結合能を保持していることは吸光測定により確認できた。続いて、本蛋白質のX線結晶構造解析を試みた。その結果、ヘム結合ドメインの構造を取得することに成功した。結晶構造及び変異体解析よりShrがヘムを認識するのに重要なアミノ酸を特定した。ポスター発表ではこのヘム認識メカニズムの詳細および他菌種のヘム結合蛋白質との比較を行い、分子標的薬の標的となりうる特徴を議論する。

  • 物理化学的手法に基づくOX40-OX40L間相互作用の精密解析

    #西牟田拓、松永英莉、妹尾暁暢、谷中冴子、長門石曉、宗孝紀、植田正、津本浩平、Caaveiro Jose

    第２３回日本蛋白質科学会年会会  2023.7 

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    Event date： 2023.7 - 2024.7

    Language：Japanese   Presentation type：Oral presentation (general)  

    Venue：名古屋国際会議場   Country：Japan  

    IOX40は腫瘍壊死因子受容体 (TNFR)ファミリーに属する蛋白質であり、OX40Lはそのリガンドとして機能する腫瘍壊死因子(TNF)である。OX40-OX40L間の蛋白質-蛋白質間相互作用(PPI)はNF-κシグナルを惹起することによるT細胞活性化に寄与しているが、これらの蛋白質の過剰発現は自己免疫疾患の原因となることも報告されている。そのため、OX40-OX40L間PPIは重要な創薬標的である。OX40-OX40Lの複合体結晶構造より、ホモ3量体を形成するOX40Lに対して3分子のOX40が相互作用する特徴的なPPIであることが報告されている。本研究では物理化学的手法によってそのようなPPIの精密解析を実施し、相互作用メカニズムの解明を目指した。
    　本研究ではまずOX40及びOX40Lの膜外ドメインを哺乳類細胞発現系により発現・精製した。得られた組換え蛋白質を用い、表面プラズモン共鳴法(SPR)によりOX40-OX40L間PPIの測定系を確立した。この系を活用して相互作用に伴い溶媒露出度が著しく低下するOX40のアミノ酸残基を中心にアラニンスキャニングを実施すると、PPIが著しく損なわれるホットスポットと呼べる残基を特定することができた。さらに、アラニンスキャニングにおける相互作用の速度論パラメーターの変化に基づき、OX40-OX40L間相互作用プロセスを考察した。

  • 膜付近のエピトープを認識する抗HIV抗体の相互作用解析

    #吉永　晴哉、谷中　冴子、妹尾　暁暢、Rujas Edurne、植田　正、Nieva Jose Luis、Caaveiro Jose

    第２３回日本蛋白質科学会年会会  2023.7 

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    Event date： 2023.7 - 2024.7

    Language：Japanese   Presentation type：Oral presentation (general)  

    Venue：名古屋国際会議場   Country：Japan  

    Iヒト免疫不全ウイルス（HIV）に対抗する抗体の開発において問題となっているのが、取得される抗HIV抗体の主なエピトープがアミノ酸保存性の低いエンベロープスパイク（ENV）部位であることにある。そのため、すべてのHIVウイルスに対して高い中和活性をもつ抗体を取得することは難しい。まれに、ほとんどのHIVウイルス間でアミノ酸が保存されている膜近位領域（MPER）に対する抗体が得られ、広い中和活性をもちうるが、その活性は低い場合が多く、医薬品への応用には至っていない。
    　一方、近年我々は、芳香環を有する低分子を抗MPER抗体に修飾することにより中和活性が著しく向上することを報告している。しかしながら、膜に埋め込まれたMPERの取り扱いが難しく、低分子付加MPER抗体とMPERの相互作用メカニズムは未だに解明されていない。本研究ではMPERと膜貫通領域（TMD）からなる疎水性が高く調製の難しいペプチドを取り扱う系を確立し、構造的および熱力学的な観点からの相互作用を評価することによって、結合に関与するアミノ酸の同定や、化学修飾基の膜環境中抗原認識への寄与について理解することを目指している。本発表では、MPERとTMDからなるペプチドの調製法と得られたペプチドを用いた抗体との相互作用の評価の結果について報告する。本研究の進展により、膜付近のウイルス抗原を標的とした抗体ベースの新規モダリティの開発の進展が期待される。

  • IgG1のヒンジの改変がFcγRIとの相互作用に及ぼす影響の解明

    #小関悠希、谷中冴子、妹尾暁暢、内橋 貴之、Caaveiro Jose

    第２３回日本蛋白質科学会年会会  2023.7 

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    Event date： 2023.7 - 2024.7

    Language：Japanese   Presentation type：Oral presentation (general)  

    Venue：名古屋国際会議場   Country：Japan  

    IgG分子はヒトの体内において主に体液性免疫に関わる重要な分子であり、創薬モダリティーとして近年研究開発が進められている。IgG分子は抗原を認識するFab領域、Fc受容体や補体系と相互作用することで免疫系を活性化するFc領域、それら二つの機能領域をつなぐヒンジ領域から構成される。IgG分子はヒンジ領域が持つ柔軟性の影響で構造解析が困難であり、分子全体としての作用機序は不明な点が多い。本研究ではヒンジ領域の役割を明らかにするために、IgG1のヒンジ領域の下部に注目して変異を導入し、IgG1と高い親和性で相互作用することが知られているFc受容体のFcγRⅠとの相互作用を評価した。本研究を通じて得られたヒンジ領域下部領域の1アミノ酸残基を欠失した変異体は、ヒンジ領域の二つのジスルフィド結合およびCH3ドメイン間の相互作用の両方が失われ、一対の重鎖と軽鎖を持つ、半分子の抗体となった。この抗体半分子は、野生型IgGと比較して親和性はやや低下していたものの、FcγRⅠとの相互作用を保っていた。また、HS-AFM計測より、この抗体半分子は1:1または1:2でFcγRⅠと相互作用することが明らかとなった。本研究より、ヒンジ領域の下部が抗体の高次構造形成に重要である一方、抗体半分子でもFcγRⅠとの相互作用が可能であることが明らかとなった

  • Biophysical screening in nanodiscs reveals novel inhibitors of the bacterial ABC transporter MsbA. International conference

    K. Fujimoto, S. Nagatoishi, K. Tsumoto, T. Ueda, and J. Caaveiro

    Protein Science Society of Japan  2020.7 

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    Event date： 2020.7

    Language：English  

    Country：Japan  

    Development of new antibiotics is urgently needed to combat emerging resistance in bacteria. MsbA is an essential ABC-transporter located in the inner membrane of E. coli. MsbA is directly responsible for the export of Lipid A, the key precursor of lipopolysaccharide (LPS, also known as endotoxin). LPS is of critical importance for the bacterium survival, and therefore MsbA is a pharmacological target. Because of continuous improvements in biophysical methodologies, these techniques are increasingly employed for the screening of chemical compounds to protein targets. In this study, we sought to perform such screening in MsbA by surface plasmon resonance (SPR), a methodology that detects molecules binding to the target with great celerity. To enable the screening, we embedded MsbA in proteo-lipidic particles known as nanodiscs, which greatly stabilized the ATPase activity of the target. Despite the large difference in mass between the dimeric MsbA in nanodiscs and the average size of fragments (>1,000-fold) we detected robust binding of several compounds. The binding of these compounds was cross-validated by dose-dependence analysis and thermodynamic techniques. Moreover, the majority of these fragment compounds did not only bind to the target molecule, but also reduced the ATPase activity of MsbA with various intensities, from partial to complete inhibition. Our research has revealed the identity of novel compounds inhibiting the activity of an essential bacterial protein. We hope to develop these fragments into potent antibacterial compounds, and take the lessons learned to apply this approach to other protein targets of bacterial and human origin.

