Kyushu University Academic Staff Educational and Research Activities Database
List of Papers
Yoshito Abe Last modified date:2020.02.26

Associate Professor / Department of Bio-Pharmaceutical Sciences / Department of Pharmaceutical Health Care and Sciences / Faculty of Pharmaceutical Sciences


Papers
1. Rattanapisit K, Phakham T, Buranapraditkun S, Siriwattananon K, Boonkrai C, Pisitkun T, Hirankarn N, Strasser R, Abe Y, Phoolcharoen W., Structural and In Vitro Functional Analyses of Novel Plant-Produced Anti-Human PD1 Antibody, Scientific Reports, 10.1038/s41598-019-51656-1., 9, 1, 15205, 2019.10.
2. Naoya Shindo, Hirokazu Fuchida, Mami Sato, Kosuke Watari, Tomohiro Shibata, Keiko Kuwata, Chizuru Miura, Kei Okamoto, Yuji Hatsuyama, Keisuke Tokunaga, Seiichi Sakamoto, Satoshi Morimoto, Yoshito Abe, Mitsunori Shiroishi, Jose M M Caaveiro, Tadashi Ueda, Tomonori Tamura, Naoya Matsunaga, Takaharu Nakao, Satoru Koyanagi, Shigehiro Ohdo, Yasuchika Yamaguchi, Itaru Hamachi, Mayumi Ono, Akio Ojida, Selective and reversible modification of kinase cysteines with chlorofluoroacetamides, Nature Chemical Biology, 10.1038/s41589-018-0204-3, 2019.01, Irreversible inhibition of disease-associated proteins with small molecules is a powerful approach for achieving increased and sustained pharmacological potency. Here, we introduce α-chlorofluoroacetamide (CFA) as a novel warhead of targeted covalent inhibitor (TCI). Despite weak intrinsic reactivity, CFA-appended quinazoline showed high reactivity toward Cys797 of epidermal growth factor receptor (EGFR). In cells, CFA-quinazoline showed higher target specificity for EGFR than the corresponding Michael acceptors in a wide concentration range (0.1-10 μM). The cysteine adduct of the CFA derivative was susceptible to hydrolysis and reversibly yielded intact thiol but was stable in solvent-sequestered ATP-binding pocket of EGFR. This environment-dependent hydrolysis can potentially reduce off-target protein modification by CFA-based drugs. Oral administration of CFA quinazoline NS-062 significantly suppressed tumor growth in a mouse xenograft model. Further, CFA-appended pyrazolopyrimidine irreversibly inhibited Bruton's tyrosine kinase with higher target specificity. These results demonstrate the utility of CFA as a new class warheads for TCI..
3. Saki Fujiyama, Yoshito Abe, Mitsunori Shiroishi, Yohei Ikeda, Tadashi Ueda, Insight into the interaction between PriB and DnaT on bacterial DNA replication restart
Significance of the residues on PriB dimer interface and highly acidic region on DnaT, Biochimica et Biophysica Acta - Proteins and Proteomics, 10.1016/j.bbapap.2019.01.008, 1867, 4, 367-375, 2019.01, When the replisome collapses at a DNA damage site, a sequence-independent replication restart system is required. In Escherichia coli, PriA, PriB, and DnaT assemble in an orderly fashion at the stalled replication fork and achieve the reloading of the replisome. PriB-DnaT interaction is considered a significant step in the replication restart. In this study, we examined the contribution of the residues Ser20, His26 and Ser55, which are located on the PriB dimer interface. These residues are proximal to Glu39 and Arg44, which are important for PriB-DnaT interaction. Mutational analyses revealed that His26 and Ser20 of PriB are important for the interaction with DnaT, and that the Ser55 residue of PriB might have a role in negatively regulating the DnaT binding. These residues are involved in not only the interaction between PriB and DnaT but also the dissociation of single-stranded DNA (ssDNA) from the PriB-ssDNA complex due to DnaT binding. Moreover, NMR study indicates that the region Asp66-Glu76 on the linker between DnaT domains is involved in the interaction with wild-type PriB. These findings provide significant information about the molecular mechanism underlying replication restart in bacteria..
