H. Anbo, M. Ota, S. Fukuchi
"Homology Modeling, Methods and Protokols" edited by Slawomir Filipek, Humana, NY (2023)
Computationa methods to predict intrinsically disorderd regiosn and functional regions in them (pp.231-245)
安保勲人,小澤侑平,太田元規,福地佐斗志
「相分離解析プロトコール」加藤昌人ら 編 羊土社 (2022)
担当項目 : 「液滴研究に関連したデータベースと解析プログラム」(pp200-206)
R. Koike, M. Ota
"Practical Guide to Life Science Databases" edited by Imad Abugessaisa, Takeya Kasukawa, Springer Nature (2022)
Protein Structural Changes Based on Structural Comparison (pp.151-170)
太田元規,福地佐斗志
「相分離生物学の全貌」 白木賢太郎 編 東京化学同人 (2020)
担当項目 : 「ドロプレット形成のデータベースと予測」(pp363-367)
太田元規
「モダンアプローチの生物科学」 美宅成樹 著 共立出版 (2015)
担当項目 : 第6章コラム「フラフラのタンパク質は大事なの?」(p155)
太田元規
「タンパク質の立体構造入門 -- 基礎からバイオインフォマティクスへ」 藤博幸 編 講談社サイエンティフィク (2010)
担当項目 : 第5章「アミノ酸配列からの構造予測とデザイン」
磯貝泰弘, 太田元規
「実践:インシリコ創薬の最前線」 武田-志鷹真由子, 梅山秀明 編 メディカル ドゥ (2009)
担当項目 : 第1章6「人口タンパク質設計の創薬への展開」 (pp66-70)
太田元規
「バイオ研究のフロンティア2 酵素・タンパク質をはかる・とらえる・利用する」 岡畑恵雄, 三原久和 編 工学図書 (2009)
担当項目 : Ⅱ-9 「バイオインフォマティクスで酵素の構造と機能をとらえる」 (pp99-110)
太田元規
「分子生物細胞学辞典」(第2版) 分担執筆 東京化学同人 (2008)
太田元規
「改訂第2版 バイオデータベースとウェブツールの手とり足とり活用法」 中村ら 編 羊土社(2007)[概要]
担当項目:「第3章 5.No.16 SCOP(Structural Classification of Proteins) タンパク質立体構造分類データベースの世界標準」
太田元規
「複雑系の構造と予測」 早稲田大学複雑系高等学術研究所 編 共立出版 (2006)
担当項目:タンパク質の立体構造予測 (pp37-58)
太田元規
「バイオインフォマティクス事典」 日本バイオインフォマティクス学会 編 (2006) 共立出版
担当項目:「立体構造予測」,「フォールド認識」,「経験的ポテンシャル関数」
太田元規
「特集:タンパク質機能解析に役立つデータベースとウェッブツール」 太田元規編 バイオテクノロジージャーナル vol.6 No.4 (2006) [概要]
担当項目:「タンパク質の配列・構造・機能相関のバイオインフォマティクスへの誘い」(pp426-427)
小池亮太郎
「特集:タンパク質機能解析に役立つデータベースとウェッブツール」 太田元規編 バイオテクノロジージャーナル vol.6 No.4 (2006)
担当項目:「DynDomによるタンパク質構造変化の解析」
西 羽美
「特集:タンパク質機能解析に役立つデータベースとウェッブツール」 太田元規編 バイオテクノロジージャーナル vol.6 No.4 (2006)
担当項目:「タンパク質複合体構造の判定
~ PQSを例に」
太田元規
「DDBJ/ CIB report」日本DNAデータバンク編 (2006)
担当項目:ゲノム,ハイパーサイクルと相転移 (p3)
太田元規,磯貝泰弘
「生物工学ハンドブック」 日本生物工学会編 コロナ社(2005)