    Other Link： https://www.proteinsociety.org/2020wcps

  • Molecular Basis for Heme Extraction of the Antimicrobial Target IsdH from Staphylococcus aureus from Human Hemoglobin International conference

    S., Valenciano-Bellido, Vu N.T., Nakakido, M., Caaveiro, J.M.M, and Tsumoto, K..

    Biophysical Society  2020.2 

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    Event date： 2020.2

    Language：English  

    Country：United States  

    Staphylococcus aureus is a pathogenic bacterium responsible for a majority of deadly hospital-acquired infections worldwide, and increasingly resistant to a broad range of antibiotics. This dangerous combination demands action to obtain more efficient antimicrobial approaches. The iron surface determinant (Isd) system comprises a group of S. aureus proteins that obtain iron from the host organism. Since iron is essential for bacterial survival and proliferation during infection, Isd has been proposed as an antibacterial target. In particular, the protein IsdH is exposed on the surface of the bacteria and able to sequester hemoglobin to acquire its heme molecule which contains an atom of iron. IsdH comprises three near-iron transporter (NEAT) domains binding hemoglobin (NEAT1 and NEAT2) and heme (NEAT3) connected by characteristic linker domains of unclear function. The objective of this study is to deciphering the molecular mechanism of heme extraction, including the role of the linker re- gion. The first evidence of the structure of IsdH linker-NEAT3 at high resolu- tion with heme bound is presented. In combination with thermodynamic and structural data we propose a extraction mechanism of heme by IsdH. Although the linker neither accelerate nor strengthen the binding of heme, it contributes to stabilize the critical NEAT3 domain necessary to capture heme. This research contributes to clarify the molecular basis for heme extraction by a po- tential antimicrobial target.

    Other Link： https://www.biophysics.org/2020meeting#/

  • Strengthening Interactions with the Membrane Interface through Grafted Aromatic Compounds produces extremely potent HIV-1 neutralizing antibodies International conference

    Biophysical Society  2020.2 

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    Event date： 2020.2

    Language：English  

    Country：United States  

    Broadly-neutralizing antibodies (bnAbs) against the Env glycoprotein guide the rational development of vaccines and therapeutic agents to prevent or treat HIV- 1 infection. In addition, bnAb-derived binding fragments are instrumental for the study of the structure-function relationships of the conformationally dynamic Env complex. Here, we demonstrate that the anti-viral activity of bnAbs against the Membrane-Proximal External Region of the Env glycoprotein can be enhanced via single-site modification of membrane-interacting Ab areas with synthetic aromatic compounds. Potency enhancement in cell-entry inhibition and standard neutraliza- tion assays correlated with an increase in affinity for the native antigen in virions and did not compromise neutralization breadth. Thus, we have established an opti- mization procedure with the potential of improving functionality of Abs that bind immunotherapeutic targets at membrane surfaces.

    Other Link： https://www.biophysics.org/2020meeting#/

  • Potency enhancement of HIV-1 neutralizing antibodies by site-specific chemical modification. International conference

    The Antibody Society / 2019 Antibody Engineering & Therapeutics  2019.12 

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    Event date： 2019.12

    Language：English  

    Country：United States  

    Engineered variants of broadly-neutralizing antibodies (bnAbs) have shown efficacy in passive immunotherapy of HIV-1 infection. Here, we demonstrate that the anti-viral activity of bnAbs against the Membrane-Proximal External Region of the HIV-1 Env glycoprotein can be enhanced up to 103-fold, via single-site modification of membrane-interacting areas with linear and polycyclic aromatic chemical compounds. In an extreme case, chemical modification of a distant site complements ablation of the heavy-chain complementarity determining region 3 (HCDR3) loop apex, resulting in the functional recovery of a fully inactive antibody. Thus, we have established a procedure based on the use of synthetic molecules to improve functionality of antibodies against HIV.

    Other Link： https://www.antibodysociety.org/2019-antibody-engineering-therapeutics/

  • Grafting synthetic aromatic compounds improves the potency of a pan-neutralizing HIV antibody International conference

    PEGS  2019.11 

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    Event date： 2019.11

    Language：English  

    Country：Portugal  

    Engineered variants of broadly-neutralizing antibodies (bnAbs) have shown efficacy in passive immunotherapy of HIV-1 infection. Particularly, bnAbs raised against the neutralizing MPER epitope have gathered much attention in the area because they can potentially block infection by the large variety of circulating HIV-1 strains and isolates. Despite their remarkable breadth, the potential clinical translation of Abs belonging to this class is hampered by their overall modest potency. Here, we employ cell-entry inhibition and ex-vivo infection neutralization assays to demonstrate that the potency of the MPER bnAb 10E8, can be enhanced up to 102-fold, via single-site modification with linear and polycyclic aromatic chemical compounds. That is, chemically modified 10E8 versions display potency levels comparable to those of bnAbs currently under clinical development. Thus, we have established a procedure based on the use of synthetic molecules to improve functionality of pan-neutralizing HIV antibodies.

  • IsdH from Staphylococcus aureus: mechanism of action and novel antibacterial strategies

    S. Valenciao-Bellido, J. Caaveiro, K. Tsumoto

    Chem-Bio Informatics Society  2019.10 

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    Event date： 2019.10 - 2020.10

    Language：English  

    Country：Japan  

    The bacterium Staphylococcus aureus is the major cause of deadly hospital-acquired infections worldwide1. The Isd (Iron surface determinant) system is a group of proteins that obtain iron from the host organism2,3, helping the bacterium to proliferate, and therefore a promising antibacterial target. The protein IsdH binds to hemoglobin and acquires the heme4,5. IsdH comprises three NEAT (Near-iron transporter) domains connected by linkers of unknown function6,7. The objectives of this study are deciphering the molecular mechanism of heme extraction, to explain the role of the linker region and to obtain an antibody that recognizes IsdH specifically while simultaneously inhibiting heme binding. The first evidence of the structure of IsdH linker-NEAT3 bound to heme was reported in this research. The heme extraction mechanism of IsdH has been deciphered and the role of the linker as key for heme extraction has been explained through structure analysis. Herein we also report a novel VHH that binds to IsdH linker-NEAT3. The crystal structure of the complex of VHH bound to -NEAT3 was determined at high-resolution, showing that the VHH specifically recognizes the heme binding pocket, and explaining why this antibody inhibits heme acquisition by IsdH.

