原著論文

2016年｜2017年｜2018年｜2019年｜2020年 ｜2021年｜2022年｜2023年｜2024年

2024年

1. Ohgita T., Sakai K., Fukui N., Namba N., Nakano M., Kiguchi Y., Morita I., Oyama H., Yamaki K., Nagao K., Kobayashi N., and Saito H.
   Generation of novel anti-apoE monoclonal antibodies that selectively recognize apoE isoforms.
   FEBS Lett. 598(8), 902-914 (2024). doi: 10.1002/1873-3468.14858
2. Gima S., Oe K., Nishimura K., Ohgita T., Ito H., Kimura H., Saito H., and Takata K.
   Host-to-graft propagation of inoculated α-synuclein into transplanted human induced pluripotent stem cell-derived midbrain dopaminergic neurons.
   Regen. Ther. 25, 229-237 (2024). doi: 10.1016/j.reth.2023.12.019

 

2023年

1. Fukuda A., Nakashima S., Oda Y., Nishimura K., Kawashima H., Kimura H., Ohgita T., Kawashita E., Ishihara K., Hanaki A., Okazaki M., Matsuda E., Tanaka Y., Nakamura S., Matsumoto T., Akiba S., Saito H., Matsuda H., and Takata K.
   Plantainoside B in Bacopa monniera binds to Aβ aggregates attenuating neuronal damage and memory deficits induced by Aβ.
   Biol. Pharm. Bull. 46(2), 320-333 (2023). doi: 10.1248/bpb.b22-00797
2. Tsuchiya M., Tachibana N., Nagao K., Tamura T., and Hamachi I.
   Organelle-selective click labeling coupled with flow cytometry allows pooled CRISPR screening of genes involved in phosphatidylcholine metabolism.
   Cell Metab. 35(6), 1072-1083 (2023). doi: 10.1016/j.cmet.2023.02.014
3. Ohgita T., Kono H., Morita I., Oyama H., Shimanouchi T., Kobayashi N., and Saito H.
   Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein.
   Sci. Rep. 13, 10885 (2023) doi: 10.1038/s41598-023-38070-4
4. Tachibana H., Minoura K., Omachi T., Nagao K., Ichikawa T., Kimura Y., Kono N., Shimanaka Y., Arai H., Ueda K., and Kioka N.
   The plasma membrane of focal adhesions has a high content of cholesterol and phosphatidylcholine with saturated acyl chains.
   J. Cell Sci. 136 (16), jcs260763 (2023). doi: 10.1242/jcs.260763
5. Namba N., Ohgita T., Tamagaki-Asahina H., Nishitsuji K., Shimanouchi T., Sato T., and Saito H.
   Amyloidogenic 60–71 deletion/ValThr insertion mutation of apolipoprotein A-I generates a new aggregation-prone segment that promotes nucleation through entropic effects.
   Sci. Rep. 13, 18514 (2023). doi: 10.1038/s41598-023-45803-y
6. Takechi-Haraya Y., Ohgita T., Usui A., Nishitsuji K., Uchimura K., Abe Y., Kawano R., Konaklieva M.I., Reimund M., Remaley A.T., Sato Y., Izutsu K., and Saito H.
   Structural flexibility of apolipoprotein E-derived arginine-rich peptides improves their cell penetration capability.
   Sci. Rep.13, 19396 (2023). doi: 10.1038/s41598-023-46754-0

 

