Researcher basic information

• 博士（理学）, 北海道大学

• https://researchmap.jp/kabe_pump?lang=en

• https://orcid.org/0000-0003-2681-5921
• https://jglobal.jst.go.jp/detail?JGLOBAL_ID=201201078597497949
• https://wwwchem.sci.hokudai.ac.jp/~molbio/
• https://wwwchem.sci.hokudai.ac.jp/~molbio/home-en/

• 60596188

• https://orcid.org/0000-0003-2681-5921

• 201201078597497949

• Cation pump
• Apoptosis
• X-ray crystallography
• Active transporters
• Flippase
• P-type ATPase
• Proton pump
• Gastric
• Cryo-EM
• membrane proteins

• Life Science, Structural biochemistry
• Life Science, Functional biochemistry

• Bachelor's degree program, School of Science
• Master's degree program, Graduate School of Chemical Sciences and Engineering
• Doctoral (PhD) degree program, Graduate School of Chemical Sciences and Engineering

Research activity information

• 11 Sep. 2013, 日本生化学会, 日本生化学会奨励賞
  Japan
• Dec. 2011, 生体エネルギー研究会, 若手奨励賞
  Japan
• Oct. 2011, ASBMB, JBC Herbert Tabor Award
  United States
• 09 Aug. 2008, P-ATPase conference, Margrethe Moller Award
  Denmark
• Aug. 2004, FASEB, FASEB SRC Young Scientist Award
  United States

• Design, synthesis, and structural analysis of an inhibitor of the gastric proton pump with a diaza-tricyclic skeleton
  Nariyoshi Umekubo; Airi Hashizume; Haruki Saito; Satoru Kato; Chisato Kanai; Chai C. Gopalasingam; Christoph Gerle; Hideki Shigematsu; Atsushi Yoshimori; Kazuhiro Abe; Satoshi Yokoshima
  Organic & Biomolecular Chemistry, 2026
  Scientific journal
• Cryo-EM Structure of the ATP11C Q79E Mutant Reveals the Structural Basis for Altered Phospholipid Recognition
  Qian Y, Gopalasingam C.C, Gerle C, Shigematsu H, Abe K, Oshima A.
  Journal of Biological Chemistry, 110935, 110935, Elsevier BV, Nov. 2025, [Peer-reviewed], [Corresponding author]
  English, Scientific journal
• A unique gating mechanism revealed by the cryo-EM structure of monomeric ATP9A flippase
  Kazuhiro Abe; Parthiban Marimuthu; Yuheng Qian; Chai C. Gopalasingam; Christoph Gerle; Hideki Shigematsu; Kotaro Tanaka; Himanshu Khandelia
  Journal of Biological Chemistry, 301, 10, 110631, 110631, Elsevier BV, Oct. 2025
  Scientific journal
• Molecular Structure of the Na+,K+-ATPase α4β1 Isoform in Its Ouabain-Bound Conformation
  Kazuhiro Abe; Jeff McDermott; Hridya Valia Madapally; Parthiban Marimuthu; Chai C. Gopalasingam; Christoph Gerle; Hideki Shigematsu; Himanshu Khandelia; Gustavo Blanco
  International Journal of Molecular Sciences, 19 Nov. 2024, [Peer-reviewed], [Lead author, Corresponding author], ［Internationally co-authored］, [International Magazine]
  Scientific journal
• Corrigendum to "Human F-ATP synthase as a drug target" [Pharmacol. Res. 209 (2024) 107423].
  Christoph Gerle; Chimari Jiko; Atsuki Nakano; Ken Yokoyama; Chai C Gopalasingam; Hideki Shigematsu; Kazuhiro Abe
  Pharmacological research, 209, 107467, 107467, Nov. 2024, [Peer-reviewed], [International Magazine]
  English
• Human F-ATP synthase as a drug target
  Christoph Gerle; Chimari Jiko; Atsuki Nakano; Ken Yokoyama; Chai C. Gopalasingam; Hideki Shigematsu; Kazuhiro Abe
  Pharmacological Research, 209, 107423, 107423, Elsevier BV, Nov. 2024, [Peer-reviewed], ［Internationally co-authored］, [International Magazine]
  Scientific journal
• Specific protonation of acidic residues confers K+ selectivity to the gastric proton pump
  Hridya Valia Madapally; Kazuhiro Abe; Vikas Dubey; Himanshu Khandelia
  Journal of Biological Chemistry, 300, 1, 105542, 105542, Elsevier BV, Jan. 2024, [Peer-reviewed], ［Internationally co-authored］, [International Magazine]
  English, Scientific journal
• A Na pump with reduced stoichiometry is up-regulated by brine shrimp in extreme salinities.
  Pablo Artigas; Dylan J Meyer; Victoria C Young; Kerri Spontarelli; Jessica Eastman; Evan Strandquist; Huan Rui; Benoît Roux; Matthew A Birk; Hanayo Nakanishi; Kazuhiro Abe; Craig Gatto
  Proceedings of the National Academy of Sciences of the United States of America, 120, 52, e2313999120, 26 Dec. 2023, [Peer-reviewed], ［Internationally co-authored］, [International Magazine]
  English, Scientific journal, Brine shrimp (Artemia) are the only animals to thrive at sodium concentrations above 4 M. Salt excretion is powered by the Na+,K+-ATPase (NKA), a heterodimeric (αβ) pump that usually exports 3Na+ in exchange for 2 K+ per hydrolyzed ATP. Artemia express several NKA catalytic α-subunit subtypes. High-salinity adaptation increases abundance of α2KK, an isoform that contains two lysines (Lys308 and Lys758 in transmembrane segments TM4 and TM5, respectively) at positions where canonical NKAs have asparagines (Xenopus α1's Asn333 and Asn785). Using de novo transcriptome assembly and qPCR, we found that Artemia express two salinity-independent canonical α subunits (α1NN and α3NN), as well as two β variants, in addition to the salinity-controlled α2KK. These β subunits permitted heterologous expression of the α2KK pump and determination of its CryoEM structure in a closed, ion-free conformation, showing Lys758 residing within the ion-binding cavity. We used electrophysiology to characterize the function of α2KK pumps and compared it to that of Xenopus α1 (and its α2KK-mimicking single- and double-lysine substitutions). The double substitution N333K/N785K confers α2KK-like characteristics to Xenopus α1, and mutant cycle analysis reveals energetic coupling between these two residues, illustrating how α2KK's Lys308 helps to maintain high affinity for external K+ when Lys758 occupies an ion-binding site. By measuring uptake under voltage clamp of the K+-congener 86Rb+, we prove that double-lysine-substituted pumps transport 2Na+ and 1 K+ per catalytic cycle. Our results show how the two lysines contribute to generate a pump with reduced stoichiometry allowing Artemia to maintain steeper Na+ gradients in hypersaline environments.
• Deep learning driven de novo drug design based on gastric proton pump structures
  Kazuhiro Abe; Mami Ozako; Miki Inukai; Yoe Matsuyuki; Shinnosuke Kitayama; Chisato Kanai; Chiaki Nagai; Chai C. Gopalasingam; Christoph Gerle; Hideki Shigematsu; Nariyoshi Umekubo; Satoshi Yokoshima; Atsushi Yoshimori
  Communications Biology, 6, 1, Springer Science and Business Media LLC, 19 Sep. 2023, [Peer-reviewed], [Lead author, Corresponding author], ［Internationally co-authored］, [International Magazine]
  Scientific journal, Abstract
  
  Existing drugs often suffer in their effectiveness due to detrimental side effects, low binding affinity or pharmacokinetic problems. This may be overcome by the development of distinct compounds. Here, we exploit the rich structural basis of drug-bound gastric proton pump to develop compounds with strong inhibitory potency, employing a combinatorial approach utilizing deep generative models for de novo drug design with organic synthesis and cryo-EM structural analysis. Candidate compounds that satisfy pharmacophores defined in the drug-bound proton pump structures, were designed in silico utilizing our deep generative models, a workflow termed Deep Quartet. Several candidates were synthesized and screened according to their inhibition potencies in vitro, and their binding poses were in turn identified by cryo-EM. Structures reaching up to 2.10 Å resolution allowed us to evaluate and re-design compound structures, heralding the most potent compound in this study, DQ-18 (N-methyl-4-((2-(benzyloxy)-5-chlorobenzyl)oxy)benzylamine), which shows a K_i value of 47.6 nM. Further high-resolution cryo-EM analysis at 2.08 Å resolution unambiguously determined the DQ-18 binding pose. Our integrated approach offers a framework for structure-based de novo drug development based on the desired pharmacophores within the protein structure.
• Structure and function of H+/K+ pump mutants reveal Na+/K+ pump mechanisms
  Victoria C. Young; Hanayo Nakanishi; Dylan J. Meyer; Tomohiro Nishizawa; Atsunori Oshima; Pablo Artigas; Kazuhiro Abe
  Nature Communications, 13, 1, Springer Science and Business Media LLC, 09 Sep. 2022, [Peer-reviewed], [Last author, Corresponding author], ［Internationally co-authored］, [International Magazine]
  Scientific journal, Abstract
  
