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Tadashi Ueda Last modified date:2019.06.20

Professor / Department of Medico-Pharmaceutical Scineces
Department of Pharmaceutical Health Care and Sciences
Faculty of Pharmaceutical Sciences


Undergraduate School
Administration Post
Director of the Research Center for Education in Health Care System
Other


E-Mail
Homepage
http://meneki.phar.kyushu-u.ac.jp/
Laboratory of Protein Structure, Funcrion and Design, Graduate School of Pharmaceutical Sciences,
Kyushu University .
Academic Degree
Ph. D.
Country of degree conferring institution (Overseas)
No
Field of Specialization
Structural biochemistry-related
Research
Research Interests
  • Preparation of the antibodies tightly bound to P2X4 molecule, which is related to Allodynia.
    keyword : structure based drug design, P2X4 molecule, Allodynia
    2007.04.
  • Improvement of enzymatic function for clinical application
    keyword : diabetes, stabilization, amino acid replacement
    2007.04.
  • Study on denaturation or detorioration of proteins
    keyword : protein detorioration, aging, aggregation, conformational deseases、isomerization of amino acid residues in proteins
    2000.01Identification and characterization of structural or chemical alterations in proteins.
  • Antibody (or Fab) engineering
    keyword : antibody, mutation, protein engineering
    2002.04Protein engineering of a mouse antibody.
  • Structural biology of proteins
    keyword : proteins, NMR, X-ray crystallography, interaction
    2000.01Analysis of structure and function of lysozymes and proteins invovled in DNA replication in Escherichia coli..
Current and Past Project
  • Prof. Ueda in Kyushu University participates in protein 3000 project. We are preparing new proteins and determining their tertiary structures.
Academic Activities
Books
1. Takatoshi Ohkuri, Tadashi Ueda, Taiji Imoto, Existence of Condensed Structures in Denatured Lysozyme and their Contributions to the Folding (ed. Tony R. Obalinsky) in Protein Folding: New Research, Nova Scieince Publisers. Inc., pp173-194, 2006.05.
2. Tadashi Ueda and Taiji Imoto, Identification of a core region and key residues in the refolding of reduced hen lysozyme (ed. by M. Gromiha and S. Selvaraj) in Recent Research Developments in Protein Folding, Stability and Design 2002, Reseach Signpost, Kerala, India,  pp.219-241, 2002.12.
Reports
1. Tadashi Ueda, Next-generation optimized biotherapeutics - A review and preclinical study., Biochim. Biophys. Acta. - Proteins and Proteomics, 2014.11.
2. Effect of Protein Structure of the Denatured State of the Formation of Amyloid Fibrils-Analysis Using Hen Egg White Lysozyme-.
Papers
1. 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..
2. 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, Background: Light chains are abnormally overexpressed from disordered monoclonal B-cells and form amyloid fibrils, which are then deposited on the affected organ, leading to a form of systemic amyloidosis known as AL (Amyloid Light chain) amyloidosis. A green tea catechin, epigallocatechin-3-O-gallate (EGCG), which is thought to inhibit various amyloidoses, is a potent inhibitor of amyloid fibril formation in AL amyloidosis. Methods: An amyloidogenic variable domain in λ6 light chain mutant, Wil was incubated in the presence of EGCG. The incubation products were analyzed by SDS-PAGE and reverse-phase HPLC. The interaction between Wil and EGCG was observed by using NMR and tryptophan fluorescence. Results: EGCG inhibited the amyloid fibril formation of Wil at pH 7.5 and 42 °C. Under these conditions, most Wil populations were in the unfolded state and several chemical reactions, i.e., oxidation and/or covalent bond oligomerization could be induced by auto-oxidated EGCG. Moreover, we found that EGCG bound to the unfolded state of Wil with higher affinity (Kd = 7 μM). Conclusions: Inhibition of amyloid fibril formation of Wil was caused by 1) EGCG binding to unfolded state rather than folded state and 2) chemical modifications of Wil by auto oxidation of EGCG. General significance: In the competitive formation of amyloid fibrils and off-pathway oligomers, EGCG produces the latter immediately after it preferentially binds to the unfolded state. It may be general mechanism of EGCG inhibition for amyloidosis..