4. Tatsuhiro Igawa, Shuhei Kishikawa, Yoshito Abe, Tomohiro Yamashita, Saki Nagai, Mitsunori Shiroishi, Chinatsu Shinozaki, Hiroyuki Tanaka, Hidetoshi Tozaki-Saitoh, Makoto Tsuda, Kazuhide Inoue, Tadashi Ueda, Evidence for detection of rat P2X4 receptor expressed on cells by generating monoclonal antibodies recognizing the native structure, Purinergic Signalling, 10.1007/s11302-019-09646-5, 2019.01, P2X purinergic receptors are ATP-driven ionic channels expressed as trimers and showing various functions. A subtype, the P2X4 receptor present on microglial cells is highly involved in neuropathic pain. In this study, in order to prepare antibodies recognizing the native structure of rat P2X4 (rP2X4) receptor, we immunized mice with rP2X4's head domain (rHD, Gln111-Val167), which possesses an intact structure stabilized by S-S bond formation (Igawa and Abe et al. FEBS Lett. 2015), as an antigen. We generated five monoclonal antibodies with the ability to recognize the native structure of its head domain, stabilized by S-S bond formation. Site-directed mutagenesis revealed that Asn127 and Asp131 of the rHD, in which combination of these amino acid residues is only conserved in P2X4 receptor among P2X family, were closely involved in the interaction between rHD and these antibodies. We also demonstrated the antibodies obtained here could detect rP2X4 receptor expressed in 1321N1 human astrocytoma cells..
5. Hinako Hatae, Koji Inaka, Ryo Okamura, Naoki Furubayashi, Masayuki Kamo, Takuya Kobayashi, Yoshito Abe, So Iwata, Naotaka Hamasaki, Crystallization of Human Erythrocyte Band 3, the anion exchanger, at the International Space Station “KIBO”, Analytical Biochemistry, 10.1016/j.ab.2018.08.009, 559, 91-93, 2018.10, Band 3 mediates the Cl and HCO3
exchange across the red blood cell membrane and plays a pivotal role for delivering oxygen appropriately to metabolically active tissues. For understanding molecular mechanisms, it is essential to know the structure and function relationship. In terrestrial environments, however, nobody could make good quality crystals of Band 3 for the X-ray crystallographic study. In this study, we purified the transmembrane domain of Band 3 from human red blood cells and crystallized the purified Band 3 without the Fab fragment at the International Space Station “KIBO” under microgravity environments..
6. Yoshito Abe, Naoki Odawara, Nantanat Aeimhirunkailas, Hinako Shibata, Naoki Fujisaki, Hirofumi Tachibana, Tadashi Ueda, Inhibition of amyloid fibril formation in the variable domain of λ6 light chain mutant Wil caused by the interaction between its unfolded state and epigallocatechin-3-O-gallate, Biochimica et Biophysica Acta - General Subjects, 10.1016/j.bbagen.2018.08.006, 1862, 12, 2570-2578, 2018.12.
7. Miyanabe K, Yamashita T, Abe Y, Akiba H, Takamatsu Y, Nakakido M, Hamakubo T, Ueda T, Caaveiro J, Tsumoto K, Tyrosine sulfation restricts the conformational ensemble of a flexible peptide, strengthening the binding affinity to an antibody., Biochemistry, 57, 28, 4177-4185, 2018.07.
8. Yoshito Abe, Seijiro Shioi, Shunsuke Kita, Hikaru Nakata, Katsumi Maenaka, Daisuke Kohda, Tsutomu Katayama, Tadashi Ueda, X‐ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation., FEBS letter, 592, 22, 3805-3816, 2017.10.
9. Shouhei Mine, Masahiro Watanabe, Saori Kamachi, Yoshito Abe, Tadashi Ueda, The structure of an archaeal β-glucosaminidase provides insight into glycoside hydrolase evolution., J. Biol. Chem., 10.1074/jbc.M116.766535., 292, 12, 4996-5006, 2017.01, 軟骨の成分で知られているグルコサミンを生成するエキソ-β-D-グルコサミニダーゼ (GlmA)の立体構造を明らかにし、これまでアミノ酸配列情報からだけでは不明であった活性部位を特定し、GlmAがなぜグルコサミンを生成できるのかを明らかにした。また、GlmAの立体構造が別酵素であるガラクトシダーゼに似ていることを示した為、これらのガラクトシダーゼが古細菌由来のGlmAから分子進化した可能性がある事が分った。.
10. Yoshito Abe, Mitsuru Kubota, Shinya Takazaki, Yuji Ito, Hiromi Yamamoto, Kang Dongchon, Tadashi Ueda, Taiji Imoto, Effect on catalysis by replacement of catalytic residue from hen egg white lysozyme to Venerupis philippinarum lysozyme, Protein Science, 10.1002/pro.2966, 25, 9, 1637-1647, 2016.06.
