2024

  1. Characterization of different-sized human αA-crystallin homomers and implications to Asp151 isomerization.
    Sun J, Matsubara T, Koide T, Lampi K, David L and Takata T. PLOS ONE. accepted (2024).

  1. Characterization of βB2-crystallin tryptophan mutants reveals two different folding states in solution. 
    Sun J, Morishima K, Inoue R, Sugiyama M and Takata T. Protein science. 33, e5092 (2024).

2023

  1. Eye lens β-crystallins are predicted by native ion mobility-mass spectrometry and computations to form compact higher-ordered heterooligomers.
    Rolland AD, Takata T, Donor MT, Lampi KJ, Prell JS. Structure (2023)

  1. Characterization of K-binding factor involved in water-soluble complex of menaquinone-7 produced by Bacillus subtilis natto. 
    Chatake T, Yanagisawa Y, Murakami R, Ohsugi T, Sumi H, Takata T, Okuda A, Morishima K, Inoue R, Sugiyama M. Journal of biochemistry (2023)

    2022
  2. 質量分析装置を用いたタンパク質中D型アミノ酸残基の同定
    髙田匠 分析化学 (2022)

    2021

  3. Isomerization of Asp is essential for assembly of amyloid-like fibrils of αA-crystallin-derived peptide.
    Magami K, Hachiya N, Morikawa K, Fujii N and Takata T. PLoS One (2021).

  1. Elucidation of the mechanism of subunit exchange in αB crystallin oligomers.
    Inoue R, Sakamaki Y, Takata T, Wood K, Morishima K, Sato N, Okuda A, Shimizu M, Urade R, Fujii N I and Sugiyama M. Sci Rep (2021).

    2020

  2. Effect of a Lens Protein in Low-Temperature Culture of Novel Immortalized Human Lens Epithelial Cells (iHLEC-NY2).
    Yamamoto N, Takeda S, Hatsusaka N, Hiramatsu N, Nagai N, Deguchi S, Nakazawa Y, Takata T, Kodera S, Hirata A, Kubo E and Sasaki H. Cells (2020).

  3. Simultaneous and Rapid Detection of Multiple Epimers and Isomers of Aspartyl Residues in Lens Proteins using an LC-MS-MRM Method.
    Fujii N, Takata T, Kim I and Matsubara T. ACS Omega (2020).

  4. Asp Isomerization Increases Aggregation of α-Crystallin and Decreases Its Chaperone Activity in Human Lens of Various Ages.
    Fujii N, Takata T, Kim I, Morihisma K, Inoue R, Magami K, Matsubara T, Sugiyama M and Koide T. Biochim Biophys Acta -Proteins Proteom, 1868, 140446 (2020).

  5. Age-related isomerization of Asp in human immunoglobulin G kappa chain.
    Ha S, Kinouchi T and Fujii N. Biochim Biophys Acta -Proteins Proteom, 1868, 140410 (2020).

  6. A single Asp isomer substitution in an αA-crystallin-derived peptide induces a large change in peptide properties.
    Magami K, Kim I and Fujii N. Exp Eye Res. 192, 107930 (2020).

  7. Site-Specific Rapid Deamidation and Isomerization in Human Lens αA-crystallin in vitro.
    Takata T, Ha S, Koide T and Fujii N. Protein science. 29, 955-965 (2020).

2019

  1. Negative Charge at Aspartate 151 is Important for Human Lens αA-crystallin Stability and Chaperone Function.
    Takata T, Toshiya M, Nakamura-Hirota T and Fujii N. Exp Eye Res. 182, 10-18 (2019).

2018

  1. Asp58 modulates lens αA-crystallin oligomer formation and chaperone function.
    Takata T, Nakamura-Hirota T, Inoue R, Morishima K, Sato N, Sugiyama M and Fujii N. FEBS J. 285, 2263-2277 (2018).

  2. Identification of Isomeric Aspartate residues in βB2-crystallin from Aged Human Lens.
    Takata T, Murakami K, Toyama A and Fujii N. Biochim Biophys Acta -Proteins Proteom, 1866, 767-774 (2018).