3. Mitsunori Shiroishi, Yuji Ito, Kenta Shimokawa, Man Lee, Takahiro Kusakabe, Tadashi Ueda, Structure–function analyses of a stereotypic rheumatoid factor unravel the structural basis for germline-encoded antibody autoreactivity, Journal of Biological Chemistry, 10.1074/jbc.M117.814475, 293, 18, 7008-7016, 2018.01, Rheumatoid factors (RFs) are autoantibodies against the fragment-crystallizable (Fc) region of IgG. In individuals with hematological diseases such as cryoglobulinemia and certain B cell lymphoma forms, the RFs derived from specific heavy- and light-chain germline pairs, so-called “stereotypic RFs,” are frequently produced in copious amounts and form immune complexes with IgG in serum. Of note, many structural details of the antigen recognition mechanisms in RFs are unclear. Here we report the crystal structure of the RF YES8c derived from the IGHV1-69/IGKV3-20 germline pair, the most common of the stereotypic RFs, in complex with human IgG1-Fc at 2.8 Å resolution. We observed that YES8c binds to the CH2–CH3 elbow in the canonical antigen-binding manner involving a large antigen–antibody interface. On the basis of this observation, combined with mutational analyses, we propose a recognition mechanism common to IGHV1-69/IGKV3-20 RFs: (1) the interaction of the Leu
432
–His
435
region of Fc enables the highly variable complementarity-determining region (CDR)-H3 to participate in the binding, (2) the hydrophobic tip in the CDR-H2 typical of IGHV1-69 antibodies recognizes the hydrophobic patch on Fc, and (3) the interaction of the highly conserved RF light chain with Fc is important for RF activity. These features may determine the putative epitope common to the IGHV1-69/IGKV3-20 RFs. We also showed that some mutations in the binding site of RF increase the affinity to Fc, which may aggravate hematological diseases. Our findings unravel the structural basis for germline-encoded antibody autoreactivity..
4. Shohei 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.
5. Hitomi Nakamura, Takatoshi Ohkuri, Takanori So, Tadashi Ueda, Relationship between the magnitude of IgE production in mice and conformational stability of the house dust mite allergen, Der p 2., Biochimica et Biophysica Acta (BBA) - General Subjects, 10.1016/j.bbagen, in press, 2016.06.
6. Yoshito Abe, Mitsuru Kubota, Shinta Takazaki, Yuji Ito, Hiromi Yamamoto, Dongchon Kang, 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.
7. 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, The Journal of Biochemistry, 10.1093/jb/mvv096, 159, 2, 217-223, 2016.02.
8. Takahiro 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., 10.1093/jb/mvv014., 157, 6, 529-537, 2015.06.
9. Yoshito Abe, Takatoshi Ohkuri, Sachiko Yoshitomi, Tadashi Ueda, Role of the osmolyte taurine on the folding of a model protein, hen egg white lysozyme, under a crowding condition, AMINO ACIDS, 10.1007/s00726-015-1918-0, 47, 5, 909-915, 2015.05.
10. Tatsuhiro Igawa, Yoshito Abe, TSUDA MAKOTO, Kazuhide Inoue, Tadashi Ueda, Solution structure of the rat P2X4 receptor head domain involved in inhibitory metal binding, FEBS LETTERS, 10.1016/j.febslet.2015.01.034, 589, 6, 680-686, 2015.03.
11. Saki Fujiyama, Yoshito Abe, Junya Tani, Masashi 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 the PriB.ssDNA complex, and formation of the DnaT.ssDNA complex, FEBS JOURNAL, 10.1111/febs.13080, 281, 23, 5356-5370, 2014.12.
12. Saki Fujiyama, Yoshito Abe, Taiichi 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.
13. Takatoshi Ohkuri, Eri Murase, Sun Shu-Lan, Jun Sugitani, Tadashi Ueda, Characterization of deamidation at Asn138 in L-chain of recombinant humanized Fab expressed from Pichia pastoris, J.Biochem, 154, 4, 333-340, 2013.10.
14. 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, 18, 9, 723-732, 2013.09.
15. 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, 22, 9, 1279-1286, 2013.09.
16. Masato Abe, Yoshito Abe, Takaoshi Ohkuri, Tomonori Mishima, Akira Monji, Shigenobu Kanba, Tadashi Ueda, Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein., Protein Science, 22,4,467-474, 4, 467-474, 2013.04.
17. Tatsuhiro Igawa, Sadayuki Higashi, Yoshito Abe, Takatoshi Ohkuri, Hiroyuki Tanaka, satoshi morimoto, 山下 智大, TSUDA MAKOTO, Kazuhide Inoue, Tadashi Ueda, Preparation and characterization of a monoclonal antibody against the refolded and functional extracellular domain of rat P2X4 receptor, J. Biochem., 153, 3, 275-282, 2013.03.