    Other Link： https://cbi-society.org/taikai/taikai19/index_e.html

  • Thermodynamic, kinetic and computational analyses of the recognition mechanism of a flexible protein antigen by an antibody

    I. Kaneda, S. Nagatoishi, D. Kuroda, M. Nakakido, J. Caaveiro, K. Tsumoto

    Chem-Bio Informatics Society  2019.10 

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    Event date： 2019.10 - 2020.10

    Language：English  

    Country：Japan  

    Many proteins have both rigid and flexible regions, and change their conformations upon ligand binding. With current methodologies of antibody generation, it is often difficult to rationally obtain specific antibodies toward flexible epitopes on antigens due to the lack of our knowledge on molecular recognition between antibodies and flexible antigens. In this study, we focused on the interaction between an antibody and an antigen binding to metal ions, to obtain quantitative relationships about antibody-antigen interactions where the antigen is highly flexible. As a model system, we used the Fab region of a monoclonal antibody 5E1 whose antigen is Sonic hedgehog (Shh) protein, which also binds to Ca2+ and Zn2+ ions. In a previous study, 5E1 Fab had exhibited high affinity toward Shh regardless of the presence or absence of the metal ions [1]. However, the details of the interactions and physicochemical properties remains unclear.
    In this study, to reveal the binding mechanism of 5E1 Fab and Shh, thermodynamic and kinetic parameters of the interactions were experimentally evaluated, and we observed drastic changes of binding enthalpy and entropy depending on the existence of the metal ions. In addition, we analyzed and discussed energetic contributions of some interface residues based on physicochemical measurements and molecular dynamics simulations with the Ala mutants as well as the wild-type. In addition to the interaction analyses, we also experimentally and computationally assessed the thermal stability of Shh with or without the metal ions, showing the dependency of the metal ions on the thermal stability of the antigen.
    A co-crystal structure of Shh and 5E1 Fab with the metal ions was already solved [1]. In this study, we also succeeded in obtaining a crystal structure of the complex without the metal ions, enabling the structure-based understanding of the interaction with or without the metal ions. Putting together, our results could be a guideline for rational design of antibodies that recognize flexible antigens.

    Other Link： https://cbi-society.org/taikai/taikai19/index_e.html

  • Membrane accommodation surfaces modulate the biological function of anti-HIV antibodies through semi-specific interactions Invited International conference

    J.L. Nieva, B. Apellaniz, Caaveiro, J.M.M., Caravilla, P, Garcia-Vesga, A., Insausti, S., Largo, E., Requejo-Isidro, J., Rujas, E., Sanchez-Eugenia, R., and Torralba, J.

    Spanish Society of Biochemistry and Molecular Biology  2019.7 

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    Event date： 2019.7

    Language：English   Presentation type：Oral presentation (general)  

    Country：Spain  

    Binding of antibodies (Abs) 4E10 or 10E8 to the envelope gly- coprotein (Env) of HIV-1 exerts one of the broadest neutralizing activities against this virus described to date. These Abs recognize the helical juncture that connects the membrane-proximal external region (MPER) and the transmembrane domain (TMD) present in the Env subunit gp41. Thus, gaining insight into the mechanism underlying MPER-mediated neutralization breadth can contribute to developing more effective vaccines and immunotherapeutic agents against HIV. Both, 4E10 and 10E8, exhibit unusual adaptations to attain specific, high-affinity binding to the helical MPER epitope presented on the surface of the viral membrane interface. We report here that manipulation through mutagenesis can adjust the 4E10 and 10E8 paratope surfaces to the viral membrane through semi-specific electrostatic interactions, and thereby modulate their biological activity.

    Other Link： https://www.sebbm.es/web/en/conferences/sebbm-conferences/3029-madrid-2019

  • The effects of protonation of a phosphorylated amino acid on the molecular recognition: Comparative studies of generic proteins and an antibody. International conference

    R. Kawade, D. Kuroda, J. Caaveiro, H. Akiba, S. Okumura, T. Maruyuma, K. Entzminger, and K. Tsumoto, K.

    Protein Society  2019.7 

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    Event date： 2019.6 - 2019.7

    Language：English  

    Country：Japan  

    Since phosphorylation of an amino acid plays important roles in various cellular processes, how phos- phorylated amino acids are recognized has been widely discussed. However, many previous studies assumed that the protonation state of a phosphate group was (PO32) despite the fact that the phosphate group (pKa ~7) would exist as an equilibrium mixture of the unprotonated state (PO32-) and the singly protonated state (PO3H) in physiological condition. To analyze effects of a protonation state on protein dynamics, we performed MD simulations of 4 different proteinphosphorylated peptide complexes in vari- ous biological processes in which each peptide contained a phosphoserine residue in the unprotonated or singly protonated state. Our result showed that the (PO32-) was more preferable to (PO3H-) in the interactions due to the larger mobility of the phosphate group in the (PO32-) state. Furthermore, we also obtained a monoclonal antibody toward a phosphorylated peptide by phage display, and X-ray crystal- lography, thermodynamic analysis, mutagenesis, and MD simulations showed this antibody captures both protonation states equally well. Putting together, our results suggest that even a single protonation could have a large effect on molecular recognition of a phosphate group.

    Other Link： https://www.proteinsociety.org/e/in/eid=4

  • Antibodies that insert into the lipid membrane to capture the antigen.

    Caaveiro, J.M.M., Rujas, E., Tsumoto, K., and Nieva, J.L.

    Faculty of Pharmaceutical Sciences  2019.3 

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    Event date： 2019.3

    Language：English   Presentation type：Oral presentation (general)  

    Country：Japan  

  • Protein-based therapeutics Invited International conference

    Caaveiro, J.M.M.

    University of Malaysia  2018.11 

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    Event date： 2018.11 - 2019.11

    Language：English   Presentation type：Oral presentation (general)  

    Country：Malaysia  

  • Reversible transformation of a metamorphic membrane protein International conference

    Caaveiro, J.M.M.

    SickKids Research Institute  2018.9 

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    Event date： 2018.9

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Canada  

  • Drug discovery efforts at the Green-Pharma Research Center for System Drug Discovery @KU International conference

    Caaveiro, J.M.M.

    NCATS - NIH  2018.9 

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    Event date： 2018.9

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：United States  

  • Integration of biophysical techniques for the screening of fragment libraries and lead optimization Invited International conference

    Caaveiro, J.M.M.