  Ion-transport mechanisms evolve by changing ion-selectivity, such as switching from Na⁺ to H⁺ selectivity in secondary-active transporters or P-type-ATPases. Here we study primary-active transport via P-type ATPases using functional and structural analyses to demonstrate that four simultaneous residue substitutions transform the non-gastric H⁺/K⁺ pump, a strict H⁺-dependent electroneutral P-type ATPase, into a bona fide Na⁺-dependent electrogenic Na⁺/K⁺ pump. Conversion of a H⁺-dependent primary-active transporter into a Na⁺-dependent one provides a prototype for similar studies of ion-transport proteins. Moreover, we solve the structures of the wild-type non-gastric H⁺/K⁺ pump, a suitable drug target to treat cystic fibrosis, and of its Na⁺/K⁺ pump-mimicking mutant in two major conformations, providing insight on how Na⁺ binding drives a concerted mechanism leading to Na⁺/K⁺ pump phosphorylation.
• Structural Basis for Binding of Potassium-Competitive Acid Blockers to the Gastric Proton Pump.
  Saki Tanaka; Mikio Morita; Tatsuya Yamagishi; Hridya Valia Madapally; Kenichi Hayashida; Himanshu Khandelia; Christoph Gerle; Hideki Shigematsu; Atsunori Oshima; Kazuhiro Abe
  Journal of medicinal chemistry, 65, 11, 7843, 7853, 23 May 2022, [Peer-reviewed], [Last author, Corresponding author], ［Internationally co-authored］, [International Magazine]
  English, Scientific journal, As specific inhibitors of the gastric proton pump, responsible for gastric acidification, K+-competitive acid blockers (P-CABs) have recently been utilized in the clinical treatment of gastric acid-related diseases in Asia. However, as these compounds have been developed based on phenotypic screening, their detailed binding poses are unknown. We show crystal and cryo-EM structures of the gastric proton pump in complex with four different P-CABs, tegoprazan, soraprazan, PF-03716556 and revaprazan, at resolutions reaching 2.8 Å. The structures describe molecular details of their interactions and are supported by functional analyses of mutations and molecular dynamics simulations. We reveal that revaprazan has a novel binding mode in which its tetrahydroisoquinoline moiety binds deep in the cation transport conduit. The mechanism of action of these P-CABs can now be evaluated at the molecular level, which will facilitate the rational development and improvement of currently available P-CABs to provide better treatment of acid-related gastrointestinal diseases.
• Cryo-EM of the ATP11C flippase reconstituted in Nanodiscs shows a distended phospholipid bilayer inner membrane around transmembrane helix 2.
  Hanayo Nakanishi; Kenichi Hayashida; Tomohiro Nishizawa; Atsunori Oshima; Kazuhiro Abe
  The Journal of biological chemistry, 298, 1, 101498, 101498, Jan. 2022, [Peer-reviewed], [Last author, Corresponding author], [International Magazine]
  English, Scientific journal, ATP11C is a member of the P4-ATPase flippase family that mediates translocation of phosphatidylserine (PtdSer) across the lipid bilayer. In order to characterize the structure and function of ATP11C in a model natural lipid environment, we revisited and optimized a quick procedure for reconstituting ATP11C into Nanodiscs using methyl-β-cyclodextrin as a reagent for the detergent removal. ATP11C was efficiently reconstituted with the endogenous lipid, or the mixture of endogenous lipid and synthetic dioleoylphosphatidylcholine (DOPC)/dioleoylphosphatidylserine (DOPS), all of which retained the ATPase activity. We obtained 3.4 Å and 3.9 Å structures using single-particle cryo-electron microscopy (cryo-EM) of AlF- and BeF-stabilized ATP11C transport intermediates, respectively, in a bilayer containing DOPS. We show that the latter exhibited a distended inner membrane around ATP11C transmembrane helix 2, possibly reflecting the perturbation needed for phospholipid release to the lipid bilayer. Our structures of ATP11C in the lipid membrane indicate that the membrane boundary varies upon conformational changes of the enzyme and is no longer flat around the protein, a change that likely contributes to phospholipid translocation across the membrane leaflets.
• Gastric proton pump with two occluded K+ engineered with sodium pump-mimetic mutations.
  Kazuhiro Abe; Kenta Yamamoto; Katsumasa Irie; Tomohiro Nishizawa; Atsunori Oshima
  Nature communications, 12, 1, 5709, 5709, 29 Sep. 2021, [Peer-reviewed], [Lead author, Corresponding author], [International Magazine]
  English, Scientific journal, The gastric H+,K+-ATPase mediates electroneutral exchange of 1H+/1K+ per ATP hydrolysed across the membrane. Previous structural analysis of the K+-occluded E2-P transition state of H+,K+-ATPase showed a single bound K+ at cation-binding site II, in marked contrast to the two K+ ions occluded at sites I and II of the closely-related Na+,K+-ATPase which mediates electrogenic 3Na+/2K+ translocation across the membrane. The molecular basis of the different K+ stoichiometry between these K+-counter-transporting pumps is elusive. We show a series of crystal structures and a cryo-EM structure of H+,K+-ATPase mutants with changes in the vicinity of site I, based on the structure of the sodium pump. Our step-wise and tailored construction of the mutants finally gave a two-K+ bound H+,K+-ATPase, achieved by five mutations, including amino acids directly coordinating K+ (Lys791Ser, Glu820Asp), indirectly contributing to cation-binding site formation (Tyr340Asn, Glu936Val), and allosterically stabilizing K+-occluded conformation (Tyr799Trp). This quintuple mutant in the K+-occluded E2-P state unambiguously shows two separate densities at the cation-binding site in its 2.6 Å resolution cryo-EM structure. These results offer new insights into how two closely-related cation pumps specify the number of K+ accommodated at their cation-binding site.
• Transport Cycle of Plasma Membrane Flippase ATP11C by Cryo-EM
  Hanayo Nakanishi; Tomohiro Nishizawa; Katsumori Segawa; Osamu Nureki; Yoshinori Fujiyoshi; Shigekazu Nagata; Kazuhiro Abe
  Cell Reports, 32, 13, 108208, 108208, Elsevier BV, Sep. 2020, [Peer-reviewed], [Last author, Corresponding author], [International Magazine]
  English, Scientific journal, ATP11C, a plasma membrane phospholipid flippase, maintains the asymmetric distribution of phosphatidylserine accumulated in the inner leaflet. Caspase-dependent inactivation of ATP11C is essential for an apoptotic "eat me" signal, phosphatidylserine exposure, which prompts phagocytes to engulf cells. We show six cryo-EM structures of ATP11C at 3.0-4.0 Å resolution in five different states of the transport cycle. A structural comparison reveals phosphorylation-driven domain movements coupled with phospholipid binding. Three structures of phospholipid-bound states visualize phospholipid translocation accompanied by the rearrangement of transmembrane helices and an unwound portion at the occlusion site, and thus they detail the basis for head group recognition and the locality of the protein-bound acyl chains in transmembrane grooves. Invariant Lys880 and the surrounding hydrogen-bond network serve as a pivot point for helix bending and precise P domain inclination, which is crucial for dephosphorylation. The structures detail key features of phospholipid translocation by ATP11C, and a common basic mechanism for flippases is emerging.
• Crystal structure of a human plasma membrane phospholipid flippase.
  Hanayo Nakanishi; Katsumasa Irie; Katsumori Segawa; Kazuya Hasegawa; Yoshinori Fujiyoshi; Shigekazu Nagata; Kazuhiro Abe
  The Journal of biological chemistry, 295, 30, 10180, 10194, 24 Jul. 2020, [Peer-reviewed], [Last author, Corresponding author], [International Magazine]
  English, Scientific journal, ATP11C, a member of the P4-ATPase flippase, translocates phosphatidylserine from the outer to the inner plasma membrane leaflet, and maintains the asymmetric distribution of phosphatidylserine in the living cell. We present the crystal structures of a human plasma membrane flippase, ATP11C-CDC50A complex, in a stabilized E2P conformation. The structure revealed a deep longitudinal crevice along transmembrane helices continuing from the cell surface to the phospholipid occlusion site in the middle of the membrane. We observed that the extension of the crevice on the exoplasmic side is open, and the complex is therefore in an outward-open E2P state, similar to a recently reported cryo-EM structure of yeast flippase Drs2p-Cdc50p complex. We noted extra densities, most likely bound phosphatidylserines, in the crevice and in its extension to the extracellular side. One was close to the phosphatidylserine occlusion site as previously reported for the human ATP8A1-CDC50A complex, and the other in a cavity at the surface of the exoplasmic leaflet of the bilayer. Substitutions in either of the binding sites or along the path between them impaired specific ATPase and transport activities. These results provide evidence that the observed crevice is the conduit along that phosphatidylserine traverses from the outer leaflet to its occlusion site in the membrane and suggest that the exoplasmic cavity is important for phospholipid recognition. They also yield insights into how phosphatidylserine is incorporated from the outer leaflet of the plasma membrane into the transmembrane.