2017

  1. Identification of ᴅ-amino acid-containing peptides in human serum.
    Ha S, Kim I, Takata T, Kinouchi T,  Isoyama M, Suzuki M, Fujii N.  PLoS ONE 12(12): e0189972. (2017).

  2. Ferulic Acid Suppresses Amyloid β Production in the Human Lens Epithelial Cell Stimulated with Hydrogen Peroxide.
    Nagai N, Kotani S, Mano Y, Ueno A, Ito Y, Kitaba T, Takata T and Fujii N. Biomed Res Int, 2017:5343010. (2017).

  3. Isomeric replacement of a single aspartic acid induces a marked change in protein function: the example of ribonuclease A.
    Sakaue H, Kinouchi T, Fujii N, Takata T and Fujii N. ACS Omega. 2, 260-267 (2017). 

2016

  1. One-shot LC-MS/MS analysis of post-translational modifications including oxidation and deamidation of rat lens α- and β-crystallins induced by γ-irradiation.
    Kim I, Saito T, Fujii N, Kanamoto T and Fujii N. Amino Acids. 48, 2855-2866 (2016). 

  2. Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.
    Serebryany E, Takata T, Erickson E, Schafheimer N, Wang Y, King JA. Protein science. 6, 1115-1128 (2016).

  3. New insight into the dynamical system of αB-crystallin oligomers.
    Inoue R, Takata T, Fujii N, Ishii K, Uchiyama S, Sato N, Oba Y, Wood K, Kato K, Fujii N and Sugiyama M. Scientific Reports. 6, 29208 (2016).

  4. Isomerization of Asp residues plays an important role in αA-crystallin dissociation.
    Takata T and Fujii N. FEBS J. 283, 850-859 (2016).

2015

  1. Site specific oxidation of amino acid residues in rat lens γ-crystallin induced by low doseγ-irradiation.
    Kim I, Saito T, Fujii N, Kanamoto T, Chatake T and Fujii N. Biochemical and Biophysical Research Communications 466, 622-628 (2015).

  2. Effect of Asp 96 isomerization on the properties of a lens αB-crystallin-derived short peptide.
    Takata T and Fujii N. J Pharm Biomed Anal. 116, 139-144 (2015).

  3. Real-time heterogeneous protein-protein interaction between αA-crystallin N-terminal mutants and αB-crystallin using quartz crystal microbalance (QCM).
    Ramkumar S, Fujii N, Sakaue H, Fujii N, Thankappan B, Kumari RP, Natarajaseenivasan K, Anbarasu K. Amino Acids. 47, 1035-1043 (2015).

  4. Rapid Survey of Four Asp Isomers in Disease-Related Proteins by LC-MS combined with Commercial Enzyme.
    Maeda H, Takata T,Fujii N,Sakaue H, Nirasawa S, Takahashi S, Sasaki H and Fujii N. Anal. Chem. 87, 561-568 (2015).

  5. αB- and βA3-crystallins containing D-Aspartic acids exist in a monomeri c state.
    Sakaue H, Takata T, Fujii N, Sasaki, H and Fujii N Biochimica et Biophysica Acta -Proteins and Proteomics. 1854, 1-9 (2015).

2014

  1. Comparison of effect of gamma ray irradiation on wild-type and N-terminal mutants of αA-crystallin.
    Ramkumar S, Fujii N, Fujii N, Thankappan B, Sakaue H, Ingu K, Natarajaseenivasan K, Anbarasu K. Mol Vis. 20:1002-1016 (2014).

  2. Effects of carotenoids on damage of biological lipids induced by gamma irradiation.
    Saito T. and Fujii N. Radiat. Phys. Chem. 98, 57-63 (2014).

2013

  1. Simultaneous ultraviolet-B induced photo-oxidation of tryptophan/tyrosine and racemization of neighboring aspartyl residues in peptides.
    Cai S, Fujii N, Saito T, and Fujii N. Free Radical Biology & Medicine 65, 1037-1046 (2013).