    NCATS- NIH  2018.9 

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    Event date： 2018.9

    Language：English   Presentation type：Symposium, workshop panel (public)  

    Country：United States  

    Other Link： https://ncats.nih.gov/expertise/preclinical/agm/training/sept2018

  • Molecular recognition of IgG-Fc by Fcgamma receptors Invited International conference

    Caaveiro, J.M.M.

    Antibodies & Complement: Effector Functions, Therapies & Technologies  2018.6 

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    Event date： 2018.6 - 2018.7

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Spain  

    Other Link： http://meetings.embo.org/event/18-antibodies

  • Molecular recognition at the membrane interface: protein-membrane electrostatic interactions modulate the biological function of anti-HIV antibodies International conference

    Nieva, J.L., Rujas, E., Insausti, S., Leaman, D.P., Apellaniz, B., Torralba, J., Zhang, L., Caaveiro, J.M.M., and Zwick, M.B.

    Biophysical Society  2018.2 

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    Event date： 2018.2

    Language：English  

    Country：United States  

    Binding of antibodies 4E10 or 10E8 to the helical juncture that connects the membrane-proximal external region (MPER) and the transmembrane domain (TMD) of the Envelope glycoprotein (Env) gp41 subunit, translates into one of the broadest neutralizing activities against HIV-1 described to date. Accordingly, these antibodies and their mechanisms of action provide timely models in the development of effective vaccination and immunotherapeutic strategies. Both, 4E10 and 10E8, exhibit unusual adaptations to attain specific, high-affinity binding to the helical MPER epitope anchored into the viral membrane interface. We report here that manipulation of the paratope surface through mutagenesis can be used to adjust the electrostatic interactions of 4E10 and 10E8 with the membrane, and modulate their biological activity (neutralization potency and polyreactivity).

    Other Link： https://www.biophysics.org/past-annual-meetings/62nd-annual-meeting

  • Interaction of alpha-thionin with lipidic vesicles Invited International conference

    Workshop on Eukaryotic Antibiotic Peptides (Organized by the Institute Juan March)  1999.2 

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    Event date： 2018.2

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Spain  

  • The Fascinating journey of a metamorphic protein to the cell membrane Invited International conference

    Caaveiro, J.M.M.

    Bioforo 5th Alumni Research Meeting  2017.12 

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    Event date： 2017.12

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Spain  

  • Protein-lipid interactions in a pore-forming toxin. Invited International conference

    Tsumoto, K. and Caaveiro, J.M.M.* (*) presenter

    55th Annual Meeting of the Biophysical Society of Japan  2017.9 

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    Event date： 2017.9

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

    Other Link： https://www.aeplan.co.jp/bsj2017/

  • Structural basis of HIV entry and its inhibition by neutralizing antibodies against the fusogenic glycoprotein subunit 41 International conference

    Nieva, J.L., Rujas, E., Caaveiro, J.M.M., Insausti, S., Apellaniz, B., Jimenez, M.A. and Julien, J.P.

    Spanish Society for Virology  2017.6 

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    Event date： 2017.6 - 2019.6

    Language：English   Presentation type：Oral presentation (general)  

    Country：Spain  

    Structural basis of HIV entry and its inhibition by neutralizing antibodies against the fusogenic glycoprotein subunit 41

  • Thermodynamic properties of the transition state in biomolecular recognition phenomena. Invited

    Caaveiro, J.M.M.

    23rd Pharma-Science Forum  2017.3 

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    Event date： 2017.3

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

  • Biomolecular recognition: a structural and physicochemical perspective. Invited International conference

    Caaveiro, J.M.M.

    Chile-Japan Academic Forum 2016 at Patagonia  2016.11 

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    Event date： 2016.11

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Chile  

  • Thermodynamic tools in fragment-based drug discovery. Invited International conference

    Caaveiro, J.M.M.

    2016 UT-PUCC Joint Workshop for Frontiers in Bioengineering and Biomedical Engineering  2016.11 

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    Event date： 2016.11

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Chile  

  • Molecular recognition phenomena involving proteins of therapeutic interest. Invited International conference

    Caaveiro, J.M.M.

    3rd HU-TMU-KU Joint Symposium for Pharmaceutical Sciences  2017.9 

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    Event date： 2016.9 - 2017.9

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

  • Pore formation assisted by lipids. Invited International conference

    Caaveiro, J.M.M.

    Membrane pores: from structure and assembly, to medicine and technology  2016.6 

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    Event date： 2016.6

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：United Kingdom  

    Other Link： https://royalsociety.org/science-events-and-lectures/2016/06/membrane-pores/

  • Basis of cell-membrane damage by a protein nanopore. Invited International conference

    Caaveiro, J.M.M., Tanaka, K., Morante, K., and Tsumoto, K.

    Todai-Tsinghua Joint Workshop for Frontiers in Bioengineering and Biomedical Engineering  2016.3 

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    Event date： 2016.3

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

  • Structural and mechanistic basis of capsular polysaccharide-synthesizing enzymes CapE/F, and the route to discovery novel inhibitors with antibacterial properties. International conference

    Caaveiro J.M.M., Miyafusa, T., Chigira, T., Nakano, K., Nagatoishi, S., and Tsumoto, K.

    7th International Chemical Congress of Pacific Basin Societies PacificChem  2015.12 

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    Event date： 2015.12

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：United States  

    Other Link： https://pacifichem.org/general-information/pacifichem-2015-interactive-pdf-program-book/

  • Use of thermodynamic tools in the early stages of fragment-based drug discovery. International conference

    Caaveiro J.M.M., Kobe, A., Mitani, T., and Tsumoto, K.

    7th International Chemical Congress of Pacific Basin Societies PacificChem  2015.12 

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    Event date： 2015.12

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：United States  

    Other Link： https://pacifichem.org/general-information/pacifichem-2015-interactive-pdf-program-book/

  • Principles of biomolecular recognition of IgG-Fc by its receptors. Invited International conference

    Caaveiro, J.M.M.

    2nd FcR Research Forum  2015.10 

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    Event date： 2015.10

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

    Other Link： http://www.biophys.jp/news/lib/newsshow.php/3146

  • Thermodynamic Tools in the Early Stages of Drug Discovery. Invited International conference

    Caaveiro J.M.M., Kobe, A., Tashiro, S., Kajihara, D., Kikkawa, M., Mitani T., and Tsumoto K.

    The 4th Asia-Pacific Protein Association (APPA) Conference  2014.5 

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    Event date： 2014.5

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Korea, Republic of  

    Other Link： http://www.pssj.jp/APPA/activity.html

  • Thermodynamic tools in the early stages of drug discovery. Invited

    Caaveiro, J.M.M.