• Isoform-selective regulation of mammalian cryptochromes
  Simon Miller; You Lee Son; Yoshiki Aikawa; Eri Makino; Yoshiko Nagai; Ashutosh Srivastava; Tsuyoshi Oshima; Akiko Sugiyama; Aya Hara; Kazuhiro Abe; Kunio Hirata; Shinya Oishi; Shinya Hagihara; Ayato Sato; Florence Tama; Kenichiro Itami; Steve A. Kay; Megumi Hatori; Tsuyoshi Hirota
  Nature Chemical Biology, 16, 6, 676, 685, Springer Science and Business Media {LLC}, 30 Jun. 2020, [Peer-reviewed], ［Internationally co-authored］, [International Magazine]
  English, Scientific journal, CRY1 and CRY2 are essential components of the circadian clock controlling daily physiological rhythms. Accumulating evidences indicate distinct roles of these highly homologous proteins, in addition to redundant functions. Therefore, the development of isoform-selective compounds represents an effective approach towards understanding the similarities and differences of CRY1 and CRY2 by controlling each isoform individually. We conducted phenotypic screenings of circadian clock modulators, and identified KL101 and TH301 that selectively stabilize CRY1 and CRY2, respectively. Crystal structures of CRY-compound complexes revealed conservation of compound-binding sites between CRY1 and CRY2. We further discovered a unique mechanism underlying compound selectivity in which the disordered C-terminal region outside the pocket was required for the differential effects of KL101 and TH301 against CRY isoforms. By using these compounds, we found a new role of CRY1 and CRY2 as enhancers of brown adipocyte differentiation, providing the basis of CRY-mediated regulation of energy expenditure.
• Purified F-ATP synthase forms a Ca2+-dependent high-conductance channel matching the mitochondrial permeability transition pore
  Andrea Urbani; Valentina Giorgio; Andrea Carrer; Cinzia Franchin; Giorgio Arrigoni; Chimari Jiko; Kazuhiro Abe; Shintaro Maeda; Kyoko Shinzawa-Itoh; Janna F. M. Bogers; Duncan G. G. McMillan; Christoph Gerle; Ildikò Szabò; Paolo Bernardi
  Nature Communications, 10, 1, 4341, 4341, Springer Science and Business Media {LLC}, Dec. 2019, [Peer-reviewed], ［Internationally co-authored］, [International Magazine]
  English, Scientific journal, The molecular identity of the mitochondrial megachannel (MMC)/permeability transition pore (PTP), a key effector of cell death, remains controversial. By combining highly purified, fully active bovine F-ATP synthase with preformed liposomes we show that Ca2+ dissipates the H+ gradient generated by ATP hydrolysis. After incorporation of the same preparation into planar lipid bilayers Ca2+ elicits currents matching those of the MMC/PTP. Currents were fully reversible, were stabilized by benzodiazepine 423, a ligand of the OSCP subunit of F-ATP synthase that activates the MMC/PTP, and were inhibited by Mg2+ and adenine nucleotides, which also inhibit the PTP. Channel activity was insensitive to inhibitors of the adenine nucleotide translocase (ANT) and of the voltage-dependent anion channel (VDAC). Native gel-purified oligomers and dimers, but not monomers, gave rise to channel activity. These findings resolve the long-standing mystery of the MMC/PTP and demonstrate that Ca2+ can transform the energy-conserving F-ATP synthase into an energy-dissipating device.
• A single K+-binding site in the crystal structure of the gastric proton pump
  Yamamoto Kenta; Dubey Vikas; Irie Katsumasa; Nakanishi Hanayo; Khandelia Himanshu; Fujiyoshi Yoshinori; Abe Kazuhiro
  ELIFE, 8, eLife Sciences Publications, Ltd, 22 Aug. 2019, [Peer-reviewed], [Last author, Corresponding author], ［Internationally co-authored］, [International Magazine]
  English, Scientific journal, The gastric proton pump (H+,K+-ATPase), a P-type ATPase responsible for gastric acidification, mediates electro-neutral exchange of H+ and K+ coupled with ATP hydrolysis, but with an as yet undetermined transport stoichiometry. Here we show crystal structures at a resolution of 2.5 Å of the pump in the E2-P transition state, in which the counter-transporting cation is occluded. We found a single K+ bound to the cation-binding site of the H+,K+-ATPase, indicating an exchange of 1H+/1K+ per hydrolysis of one ATP molecule. This fulfills the energy requirement for the generation of a six pH unit gradient across the membrane. The structural basis of K+ recognition is resolved and supported by molecular dynamics simulations, establishing how the H+,K+-ATPase overcomes the energetic challenge to generate an H+ gradient of more than a million-fold—one of the highest cation gradients known in mammalian tissue—across the membrane.
• K+ binding and proton redistribution in the E2P state of the H+, K+-ATPase
  Dubey, Vikas; Han, Minwoo; Kopec, Wojciech; Solov'yov, Ilia A.; Abe, Kazuhiro; Kh; elia, Himanshu
  Scientific Reports, 8, 24 Aug. 2018, [Peer-reviewed], ［Internationally co-authored］, [International Magazine]
  English
• Crystal structures of the gastric proton pump.
  Kazuhiro Abe; Katsumasa Irie; Hanayo Nakanishi; Hiroshi Suzuki; Yoshinori Fujiyoshi
  Nature, 556, 7700, 214, 218, Apr. 2018, [Peer-reviewed], [Lead author, Corresponding author], ［Internationally co-authored］, [International Magazine]
  English, Scientific journal, The gastric proton pump-the H+, K+-ATPase-is a P-type ATPase responsible for acidifying the gastric juice down to pH 1. This corresponds to a million-fold proton gradient across the membrane of the parietal cell, the steepest known cation gradient of any mammalian tissue. The H+, K+-ATPase is an important target for drugs that treat gastric acid-related diseases. Here we present crystal structures of the H+, K+-ATPase in complex with two blockers, vonoprazan and SCH28080, in the luminal-open state, at 2.8 Å resolution. The drugs have partially overlapping but clearly distinct binding modes in the middle of a conduit running from the gastric lumen to the cation-binding site. The crystal structures suggest that the tight configuration at the cation-binding site lowers the pK a value of Glu820 sufficiently to enable the release of a proton even into the pH 1 environment of the stomach.
• The Elusive Proton in the Gastric Proton Potassium ATPase
  Dubey Vikas; Abe Kazuhiro; Solov'yov Ilia; Khandelia Himanshu
  BIOPHYSICAL JOURNAL, 114, 3, 146A-146A, 02 Feb. 2018, [Peer-reviewed]
  English, Scientific journal
• The cryo-EM structure of gastric H+, K+-ATPase with bound BYK99, a high-affinity member of K+-competitive, imidazo[1,2-a]pyridine inhibitors
  Kazuhiro Abe; Jun Shimokawa; Mao Naito; Keith Munson; Olga Vagin; George Sachs; Hiroshi Suzuki; Kazutoshi Tani; Yoshinori Fujiyoshi
  SCIENTIFIC REPORTS, 7, 6632, Jul. 2017, [Peer-reviewed], [Lead author, Corresponding author], ［Internationally co-authored］, [International Magazine]
  English, Scientific journal
• Cryo-electron microscopy for structure analyses of membrane proteins in the lipid bilayer
  Kazuhiro Abe; Yoshinori Fujiyoshi
  CURRENT OPINION IN STRUCTURAL BIOLOGY, 39, 71, 78, Aug. 2016, [Peer-reviewed], [Lead author, Corresponding author], [International Magazine]
  English
• Two-Dimensional Crystallization of Gastric H+,K+-ATPase for Structural Analysis by Electron Crystallography
  Abe, Kazuhiro
  P-Type Atpases: Methods and Protocols, 1377, 2016, [Peer-reviewed], [Lead author, Last author, Corresponding author], [International Magazine]
  Scientific journal
• Isolation of H+,K+-ATPase-enriched Membrane Fraction from Pig Stomachs
  Abe, Kazuhiro; Olesen, Claus
  P-Type Atpases: Methods and Protocols, 1377, 2016, [Peer-reviewed], [Lead author, Corresponding author], [International Magazine]
  Scientific journal
• Systematic comparison of molecular conformations of H+,K+-ATPase reveals an important contribution of the A-M2 linker for the luminal gating.
  Abe, K; Tani, K; Fujiyoshi, Y
  J. Biol. Chem., 289, 44, 30590-30601, 17 Sep. 2014, [Peer-reviewed], [Lead author, Corresponding author], [International Magazine]