11. Takatoshi Arakawa, Takami Kobayashi-Yurugi,, Yilmaz Alguel, Hiroko Iwanari, Hinako Hatae, Momi Iwata, Yoshito Abe, Tomoya Hino, Chiyo Ikeda-Suno, Hiroyuki Kuma, Dongchon Kang, Takeshi Murata, Takao Hamakubo, Alexander D. Cameron, Takuya Kobayashi, Naotaka Hamasaki, Iwata So, Crystal structure of the anion exchanger domain of human erythrocyte band 3, Science, 350, 6261, 680-684, 2015.10, ヒト赤血球膜タンパク質Band3のX線結晶構造解析に携わった。.
12. Yoshito Abe, Naoki Fujisaki, Takanori Miyoshi, Noriko Watanabe, Tsutomu Katayama, Tadashi Ueda, Functional analysis of CedA based on its structure: residues important in binding of DNA and RNA polymerase and in the cell division regulation., J. Biochem., 159, 2, 217-223, 2015.09.
13. Takahiko Aramaki, Yoshito Abe, Kaori Furutani, Tsutomu Katayama, Tadashi Ueda, Basic and aromatic residues in the C-terminal domain of PriC are involved in ssDNA and SSB binding., J. Biochem., 157, 529-537, 2015.02.
14. Tatsuhiro Igawa, Yoshito Abe, Tsuda Makoto, Kazuhiko Inoue, Tadashi Ueda, Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding., FEBS letter, 589, 6, 680-686, 2015.03.
15. Yoshito Abe, Takatoshi Ohkuri, Sachiko Yoshitomi, Shigeru Murakami, Tadashi Ueda, Role of the osmolyte taurine on the folding of a model protein, hen egg white lysozyme, under the crowding condition., Amino Acids, 47, 5, 909-915, 2015.01.
16. Futami J., Fujiyama H., Kinoshita R., Nonomura H., Tada H., Matsushita H., Abe Y., Kakimi K., Denatured mammalian protein mixtures exhibit unusually high solubility in nucleic acid-free pure water., PLOS ONE, 2014.11.
17. Saki Fujiyama, Yoshito Abe, Junya Tani, Masahi Urabe, Kenji Sato, Takahiko Aramaki, Tsutomu Katayama, Tadashi Ueda, Structure and mechanism of the primosome protein DnaT: functional structures for homotrimerization, dissociation of ssDNA from PriB-ssDNA complex and formation of DnaT-ssDNA complex, FEBS journal, 10.1111/febs.13080., 281, 23, 5356-5370, 2014.09.
18. Shouhei Mine, Yuji Kado, Masahiro Watanabe, Yohta Fukuda, Yoshito Abe, Tadashi Ueda, Yutaka Kawarabayashi, Tsuyoshi Inoue, Kazuhiko Ishikawa, The structure of hyperthermophilic β-N-acetylglucosaminidase reveals a novel dimer architecture associated with the active site, FEBS journal, 10.1111/febs.13049, 281, 22, 5092-5103, 2014.08.
19. Shouhei Mine, Mayumi Niiyama, Wakana Hashimoto, Takahisa Ikegami, Daisuke Koma, Takashi Ohmoto, Yohta Fukuda, Tsuyoshi Inoue, Yoshito Abe, Tadashi Ueda, Junji Morita, Koichi Uegaki, Tsutomu Nakamura, Expression from engineered Escherichia coli chromosome and crystallographic study of archaeal N,N′-diacetylchitobiose deacetylase, FEBS journal, 10.1111/febs.12805, 281, 11, 2584-2596, 2014.04.
20. Saki Fujiyama, Yoshito Abe, Taichi Takenawa, Takahiko Aramaki, Seijiro Shioi, Tsutomu Katayama, Tadashi Ueda, Involvement of histidine in complex formation of PriB and single-stranded DNA. , BBA proteins and proteomics, 1844, 2, 299-307, 2014.02.
21. Takahiko Aramaki, Yoshito Abe, Tsutomu Katayama, Tadashi Ueda, Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli., Protein Science, 10.1002/pro.2314, 22, 9, 1279-1286, 2013.07.
22. Takahiko Aramaki, Yoshito Abe, Takatoshi Ohkuri, Tomonori Mishima, Shoji Yamashita, Tsutomu Katayama, Tadashi Ueda, Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli. , Genes to Cells, 10.1111/gtc.12069, 18, 9, 723-732, 2013.07.