18. Kameoka D, Ueda T, Imoto T., Effect of the Conformational Stability of the CH2 Domain on the Aggregation and Peptide Cleavage of a Humanized IgG., Appl Biochem Biotechnol., 164, 5, 642, 2011.07.
19. Ohkuri T, Nagatomo S, Oda K, So T, Imoto T, Ueda T, A Protein's conformational stability is an immunolgically dominant factor: Evidence that free-energy barriers for protein unfolding limit the immunolgenicity of foreign proteins, The Journal of Immunlogy, 185, 4199-4205, 2010.10, 蛋白質は立体構造を保持した状態でその機能を発揮する。蛋白質は往々にして、その安定性を高めることで有用性が上がることが知られている。一方、生体内で蛋白質抗原は、立体構造が壊れた状態で細胞内プロテアーゼにより分解され抗原性を発揮する。従って、免疫応答にも蛋白質の安定性が関与するということを示唆する知見は得られていた。本報告では、蛋白質抗原が免疫応答を引き起こす主要な要因の一つは、蛋白質抗原の構造安定性であることを世界で初めて実証した。この研究成果は,最近世界的に使用が広がっている抗体医薬品の機能を高めるためにアミノ酸配列を改変したとしても、不測の免疫応答を回避する方策を示唆したものである。この成果によって、今後、高機能化蛋白質医薬品の研究が一層進展することが期待される.
20. Tomonori Mishima, Takatoshi Ohkuri, Akira Monji, Takaaki Kanemaru, Yoshito Abe, Tadashi Ueda, Effect of His mutantions on the fibrillation of amyloidogenid Vλ6 protein Wil under acidic and physicological conditions, Biochemical and Biophysical Research Communication, 391, 1, 615, 2010.01.
21. 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(4):1033-43, 2009.10.
22. 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(37):25038-50, 2009.09.
23. 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-Glucan, J Immnol, 183(6):3810-8, 2009.09.
24. Kameoka D, Matsuzaki E, Ueda T, Imoto T, Effect of buffer species on the unfolding and the aggregation of humanized IgG, The Journal of Biochemistry, 142、3、383, 2007.09.
25. Goto T, Abe Y, Kakuta Y, Takeshita K, Imoto T, 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, Jounal of Biological Chemistry, 282、37、27459, 2007.09.
26. Makiko Nagata-Uchiyama, Masashi Yaguchi, Yugo Hirano and Tadashi Ueda, Expression and Purification of Uniformly 15N-Labeled Amyloid beta Peptide 1-40 in Escherichia coli, Protein & Peptide Letters, 14, 8, 788-792, 2007.09.
27. Abe Y, Jo T, Matsuda Y, Matsunaga C, Katayama T, Ueda T, Structure and function of DnaA N-terminal domains: Specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on Ori C, Jounal of Biological Chemistry, 282、24、17816-17827, 2007.06.
28. Yoshida Y, Ohkuri T, Takeda C, Kuroki R, Izuhara K, Imoto T, Ueda T, Analysis of internal motions of interleukin 13 variant associated with severe bronchial asthma using 15N relaxation measurements, Biochem. Biophys. Res. Commun., 358、1、292-297, 2007.06.
29. Mishima T, Ohkuri T, Monji A, Imoto T, Ueda T, A paticular hydrophobic cluster in the residual structure of reduced lysozyme drastically affects the amyloid fibrils formation, Biochem. Biophys. Res. Commun., 356, 3, 769-772, 2007.05.
30. Fujii T, Ohkuri T, Onodera R, Ueda T, Stable supply of large amounts of human Fab from the inclusion bodies in E. coli., The Journal of Biochemistry, 141、5、699-707, 2007.05.
31. Mishima T, Ohkuri T, Monji A, Imoto T, Ueda T, Amyloid formation in denatured single-mutant lysozyme where residual structures are modulated, Protein Science, 15, 10, 2448-2452, 2006.10.
32. Ohkuri T, Imoto T, Ueda T, Effect of W62G mutation of hen lysozyme on the folding in vivo, Biochem. Biophys Res. Commun., 10.1016/j.bbrc.2005.10.009, 338, 2, 820-824, 338, 2, 820-824, 2005.12.