担当項目:I編3.2.3 [3] タンパク質の分子設計(pp. 188-195)
太田元規
「生命情報学」五條堀孝編 シュプリンガーフェアラーク東京(2003)
担当項目:第5章 タンパク質の理論構造生物学(pp. 109-149)
太田元規
バイオインフォマティクスがわかる」菅原秀明編 羊土社(2003)
担当項目:第4章 タンパク質立体構造のバイオインフォマティクス(pp. 44-51)
太田元規
あなたにも役立つバイオインフォマティックス」菅原秀明編 共立出版 (2002)
担当項目:第9章 アミノ酸配列から2次構造を予測する(pp. 69-76)
第10章 アミノ酸配列から立体構造を予測する(p77-84)
磯貝泰弘,太田元規
シリーズ・ニューバイオフィジックス9巻「生体ナノマシンの分子設計」城所俊一編 共立出版(2001)
担当項目:2-2章 人工タンパク質の合理的設計(pp.102-121)
太田元規
複雑系の事典 ー適応複雑系のキーワード150ー 複雑系の事典 編集委員会編 朝倉書店 (2001)
担当項目:「相関係数」,「モンテカルロ法」
太田元規,西川建
プロテオミクスの基礎」綱沢進,平野久編 講談社サイエンティフィク(2000)
担当項目:6.2章 タンパク質高次構造の予測(pp. 82-111)
太田元規
CASPy奮闘記およびCASPyアシロマへ行く(1999)
太田元規
「遺伝子情報処理への挑戦」星野昌紀編 共立出版(1994)
担当項目:10章 島模型ーキリンを三工程で冷蔵庫に入れる方法(pp. 120-138)
太田元規
「軸」 生物物理 361 (2022) 155.
福地佐斗志,小澤侑平,太田元規
「液−液相分離データベースを天然変性タンパク質の観点から整理する」 生化学 94 (2022) 548-556.
太田元規,安保勲人,福地佐斗志
「捉えられない天然変性タンパク質」 実験医学 40 (2022) 2062-2067.
福地佐斗志,太田元規
「天然変性タンパク質の機能部位:理解の変容と進展」 細胞 53 (2021) 533-536.
土方敦司,塩生くらら,中江摂,太田元規,金谷重彦,白井剛
「SARS-CoV-2タンパク質構造モデルによる薬剤候補予測」 生物物理 354 (2021) 102-106.
太田元規,福地佐斗志
「天然変性タンパク質:既知のこと,未知のこと」 実験医学 37 (2019) 3077-3082.
太田元規,小池亮太郎,福地佐斗志
「天然変性,ハブ性,細胞内局在を整理する」 生物物理 57 (2017) 85-89.
南慎太朗, 千見寺浄慈
「タンパク質における配列順序非保存な構造類似性」 生物物理 56 (2016) 27-29.
小池亮太郎, 太田元規
「蛋白質の複雑な構造変化とMotion Treeによる階層的記述」 生物物理 55 (2015) 142-144.
福地佐斗志, 太田元規
「天然変性タンパク質のプロミスキャスな相互作用」 細胞工学 33 (2014) 764-769.
太田元規
書評:バイオインフォマティクス(A.ポランスキ, M. キンメル著) 生物物理 51 (2011) 117.
磯貝泰弘, 太田元規
「λ Croフォールドのデノボデザイン」 生物物理 47 (2007) 185-189.
東祐介, 太田元規
「最小細胞機能セットの探求」 化学と工業 60 (2007) 590-592.
太田 元規
創薬インフォマティクスとタンパク質間相互作用 日本バイオインフォマティクス学会ニュースレター (2006) Vol.13, 6.
太田元規
タンパク質フォールディングのバイオインフォマティクス パリティ21 (2006) 63-65.
太田 元規, 池口 満徳
“タンパク質フォールディング博物学の曙” 生物物理 (2006) Vol. 46, 224-227.
[PDF]
太田元規
タンパク質のフォールディングシミュレーション シミュレーション (2005) 第24巻第3号, 29-34.
太田元規;
“タンパク質の安定性と機能部位” 生物物理 (2004) Vol. 44, 230-232 .
[PDF]
Tomii K., Ota M., Noguchi T. and Akiyama Y.