23. Masayuki Su'etsugu, Yuji Harada, Kenji Keyamura, Chika Matsunaga, Kazutoshi Kasho, Yoshito Abe, Tadashi Ueda, Tsutomu Katayama, The DnaA N-terminal domain interacts with Hda to facilitate replicase clamp-mediated inactivation of DnaA., Environmental Microbiology, 10.1111/1462-2920.12147., 15, 12, 3183-3195, 2013.04.
24. Masahiro Abe, Yoshito Abe, Takatoshi Ohkuri, mishima tomonori, 門司 晃, Shigenobu Kanba, Tadashi Ueda, Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein., Protein Science, 22, 4, 467-474, 2013.02.
25. Igawa T, Higashi S, Abe Y, Okuri T, Tanaka H, Morimoto S, Yamashita T, Tsuda M, Inoue K, Ueda T, Preparation and characterization of a monoclonal antibody against the refolded and functional extracellular domain of rat P2X4 receptor, J. Biochem., 153, 275-283, 2013.05.
26. Takazaki S, Abe Y, Yamaguchi T, Yagi M, Ueda T, Kang D, Hamasaki N, Arg 901 in the AE1 C-terminal tail is involved in conformational change but not in substrate binding, BBA – Biomembranes , 1818, 3, 658-65, Epub 2011 Dec 1, 2012.03.
27. Nagata-Uchiyama M, Abe Y, Monji A, Kanba S, Ueda T, Evidence for the binding of phosphate ion to the C-terminus region in Aβ1-40 using heteronuclear NMR analyses, Protein Peptide lett., 17,176-180, 2010.02.
28. Goto T, Abe Y, Imoto T, Ueda T, Effect of protein concentration and pH on the chitinase activity of Tapes japonica lysozyme, Protein Peptide lett., 17, 172-175, 2010.02.
29. Yamaguchi T, Ikeda Y, Abe Y, Kuma H, Kang D, Hamasaki N, Hirai T, Structure of membrane domain of human erythrocyte anion exchanger 1 revealed by electron crystallography, J Mol Biol, 397, 1, 179-189, 2010.03.
30. Takazaki S, Abe Y, Yamaguchi T, Yagi M, Ueda T, Kang D, Hamasaki N, Mutation of His 834 in human anion exchanger 1 affects substrate binding, BBA – Biomembranes , 1798, 5, 903-908, 2010.03.
31. Oda M, Kitai A, Murakami A, Nishimura M, Ohkuri T, Abe Y, Ueda T, Nakamura H, Azuma T, Evaluation of the conformational equilibrium of reduced hen egg lysozyme by antibodies to the native form, Arch Biochem Biophys, 494, 2, 145-150, 2010.02.
32. Yamaguchi T, Fujii T, Abe Y, Hirai T, Kang D, Namba K, Hamasaki N, Mitsuoka K, Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals, J Struc Biol, 169, 3, 406-12, 2010.03.
33. Mishima T, Ohkuri T, Monji A, Kanemaru T, Abe Y, Ueda T, Effects of His mutations on the fibrillation of amyloidogenic Vλ6 protein Wil under acidic and physiological conditions, Biochem Biophys Res Commun, 391, 1, 615-20, 2010.01.
34. Mishima T, Ohkuri T, Monji A, Kanemaru T, Abe Y, Ueda T, Residual Structures in the Acid-Unfolded States of Vlambda6 Proteins Affect Amyloid Fibrillation., J. Mol. Biol, 392, 1033-1043, 2009.07.
35. Keyamura K, Abe Y, Higashi M, Ueda T, Katayama T, DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading., J. Biol. Chem., 284, 25038-25050, 2009.07.
36. Ueda Y, Ohwada S, Abe Y, Shibata T, Iijima M, Yoshimitsu Y, Koshiba T, Nakata M, Ueda T, Kawabata SI., Factor G Utilizes a Carbohydrate-Binding Cleft That Is Conserved between Horseshoe Crab and Bacteria for the Recognition of {beta}-1,3-d-Glucans., J. Immunol., 183, 3810-3818, 2009.07.
37. Goto T, Ohkuri T, Shioi S, Abe Y, Imoto T, Ueda T, Crystal structures of K33 mutant hen lysozymes with enhanced activities., J Biochem. , 144(5):619-23, 2008.09.