    6th GCOE Medical Sciences Mini-symposium  2013.2 

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    Event date： 2013.2

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

  • Expanding the horizons of isothermal titration calorimetry Invited International conference

    Caaveiro, J.M.M. and Tsumoto, K.

    The Japan Society for Calorimetry and Thermal Analysis  2012.9 

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    Event date： 2012.9

    Language：English   Presentation type：Symposium, workshop panel (public)  

    Country：Japan  

  • Detection and analysis of molecular interactions in the membrane protein transporter MsbA. Invited

    Caaveiro, J.M.M.

    Kyoto University  2012.4 

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    Event date： 2012.4

    Language：Japanese   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

  • Sources of specificity in weak and ultraweak biomolecular interactions. Invited

    Caaveiro, J.M.M.

    Alumni association of the Institute of Medical Science, The University of Tokyo  2011.12 

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    Event date： 2011.12

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

  • Thermodynamic analysis of binding and transfer of heme: Isd system. Invited International conference

    Caaveiro, J.M.M., Moriwaki, Y, Abe, R., Watanabe, M., Tanaka, Y., Vu, N., and Tsumoto, K.

    14th Asian Chemistry Congress  2011.9 

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    Event date： 2011.9

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

  • Aromatic interactions are essential for the binding of galactose to a sugar processing enzyme. International conference

    Caaveiro, J.M.M., Kobe, A., Clifton, J., Ringe, D., Petsko, G.A., and Tsumoto, K.

    6th International Chemical Congress of Pacific Basin Societies PacificChem  2010.12 

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    Event date： 2010.12

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：United States  

  • Enzyme active sites: and after all these years still plenty of opportunities. Invited

    Caaveiro, J.M.M.

    Kyoto University  2007.12 

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    Event date： 2007.12

    Language：Japanese   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Japan  

  • Binding of hydrophobic hydroxamic acids enhances peroxidase’s stereoselectivity in aqueous sulfoxidations. Invited International conference

    2002.8 

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    Event date： 2002.8

    Language：Japanese   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Venue：Boston, MA   Country：United States  

  • Enzymology in silico. Invited International conference

    Caaveiro, J.M.M.

    University of the Basque Conuntry  2002.1 

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    Event date： 2002.1

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Spain  

  • Enzymology in silico Invited International conference

    Caaveiro, J.M.M.

    University of Zaragoza  2002.1 

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    Event date： 2002.1

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Spain  

  • Forum-Iberia for the promotion of science and knowledge in Spain International conference

    Caaveiro, J.M.M.

    National Biotechnology Center (CSIC)  2001.12 

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    Event date： 2001.12

    Language：English   Presentation type：Symposium, workshop panel (public)  

    Country：Spain  

  • An evaluation of some model systems commonly used in the study of the interaction of the sea anemone toxin equinatoxin II with membranes. Invited International conference

    3rd Meeting of the Slovenian Biochemical Society  2001.9 

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    Event date： 2001.9

    Language：English   Presentation type：Public lecture, seminar, tutorial, course, or other speech  

    Country：Slovenia  

    Other Link： http://bio.ijs.si/SBD/partic99.htm

  • A群レンサ球菌の表層蛋白質の機能を阻害する抗体の探索

    山脇 つくし, 中木戸 誠, 相川 知宏, Caaveiro Jose, 中川 一路, 津本 浩平

    日本細菌学雑誌  2023.2  日本細菌学会

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    Language：Japanese  

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MISC

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Professional Memberships

  • American Chemical Society

  • American Society for Biochemistry and Molecular Biology

  • The Japanese Biochemical Society

  • Protein Science Society of Japan

  • The Biophysical Society of Japan

  • The Pharmaceutical Society of Japan

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Committee Memberships

  • Association of Spanish Scientists in Japan   Executive   Foreign country

    2024.4 - 2025.12   

  • Association of Spanish Scientists in Japan   Secretary   Foreign country

    2024.4 - 2025.12   

  • Association of Spanish Scientists in Japan   Executive   Foreign country

    2020.4 - 2024.3   

  • Association of Spanish Scientists in Japan   Treasurer   Foreign country

    2020.4 - 2024.3   

Academic Activities

  • 組織委員会名簿、国際担当委員

    日本薬学会第 145 年会  （ 福岡市、福岡国際会議場、マリンメッセ福岡 B 館、福岡サンパレス ） 2025.3

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    Type：Competition, symposium, etc. 

    Number of participants：7,000

  • Organizing committee

    4th Meeting ACE Japon  （ Minatoku, Tokyo Japan ） 2023.11

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    Type：Competition, symposium, etc. 

    Number of participants：50

  • Screening of academic papers

    Role(s)： Peer review

    2023

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    Type：Peer review 

    Number of peer-reviewed articles in foreign language journals：11

    Number of peer-reviewed articles in Japanese journals：0

    Proceedings of International Conference Number of peer-reviewed papers：0

    Proceedings of domestic conference Number of peer-reviewed papers：0

  • Organizing committee

    （ Minatoku, Tokyo Japan ） 2022.11

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    Type：Competition, symposium, etc. 

    Number of participants：40

  • Journal of Biochemistry International contribution

    2022.1 - 2025.12

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    Type：Academic society, research group, etc. 

  • Screening of academic papers

    Role(s)： Peer review

    2022

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    Type：Peer review 

    Number of peer-reviewed articles in foreign language journals：9

    Number of peer-reviewed articles in Japanese journals：0

    Proceedings of International Conference Number of peer-reviewed papers：0

    Proceedings of domestic conference Number of peer-reviewed papers：0

  • Screening of academic papers

    Role(s)： Peer review

    2020

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    Type：Peer review 

    Number of peer-reviewed articles in foreign language journals：9

    Number of peer-reviewed articles in Japanese journals：0

    Proceedings of International Conference Number of peer-reviewed papers：0

    Proceedings of domestic conference Number of peer-reviewed papers：0

  • Organizing committee

    2nd Meeting ACE Japon  （ OIST, Okinawa Japan ） 2019.11

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    Type：Competition, symposium, etc. 

    Number of participants：40

  • Organizing committee International contribution

    1st meeting Asia-Pacific  （ OIST, Okinawa Japan ） 2019.9

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    Type：Competition, symposium, etc. 

    Number of participants：45

  • Organizing committee

    1st Meeting ACE Japon  （ Embassy of Spain in Tokyo Japan ） 2018.11

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    Type：Competition, symposium, etc. 

    Number of participants：50

  • Journal of Biochemistry International contribution

    2018.1 - 2021.12

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    Type：Academic society, research group, etc. 

  • Co-Organizer

    Present and future of molecular medicine: From basic research to the design of new therapeutics.  （ Embassy of Spain, Tokyo Japan ） 2017.12

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    Type：Competition, symposium, etc. 