2022年

1. Nomura T., Nagao K., Shirai R., Gotoh H., Umeda M., and Ono K.
   Temperature sensitivity of Notch signaling underlies species-specific developmental plasticity and robustness in amniote brains.
   Nat. Commun. 13, 96 (2022). doi: 10.1038/s41467-021-27707-5
2. Takechi-Haraya Y., Ohgita T., Kotani M., Kono H., Saito C., Tamagaki-Asahina H., Nishitsuji K., Uchimura K., Sato T., Kawano R., Sakai-Kato K., Izutsu K., and Saito H.
   Effect of hydrophobic moment on membrane interaction and cell penetration of apolipoprotein E-derived arginine-rich amphipathic α-helical peptides.
   Sci. Rep. 12(1), 4959 (2022). doi: 10.1038/s41598-022-08876-9
3. Murakami A., Nagao K., Sakaguchi R., Kida K., Hara Y., Mori Y., Okabe K., Harada Y., and Umeda M.
   Cell-autonomous control of intracellular temperature by unsaturation of phospholipid acyl chains.
   Cell Rep. 38(11), 110487 (2022). doi: 10.1016/j.celrep.2022.110487
4. Ohgita T., Namba N., Kono H., Shimanouchi T., and Saito H.
   Mechanisms of enhanced aggregation and fibril formation of Parkinson’s disease–related variants of α-synuclein.
   Sci. Rep. 12, 6770 (2022). doi: 10.1038/s41598-022-10789-6
5. Nakano M., Takechi-Haraya Y., Ohgita T., Saito H., Demizu Y., Izutsu K., and Sakai-Kato K.
   Analysis of the interaction of cyclosporine congeners with cell membrane models.
   J. Pharm. Biomed. Anal. 218(5), 114874 (2022). doi: 10.1016/j.jpba.2022.114874
6. Uchimura K., Nishitsuji K, Chiu L.-T., Ohgita T., Saito H., Allain F., Gannedi V., Wong C.-H., and Hung S.-C.
   Design and Synthesis of 6-O-Phosphorylated Heparan Sulfate Oligosaccharides to Inhibit Amyloid β Aggregation.
   ChemBioChem. 23, e202200191 (2022). doi: 10.1002/cbic.202200191
7. Suito T., Nagao K., Juni N., Hara Y., Sokabe T., Atomi H., and Umeda M.
   Regulation of thermoregulatory behavior by commensal bacteria in Drosophila.
   Biosci. Biotechnol. Biochem. 86(8), 1060–1070 (2022). doi: 10.1093/bbb/zbac087
8. Hirano K., Tsuchiya M., Shiomi A., Takabayashi S., Suzuki M., Ishikawa Y., Kawano Y.,
   Takabayashi Y., Nishikawa K., Nagao K., Umemoto E., Kitajima Y., Ono Y., Nonomura K.,
   Shintaku H., Mori Y., Umeda M., and Hara Y.
   The mechanosensitive ion channel PIEZO1 promotes satellite cell function in muscle regeneration.
   Life Sci. Alliance. 6(2), e202201783 (2022). doi: 10.26508/lsa.202201783

 

2021年

1. Ohgita T., Furutani Y., Nakano M., Hattori M., Suzuki A., Nakagawa M., Naniwa S., Morita I., Oyama H., Nishitsuji K., Kobayashi N., and Saito H.
   Novel conformation-selective monoclonal antibodies against apoA-I amyloid fibrils.
   FEBS J. 288(5), 1496-1513 (2021). doi: 10.1111/febs.15487
2. Shiomi A., Nagao K., Yokota N., Tsuchiya M., Kato U., Juni N., Hara Y., Mori M.X., Mori Y., Ui-Tei K., Murate M., Kobayashi T., Nishino Y., Miyazawa A., Yamamoto A., Suzuki R., Kaufmann S., Tanaka M., Tatsumi K., Nakabe K., Shintaku H., Yesylevsky S., Bogdanov M., and Umeda M.
   Extreme deformability of insect cell membranes is governed by phospholipid scrambling.
   Cell Rep. 35(10), 109219 (2021). doi: 10.1016/j.celrep.2021.109219

 