33. Yoshida Y, Ohkuri T, Kino T, Ueda T and Imoto T, Elucidation of the relationship between enzyme activity and internal motion using a lysozyme stabilized by cavity-filling mutations, Cellular and Molecular Life Sciences, 10.1007/s00018-005-5053-z, 62, 9, 1047-1055, 62, 5, 1047-1055, 2005.05.
34. Ohkuri T, Shioi S, Imoto T, Ueda T, Effect of the structure of the denatured state of lysozyme on the aggregation reaction at the early stages of folding from the reduced form, J. Mol. Biol., 10.1016/j.jmb.2005.01.022, 347, 1, 159-168, 347、1、159-168, 2005.03.
35. 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, Cellular and Molecular Life Sciences, 10.1007/s00018-004-4412-5, 62, 2, 199-205, 62、2、199-205, 2005.01.
36. 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, 326、4、766-776, 2005.01.
37. Wirmer J, Schlorb C, Klein-Seetharaman J, Hirano R, Ueda T, Imoto T, Schwalbe H, Modulation of compactness and long-range interactions of unfolded lysozyme by single point mutations, Angewandte Chemie-International Edition, 10.1002/anie.200460907, 43, 43, 5780-5785, 43、43、5780-5785, 2004.11.
38. Shioi S, Imoto T, Ueda T, Analysis of the early stage of the folding process of reduced lysozyme using all lysozyme variants containing a pair of cysteines, Biochemistry, 10.1021/bi036048h, 43, 18, 5488-5493, 43、18、5488-5493, 2004.05.
39. Yoshida Y, Obita T, Kokusho Y, Ohmura T, Katayama T, Ueda T, Imoto T., Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box., Cell Mol Life Sci., 10.1007/s00018-003-3176-7, 60, 9, 1998-2008, 60, 9, 1998-2008, 2003.09.
40. Kameoka D, Ueda T, Imoto T., Method for the Detection of Asparagine Deamidation and Aspartate Isomerization of Proteins by MALDI/TOF-Mass Spectrometry Using Endoproteinase Asp-N., J Biochem., 134, 1, 129-135, 2003.07.
41. Obita T. Ueda T. Imoto T., Solution structure and activity of mouse lysozyme M., Cell. Mol. Life Sci., 10.1007/s000180300012, 60, 1, 176-184, 60, 1, 176-184, 2003.01.
42. Obita T. Iwura T. Su'etsugu M. Yoshida Y. Tanaka Y. Kayatama T. Ueda T. Imoto T., Determination of the secondary structure in solution of the Escherichia coli DnaA DNA-binding domain., Biochem. Biophys. Res. Commun., 10.1016/S0006-291X(02)02590-1, 299, 1, 42-48, 299, 1, 42-48, 2002.11.
43. Klein-Seetharaman J, Oikawa M, Grimshaw S B, Wirmer J, Durchardt E, Ueda T.他4名, Long-range interactions within a nonnative protein., Science, 10.1126/science.1067680, 295, 5560, 1719-1722, 295, 5560, 1719-1722, 2002.03.
44. Nishida S. Fujimitsu K. Sekimizu K. Ohmura T. Ueda T. Katayama T., A nucleotide switch in the E. coli DnaA protein initiates chromosomal replication: Evidence from a mutant DnaA protein defective in regulatory ATP hydrolysis in vitro and in vivo., J. Biol. Chem., 10.1074/jbc.M108303200, 277, 17, 14986-14995, 277, 17, 14986-14995, 2002.02.
45. 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., Biopolymers, 10.1002/bip.10153, 64, 2, 106-114, 642, 2, 106-114, 2002.02.
46. Masumoto K. Ueda T. Nagata M. Yamada Y. Yoshida Y. Hashimoto Y. Imoto T., Effects of stereochemistry of sugars on protein stabilities., Protein Peptide Lett., 10.2174/0929866023408553, 9, 5, 435-439, 9, , 435-439, 2002.01.
47. Ohmura T. Ueda T. Ootsuka K. Saito M. Imoto T., Stabilization of hen egg white lysozyme by a cavity-filling mutation., Protein Sci., 10.1110/ps.37401, 10, 2, 313-320, 10, 9, 313-320, 2001.09.
48. Tsujihata Y. So T. Hashimoto Y. Ueda T. Imoto T., A single amino acid substitution in a self protein is sufficient to trigger autoantibody response., Mol. Immunol., 10.1016/S0161-5890(01)00068-2, 38, 5, 375-381, 38, , 375-381, 2001.01.