  English, Scientific journal
• Biochemical and electron crystallographic studies of gastric proton pump
  Abe, K
  Seikagaku, 86, 4, 429-440, 440, Japanese Biochemical Society, Aug. 2014, [Peer-reviewed], [Lead author, Last author, Corresponding author], [Domestic magazines]
  Japanese
• Carbon sandwich preparation preserves quality of two-dimensional crystals for cryo-electron microscopy
  Fan Yang; Kazuhiro Abe; Kazutoshi Tani; Yoshinori Fujiyoshi
  MICROSCOPY, 62, 6, 597, 606, Dec. 2013, [Peer-reviewed], [Lead author], [International Magazine]
  English, Scientific journal
• The four-transmembrane protein IP39 of Euglena forms strands by a trimeric unit repeat.
  Hiroshi Suzuki; Yasuyuki Ito; Yuji Yamazaki; Katsuhiko Mineta; Masami Uji; Kazuhiro Abe; Kazutoshi Tani; Yoshinori Fujiyoshi; Sachiko Tsukita
  Nature communications, 4, 1766, 1766, 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Strand formation by a trimeric unit repeat of four-transmembrane proteins in Euglena
  H. Suzuki; Y. Ito; Y. Yamazaki; K. Mineta; M. Uji; K. Abe; K. Tani; Y. Fujiyoshi; S. Tsukita
  Nat. Commun, 4, 2013, [Peer-reviewed]
  English, Scientific journal
• Cryo-EM structure of gastric H+,K+-ATPase with a single occupied cation-binding site
  Kazuhiro Abe; Kazutoshi Tani; Thomas Friedrich; Yoshinori Fujiyoshi
  PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 109, 45, 18401, 18406, Nov. 2012, [Peer-reviewed], [Lead author, Corresponding author], ［Internationally co-authored］, [International Magazine]
  English, Scientific journal
• [Unique properties of gastric H+, K(+)-ATPase and conserved conformational changes among P-type ATPases].
  Abe, Kazuhiro
  Seikagaku. The Journal of Japanese Biochemical Society, 84, 2, 115-119, Feb. 2012, [Peer-reviewed]
  Japanese, Scientific journal
• Conformational rearrangement of gastric H+,K+-ATPase induced by an acid suppressant
  Kazuhiro Abe; Kazutoshi Tani; Yoshinori Fujiyoshi
  NATURE COMMUNICATIONS, 2, 155, 1-9, Jan. 2011, [Peer-reviewed]
  English, Scientific journal
• A novel ratchet mechanism of gastric H+,K+-ATPase revealed by electron crystallography of two-dimensional crystals
  Kazuhiro Abe; Kazutoshi Tani; Tomohiro Nishizawa; Yoshinori Fujiyoshi
  Yakugaku Zasshi, 130, 2, 205, 210, Feb. 2010, [Peer-reviewed]
  Japanese
• Structural analysis of gastric proton pump by cryo-electron microscopy.
  Abe, K
  顕微鏡, 45, 264-267, 2010, [Peer-reviewed]
  Japanese, Scientific journal
• Structural and functional characterization of H+,K+-ATPase with bound fluorinated phosphate analogs.
  Abe, K; Tani, K; Fujiyoshi, Y
  Journal of Structural Biology, 170, 60-68, 2010, [Peer-reviewed]
  English, Scientific journal
• Epigallocatechin-3-gallate is an inhibitor of Na+,K+-ATPase by favoring the E-1 conformation
  Hideo Ochiai; Kazuo Takeda; Shiori Soeda; Yoshikazu Tahara; Hitoshi Takenaka; Kazuhiro Abe; Yutaro Hayashi; Shunsuke Noguchi; Masumi Inoue; Silvia Schwarz; Wolfgang Schwarz; Masaru Kawamura
  BIOCHEMICAL PHARMACOLOGY, 78, 8, 1069, 1074, Oct. 2009, [Peer-reviewed]
  English, Scientific journal
• E2P State Stabilization by the N-terminal Tail of the H,K-ATPase beta-Subunit Is Critical for Efficient Proton Pumping under in Vivo Conditions
  Katharina L. Duerr; Kazuhiro Abe; Neslihan N. Tavraz; Thomas Friedrich
  JOURNAL OF BIOLOGICAL CHEMISTRY, 284, 30, 20147, 20154, Jul. 2009, [Peer-reviewed]
  English, Scientific journal
• Inter-subunit interaction of gastric H+,K+-ATPase prevents reverse reaction of the transport cycle.
  Abe, K; Tani, K; Nishizawa, T; Fujiyoshi, Y
  EMBO Journal, 28, 11, 1637-1643, 1643, 2009, [Peer-reviewed]
  English, Scientific journal
• Structural analysis of 2D crystals of gastric H+,K+-ATPase in different states of the transport cycle.
  Nishizawa, T; Abe, K; Tani, K; Fujiyoshi, Y
  Journal of Structural Biology, 162, 2, 219-228, 228, 2008, [Peer-reviewed], [Lead author]
  English, Scientific journal
• Relationship between activity and tetraprotomeric structure of ion-transporting ATPases
  Kazuhiro Abe; Shunji Kaya
  SEIKAGAKU, 79, 6, 527, 534, Jun. 2007, [Peer-reviewed]
  Japanese, Scientific journal
• New evidence for ATP binding induced catalytic subunit interactions in pig kidney Na/K-ATPase
  Kan Tanoue; Shunji Kaya; Yutaro Hayashi; Kazuhiro Abe; Toshiaki Imagawa; Kazuya Taniguchi; Kazuyasu Sakaguchil
  JOURNAL OF BIOCHEMISTRY, 140, 4, 599, 607, Oct. 2006, [Peer-reviewed]
  English, Scientific journal
• Evidence for a relationship between activity and the tetraprotomeric assembly of solubilized pig gastric H/K-ATPase
  K Abe; S Kaya; K Taniguchi; Y Hayashi; T Imagawa; M Kikumoto; K Oiwa; K Sakaguchi
  JOURNAL OF BIOCHEMISTRY, 138, 3, 293, 301, Sep. 2005, [Peer-reviewed]
  English, Scientific journal
• Correlation between the activities and the oligomeric forms of pig gastric H/K-ATPase
  K Abe; S Kaya; Y Hayashi; T Imagawa; M Kikumoto; K Oiwa; T Katoh; M Yazawa; K Taniguchi
  BIOCHEMISTRY, 42, 51, 15132, 15138, Dec. 2003, [Peer-reviewed]
  English, Scientific journal
• The tetrameric nature of kidney Na/K-ATPase and gastric H/K-ATPase
  Taniguchi, K; Kaya, S; Abe, K; Imagawa, T; Hayashi, Y; Katoh, T
  Biophysical Journal, 84, 2, 2003, [Peer-reviewed]
  Scientific journal
• K+ induced simultaneous liberation of two moles of Pi, one from one mole of EP and the other from EATP, of oligomeric H/K-ATPase from pig stomach
  Abe, K.; Kaya, S.; Imagawa, T.; Taniguchi, K.
  Annals of the New York Academy of Sciences, 986, 2003, [Peer-reviewed]
  Scientific journal
• Oligomeric structure of P-type ATPases observed by single molecule detection technique
  S Kaya; K Abe; K Taniguchi; M Yazawa; T Katoh; M Kikumoto; K Oiwa; Y Hayashi
  NA,K-ATPASE AND RELATED CATION PUMPS, 986, 278, 280, 2003, [Peer-reviewed]
  English, Scientific journal
• Gastric H/K-ATPase liberates two moles of P(i) from one mole of phosphoenzyme formed from a high-affinity ATP binding site and one mole of enzyme-bound ATP at the low-affinity site during cross-talk between catalytic subunits
  K Abe; S Kaya; T Imagawa; K Taniguchi
  BIOCHEMISTRY, 41, 7, 2438, 2445, Feb. 2002, [Peer-reviewed]
  English, Scientific journal
• The oligomeric nature of Na/K-transport ATPase
  K Taniguchi; S Kaya; K Abe; S Mardh
  JOURNAL OF BIOCHEMISTRY, 129, 3, 335, 342, Mar. 2001, [Peer-reviewed]
  English
• Simultaneous presence of 0.5 mol of phosphoenzyme and acid labile enzyme bound ATP in pig stomach H/K-ATPase
  Abe, K; Kaya, S; Taniguchi, K
  Biophysical Journal, 80, 1, 2001, [Peer-reviewed]
  Scientific journal
• New aspects of Na/K-ATPase; Acid labile ATP and/or ADP/Pi binding to the tetraprotomer
  Taniguchi, K; Kaya, S; Yokoyama, T; Abe, K; Katoh, T; Yazawa, M; Hayashi, Y; Mardh, S
  Biophysical Journal, 78, 1, 2000, [Peer-reviewed]
  Scientific journal
• Acid-labile ATP and/or ADP/P-i binding to the tetraprotomeric form of Na/K-ATPase accompanying catalytic phosphorylation-dephosphorylation cycle
  T Yokoyama; S Kaya; K Abe; K Taniguchi; T Katoh; M Yazawa; Y Hayashi; S Mardh
  JOURNAL OF BIOLOGICAL CHEMISTRY, 274, 45, 31792, 31796, Nov. 1999, [Peer-reviewed]
  English, Scientific journal
• Tetraprotomeric hypothesis of Na/K-ATPase
  TANIGUCHI Kazuya; KAYA Shunnji; YOKOYAMA Takeshi; ABE Kazuhiro
  Folia Pharmacologica Japonica, 114, 3, 179, 184, The Japanese Pharmacological Society, 01 Sep. 1999, [Peer-reviewed]
  Japanese, Since the discovery of Na/K-ATPase by Skou, the mechanism of Na K-dependent ATP hydrolysis and Na and K transport has been extensively studied. The hydrolysis appears to occur sequentially via the Na-Enzyme-ATP complex (NaE1ATP), ADP-sensitive phosphoenzyme (NaE1P), the K-sensitive phosphoenzyme (E2P) and the K-occluded enzyme (KE2), known the Post-Albers mechanism, in a protomer or diprotomer that consists of α- and β-chains. The tetrameric nature of the enzyme such as a quarter, half, third to fourth and full site reactivity and the visualization by electron microscopy show direct biochemical evidence for the presence of a tetraprotomer structure of Na/K-ATPase during ATP hydrolysis. ATP binding is followed by two parallel paths, which occur at each of the two half sites for phosphorylation-dephosphorylation, and direct ATP hydrolysis via (NaE1P : E·ATP)₂, (E2P : E·ATP : E2P : E·ADP/Pi) and (KE2 : E·ADP/Pi)₂, respectively. The sequential formation of E2P from NaE1P and KE2 from E2P is accompanied by, respectively, hydrolysis of half of the TCA-labile bound ATP to ADP/Pi and of another half of the bound ATP to ADP/Pi. All reaction intermediates detectable in the Post-Albers scheme bind ATP and/or ADP/Pi.