2020年

1. Kurimitsu N., Mizuguchi C., Fujita K., Taguchi S., Ohgita T., Nishitsuji K., Shimanouchi T., and Saito H.
   Phosphatidylethanolamine accelerates aggregation of the amyloidogenic N-terminal fragment of apoA-I.
   FEBS Lett. 594(9), 1443-1452 (2020). doi: 10.1002/1873-3468.13737
2. Ohgita T., Takechi-Haraya Y., Okada K., Matsui S., Takeuchi M., Saito C., Nishitsuji K., Uchimura K., Kawano R., Hasegawa K., Sakai-Kato K., Akaji K., Izutsu K., and Saito H.
   Enhancement of direct membrane penetration of arginine-rich peptides by polyproline II helix structure.
   BBA – Biomembranes 1862, 183403 (2020). doi: 10.1016/j.bbamem.2020.183403
3. Trusova V., Vus K., Zhytniakivska O., Tarabara U., Saito H., and Gorbenko G.
   Nanomechanical characterization of apolipoprotein A-I amyloid fibrils.
   East Eur. J. Phys. 2, 118-123 (2020). doi: 10.26565/2312-4334-2020-2-11
4. Iwahashi N., Ikezaki M., Nishikawa T., Namba N., Ohgita T., Saito H., Ihara Y., Shimanouchi T., Ino K., Uchimura K., and Nishitsuji K.
   Sulfated Glycosaminoglycans Mediate Prion-like Behavior of p53 Aggregates.
   PNAS 117(52), 33225-33234 (2020). doi: 10.1073/pnas.2009931117
5. Suito T., Nagao K., Takeuchi K., Juni N., Hara Y., amd Umeda M.
   Functional expression of Δ12 fatty acid desaturase modulates thermoregulatory behaviour in Drosophila.
   Sci. Rep. 10, 11798 (2020). doi: 10.1038/s41598-020-68601-2
6. Shiomi A., Nagao K., Kasai H., Hara Y., and Umeda M.
   Changes in the physicochemical properties of fish cell membranes during cellular senescence.
   Biosci. Biotechnol. Biochem. 84(3), 583-593 (2020). doi: 10.1080/09168451.2019.1695576

 

2019年

1. Kameyama H., Uchimura K.,Yamashita T., Kuwabara K., Mizuguchi M., Hung S.-C., Okuhira K., Masuda T., Kosugi T., Ohgita T., Saito H., Ando Y., and Nishitsuji K.
   The Accumulation of Heparan Sulfate S-Domains in Kidney Transthyretin Deposits Accelerates Fibril Formation and Promotes Cytotoxicity.
   Am. J. Pathol. 189(2), 308-319 (2019). doi: 10.1016/j.ajpath.2018.09.015
2. Ohgita T., Takechi-Haraya Y., Nadai R., Kotani M., Tamura Y., Nishikiori N., Nishitsuji K., Uchimura K., Hasegawa K., Sakai-Kato K., Akaji K., and Saito H.
   A novel amphipathic cell-penetrating peptide based on the N-terminal glycosaminoglycan binding region of human apolipoprotein E.
   BBA - Biomembranes 1861(3), 541-549 (2019). doi: 10.1016/j.bbamem.2018.12.010
3. Mizuguchi C., Nakagawa M., Namba N., Sakai M., Kurimitsu N., Suzuki A., Fujita K., Horiuchi S., Baba T., Ohgita T., Nishitsuji K., and Saito H.
   Mechanisms of Aggregation and Fibril Formation of the Amyloidogenic N-terminal Fragment of Apolipoprotein A-I.
   J. Biol. Chem. 294(36), 13515-13524 (2019). doi: 10.1074/jbc.RA119.008000
4. Gorbenko G., Trusova V., Gadjev N., Deligeorgiev T., Mizuguchi C., and Saito H.
   Two-step FRET as a tool for probing the amyloid state of proteins.
   J. Mol. Liquids 294, 111675 (2019). doi: 10.1016/j.molliq.2019.111675
5. Sakai-Kato K., Yoshida K., Ohgita T., Takechi-Haraya Y., Demizu Y., and Saito H.
   Refining Calibration Procedures of Circular Dichroism Spectrometer to Improve Usability.
   Anal. Sci. 35, 1275-1278 (2019). doi: 10.2116/analsci.19N022
6. Matsuo N., Nagao K., Suito T., Juni N., Kato U., Hara Y., and Umeda M.
   Different mechanisms for selective transport of fatty acids using a single class of lipoprotein in Drosophila.
   J. Lipid Res. 60(7), 1199-1211 (2019). doi: 10.1194/jlr.M090779

 