Construction of a fold recognition server, PILOT based on PSI-BLAST, IMPALA, and LIBRA-rotamer, Pacific
Symposium on Biocomputing (2003), 133.
若山守,森口充瞭,太田元規,西川建
タンパク質の立体構造予測 結晶化しない酵素への応用 化学と生物 (2002), 40, 452-459.
Isogai Y., Ishii A., Ishida M., Mukai M., Ota M., Nishikawa K. and Iizuka T.
Structural and functional properties of designed globins, Proc. Indian Acad. Sci (Chem. Sci.)
(2000) 112, 215-221.
太田元規
3D-1D法の可能性 生物物理 (1998) 38, 111-115.
Nakashima H., Ota M., Nishikawa K. and Ooi T.
Nucleotide sequence of a gene encodes characteristic features of an organism as well as an amino acid
sequence, Genome Informatics (1998).
Mizunuma T., Misu S., Ota M. and Nishikawa K.
PDB Retriever: a simple and integrated browser for protein data bank, Genome Informatics (1997)
246-247.
Ota M. and Nishikawa K.
Performance of a 3D-1D homology search, Protein Eng. (1995) 8, 950-951.
太田元規
蛋白質の構造予測法:「島模型」 物性研究 (1994) 61, 394-397.
Ota M., Kikkoji H. and Saitô N.
Method of prediction of tertiary structure of globular proteins using
the exon information -Case of lysozyme-, Computer Aided Innovation of
New Materials II, (M. Doyama., ed.), Elsevier, (1993) 1267-1270.
R, Koike, M. Ota
Elastic network model reveals distinct flexibilities of capping proteins bound to CARMIL and twinfilin-tail.
Proteins in press, doi:10.1002/prot.26560
S. Minami, T. Niwa, E. Uemura, R, Koike, H. Taguchi, M. Ota
Prediction of chaperonin GroE substrates using small structural patterns of proteins.
FEBS Open Bio, doi:10.1002/2211-5463.13590.
H. Anbo, K. Sakuma, S. Fukuchi, M. Ota
How AlphaFold2 predicts conditionally folding regions annotated in an intrinsically disordered protein database, IDEAL.
Biology 12 (2023) 182, doi: 10.3390/biology12020182.
Y. Ozawa, H. Anbo, M. Ota, S. Fukuchi
Classification of proteins inducing liquid-liquid phase separation: sequential, structural and functional characterization.
J. Biochem. 173 (2023) 255–264, doi: 10.1093/jb/mvac106
Y. Kanematsu, A. Narita, T. Oda, R. Koike, M. Ota, Y. Takano, K. Moritsugu, I. Fujiwara, K. Tanaka, H. Komatsu, T. Nagae, N. Watanabe, M. Iwasa, Y. Maéda, S. Takeda
Structures and mechanisms of actin ATP hydrolysis.
Proc. Natl. Acad. Sci. USA. 119 (2022) e2122641119. doi: 10.1073/pnas.2122641119.
A. Hijikata, C. Shionyu-Mitsuyama, S. Nakae, M. Shionyu, M. Ota, S. Kanaya, T. Hirokawa, S. Nakajima, K. Watashi, T. Shirai
Evaluating cepharantine analogues aws natural drugs against SARS-CoV-2.
FEBS Open Bio 12 (2022) 285-294, doi:10.1002/2211-5463.13337.
S. Takeda, R. Koike, I. Fujiwara, A. Narita, M. Miyata, M. Ota, Y. Maéda
Insights into the Regulation of Actin Capping Protein by Twinfilin C-terminal Tail.
J. Mol. Biol. 433 (2021) 166891, doi: 10.1016/j.jmb.2021.166891.
A. Hijikata, C. Shionyu, S. Nakae, M. Shionyu, M. Ota, S. Kanaya, T. Shirai
Current Status of Structure-based Drug Repurposing against COVID-19 by Targeting SARS-CoV-2 Proteins.
Biophys. Physicobiol. 18 (2021) 226-240, doi:10.2142/biophysico.bppb-v18.025
S. Takeda, R. Koike, T. Nagae, I. Fujiwara, A. Narita, Y. Maéda, M. Ota
Crystal structure of human V-1 in the apo form.