• Crystal and cryo-EM structures of phospholipid flippase ATP11C, a ”Death Pump”
  中西華代; 西澤知宏; 瀬川勝盛; 濡木理; 藤吉好則; 長田重一; 阿部一啓; 阿部一啓, 日本生体エネルギー研究会討論会講演要旨集, 46th, 2020
• Structural determinants for the K⁺-binding stoichiometry in the E2P state of gastric H⁺,K⁺-ATPase
  山本健太; 入江克雅; 藤吉好則; 阿部一啓; 山本健太; 入江克雅; 藤吉好則; 阿部一啓, 日本生体エネルギー研究会討論会講演要旨集, 45th, 2019
• 胃プロトンポンプH⁺,K⁺-ATPaseのK⁺結合構造解析
  山本健太; 山本健太; 入江克雅; 入江克雅; 藤吉好則; 藤吉好則; 阿部一啓; 阿部一啓, 日本生体エネルギー研究会討論会講演要旨集, 44th, 2018
• 胃プロトンポンプH⁺,K⁺-ATPaseのK⁺結合構造解析
  山本健太; 山本健太; 入江克雅; 入江克雅; 藤吉好則; 藤吉好則; 阿部一啓; 阿部一啓, 日本生体エネルギー研究会討論会講演要旨集, 44th, 2018
• 胃プロトンポンプの2.8Å分解能結晶構造解析
  阿部一啓; 阿部一啓; 阿部一啓; 入江克雅; 入江克雅; 中西華代; 中西華代; 藤吉好則; 藤吉好則, 日本生体エネルギー研究会討論会講演要旨集, 43rd, 2017
• Unique properties of gastric H+ K+-ATPase and conserved conformational changes among P-type ATPases
  Kazuhiro Abe, Seikagaku, 84, 2, 115, 119, 2012
  Japanese, Book review
• Conformational rearrangement of gastric H+,K+-ATPase with an acid suppressant.
  Abe, K; Tani, K; Fujiyoshi, Y, Nature Communications, 2, 155, 1-9, Jan. 2011
  English, Report scientific journal
• Structural and functional characterization of H+,K+-ATPase with bound fluorinated phosphate analogs
  Kazuhiro Abe; Kazutoshi Tani; Yoshinori Fujiyoshi, JOURNAL OF STRUCTURAL BIOLOGY, 170, 1, 60, 68, Apr. 2010
  English, Report scientific journal
• High and low affinity ATP effects on both NaE1 and KE2 of Na/K-ATPase studied by substrate analogues.
  K Tanoue; S Kaya; K Abe; T Imagawa; Y Hayashi; K Sakaguchi; K Taniguchi, JOURNAL OF GENERAL PHYSIOLOGY, 126, 1, 41A, 42A, Jul. 2005
  English, Summary international conference
• K+-induced change in oligomeric assembly of C12E8-solubilized pig gastric H/K-ATPase observed by single-molecule detection techniques.
  K Abe; S Kaya; K Sakaguchi; T Imagawa; Y Hayashi; K Taniguchi, JOURNAL OF GENERAL PHYSIOLOGY, 126, 1, 34A, 35A, Jul. 2005
  English, Summary international conference
• Presence of two different ATP effects on both Na-bound and Rb-occluded Na/K-ATPase
  K Taniguchi; K Tanoue; K Abe; S Kaya; T Imagawa; K Sakaguchi, BIOPHYSICAL JOURNAL, 86, 1, 192A, 192A, Jan. 2004
  English, Summary international conference