2018年

1. Mizuguchi C., Nakamura M., Kurimitsu N., Ohgita T., Nishitsuji K., Baba T., Shigenaga A., Shimanouchi T., Okuhira K., Otaka A., and Saito H.
   Effect of Phosphatidylserine and Cholesterol on Membrane-mediated Fibril Formation by the N-terminal Amyloidogenic Fragment of Apolipoprotein A-I.
   Sci. Rep. 8(1), 5497 (2018). doi: 10.1038/s41598-018-23920-3
2. Gorbenko G., Trusova V., Mizuguchi C., Saito H. Lipid bilayer interactions of amyloidogenic N-terminal fragment of apolipoprotein A-I probed by Förster resonance energy transfer and molecular dynamics simulations.
   J. Fluoresc. 28(5), 1037-1047 (2018). doi: 10.1007/s10895-018-2267-7

3. Suito T., Nagao K., Hatano M., Kohashi K., Tanabe A., Ozaki H., Kawamoto J., Kurihara T., Mioka T., Tanaka K., Hara Y., Umeda M.
   Synthesis of omega-3 long-chain polyunsaturated fatty acid-rich triacylglycerols in an endemic goby, Gymnogobius isaza, from Lake Biwa, Japan.

   J. Biochem. 164(2), 127-140 (2018). doi: 10.1093/jb/mvy035

 

2017年

1. Okuhira K., Shoda T., Omura R., Ohoka N., Hattori T., Shibata N., Demizu Y. , Sugihara R., Ichino A., Kawahara H., Itoh Y., Ishikawa M., Hashimoto Y., Kurihara M., Itoh S., Saito H., and Naito M.
   Targeted Degradation of Proteins Localized in Subcellular Compartments by Hybrid Small Molecules.
   Mol. Pharmacol. 91(3), 159-166 (2017). doi: 10.1124/mol.116.105569
2. Kimura H., Mikawa S., Mizuguchi C., Horie Y., Morita I., Oyama H., Ohgita T., Nishitsuji K., Takeuchi A., Sissel Lund-Katz, Akaji K., Kobayashi N., and Saito H.
   Immunochemical Approach for Monitoring of Structural Transition of ApoA-I upon HDL Formation Using Novel Monoclonal Antibodies.
   Sci. Rep. 7, 2988 (2017). doi: 10.1038/s41598-017-03208-8
3. Vus K., Girych M., Trusova V., Gorbenko G., Kinnunen P., Mizuguchi C., and Saito H.
   Fluorescence study of the effect of the oxidized phospholipids on amyloid fibril formation by the apolipoprotein A-I N-terminal fragment.
   Chem. Phys. Lett. 688, 1-6 (2017). doi: 10.1016/j.cplett.2017.09.037
4. Takechi-Haraya Y., Aki K., Tohyama Y., Harano Y., Kawakami T., Saito H., and Okamura E.
   Glycosaminoglycan Binding and Non-Endocytic Membrane Translocation of Cell-Permeable Octaarginine Monitored by Real-Time In-Cell NMR Spectroscopy.
   Pharmaceuticals 10(2), 42 (2017). doi: 10.3390/ph10020042
5. Murakami A., Nagao K., Hara Y., Juni N., and Umeda M.
   An N-terminal di-proline motif is essential for fatty acid-dependent degradation of Δ9-desaturase in Drosophila.
   J. Biol. Chem. 292(49), 19976-19986 (2017). doi: 10.1074/jbc.M117.801936

 