Acta Cryst. F 77 (2021) 13-21, doi:10.1107/S2053230X20016829.
A. Hijikata, C. Shionyu-Mitsuyama, S. Nakae, M. Shionyu, M. Ota, S. Kanaya, T. Shirai
Knowledge-based strutural models of SARS-CoV-2 proteins and their complexes with potential drugs.
FEBS Lett. 594 (2020) 1960-1973, doi: 10.1002/1873-3468.13806.
R. Koike, M. Amano, K. Kaibuchi, M. Ota
Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins.
Protein Sci. 29 (2020) 564-571, doi: 10.1002/pro.3789.
R. Koike, M. Ota
All Atom Motion Tree detects side chain-related motions and their coupling with domain motion in proteins.
Biophys. Physicobiol. 16 (2019) 280-286, doi: 10.2142/biophysico.16.0_280.
H. Okazaki, N. Matsuo, T. Tenno, N. Goda, Y. Shigemitsu, M. Ota, H. Hiroaki
Using 1 H N amide temperature coefficients to define intrinsically disordered regions: An alternative NMR method.
Protein Sci. 27 (2018) 1821-1830, doi: 10.1002/pro.3485.
S. Minami, K. Sawada, M. Ota, G. Chikenji
MICAN-SQ: a sequential protein structure alignment program that is applicable to monomers and all types of oligomers.
Bioinformatics 34 (2018) 3324-3331, doi: 10.1093/bioinformatics/bty369.
R. Koike, T. Amemiya, T. Horii, M. Ota
Structural changes of homodimers in the PDB.
J. Str. Biol. 202 (2018) 42-50, doi. 10.1016/j.jsb.2017.12.004.
N. Matsuo, N. Goda, K. Shimizu, S. Fukuchi, M. Ota, H. Hiroaki
Discovery of Cryoprotective Activity in Human Genome-Derived Intrinsically Disordered Proteins.
Int. J. Mol. Sci. 19 (2018) 401. doi.10.3390/ijms19020401.
S. Minami, G. Chikenji, M. Ota
Rules for connectivity of secondary structure elements of proteins: Two-layer αβ sandwiches.
Prot. Sci. 26 (2017) 2257-2267, doi.10.1002/pro.3285.
M. Ota, M. Ikeguchi, A. Kidera.
Itinerary profiling to analyze a large number of protein-folding trajectories.
Biophys. Physicobiol. 13 (2016) 295-304.
[PMID: 28409081]
D. Shaji.
The relationship between relative solvent accessible surface area (rASA) and irregular structures in protean segments (ProSs).
Bioinformation. 12 (2016) 381-387.
[PMID: 28250616]
D. Shaji, T. Amemiya, R. Koike R, M. Ota.
Interface property responsible for effective interactions of protean segments: Intrinsically disordered regions that undergo disorder-to-order transitions upon binding.
BBRC. 478 (2016) 123-127.
[PMID: 27450808]
H. Oda , M. Ota, H. Toh.
Profile comparison revealed deviation from structural constraint at the positively selected sites.
Biosystems. 147 (2016) 67-77.
[PMID: 27443483]
M. Ota, H. Gonja, R. Koike, S. Fukuchi.
Multiple-localization and hub proteins.
PLos One. 11 (2016) e0156455.
[PMID: 27285823]
R. Koike, S. Takeda, Y. Maéda, M. Ota.
Comprehensive analysis of motions in molecular dynamics trajectories of the actin capping protein and its inhibitor complexes.
Proteins. 84 (2016) 948-956.
[PMID: 27028786]
C. Kobayashi, Y. Matsunaga, R. Koike, M. Ota, Y. Sugita.
Domain-motion enhanced (DoME) model for efficient conformational sampling of multi-domain proteins.