38. Goto T,Abe Y, Kakuta Y, Takeshita K, Imoto T, and Ueda T, Crystal structure of Tapes japonica lysozyme with substrate analogue ; Structural basis of the catalytic mechanism and manifestation of its chitinase activity accompany with quaternary structural change, J. Biol. Chem., 282; 27459-67, 2007.10.
39. Abe Y, Jo T, Matsuda Y, Matsunaga C, Katayama T and Ueda T, Structure and function of DnaA N-terminal domains: specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC, J Biol Chem, 282: 17517-17529, 2007.07.
40. Abe Y, Watanabe Y, Yoshida Y, Ebata F, Katayama T and Ueda T, Assignment of 1H,13C and 15N resonances of N-terminal Domain of DnaA protein, Bio NMR assignments, 1; 57-9, 2007.07.
41. Li C, Takazaki S, Jin X, Kang D, Abe Y and Hamasaki N, Identification of Oxidized Methionine Sites in Erythrocyte Membrane Protein using LC/ESI MS Peptide Mapping, Biochemistry, 45(39), 12117 -12124, 2006.10.
42. Abe Y, Hamasaki T, Turusaki S, Takazaki S, Jin X, Kang D, Hamasaki N, A Simple Search of TM Segments in Polytopic Membrane Protein Using Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry, Protein & Peptide Letters, 13(8):761-767, 2006.08.
43. Takazaki S, Abe Y, Kang D, Li C, Jin X, Ueda T, Hamasaki N, The Functional Role of Arginine 901 at the C-Terminus of the Human Anion Transporter Band 3 Protein, J Biochem (Tokyo), Vol. 139, pp. 903 - 912, 2006.05.
44. Shioi S, Ose T, Maenaka K, Shiroishi M, Abe Y, Kohda D, Katayama T, Ueda T., Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site., Biochem. Biophys. Res. Commun., 10.1016/j.bbrc.2004.11.104, 326, 4, 766-776, 28;326(4):766-76, 2005.01.
45. Ueno K, Ueda T, Sakai K, Abe Y, Hamasaki N, Okamoto M, Imoto T., Evidence for a novel racemization process of an asparaginyl residue in mouse lysozyme under physiological conditions., Cell Mol Life Sci., 10.1007/s00018-004-4412-5, 62, 2, 199-205, 62(2):199-205., 2005.01.
46. Abe Y, Chaen T, Jin XR, Hamasaki T, Hamasaki N., Massspectrometric analyses of transmembrane proteins in human erythrocyte membrane., J. Biochem. (Tokyo), 10.1093/jb/mvh100, 136, 1, 97-106, 136(1):97-106., 2004.08.
47. Jin X, Abe Y, Li C, and Hamasaki N, Histidine-834 of Human Erythrocyte Band 3 has an essential role in the Conformational Changes that occur during the Band 3-mediated Anion Exchange, Biochemistry, 10.1021/bi0350809, 42, 44, 12927-12932, 42: 12927-12932, 2003.11.
48. Alam TI, Kanki T, Muta T, Ukaji K, Abe Y, Nakayama H, Takio K, Hamasaki N, Kang D, Human mitochondrial DNA is packaged with TFAM, Nucleic Acid Research, 10.1093/nar/gkg251, 31, 6, 1640-1645, 31(6):1640-5, 2003.01.
49. Ohkuri T, Ueda T, Yoshida Y, Abe Y, Hamasaki N, Imoto T, A metal binding in the polypeptide chain improves the folding efficiency of a denatured and reduced protein, Biopolymer, 10.1002/bip.10153, 64, 2, 106-114, 64:106-114, 2002.07.
50. Takamatsu C, Umeda S, Ohsato T, Ohno T, Abe Y, Fukuoh A, Shinagawa H, Hamasaki N, Kang D, Regulation of mitochondrial D-loops by transcription factor A and single-stranded DNA-binding protein, EMBO report, 10.1093/embo-reports/kvf099, 3, 5, 451-456, 3:451-456, 2002.05.
51. Kuma H, Abe Y, Askin D, Bruce LJ, Hamasaki T, Tanner MJ, Hamasaki N, Molecular basis and functional consequences of the dominant effects of the mutant band 3 on the structure of normal band 3 in Southeast Asian ovalocytosis, Biochemistry, 10.1021/bi011678+, 41, 10, 3311-3320, 41:3311-3320, 2002.03.
52. Muto T, Obita T, Abe Y, Shodai T, Endo T, Kohda D, NMR identification of the Tom20 binding segment in mitochondrial presequences, Journal of Molecular Biology, 306:137-143, 2001.01.