2016年

1. Daimon Y., Kamei N., Kawakami K., Takeda-Morishita M., Izawa H., Takechi-Haraya Y., Saito H., Sakai H., Abe M., and Ariga K.
   Dependence of intestinal absorption profile of insulin on carrier morphology composed of β-cyclodextrin-grafted chitosan.
   Mol. Pharm. 13(12), 4034-4042 (2016). doi: 10.1021/acs.molpharmaceut.6b00561
2. Hasan M., Tarashima N., Fujikawa K., Ohgita T., Hama S., Tanaka T., Saito H., Minakawa N., and Kogure K.
   The novel functional nucleic acid iRed effectively regulates target genes following cytoplasmic delivery by faint electric treatment.
   Sci. Technol. Adv. Mater. 17(1), 554-562 (2016). doi: 10.1080/14686996.2016.1221726
3. Mikawa S., Mizuguchi C., Nishitsuji K., Baba T., Shigenaga A., Shimanouchi T., Sakashita N., Otaka A., Akaji K., and Saito H.
   Heparin Promotes Fibril Formation by the N-Terminal Fragment Amyloidogenic Apolipoprotein A-I.
   FEBS Lett. 590(20), 3492-3500 (2016). doi: 10.1002/1873-3468.12426
4. Sakane A., Yoshizawa S., Nishimura M., Tsuchiya Y., Matsushita N., Miyake K., Horikawa K., Imoto I., Mizuguchi C., Saito H., Ueno T., Matsushita S., Haga H., Deguchi S., Mizuguchi K., Yokota H., and Sasaki T.
   Conformational plasticity of JRAB/MICAL-L2 provides 'law and order' in collective cell migration.
   Mol. Biol. Cell 27(20), 3095-3108 (2016). doi: 10.1091/mbc.E16-05-0332
5. Girych M., Gorbenko G., Maliyov I., Trusova V., Mizuguchi C., Saito H., and Kinnunen P.
   Combined Thioflavin T - Congo Red Fluorescence Assay for Amyloid Fibril Detection.
   Methods Appl. Fluoresc. 4(3), 034010 (2016). doi: 10.1088/2050-6120/4/3/034010
6. Kameyama H., Nakajima H., Nishitsuji K., Mikawa S., Uchimura K., Kobayashi N., Okuhira K., Saito H., and Sakashita N.
   Iowa Mutant Apolipoprotein A-I (ApoA-IIowa) Fibrils Target Lysosomes.
   Sci. Rep. 6, 30391 (2016). doi: 10.1038/srep30391
7. Takechi-Haraya Y., Nadai R., Kimura H., Nishitsuji K., Uchimura K., Sakai-Kato K., Kawakami K.,Shigenaga A., Kawakami T., Otaka A., Hojo H., Sakashita N., and Saito H.
   Enthalpy-driven interactions with sulfated glycosaminoglycans promote cell membrane penetration of arginine peptides.
   BBA - Biomembranes 1858(6), 1339-1349 (2016). doi: 10.1016/j.bbamem.2016.03.021
8. Kariyazono H., Nadai R., Miyajima R., Takechi-Haraya Y., Baba T., Shigenaga A., Okuhira K., Otaka A., and Saito H.
   Formation of stable nanodiscs by bihelical apolipoprotein A-I mimetic peptide.
   J. Peptide Sci. 22(2), 116-122 (2016). doi: 10.1002/psc.2847
9. Nakajima H., Nishitsuji K., Kawashima H., Kuwabara K., Mikawa S., Uchimura K., Akaji K., Kashiwada Y., Saito H., and Sakashita N.
   The polyphenol (-)-epigallocathechin -3-gallate prevents apoA-I Iowa amyloidosis in vitro and protects human embryonic kidney 293 cells from the amyloid cytotoxicity.
   Amyloid 23(1), 17-25 (2016). doi: 10.3109/13506129.2015.1113167
10. 新村　航，假屋園大和，木村　仁，斎藤博幸.
    ナノディスクのサイズ制御と安定性におけるアポA-Iへリックス構造の役割．
    膜（Membrane）41(2), 74-80 (2016).
11. Hasan M., Nishimoto A., Ohgita T., Hama S., Kashida H., Asanuma H., and Kogure K.
    Faint electric treatment-induced rapid and efficient delivery of extraneous hydrophilic molecules into the cytoplasm.
    J. Control. Release 228, 20-25 (2016). doi: 10.1016/j.jconrel.2016.02.048
12. Takagi K., Ohgita T., Yamamoto T., Shinohara Y., and Kogure K.
    Transmission of External Environmental pH Information to the Inside of Liposomes via Pore-Forming Proteins Embedded within the Liposomal Membrane.
    Chem. Pharm. Bull. 64(5), 432-438 (2016). doi: 10.1248/cpb.c15-00985