J. Phys. Chem. B 119 (2015) 14584-14593.
[PMID: 26536148]
M. Maekawa, Y. Iwayama, T. Ohnishi, M. Toyoshima, C. Shimamoto, Y. Hisano, T. Toyota, S. Balan, H. Matsuzaki, Y. Iwata, S. Takagai, K. Yamada, M. Ota, S. Fukuchi, Y. Okada, W. Akamatsu, M. Tsujii, N. Kojima, Y. Owada, H. Okano, N. Mori, T. Yoshikawa.
Investigation of the fatty acid transporter-encoding genes SLC27A3 and SLC27A4 in autism.
Sci. Rep. 10 (2015) 16239.
[PMID: 26548558]
K. Moritsugu, R. Koike, K. Yamada, H. Kato, A. Kidera.
Motion tree delineates hierarchical structure of protein dynamics observed in molecular dynamics simulation.
PLoS One 10 (2015) e0131583.
[PMID: 26148295]
N. Goda, K. Shimizu, Y. Kuwahara, T. Noguchi, T. Ikegami, M. Ota, H. Hiroaki.
A method for systematics assessment of intrinsically disordered protein regions by NMR.
Int. J. Mol. Sci. 16 (2015) 15743-15760.
[PMID: 26184172]
C. Kobayashi, R. Koike, M. Ota, Y. Sugita.
Hierarchical domain-motion analysis of conformational changes in Sarcoplasmic Reticulum Ca2+-ATMase.
Proteins. 83 (2015) 746-756.
[PMID: 25641564]
R. Koike, M. Ota, A. Kidera.
Hierarchical description and extensive classification of protein structural changes by Motion Tree.
J. Mol. Biol. 426 (2014) 752-762.
[PMID: 24189051]
S. Balan, Y. Iwayama, M. Maekawa, T. Toyota, T. Ohnishi, M. Toyoshima, C. Shimamoto, K. Esaki, K. Yamada, Y. Iwada, K. Suzuki, M. Ide, M. Ota, S. Fukuchi, M. Tsujii, N. Mori, Y. Shinkai, T. Yoshikawa.
Exon resequencing of H3K9 methyltransferase complex genes, EHMT1, EHMT2 and WIZ, in Japanese autism subjects.
Molecular Autism. 5 (2014) 49.
[PMID: 25400900]
S. Fukuchi, T. Amemiya, S.Sakamoto, Y. Nobe, K. Hosoda, Y. Kado, SD. Murakami, R. Koike, H. Hiroaki, M. Ota.
IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners.
Nucleic Acids Res. 42 (2014) D320-D325.
[PMID: 24178034]
S. Minami, K. Sawada, G. Chikenji.
How a spatial arrangement of secondary structure elements is dispersed in the universe of protin folds.
PLoS One. 9 (2014) e107959.
[PMID: 25243952]
T. Tenno, N. Goda, Y. Umetsu, M. Ota, K. Kinoshita, H. Hroaki.
Accidental interaction between PDZ domains and diclofenac revealed by NMR-assisted virtual screening.
Molecules. 18 (2013) 9567-9581.
[PMID: 23966078]
Y. Kanematsu, R. Koike, T. Amemiya, M. Ota.
Substrate-shielding and hydrolytic reaction in hydrolases.
Proteins. 81 (2013) 926-932.
[PMID: 23345013]
M. Ota, R. Koike, T. Amemiya, T. Tenno, P. R. Romero, H. Hiroaki, A. K. Dunker, S. Fukuchi.
An assignment of intrinsically disordered regions of proteins based on NMR structures.
J. Str. Biol. 181 (2013) 29-36.
[PMID: 23142703]
Y. Matsunaga, R. Koike, M. Ota, J. Tame, A. Kidera.
Influence of structural symmetry on protein dynamics.
PLoS One. 7 (2012) e50011.
[PMID: 23189176]
S. Sutheworapong, M. Ota, H. Ohta, K. Kinoshita.
A nobel biclustering approach with iterative optimization to analyze gene expression data.
Adv. Appl. Bioinform. Chem. 5 (2012) 23-59.
[PMID: 23055751]
R. Koike, M. Ota.
SCPC: a method to structurally compare protein complexes.
Bioinformatics. 28 (2012) 324-330.