    Number of participants：40

  • Organizing committee International contribution

    Forum Iberia for the advancement of science and technology in Spain  （ Massachusetts Institute of Technology, Cambridge, MA UnitedStatesofAmerica ） 2002.5

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    Type：Competition, symposium, etc. 

    Number of participants：250

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Research Projects

  • Understanding the efficacy of therapeutic antibodies through their interaction with cellular receptors.

    Grant number：20H03228  2020 - 2022

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (B)

    CAAVEIRO Jose

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    Authorship：Principal investigator  Grant type：Scientific research funding

    We advanced the understanding of the interaction between antibodies of the IgG family and their cellular receptors at the molecular level. We have described the less-than expected effect of mutations in the middle hinge region to the strength of the interaction with receptors (the middle hinge is where the disulfide bond is located). However, residues in close proximity to the binding interface had a profound effect. Our studies support the engineering of antibodies in the hinge region without major effect in the potency of Abs.
    Additionally, we made an important contribution to improve the potency of Abs. This process was patented and consist on (i) the introduction of a CYS residue in a strategic location and (2) chemical modification of the CYS residue by a yodo acetamide molecule of specific atomic structure. Using this approach we have improved the potency of anti-HIV-1 Abs by more than 500-fold.

    CiNii Research

Class subject

  • 病態生理

    2024.12 - 2025.2   Winter quarter

  • タンパク質医薬品論

    2024.12 - 2025.2   Winter quarter

  • 専門英語（科学英語１）

    2024.10 - 2025.3   Second semester

  • 創薬科学総論III-IV

    2024.10 - 2024.12   Fall quarter

  • 生物薬学研究

    2024.10 - 2024.12   Fall quarter

  • 生命薬学ⅠB

    2024.10 - 2024.12   Fall quarter

  • 医療薬学系英語討論Ⅱ

    2024.4 - 2025.3   Full year

  • 物理薬学系英語討論Ⅱ

    2024.4 - 2025.3   Full year

  • 生物薬学系英語討論Ⅱ

    2024.4 - 2025.3   Full year

  • 医薬化学系英語討論Ⅱ

    2024.4 - 2025.3   Full year

  • 医療薬学系英語講義Ⅱ

    2024.4 - 2025.3   Full year

  • 物理薬学系英語講義Ⅱ

    2024.4 - 2025.3   Full year

  • 生物薬学系英語講義Ⅱ

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  • 医薬化学系英語講義Ⅱ

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  • 医療薬学系英語討論Ⅰ

    2024.4 - 2025.3   Full year

  • 物理薬学系英語討論Ⅰ

    2024.4 - 2025.3   Full year

  • 生物薬学系英語討論Ⅰ

    2024.4 - 2025.3   Full year

  • 医薬化学系英語討論Ⅰ

    2024.4 - 2025.3   Full year

  • 生物薬学系英語講義Ⅰ

    2024.4 - 2025.3   Full year

  • 医薬化学系英語講義Ⅰ

    2024.4 - 2025.3   Full year

  • 医療薬学系英語講義Ⅰ

    2024.4 - 2025.3   Full year

  • 物理薬学系英語講義Ⅰ

    2024.4 - 2025.3   Full year

  • 専門英語（科学英語２）

    2024.4 - 2024.9   First semester

  • 創薬科学総論Ⅰ

    2024.4 - 2024.6   Spring quarter

  • 病態生理

    2023.12 - 2024.2   Winter quarter

  • 専門英語（科学英語１）

    2023.12 - 2024.2   Winter quarter

  • タンパク質医薬品論

    2023.12 - 2024.2   Winter quarter

  • 創薬科学総論III-IV

    2023.10 - 2023.12   Fall quarter

  • 専門英語（科学英語１）

    2023.10 - 2023.12   Fall quarter

  • 生物薬学研究

    2023.10 - 2023.12   Fall quarter

  • 生命薬学ⅠB

    2023.10 - 2023.12   Fall quarter

  • 医療薬学系英語討論Ⅱ

    2023.4 - 2024.3   Full year

  • 物理薬学系英語討論Ⅱ

    2023.4 - 2024.3   Full year

  • 生物薬学系英語討論Ⅱ

    2023.4 - 2024.3   Full year

  • 医薬化学系英語討論Ⅱ

    2023.4 - 2024.3   Full year

  • 医療薬学系英語講義Ⅱ

    2023.4 - 2024.3   Full year

  • 物理薬学系英語講義Ⅱ

    2023.4 - 2024.3   Full year

  • 生物薬学系英語講義Ⅱ

    2023.4 - 2024.3   Full year

  • 医薬化学系英語講義Ⅱ

    2023.4 - 2024.3   Full year

  • 医療薬学系英語討論Ⅰ

    2023.4 - 2024.3   Full year

  • 物理薬学系英語討論Ⅰ

    2023.4 - 2024.3   Full year

  • 生物薬学系英語討論Ⅰ

    2023.4 - 2024.3   Full year

  • 医薬化学系英語討論Ⅰ

    2023.4 - 2024.3   Full year

  • 生物薬学系英語講義Ⅰ

    2023.4 - 2024.3   Full year

  • 医薬化学系英語講義Ⅰ

    2023.4 - 2024.3   Full year

  • 医療薬学系英語講義Ⅰ

    2023.4 - 2024.3   Full year

  • 物理薬学系英語講義Ⅰ

    2023.4 - 2024.3   Full year

  • 専門英語（科学英語２）

    2023.4 - 2023.9   First semester

  • 創薬科学総論Ⅰ

    2023.4 - 2023.6   Spring quarter

  • 病態生理

    2022.12 - 2023.2   Winter quarter

  • タンパク質医薬品論

    2022.12 - 2023.2   Winter quarter

  • 生物薬学研究

    2022.10 - 2023.3   Second semester

  • 専門英語（科学英語１）

    2022.10 - 2023.3   Second semester

  • 医療薬学系英語討論Ⅱ

    2022.4 - 2023.3   Full year

  • 物理薬学系英語討論Ⅱ

    2022.4 - 2023.3   Full year

  • 生物薬学系英語討論Ⅱ

    2022.4 - 2023.3   Full year

  • 医薬化学系英語討論Ⅱ

    2022.4 - 2023.3   Full year

  • 医療薬学系英語講義Ⅱ