49. Ohkuri T. Ueda T. Tsurumaru M. Imoto T., Evidence for an initiation site for hen lysozyme folding from reduced form using its dissected peptide fragments., Protein Eng., 10.1093/protein/14.11.829, 14, 11, 829-833, 14, , 829-833, 2001.01.
50. Ueda T. Nagata M. Imoto T., Aggregation and chemical reaction in hen lysozyme caused by heating at pH 6 are depressed by osmolytes, sucrose and trehalose., J. Biochem., 130, 4, 491-496, 130, ,491-496, 2001.01.
51. Mine S. Ueda T. Hashimoto Y. Imoto T., Analysis of the internal motion of free and ligand-bound human lysozyme by use of N-15 NMR relaxation measurement: A comparison with those of hen lysozyme., Protein Sci., 9, 9, 1669-1684, 9, 9,1669-1684, 2000.09.
52. Tsujihata Y. So T. Chijiiwa Y. Hashimoto Y. Hirata M. Ueda T. Imoto T., Mutant mouse lysozyme carrying a minimal T cell epitope of hen egg lysozyme evokes high autoantibody, J. Immunol., 165, 7, 3606-3611, 165, 3, 606-3611, 2000.01.
53. Ueda T. Masumoto K. Ishibashi R. So T. Imoto T., Remarkable thermal stability of doubly intramolecularly cross-linked hen lysozyme., Protein Eng., 10.1093/protein/13.3.193, 13, 3, 193-196, 13, , 193-196, 2000.01.
54. Mine S, Tate S, Ueda T, Kainosho M, Imoto T, Analysis of the relationship between enzyme activity and its internal motion using nuclear magnetic resonance:15N relaxation studies of wild-type and mutant lysozyme, Journal of Molecular Biology, 10.1006/jmbi.1999.2572, 286, 5, 1547-1565, 285、5、1547-1565, 1999.02.
55. So T. Ito HO. Hirata M. Ueda T. Imoto T., Extended blood half-life of monomethoxypolyethylene glycol-conjugated hen lysozyme is a key parameter controlling immunological tolerogenicity., Cell. Mol. Life Sci., 10.1007/s000180050365, 55, 8-9, 1187-1194, 55, , 1187-1194, 1999.01.
56. Mine S. Ueda T. Hashimoto Y. Tanaka Y. Imoto T., High-level expression of uniformly 15N-labeled hen lysozyme in Pichia pastoris and identification of the site in hen lysozyme where phosphate ion binds using NMR measurements., FEBS Letters, 10.1016/S0014-5793(99)00332-4, 448, 1, 33-37, 488, 1, 33-37, 1999.01.
57. 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, , 19982-19987, 1998.01.
58. Maeda Y. Ueda T. Imoto T., Effective renaturation of Met-1 lysozyme expressed in Escherichia coli as inclusion bodies., Protein and Peptide Letters, 5, 2, 67-74, 5, , 67-74, 1998.01.
Presentations
1. Tadashi Ueda, The effect of long-range interactions in the denatured state of a protein on the amyloid formations., Institue for Protein Research Seminar JSPS Japan Hungary Joint Seminar " Mechanism and regulation of aberrant protein aggregation", 2014.11.
2. Reina Fujita, 三次 百合香, Kenji Hamase, Takashi Saitoh, Fumina Ohsaka, Katsumi Maenaka, Mitsunori Shiroishi, Yoshito Abe, Tadashi Ueda, ANALYSIS OF ISOMERIZATION AT ASN127 IN MOUSE LYSOYME AT pH 7 WITHOUT DEAMIDATION, The 2nd International Conference of D-Amino Acid Research , 2014.09.
3. 荒牧峻彦, 阿部 義人, 大栗誉敏, 三島朋徳, 古谷佳織, 山下 昭二, 片山 勉, 植田 正, Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli., Protein Society 2013 symposium, 2013.07.
4. High expression of human interleukin-13 receptor alpha 2 chain using Pichia pastoris.
5. Induction of antigen specific immunological tolerance using sugar mofidication or polymerization of antigen.
6. Tertiary structure of PriB involved in the formation of primosome complex in E. coli and its interaction with DNA.
7. Effect of staility of antigen protein on antibody production.
8. Evidence for the relation between enzymatic activity and internal motions using hen lysozyme stabilized by cavity filling mutations..
9. X-ray crystal structure of heat shock protein Q (Hsp Q) from Escherichia coli.