53. Heinzmann A, Mao XQ, Akaiwa M, Kreomer RT, Gao PS, Ohshima K, Umeshita R, Abe Y, Braun S, Yamashita T, Roberts MH, Sugimoto R, Arima K, Arinobu Y, Yu B, Kruse S, Enomoto T, Dake Y, Kawai M, Shimazu S, Sasaki S, Adra CN, Kitaichi M, Inoue H, Yamauchi K, To, Genetic variants of IL-13 signalling and human asthma and atopy, Human Molecular Genetics, 10.1093/hmg/9.4.549, 9, 4, 549-559, 9:549-559, 2000.05.
54. Abe Y, Shodai T, Muto T, Mihara K, Torii H, Nishikawa S, Endo T, Kohda D, Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20, Cell, 10.1016/S0092-8674(00)80691-1, 100, 5, 551-560, 100:551-560, 2000.03.
55. Sato C, Kim JH, Abe Y, Saito K, Yokoyama S, Kohda D, Characterization of the N-oligosaccharides attached to the atypical Asn- X-Cys sequence of recombinant human epidermal growth factor receptor, Journal of Biochemistry (Tokyo), 127:65-72, 2000.01.
56. Kawamura S, Abe Y, Ueda T, Masumoto K, Imoto T, Yamasaki N, Kimura M, Investigation of the structural basis for thermostability of DNA- binding protein HU from Bacillus stearothermophilus., Journal of Biological Chemistry, 10.1074/jbc.273.32.19982, 273, 32, 19982-19987, 273:11150-11157, 1998.08.
57. Abe Y, Odaka M, Inagaki F, Lax I, Schlessinger J, Kohda D, Disulfide bond structure of human epidermal growth factor receptor, Journal of Biological Chemistry, 273:11150-11157, 1998.05.
58. Abe Y, Ueda T, Kawano K, Tanaka Y, Imoto T, Detection of a local interaction of hen lysozyme under highly denaturing conditions using chemically 13C-enriched methionine resonance, Journal of Biochemistry (Tokyo), 123, 2, 313-317, 123:313-317, 1998.02.
59. Abe Y, Ueda T, Imoto T, An improved method for preparing lysozyme with chemically 13C-enriched methionine residues using 2-aminothiophenol as a reagent of thiolysis., J Biochem (Tokyo), 121(6):1076-81., 1997.06.
60. Motoshima H, Mine S, Masumoto K, Abe Y, Iwashita H, Hashimoto Y, Chijiiwa Y, Ueda T, Imoto T., Analysis of the stabilization of hen lysozyme by helix macrodipole and charged side chain interaction., J Biochem (Tokyo)., 121, 6, 1076-1081, 121(6):1076-81, 1997.06.
61. So T, Ueda T, Abe Y, Nakamata T, Imoto T, Situation of monomethoxypolyethylene glycol covalently attached to lysozyme., J Biochem (Tokyo), 119, 6, 1086-1093, 119(6):1086-93, 1996.06.
62. Ueda T, Abe Y, Ohkuri T, Kawano K, Terada Y, Imoto T, Kinetically trapped structure in the renaturation of reduced oxindolealanine 62 lysozyme, Biochemistry, 10.1021/bi00049a033, 34, 49, 16178-16185, 34(49):16178-85, 1995.12.
63. Abe Y, Ueda T, Iwashita H, Hashimoto Y, Motoshima H, Tanaka Y, Imoto T, Effect of salt concentration on the pKa of acidic residues in lysozyme, J Biochem (Tokyo), 118, 5, 946-952, 118(5):946-52, 1995.11.
64. Abe Y, Ueda T, Imoto T, Reduction of disulfide bonds in proteins by 2-aminothiophenol under weakly acidic conditions., J Biochem (Tokyo), 115, 1, 52-57, 15(1):52-7, 1994.01.
65. Ueda T, Abe Y, Akasaki K, Yamaguchi Y, Tsuji H, Kawano K, Yamada H, Imoto T, Detection of subtle differences in the surface structure of lysozymes by use of an immobilized Fab fragment, J Biochem (Tokyo), 113, 2, 174-179, 113(2):174-9, 1993.02.
66. Ueda T, Yamada H, Sakamoto N, Abe Y, Kawano K, Terada Y, Imoto T, Preparation and properties of a lysozyme derivative in which two domains are cross-linked intramolecularly between Trp62 and Asp101., J Biochem (Tokyo), 110, 5, 719-725, 110(5):719-25, 1991.11.