    2022.4 - 2023.3   Full year

  • 物理薬学系英語講義Ⅱ

    2022.4 - 2023.3   Full year

  • 生物薬学系英語講義Ⅱ

    2022.4 - 2023.3   Full year

  • 医薬化学系英語講義Ⅱ

    2022.4 - 2023.3   Full year

  • 医療薬学系英語討論Ⅰ

    2022.4 - 2023.3   Full year

  • 物理薬学系英語討論Ⅰ

    2022.4 - 2023.3   Full year

  • 生物薬学系英語討論Ⅰ

    2022.4 - 2023.3   Full year

  • 医薬化学系英語討論Ⅰ

    2022.4 - 2023.3   Full year

  • 生物薬学系英語講義Ⅰ

    2022.4 - 2023.3   Full year

  • 医薬化学系英語講義Ⅰ

    2022.4 - 2023.3   Full year

  • 専門英語（科学英語２）

    2022.4 - 2022.9   First semester

  • 専門英語（科学英語１）

    2021.12 - 2022.2   Winter quarter

  • 創薬科学総論-3

    2021.10 - 2022.3   Second semester

  • 専門英語（科学英語１）

    2021.10 - 2022.3   Second semester

  • 生物薬学研究

    2021.10 - 2022.3   Second semester

  • 専門英語 （科学英語1）

    2021.10 - 2022.3   Second semester

  • 物理薬学系英語討論Ⅱ

    2021.4 - 2022.3   Full year

  • 医療薬学系英語討論Ⅱ

    2021.4 - 2022.3   Full year

  • 生物薬学系英語討論Ⅱ

    2021.4 - 2022.3   Full year

  • 医薬化学系英語講義Ⅰ

    2021.4 - 2022.3   Full year

  • 生物薬学系英語講義Ⅰ

    2021.4 - 2022.3   Full year

  • 物理薬学系英語講義Ⅰ

    2021.4 - 2022.3   Full year

  • 医療薬学系英語講義Ⅰ

    2021.4 - 2022.3   Full year

  • 医薬化学系英語講義ⅠI

    2021.4 - 2022.3   Full year

  • 生物薬学系英語講義ⅠI

    2021.4 - 2022.3   Full year

  • 物理薬学系英語講義ⅠI

    2021.4 - 2022.3   Full year

  • 医療薬学系英語講義ⅠI

    2021.4 - 2022.3   Full year

  • 医療薬学系英語討論Ⅰ

    2021.4 - 2022.3   Full year

  • 物理薬学系英語討論Ⅰ

    2021.4 - 2022.3   Full year

  • 生物薬学系英語討論Ⅰ

    2021.4 - 2022.3   Full year

  • 医薬化学系英語討論Ⅰ

    2021.4 - 2022.3   Full year

  • 医薬化学系英語討論ⅠI

    2021.4 - 2022.3   Full year

  • 生物薬学系英語討論ⅠI

    2021.4 - 2022.3   Full year

  • 物理薬学系英語討論ⅠI

    2021.4 - 2022.3   Full year

  • 医療薬学系英語討論ⅠI

    2021.4 - 2022.3   Full year

  • 医薬化学系英語講義Ⅰ

    2021.4 - 2022.3   Full year

  • 生物薬学系英語講義Ⅰ

    2021.4 - 2022.3   Full year

  • 物理薬学系英語講義Ⅰ

    2021.4 - 2022.3   Full year

  • 医療薬学系英語講義Ⅰ

    2021.4 - 2022.3   Full year

  • 医薬化学系英語討論Ⅰ

    2021.4 - 2022.3   Full year

  • 生物薬学系英語討論Ⅰ

    2021.4 - 2022.3   Full year

  • 物理薬学系英語討論Ⅰ

    2021.4 - 2022.3   Full year

  • 医療薬学系英語討論Ⅰ

    2021.4 - 2022.3   Full year

  • 医薬化学系英語講義Ⅱ

    2021.4 - 2022.3   Full year

  • 生物薬学系英語講義Ⅱ

    2021.4 - 2022.3   Full year

  • 物理薬学系英語講義Ⅱ

    2021.4 - 2022.3   Full year

  • 医療薬学系英語講義Ⅱ

    2021.4 - 2022.3   Full year

  • 医薬化学系英語討論Ⅱ

    2021.4 - 2022.3   Full year

  • 専門英語

    2021.4 - 2021.9   First semester

  • 専門英語 （科学英語２）

    2021.4 - 2021.9   First semester

  • 専門英語

    2020.10 - 2021.3   Second semester

  • 医薬化学系英語講義Ⅰ

    2020.4 - 2021.3   Full year

  • 医療薬学系英語討論Ⅰ

    2020.4 - 2021.3   Full year

  • 物理薬学系英語討論Ⅰ

    2020.4 - 2021.3   Full year

  • 生物薬学系英語討論Ⅰ

    2020.4 - 2021.3   Full year

  • 医薬化学系英語討論Ⅰ

    2020.4 - 2021.3   Full year

  • 医療薬学系英語講義Ⅰ

    2020.4 - 2021.3   Full year

  • 物理薬学系英語講義Ⅰ

    2020.4 - 2021.3   Full year

  • 生物薬学系英語講義Ⅰ

    2020.4 - 2021.3   Full year

  • 専門英語

    2020.4 - 2020.9   First semester

  • 専門英語

    2019.10 - 2020.3   Second semester

  • 生物薬学研究（英語講義）

    2019.10 - 2020.3   Second semester

  • 医療薬学系英語討論Ⅰ

    2019.4 - 2020.3   Full year

  • 医薬化学系英語講義Ⅰ

    2019.4 - 2020.3   Full year

  • 生物薬学系英語講義Ⅰ

    2019.4 - 2020.3   Full year

  • 物理薬学系英語講義Ⅰ

    2019.4 - 2020.3   Full year

  • 医療薬学系英語講義Ⅰ

    2019.4 - 2020.3   Full year

  • 医薬化学系英語討論Ⅰ

    2019.4 - 2020.3   Full year

  • 生物薬学系英語討論Ⅰ

    2019.4 - 2020.3   Full year

  • 物理薬学系英語討論Ⅰ

    2019.4 - 2020.3   Full year

  • 学術英語３・科学英語

    2019.4 - 2019.9   First semester

  • 学術英語３・科学英語

    2018.10 - 2019.3   Second semester

  • 生物薬学研究（英語講義）

    2018.10 - 2019.3   Second semester

  • 創薬科学総論Ⅲ

    2018.10 - 2019.3   Second semester

  • 学術英語３　科学英語

    2018.4 - 2018.9   First semester

  • 創薬科学総論Ⅲ

    2017.10 - 2018.3   Second semester

  • 学術英語３　科学英語

    2017.10 - 2018.3   Second semester

  • 生物薬学研究（英語講義）

    2017.10 - 2018.3   Second semester

  • 学術英語３　科学英語

    2017.4 - 2017.9   First semester

▼display all

FD Participation

  • 2024.9   Role：Participation   Title：九州大学公開全学FD(未来人材育成機構)「共創学部—その新しい取り組みと展望」

    Organizer：University-wide

  • 2024.9   Role：Participation   Title：第７回全学ＦＤ「薬物依存対策研修会」

    Organizer：University-wide

  • 2024.9   Role：Participation   Title：男女共同参画FD、福岡市副市長・荒瀬泰子先生「増える認知症と対策（福岡市）」

    Organizer：University-wide

  • 2024.9   Role：Participation   Title：COIL in ISI (Kyoso) & U. of Glasgow

    Organizer：University-wide

  • 2024.7   Role：Participation   Title：第5回創薬産学官連携セミナー（新モダリティ）

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2024.6   Role：Participation   Title：Scholars and Students at Risk: How can Kyushu University respond to transnational threats to academic freedom?