[PMID: 22130591 ]
T. Amemiya, R. Koike, A. Kidera, M. Ota.
PSCDB: a database for protein structural change upon ligand binding.
Nucleic Acids Res. 40 (2012) D554-D558.
[PMID: 22080505 ]
S. Fukuchi, S. Sakamoto, Y. Nobe, S. D. Murakami, T. Amemiya, K. Hosoda, R. Koike, H. Hiroaki, M. Ota.
IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature.
Nucleic Acids Res. 40 (2012) D507-D511.
[PMID: 22067451 ]
H. Nishi, R. Koike, M. Ota.
Cover and spacer insertions: small nonhydrophobic accessories that assist protein oligomerization.
Proteins. 79 (2011) 2372-2379.
[PMID: 21656571 ]
S. Takeda, R. Koike, Y. Nitanai, S. Minakata, Y. Maéda, M. Ota.
Actin capping protein and its inhibitor CARMIL: how intrinsically disordered regions function.
Phys. Biol. 8 (2011) 035005.
[PMID: 21572169 ]
C. Motono, J. Nakata, R. Koike, K. Shimizu, M. Shirota, T. Amemiya, K. Tomii, N. Nagano, N. Sakaya, K. Misoo, M. Sato, A. Kidera, H. Hiroaki, T. Shirai, K. Kinoshita, T. Noguchi, M. Ota.
SAHG, a comprehensive database of predicted structures of all human proteins.
Nucleic Acids Res. 39 (2011) D487-D493.
[PMID: 21051360]
S. Takeda, S. Minakata, R. Koike, I. Kawahata, A. Narita, M. Kitazawa, M. Ota, T. Yamakuni, Y. Maéda, Y. Nitanai.
Two Distinct Mechanisms for Actin Capping Protein Regulation—Steric and Allosteric Inhibition.
PLoS Biol. 8 (2010) e1000416.
[PMID: 20625546]
H. Nishi, M. Ota.
Amino acid substitutions at protein-protein interfaces that modulate the oligomeric state.
Proteins. 78 (2010) 1563-1574.
[PMID:
20112251]
Y. Azuma, M. Ota.
An evaluation of minimal cellular functions to sustain a bacterial cell.
BMC Syst. Biol. 3 (2009) 111.
[PMID:
19943949]
R. Koike, A. Kidera, M. Ota.
Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.
Protein Sci. 18 (2009) 2060-2066.
[PMID:
19670211]
H. Sun, H. Ferhatosmanoglu, M. Ota, Y. Wang.
An enhanced partial order curve comparison algorithm and its application to analyzing protein folding trajectories.
BMC Bioinformatics 9 (2008) 344.
[PMID:
18710565]
R. Koike, T. Amemiya, M. Ota, A. Kidera.
Protein structural change upon ligand binding correlates with enzymatic reaction mechanism.
J. Mol. Biol. 379 (2008) 397-401
[PMID:
18455184]
T. Oroguchi, M. Ikeguchi, M. Ota, K. Kuwajima and A. Kidera.
Unfolding pathways of goat α-lactalbumin as revealed in multiple alignment of molecular dynamics trajectories. J. Mol. Biol. 371 (2007)1354-64
[PMID:
17610894]
H. Sun, H. Ferhatosmanoglu, M. Ota, Y. Wang.
Enhanced partial order curve comparison over multiple protein folding trajectories.
Comput. Syst. Bioinformatics. Conf. 6 (2007) 299-310
[PMID:
17951833]
A. Mukaiyama, M. Haruki, M. Ota, Y. Koga, K. Takano and S. Kanaya.
A hyperthermophilic protein acquires function at the cost of stability.
Biochemistry. (2006) 45, 12673–12679
[PMID:
17042484]
M. Haruki, Y. Saito, M. Ota, K. Nishikawa, S. Kanaya.
E. coli ribonuclease HI by the 'stability profile of mutant protein' (SPMP)-inspired random and non-random mutagenesis.
J. Biotech. (2006) 25, 512-522.
[PMID:16545882]
Isogai Y., Ito Y., Ikeya T., Shiro Y., Ota M.