  2. Kinetics of isomerization and inversion of aspartate 58 of αA-crystallin peptide mimics under physiological conditions.
    Kenzo Aki, Norihiko Fuji and Noriko Fujii. PLoS One. 8 (3):e58515. (2013).

2012

  1. A rapid comprehensive LC-MS based survey of the Asp isomers in crystallins from human cataract lenses.
    Fujii N, Sakaue H. Sasaki H. and *Fujii N. J. Biol Chem. VOL.287, NO.47, PP.39992-40002, (2012).

  2. Characterization of an antibody that recognizes peptides containing D-β-aspartyl residues.
    Kenzo Aki, Norihiko Fujii, Takeshi Saito and Noriko Fujii, Molecular Vision, 18,996-1003(2012).

2011

  1. Characterization and Radio-resistant Function of Manganese Superoxide Dismutase of Rubrobacter radiotolerans.
    H. Terato, K. Suzuki, N. Nishioka, A. Okamoto, Y. Shimazaki-Tokuyama, Y. Inoue and T. Saito J. Radiat. Res. 22, 735-742. (2011).

  2. Simultaneous stereoinversion and isomerization at the Asp-4 residue in βB2-crystallin from the aged human eye lenses.
    Norihiko Fujii, Takeshi Kawaguchi, Hiroshi Sasaki and Noriko Fujii. Biochemistry 50, 8628-8635 (2011).

  3. UV B-irradiation enhances the racemization and isomerizaiton of aspartyl residues and production of Nε-carboxymethyl lysine (CML) in keratin of skin.
    Yuhei Mori, Kenzo Aki, Katsunori Kuge, Natsuko Yamanaka, Shingo Tajima, Yuichi Kaji, Ryoji Nagai, Hanako Yoshii, Naoki Yamamoto, Norihiko Fujii, Masami Watanabe, Tadatoshi Kinouchi and Noriko Fujii. J. Chromatogr. B 879, 3303-3309 (2011).

  4. Substrate stereoselectivity of mammalian D-aspartyl endopeptidase.
    Tadatoshi Kinouchi, Norihiko Fujii and Noriko Fujii. J. Chromatogr. B Analyt Technol Biomed Life Sci. 879, 3349-3352. (2011).

2010

  1. Influence of Lβ-, Dα-, and Dβ-Asp isomers of the Asp-76 residue on the properties of αA-crystallin 70-88 peptide.
    Noriko Fujii, Norihiko Fujii, Masashi Kida and Tadatoshi Kinouchi. Amino Acids 39, 1393-1399 (2010).

  2. The Protective Effects of Metallothionein I and II against Metal- or Ultraviolet Radiation-Induced Damages in Cultured Lens Epithelial Cells.
    Saito T, Tezuka T, Konno R. and Fujii N. Jpn J. Ophthalmol. 54, 486-493 (2010)

  3. Influence of oxidative stress on D-aspartyl endopeptidase activity.
    Tadatoshi Kinouchi, Takahiko Shimizu, Takuji Shirasawa and Noriko Fujii. Chemistry and Biodiversity 7, 1398-1402 (2010).

  4. Structural consideration of mammalian D-aspartyl endopeptidase.
    Tadatoshi Kinouchi and Noriko Fujii. Chemistry and Biodiversity 7, 1403-1407 (2010).

  5. Oxidative Stress Indces the Formation of D-Aspartyl Residues in the Elastin Mimic Peptide.
    Kuge K, Kitamura K, Nakaoji K, Hamada K, Fujii N, Saito T. and Fujii N. Chemistry and Biodiversity 7, 1408-1412 (2010).

  6. Genome-wide expression changes in Saccharomyces cerevisiae in response to high-LET ionizing radiation.
    S. Mizukami-Murata, H. Iwahashi, S. Kimura, K. Nojima, Y. Sakurai, T. Saitou, N. Fujii, Y. Murata, S. Suga, K. Kitagawa, K. Tanaka, S. Endo and M. Hoshi Appl. Biochem. Biotechnol. 162, 855-870.(2010).