    Organizer：University-wide

  • 2023.6   Role：Participation   Title：Navigating the Undergraduate Classroom

    Organizer：University-wide

  • 2023.6   Role：Planning   Title：Navigating the Undergraduate Classroom

    Organizer：University-wide

  • 2023.6   Role：Panelist   Title：Navigating the Undergraduate Classroom

    Organizer：University-wide

  • 2023.1   Role：Participation   Title：Boosting your KAKENHI Success Rate – all about the grant system and Kyushu University’s Support Program

    Organizer：University-wide

  • 2022.9   Role：Panelist   Title：Understanding the Faculty Evaluation Systems at Kyushu University

    Organizer：University-wide

  • 2022.9   Role：Moderator   Title：Understanding the Faculty Evaluation Systems at Kyushu University

    Organizer：University-wide

  • 2022.9   Role：Planning   Title：Understanding the Faculty Evaluation Systems at Kyushu University

    Organizer：University-wide

  • 2022.5   Role：Participation   Title：Toward a bilingual environment at Kyushu University

    Organizer：University-wide

  • 2022.4   Role：Participation   Title：学生の多様性に対応した教育とは：障害学生への合理的配慮を中心に)

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2022.3   Role：Participation   Title：第3回創薬産学官連携セミナー（感染症研究拠点WG共催)

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2021.9   Role：Participation   Title：Medical System, Insurance and Finances in Japan

    Organizer：University-wide

  • 2021.5   Role：Participation   Title：Workshop: Online Teaching Experiences

    Organizer：University-wide

  • 2021.5   Role：Participation   Title：第2回創薬産学官連携セミナー

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2021.2   Role：Participation   Title：第１回創薬産学官連携セミナー

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2019.12   Role：Participation   Title：英語によるSTEM教育に関するFD (Day2) / Faculty Development: New Teaching Approaches in STEM Education through EMI (Day2)

    Organizer：University-wide

  • 2019.12   Role：Participation   Title：英語によるSTEM教育に関するFD (Day1) / Faculty Development: New Teaching Approaches in STEM Education through EMI (Day1),

    Organizer：University-wide

  • 2019.11   Role：Participation   Title：Scopusの論文データを用いた薬学研究院の研究力分析およびBIツールを用いた研究力分析の紹介

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2019.10   Role：Participation   Title：令和元年度馬出地区４部局合同男女共同参画ＦＤ

    Organizer：University-wide

  • 2019.9   Role：Participation   Title：化学物質の使用に関してリスクアセスメント

    Organizer：University-wide

  • 2019.9   Role：Participation   Title：外国人研究者・留学生受け入れ、貨物輸出と技術の提供に関して

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2019.7   Role：Participation   Title：What All Researcher Should Know about Copyright and Patents - Opportunity, Rights and Obligations

    Organizer：University-wide

  • 2019.2   Role：Participation   Title：Internationalization of Kyushu University: How would you change it?

    Organizer：University-wide

  • 2018.10   Role：Participation   Title：薬学部でM2B/Moodleに関するFD

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2018.10   Role：Participation   Title：本学の男女共同参画の取り組みについて

    Organizer：University-wide

  • 2018.9   Role：Participation   Title：全学FD「学習支援システム講習会」九州大学Web学習システム（Moodleほか）

    Organizer：University-wide

  • 2018.7   Role：Participation   Title：第２回全学ＦＤ、平成３３年度入学者選抜改革 【九州大学新入試ＱＵＢＥ】

    Organizer：University-wide

  • 2018.5   Role：Participation   Title：総合的創薬ソリューションプロバイダーによる創薬研究支援の新たな形

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2018.5   Role：Participation   Title：Life in Japan: Informative pension system

    Organizer：University-wide

  • 2018.1   Role：Participation   Title：Setting up international collaborations

    Organizer：University-wide

  • 2018.1   Role：Participation   Title：Pre-clinical development workshop

    Organizer：[Undergraduate school/graduate school/graduate faculty]

  • 2017.10   Role：Participation   Title：Unconscious Bias

    Organizer：University-wide

  • 2017.9   Role：Participation   Title：English Medium Instruction: An introduction to aspects of language and methodology for university lecturers

    Organizer：University-wide

  • 2017.6   Role：Participation   Title：Enhanced education program

    Organizer：University-wide

  • 2017.5   Role：Participation   Title：Copyright and digital resources in Education

    Organizer：University-wide

  • 2017.4   Role：Participation   Title：Orientation for new faculty members

    Organizer：University-wide

  • 2017.3   Role：Participation   Title：Usage of research funds

    Organizer：University-wide

  • 2017.3   Role：Participation   Title：Network Security

    Organizer：[Undergraduate school/graduate school/graduate faculty]

▼display all

Participation in international educational events, etc.

  • 2024.3

    Chulalongkorn University and Kyushu University

    International Collaborative Innovation Program (Thailand)

    　 More details

    Venue：Thailand, Bangkok

    Number of participants：12

  • 2023.12

    Chulalongkorn University and Kyushu University

    International Collaborative Innovation Program (Japan)

    　 More details

    Venue：Japan, Fukuoka

    Number of participants：12

Outline of Social Contribution and International Cooperation activities

  • - Director of Global Relations Office
    - Board member of Strategic International Advisory Group (Headquarters)
    - Executive of ACE Japón (2020-2026)

Social Activities

  • Invited speaker at the "Europa House" in the event "Past, Present and Future Cross-continental Connections between Europe and Japan" (October 21, 2023.

    2023

    　More details

    Invited speaker at the "Europa House" in the event "Past, Present and Future Cross-continental Connections between Europe and Japan" (October 21, 2023.

Media Coverage

  • Researchers around the world. 30 minutes interview about one of the themes of research, the Antibodies https://libertadfm.es/ https://www.investigadoresporelmundo.com/ TV or radio program

    Libertad FM (Spain)  2020.6

    　More details

    Researchers around the world. 30 minutes interview about one of the themes of research, the Antibodies
    https://libertadfm.es/
    https://www.investigadoresporelmundo.com/

Activities contributing to policy formation, academic promotion, etc.

  • 2019.6   1. EURAXESS (European researchers, backed by the European Union) 2. ACE Japon (Association of Spanish researchers in Japan)

    Help to prepare the program.
    Organization of activity.

Acceptance of Foreign Researchers, etc.

  • Chulalongkorn

    Acceptance period： 2023.3 - 2023.5   （Period）：1 month or more

    Nationality：Thailand

    Business entity：On-campus funds