• AIが描く胃薬の未来図 cryo-EMとDeep Quartetが拓く新たな阻害剤のデザイン「実験医学増刊：構造生命科学 AlphaFold時代にどう活かす？〜生命機能を解く、変える、創るための技術と研究戦略」
  阿部一啓; 横島 聡; 吉森篤史
  羊土社, 05 Sep. 2025, 9784758104296, 214, 163, Japanese, Scholarly book, [Contributor]
• Methods in Molecular Biology, P-type ATPases, 39 Two-dimensional crystallization of gastric H+,K+-ATPase for structural analysis by electron crystallography
  Abe K
  Springer, Jan. 2016, 9781493931781, 433-458, English, [Single work]
• Methods in Molecular Biology, P-type ATPases, 4 Isoration of H+,K+-ATPase-enriched membrane fraction from pig stomach
  Abe K; Olesen C
  Springer, Jan. 2016, 9781493931781, 19-28, English, [Joint work]

• Development of de novo inhibitors for the gaslrlc proton pump with cryo-EM structure and deepgenerallve model
  Kazuhiro Abe
  The 82nd Annual Meeting of the Japanese Society of Microscopy, 27 May 2026, The Japanese Society of Microscopy, Japanese, Invited oral presentation
  25 May 2026 - 27 May 2026, 仙台市, Japan, [Invited]
• 胃の酸性化の秘密～胃プロトンポンプの構造生理学
  阿部 一啓
  13 Mar. 2026, Japanese, Invited oral presentation
  13 Mar. 2026 - 13 Mar. 2026, Japan, [Invited], [Domestic Conference]
• 疾病変異体を模したATP11CフリッパーゼQ79E変異体の構造機能解析によって明らかにされたリン脂質認識の分子基盤
  阿部 一啓
  日本生体エネルギー研究会 第51回討論会, 11 Dec. 2025, Japanese, Oral presentation
  11 Dec. 2025 - 13 Dec. 2025, Japan, [Domestic Conference]
• P2-type ATPaseによるH⁺ とNa⁺ の特異性についての考察
  阿部一啓
  cQUESTシンポジウム「膜タンパク質内部のイオン透過を考える」, 10 Dec. 2025, Japanese, Invited oral presentation
  10 Dec. 2025 - 11 Dec. 2025, Japan, [Invited]
• Structural physiology of the primary transporters P-type ATPase
  Kazuhiro Abe
  The 55th NIPS International Symposium "The forefront and future prospects of ion channel. research", 03 Dec. 2025, English, Invited oral presentation
  01 Dec. 2025 - 04 Dec. 2025, Japan, [Invited]
• Regulation of cell function and fate by cell membrane assembly
  Kazuhiro Abe
  The 98th Annual Meeting of the Japanese Biochemical Society, Symposium 2S07e, 04 Nov. 2025, English, Nominated symposium
  03 Nov. 2025 - 05 Nov. 2025, 京都市, Japan, [Invited], [International presentation]
• 胃プロトンポンプの構造情報と AI によって駆動された新規阻害剤のde novo デザイン
  阿部一啓
  第 53 回構造活性相関シンポジウム, 04 Sep. 2025, Japanese, Invited oral presentation
  04 Sep. 2025 - 05 Sep. 2025, 東大阪市, Japan, [Invited]
• AI-driven de novo drug design based on the cryo-EM structure of the gastric proton pump
  Kazuhiro Abe
  The 1st HU-NYCU DDP Symposium on Chemistry, 04 Jul. 2025, English, Invited oral presentation
  04 Jul. 2025 - 05 Jul. 2025, Sapporo, Japan, [Invited], [International presentation]
• Molecular biochemistry of the gastric proton pump and related P-ATPases
  Kazuhiro Abe
  Academia Sinica IBC seminar, 27 Jun. 2025, Academia Sinica, English, Invited oral presentation
  Academia Sinica, Taipei, Taiwan, Province of China, [Invited]
• Structural physiology of plasma membrane flippase ATP11C
  阿部一啓
  The 25th Annual Meeting of the Protein Science Society of Japan, 18 Jun. 2025, Japanese, Invited oral presentation
  18 Jun. 2025 - 20 Jun. 2025, [Invited]
• 細胞膜脂質フリッパーゼATP11Cの構造生理学
  阿部一啓
  第45回生体膜と薬物の相互作用 シンポジウム, 10 Oct. 2024, 日本薬学会物理系薬学部会, Japanese, Invited oral presentation
  徳島, [Invited]
• Structural physiology of P-type ATPases that generate asymmetric distributions of cations and phospholipids
  Kazuhiro Abe
  "Biased assembly" in Neuroscience and Cell Biology, 23 Sep. 2024, Academia Sinica, English, Invited oral presentation
  23 Sep. 2024 - 24 Sep. 2024, Academia Sinica, Taipei, Taiwan, Province of China, [Invited]
• 能動輸送体 P-type ATPase の構造生理学
  阿部一啓
  2024年度生理研研究会「生理機能の理解に向けた膜タンパク質機能ダイナミクス研究の最前線と未来開拓」, 02 Sep. 2024, Japanese, Invited oral presentation
  Japan, [Invited]
• Structural physiology of gastric proton pump and related cation pumps
  Kazuhiro Abe
  The 15th CSE International Summer School & The 12th ALP International Symposium, 24 Aug. 2024, 北海道大学大学院総合化学院, English, Invited oral presentation
  Japan, [Invited]
• 能動輸送体 P-type ATPaseの分子生命化学
  阿部一啓
  第61回日本生化学会北海道支部例会, 20 Jul. 2024, Japanese, Invited oral presentation
  [Invited]
• Structural physiology of gastric proton pump and related cation pumps
  Kazuhiro Abe
  IUPAB2024, 24 Jun. 2024, English, Invited oral presentation
  [Invited]
• 胃プロトンポンプのクライオ電顕構造に基づいたAIによる新規薬剤のデザイン
  阿部一啓
  第80回顕微鏡学会, 04 Jun. 2024, Japanese, Invited oral presentation
  [Invited]
• カチオン能動輸送体の構造生理学と創薬
  阿部一啓
  第101回日本生理学会大会, 28 Mar. 2024, Japanese, Invited oral presentation
  [Invited]
• 構造解析による胃の酸性化メカニズムとAIを利用した胃酸抑制剤の開発
  阿部一啓
  循環器研究ユニットシンポジウム, 29 Feb. 2024, Japanese, Invited oral presentation
  [Invited]
• Structural physiology of Gastric proton pump
  Kazuhiro Abe
  Lecture Biochemistry Molecular Medicine Special Lecture, 05 Feb. 2024, English, Invited oral presentation
  [Invited]
• Deep learning driven de novo drug design based on gastric proton pump structures
  Kazuhiro Abe
  4th Alpine Conference on Medicinal and Synthetic Chemistry, 01 Feb. 2024, English, Invited oral presentation
  [Invited]
• Crystal structures of the gastric proton pump - molecular basis for the binding of acid suppressants, H+-extrusion and K+-counter-transport
  Kazuhiro Abe
  日本薬学会, 27 Mar. 2020, English, Invited oral presentation
  京都, [International presentation]
• Structural basis of the proton extrusion mechanism of the gastric proton pump
  Kazuhiro Abe
  第97回日本生理学会大会, 17 Mar. 2020, English, Invited oral presentation
  大分, [Invited], [International presentation]
• Molecular mechanisms for the drug binding, H+-extrusion and the K+ counter-transport
  Kazuhiro Abe
  Academia Sinica IBC seminar, 12 Dec. 2019, Academia Sinica, English, Invited oral presentation
  Academia Sinica, Taipei, [Invited], [Domestic Conference]
• Crystal structure of the gastric proton pump
  Kazuhiro Abe
  World Laureates Forum 2nd conference, 28 Oct. 2019, World Laureates Association, English, Poster presentation
  Shanghai, China, [Invited], [Domestic Conference]
• X線結晶学とクライオ電顕で得られた構造情報の上手な活用法 ～胃プロトンポンプの構造解析を例として～
  阿部一啓
  2019年度生理研研究会, 30 Sep. 2019, 生理学研究所, Japanese, Keynote oral presentation
  大阪, [Invited], [Domestic Conference]
• 胃プロトンポンプの輸送機構に対する構造基盤
  阿部一啓
  生物物理第57回年会 台湾‐日本 二国間シンポジウム：X線結晶構造解析とクライオ電顕2019, 24 Sep. 2019, 日本生物物理学会, English, Invited oral presentation
  宮崎, [Invited], [Domestic Conference]
• Structural basis for the H+-extrusion and the K+-occlusion of the gastric proton pump
  Abe K
  Society of General Physiology /SOBLA 2019, 03 Sep. 2019, Society of General Physiology /SOBLA, English, Invited oral presentation
  Valparaiso, Chile, [Invited], [Domestic Conference]
• Crystal structure of the gastric proton pump
  Kazuhiro Abe; Kenta Yamamoto; Katsumasa Irie; Hanayo Nakanishi; Yoshinori Fujiyoshi
  GRC membrane transport, 01 Jul. 2019, English, Oral presentation
  Colby Sawyer, NH, USA, [Domestic Conference]
• 胃の強酸性化の分子メカニズム ‐胃プロトンポンプの結晶構造解析
  阿部一啓
  日本生体エネルギー研究会 第４４回討論会, 06 Dec. 2018, Japanese, Invited oral presentation
  千葉大学, [Invited], [International presentation]
• Crystal structures of the gastric proton pump
  Kazuhiro Abe
  AsCA2018, 02 Dec. 2018, English, Oral presentation
  Auckland, NZ, [Invited], [Domestic Conference]
• 1. 胃プロトンポンプの結晶構造によって明らかになったH+排出機構
  阿部一啓
  大阪大学蛋白質研究所セミナー 構造生物学と計算科学の融合による動的構造生物学の新しい展開, Sep. 2018, Japanese, Invited oral presentation
  [Invited], [International presentation]
• 胃プロトンポンプの結晶構造
  阿部一啓
  第９１回日本生化学会大会 シンポジウム 生化学から広がる膜輸送体研究の深化,, Sep. 2018, Japanese, Invited oral presentation
  [Domestic Conference]
• 3. 胃の強酸性化の秘密
  阿部一啓
  創薬等ライフサイエンス研究支援基盤事業 平成30年度BINDS公開 シンポジウム「知って、使って、進む あなたの研究」, Sep. 2018, Japanese, Invited oral presentation
  [Invited], [International presentation]
• 4. 胃プロトンポンプの構造生理学～胃酸に対してプロトンを押し出すメカニズム～
  阿部一啓
  大阪大学蛋白質研究所セミナー 構造情報に基づいた膜イオン輸送タ ンパク質の生理機能の解明に向けて, Sep. 2018, 大阪大学蛋白質研究所, Japanese, Invited oral presentation
  [Invited], [International presentation]
• Structural basis for the H+ extrusion and the transport stoichiometry of the gastric proton pump
  Kazuhiro Abe
  Frontiers in P-type ATPase Research 2018, Institute for Quantitative Bioscience, Jul. 2018, The University of Tokyo, English, Invited oral presentation
  The University of Tokyo, [Invited], [International presentation]
• Crystal structure of the gastric proton pump at 2.8A resolution
  Kazuhiro Abe
  日本生体エネルギー研究会, 19 Dec. 2017, Japanese, Oral presentation
  [International presentation]
• Structural and functional analysis of gastric proton pump and acid suppressants
  Kazuhiro Abe
  ConBio2017, 06 Dec. 2017, English, Nominated symposium
  神戸国際会議場, [International presentation]
• Structural and functional analysis of gastric H+,K+-ATPase
  Kazuhiro Abe
  The 15th international conference on Na,K-ATPase and related transport ATPases, 24 Sep. 2017, English, Invited oral presentation
  Otsu, Japan, [Invited], [Domestic Conference]
• 胃プロトンポンプの構造生理学
  阿部一啓
  日本物理学会 第72回年次大会, 18 Mar. 2017, Japanese, Invited oral presentation
  大阪大学, [Invited], [International presentation]
• Binding model of the acid suppressant to the gastric proton pump
  Abe K
  Japan Biophysical Society meeting, 25 Nov. 2016, English, Invited oral presentation
  筑波, [Invited], [International presentation]
• 日本生化学会
  阿部一啓
  第89回日本生化学会大会, 25 Sep. 2016, 日本生化学会, Japanese, Invited oral presentation
  東北大学, [Invited], [International presentation]
• 電子線結晶学と機能解析に基づいた胃プロトンポンプの構造生理学
  阿部一啓
  大阪大学蛋白質研究所セミナー 『膜タンパク質の構造ダイナミクス』 Structural dynamics of membrane proteins, 12 May 2016, Japanese, Invited oral presentation
  大阪大学, [Invited], [International presentation]
• 胃プロトンポンプの構造生理学
  阿部一啓
  千里ライフサイエンスセミナーＫ２ トランスポーターと創薬～構造と病態からのアプローチ～, 06 May 2016, 公益財団法人 千里ライフサイエンス振興財団, Japanese, Invited oral presentation
  千里ライフサイエンスセンタービル 5階 山村雄一記念ライフホール, [Invited], [International presentation]
• Electron crystallographic analysis of gastric proton pump
  Kazuhiro Abe
  IPR Seminar "Introduction and overview of cryo-electron microscopy", 19 Feb. 2016, English, Invited oral presentation
  [International presentation]
• 胃H+,K+-ATPaseの 胃酸抑制剤結合状態についての考察
  阿部一啓
  日本生体エネルギー研究会 第４１回 討論会, 22 Dec. 2015, Japanese, Oral presentation
  [International presentation]
• Mutational analysis of acid surppressant binding site of gastric proton pump based on its structural model
  Kazuhiro ABE; Kazutoshi Tani; Mao Naito; Jun Shimokawa; Yoshinori Fujiyoshi
  第38回日本分子生物学会年会 第88回日本生化学会大会 合同大会, 01 Dec. 2015, English, Poster presentation
  [International presentation]
• Antagonist-bound structure of gastric proton pump
  Abe K
  第５３回日本生物物理学会年会, 13 Sep. 2015, English, Invited oral presentation
  金沢, [International presentation]
• Structural physiology of gastric proton pump
  Abe K
  Denmark-Japan Joint Workshop on Ion Transport Proteins, 02 Sep. 2015, English, Invited oral presentation
  RIKEN, Yokohama, [Domestic Conference]
• Electron crystallographic and mutational analysis of acid suppressant-bound gastric proton pump
  阿部 一啓
  日本顕微鏡学会第７１回学術講演会, 10 May 2015, Japanese, Oral presentation
  [International presentation]
• Systematic comparison of the molecular conformation of gastric H+,K+-ATPase in E2P state analogs
  阿部一啓
  日本生体エナルギー研究会 第40回討論会, 11 Dec. 2014, Japanese, Invited oral presentation
  [International presentation]
• 胃プロトンポンプH+,K+-ATPaseの構造生理学
  阿部一啓
  第3回 九州地区 生理薬理系研究会, 04 Dec. 2014, Japanese, Keynote oral presentation
  [International presentation]
• Electron crystallographic analysis of gastric proton pump
  Abe, K
  JEM Next-Generation Microscopic Science, 03 Nov. 2014, English, Invited oral presentation
  [International presentation]
• Systematic comparison of the molecular conformation of gastric H+,K+-ATPase in E2P state analogs
  阿部一啓
  日本生化学会第87回大会, Oct. 2014, Japanese, Oral presentation
  [International presentation]
• Structural and biochemical analysis of gastric H+,K+-ATPase in E2P-analogue conformations
  Abe, K
  ASBMB Special symposia, Na,K-ATPase and related transport ATPases: Structure, Mechanism, Cell Biology, Health and Disease, 30 Aug. 2014, English, Invited oral presentation
  Luteren, Netherlands, [Domestic Conference]
• 胃プロトンポンプの構造生理学
  阿部一啓
  第9回トランスポーター研究会, Jun. 2014, Japanese, Invited oral presentation
  [Domestic Conference]
• 胃プロトンポンプの阻害剤結合構造から見えてきたE2P遷移状態における構造変化
  阿部一啓
  日本生体エネルギー研究会第39回討論会, 18 Dec. 2013, 日本生体エネルギー研究会, Japanese, Poster presentation
  静岡, [International presentation]
• 胃プロトンポンプの極低温電子顕微鏡による構造解析
  阿部一啓
  第４回神経科学と構造生物学の融合研究会, 20 Nov. 2013, Japanese, Invited oral presentation
  岡崎コンファレンスセンター, [International presentation]
• 電子顕微鏡のイメージから膜タンパク質の立体構造を再構成する～胃プロトンポンプの例を中心として～
  阿部一啓
  分析化学会中部支部愛知地区講演会, 24 Oct. 2013, 日本分析化学会, Japanese, Invited oral presentation
  名古屋大学, [International presentation]
• Biochemical and electron crystallographic studies of gastric proton pump
  Kazuhiro Abe
  The 86th Annual Meeting of the Japanese Biochemical Society, 11 Sep. 2013, Japanese Biochemical Society, English, Oral presentation
  Yokohama, [International presentation]
• 胃プロトンポンプの生化学と電子線結晶構造解析
  阿部一啓
  第86回日本生化学会 奨励賞受賞講演, 11 Sep. 2013, 日本生化学会, Japanese, Invited oral presentation
  横浜, [International presentation]
• Cryo-EM structures of gastric proton pump
  Abe K
  FAOBMB mini-symposium, Apr. 2013, FAOBMB, English, Invited oral presentation
  Iwate Medical University, [Domestic Conference]
• Unique properties and conserved conformational changes found in gastric H+,K+-ATPase
  Abe K; Tani K; Fujiyoshi Y
  Nagoya Symposium, Jan. 2013, English, Poster presentation
  Nagoya University, [Domestic Conference]
• 電子線結晶学による胃プロトンポンプの立体構造解析
  阿部一啓
  生体エネルギー研究会第38回討論会, Dec. 2012, 日本生体エネルギー研究会, Japanese, Invited oral presentation
  岡山大学, [Domestic Conference]
• 胃H+,K+-ATPaseの逆反応防止機構とその解除-- (K+)E2~P構造を中心として
  阿部一啓
  生体エネルギー研究会 第37回討論会, Dec. 2011, Japanese, Oral presentation
  京都産業大学 京都, [International presentation]
• Unique structures and conserved conformational changes found in gastric H+,K+-ATPase
  Kazuhiro Abe
  2011 ASBMB sepcial symposia, Na/K-ATPase and related P-ATPases, 27 Sep. 2011, English, Invited oral presentation
  Asilomar Conference ground, Pacific grove, CA, [Domestic Conference]
• 電子線結晶学によって明らかになった胃H+,K+-ATPaseのユニークな構造とP型ATPaseファミリー間で保存された構造変化
  阿部一啓
  第84回日本生化学会大会, Sep. 2011, Japanese, Oral presentation
  京都国際会議場 京都, [International presentation]
• Conformational rearrangement of gastric H+,K+-ATPase induced by an acid suppressant
  Kazuhiro Abe
  Direct imaging in Bio/Medical science, 18 Jan. 2011, JSPS Stockholm office, English, Poster presentation
  Lund University, Sweden, [Domestic Conference]
• Three-dimensional structure of gastric H+,K+-ATPase with unti-ulcer drug
  Kazuhiro Abe
  FASEB SRC, transport ATPase, Jun. 2010, FASEB, English, Oral presentation
  Snowmass, CO, [Domestic Conference]
• 電子線結晶学により明らかになった胃プロトンポンプの逆反応防止機構
  阿部一啓
  生体エネルギー研究会 第35回討論会, 18 Dec. 2009, 生体エネルギー研究会, Japanese, Invited oral presentation
  旭川医科大学, [International presentation]
• 胃プロトンポンプのサブユニット間相互作用による逆反応防止機構
  阿部一啓
  第82回日本生化学会大会, 19 Oct. 2009, 日本生化学会, Japanese, Invited oral presentation
  神戸国際会議場, [International presentation]
• A Novel Ratchet Mechanism of Gastric H+,K+-ATPase Revealed by Cryo-Electron Microscopy
  阿部一啓; 谷一寿; 西澤知宏; 藤吉好則
  日本薬学会年会 第129年会, 26 Mar. 2009, 日本薬学会, Japanese, Invited oral presentation
  京都国際会議場 京都, [International presentation]
• A Novel Ratchet Mechanism of Gastric H+,K+-ATPase Revealed by Electron Crystallography of Two-Dimensional Crystals
  阿部一啓; 谷一寿; 西澤知宏; 藤吉好則
  トランスポートソーム若手WS, Jan. 2009, 特定領域 トランスポートソーム, Japanese, Oral presentation
  神戸セミナーハウス, [International presentation]
• Three-dimensional structure of gastric H/K-ATPase at 6.5 Å resolution determined by electron crystallography of two-dimensional crystals
  Kazuhiro Abe; Kazutoshi Tani; Tomohiro Nishizawa; Yoshinori Fujiyoshi
  17th Meeting of Methods in Protein Structure Analysis (MPSA2008), 26 Aug. 2008, English, Invited oral presentation
  Hokkaido University, Japan, [Domestic Conference]
• Structure of gastric H+,K+-ATPase at 8-Å resolution
  Kazuhiro Abe
  12th International PATPase conference, Na,K-ATPase and Related Transport ATPases, 05 Aug. 2008, English, Invited oral presentation
  Aahus University, Demmark, [Domestic Conference]
• Structural Analysis of 2D crystals of Gastric H+, K+-ATPase in different states of the transport cycle
  阿部一啓
  日本電子顕微鏡学会, 20 Dec. 2007, Japanese, Oral presentation
  産総研 台場 東京, [International presentation]
• Two-dimensional crystallization of pig gastric H/K-ATPase
  Kazuhiro Abe; Tomohiro Nishizawa; Kazutoshi Tani; Yoshinori Fujiyoshi
  The 16th International Microscopy Congress, 03 Sep. 2006, IFSM, SCJ, JSM, English, Poster presentation
  Sapporo Convention Center, Sapporo, Japan, [Domestic Conference]
• Two-dimensional Crystallografic Study of Pig Gastric H/K-ATPase
  Kazuhiro Abe; Tomohiro Nishizawa; Kazutoshi Tani; Yoshinori Fujiyoshi
  IUBMB Cation pump meeting, Jul. 2006, IUBMB, English, Poster presentation
  Kyoto research park, Kyoto, Japan, [Domestic Conference]
• K+-induced change in oligomeric assembly of C12E8-solubilized pig gastric H/K-ATPase observed by single-molecule detection technique.
  Kazuhiro Abe; Shunji Kaya; Kazuyashu Sakaguchi; Toshiaki Imagawa; Yutaro Hayashi; Kazuya Taniguchi
  Na,K-ATPase & Related Cation Pumps, 05 Sep. 2005, Society of General Physiology, English, Poster presentation
  MBL, Woods Hole, MA, [Domestic Conference]
• Investigation of tetraprotomeric structure of pig gastric H/K-ATPase based on single-molecule detection techniques
  Abe K; Kaya S; Kikumoto M; Oiwa K; Katoh T; Yazawa M; Taniguchi K
  FASEB Summer Research Conference, Transport ATPases: Genomics to Mechanism and Releavnce to Diseases, Jul. 2003, FASEB, English, Oral presentation
  Saxton River, Vermont, [Domestic Conference]
• K+ induced simultaneous liberation of two moles of Pi one from mole of EP and the other from EATP of oligomeric H/K-ATPase from pig stomach
  Kazuhiro Abe; Shunji Kaya; Toshiaki Imagawa; Kazuya Taniguchi
  10th International Conference on Na/K-ATPase and Related Cation Pumps, Aug. 2002, English, Invited oral presentation
  Elsinore, Denmark, [Domestic Conference]

• 生物化学Ａ（Ⅰ）, 2024年, 修士課程, 総合化学院
• 基礎生物化学特論, 2024年, 修士課程, 総合化学院
• 先端総合化学特論Ⅱ, 2024年, 博士後期課程, 総合化学院
• 機能生化学, 2024年, 学士課程, 理学部
• 生物化学Ⅱ, 2024年, 学士課程, 理学部

• The Biophysical Society of Japan
• 日本生化学会

• Elucidation of the molecular basis of novel ribitol phosphate modifications and their pathophysiological roles
  Grants-in-Aid for Scientific Research
  01 Apr. 2025 - 31 Mar. 2030
  金川 基; 阿部 一啓; 山口 芳樹; 永森 收志
  Japan Society for the Promotion of Science, Grant-in-Aid for Scientific Research (A), Ehime University, 25H01023
• 物質不均衡分布形成原理の理解を目指した能動輸送体P型ATPaseの構造機能生理学
  科学研究費助成事業
  01 Apr. 2024 - 31 Mar. 2027
  阿部 一啓
  日本学術振興会, 基盤研究(B), 北海道大学, 24K01975
• 物質不均衡分布を司る能動輸送体P型ATPaseの構造機能生理学
  科学研究費助成事業
  01 Apr. 2021 - 31 Mar. 2024
  阿部 一啓
  日本学術振興会, 基盤研究(B), 名古屋大学, 21H02426
• クライオ電子顕微鏡のフィードバックに基づく膜タンパク質複合体の生産と技術支援
  創薬等ライフサイエンス研究支援基盤事業
  Apr. 2017 - Mar. 2022
  大嶋篤典
  国立研究開発法人日本医療研究開発機構, Competitive research funding
• 胃プロトンポンプを初めとしたヒト能動輸送体の構造機能解析と創薬への展開
  内藤記念科学奨励金・研究助成
  Dec. 2019 - Sep. 2021
  阿部一啓
  公益財団法人 内藤記念科学振興財団, Competitive research funding
• 物質不均衡を司る能動輸送体の構造解析と創薬
  上原記念生命科学財団 研究助成金
  Dec. 2019 - Apr. 2021
  阿部一啓
  公益財団法人 上原記念生命科学財団, Competitive research funding
• 胃酸分泌の分子メカニズム解明と新規薬剤開発の為の構造基盤
  生命科学研究助成
  Nov. 2018 - Mar. 2021
  阿部一啓
  武田科学振興財団, Principal investigator, Competitive research funding
• 胃プロトンポンプの構造生理学研究
  科学研究費助成事業
  Apr. 2017 - Mar. 2021
  日本学術振興会, 基盤研究(B), Competitive research funding
• Studies in structural physiology of channels
  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (S)
  29 May 2015 - 31 Mar. 2020
  FUJIYOSHI Yoshinori
  Structural information of membrane proteins including channels is crucial toward gaining a better understanding of biologic functions. The information that can be gained from a protein structure strongly depends on its resolution - the higher the resolution, the more insight gained into the structure-function relationship of biologic macromolecules. We analyzed structures of proton pump, water channel AQP4, whose inhibitor could be a drug for brain edema, Na+ channel, gap junction channels and tight junction channels at high resolutions. While we could not get significant results of AChR, we analyzed structures of endothelin receptor and its complexes with the agonist and antagonists. In this project, we could get important knowledge in the research field named as structural physiology and partly elucidate how the channels work and regulate functions of the human body. We also contributed advancement of cryo-electron microscopy by developing cryo-electron microscopes.
  Japan Society for the Promotion of Science, Grant-in-Aid for Scientific Research (S), 15H05775
• 細胞膜におけるリン脂質の非対称分布とその崩壊
  戦略的創造研究推進事業
  Oct. 2014 - Mar. 2020
  文部科学省, Competitive research funding
• 最大級のイオン濃度勾配を形成する胃プロトンポンプ作動機構の解明
  科学研究費助成事業
  Apr. 2014 - Mar. 2018
  日本学術振興会, 若手研究(A), Competitive research funding
• 多様な顕微鏡技術による膜タンパク質複合体の多階層での機能構造研究
  創薬等支援技術基盤プラットフォーム補助金
  Oct. 2012 - Mar. 2017
  文部科学省, Competitive research funding
• Structural and functional study of membrane proteins based on electron crystallography
  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (S)
  01 Apr. 2010 - 31 Mar. 2015
  FUJIYOSHI Yoshinori; OHSHIMA Atsunori; ABE Kazuhiro
  In this project, we studied structure and function of water channels, ion channels, gap junction channels, acetylcholine receptor, claudins and H+,K+-ATPase, because these membrane proteins are important components in biological systems. We could obtain significant results in these research subjects by mainly electron and X-ray crystallography.
  For example, we intensively studied adhennels, channels with adhesive function. Claudin is an adhennel family protein and a key molecule in tight junctions. We analyzed structure of claudin-15 and proposed a paracellular channel model to explain channel function through epithelial cell sheets. We also analyzed the complex structure of claudin-19 and the C-terminal domain of Clostridium perfringens enterotoxin, which causes disintegration of tight junctions. These results are of great interest for both basic biology and the rational design of therapeutic agents that can potentially be used to deliver drugs across tissue barriers.
  Japan Society for the Promotion of Science, Grant-in-Aid for Scientific Research (S), 22227004
• Electron crystallographic analysis of two dimensional crystals of membrane proteins maintaining proton gradient
  Grants-in-Aid for Scientific Research
  01 Apr. 2010 - 31 Mar. 2014
  TANI Kazutoshi; FUJIYOSHI Yoshinori; ABE Kazuhiro
  Our developed software package for electron crystallography is very powerful and effective to determine three dimensional structures of membrane proteins reconstituted into lipid bilayers including aquaporin-4 and gastric H+,K+-ATPase. Using electron crystallography of two-dimensional crystals, we could elucidate their structures and conformational changes during molecular passages.
  Japan Society for the Promotion of Science, Grant-in-Aid for Young Scientists (B), 22770147
• 電子線結晶学と酵素化学的研究に基づいた胃プロトンポンプのユニークな作動機構の解明
  科学研究費助成事業
  Apr. 2012 - Mar. 2014
  日本学術振興会, 若手研究(スタートアップ), Competitive research funding
• ４量体Ｈ／Ｋ－ＡＴＰaseの構造機能連関～４量体構造の生理的意義の解明～ (1701307)
  科学研究費助成事業
  Apr. 2006 - Mar. 2009
  阿部 一啓
  日本学術振興会, 特別研究員奨励費, Principal investigator, Competitive research funding
• P型‐ATPaseの多量体構造と機能の相関 (1509844)
  科学研究費助成事業
  Apr. 2004 - Mar. 2006
  阿部 一啓
  日本学術振興会, 特別研究員奨励費, Principal investigator, Competitive research funding