Design of λ Cro Fold: Solution Structure of a Monomeric Variant of the De Novo Protein.
J. Mol. Biol. (2005) 354, 801-814.
[PMID:
16289118] [PDB:
2CW1]
Asada Y., Sawano M., Ogasahara K., Nakamura J., Ota M., Kuroishi C., Sugahara M., Yutani K., Kunishima N.
Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry.
J. Biochem (Tokyo). (2005) 4, 343-353.
[PMID:
16272128]
Kinoshita K., Ota M.
P-cats: Prediction of catalytic residues in proteins from the tertiary structures.
Bioinformatics. (2005) 17, 3570-3571.
[PMID:
15994193]
Ota M., Ikeguchi M., Kidera A.
Phylogeny of protein-folding trajectories reveals a unique pathway to native structure. Proc. Natl. Acad. Sci. USA (2004) 101,
17658-17663.
[PMID:
15591340]
Hioki Y., Ogasahara K., Lee SJ., Ma J., Ishida M., Yamagata Y., Matsuura Y., Ota M., Ikeguchi M., Kuramitsu S. and Yutani K.
The crystal structure of the tryptophan synthase beta subunit from the hyperthermophile Pyrococcus furiosus. Investigation of stabilization factors. Eur. J. Biochem. (2004) 271, 2624-2635.
[PMID:
15206928]
Imanishi T, et al.
Integrative annotation of 21,037 human genes validated by full-length cDNA clones. PLoS. Biol. (2004) 2, 856-875.
[PMID:
15103394 ]
Ota M., Kinoshita K., and Nishikawa K.
Prediction of catalytic residues in enzymes based on known tertiary structure, stability profile, and sequence conservation. J. Mol. Biol. (2003) 327, 1053-1064.
[PMID:
12662930]
Aita T., Ota M. and Husimi Y.
An in silico exploration of the neutral network in protein sequence space. J. Theor. Biol. (2003) 221, 599-613.
[PMID:
12713943]
Handa N., Terada T., Kamewari Y., Hamana H., Tame JR., Park SY., Kinoshita K., Ota M., Nakamura H., Kuramitsu S., Shirouzu M. and Yokoyama S.
Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8. Protein Sci. (2003) 12, 1621-1632.
[PMID:
12876312]
Isogai Y., Ota M., Ishii A., Ishida M. and Nishikawa K.
Identification of amino acids involved in protein structural uniqueness: Implication for de novo protein design. Protein Eng. (2002) 15, 555-560.
Homma K., Fukuchi S., Kawabata T., Ota M. and Nishikawa K.
A systematic investigation identifies a significant number of probable pseudogenes in the Escherichia coli genome. Gene (2002) 294, 25-33.
Kawabata T., Fukuchi S., Homma K., Ota M., Araki T., Ito N., Ichiyoshi N. and Nishikawa K.
GTOP: a database of protein structures predicted from genome sequences. Nucleic Acids Res. (2002) 30, 294-298.
Ota M., Isogai Y. and Nishikawa K.
Knowledge-based potential defined for a rotamer library to design protein sequences, Protein Eng. (2001) 14, 557-564.
Tanaka H., Chinami M., Mizushima T., Ogasahara K., Ota M., Tsukihara T., Yutani K.
X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus and its cys-free mutant. J. of Biochem. (Tokyo) (2001) 130, 107-118.
Isogai Y., Ishii A., Fujisawa, T., Ota M. and Nishikawa K.
Redesign of artificial globins: effects of residue replacements at hydrophobic sites on the structural properties. Biochemistry (2000) 39, 5683-5690.
Tateno Y., Miyazaki S., Ota M., Sugawara H., Gojobori T.
DNA data bank of Japan (DDBJ) in collaboration with mass sequencing teams. Nucleic Acids Res. (2000) 28, 24-26.
Ota M., Kawabata T., Kinjo AR., Nishikawa K.
Cooperative approach for the protein fold recognition. Proteins (1999) suppl. 3, 126-132.
Nagano N, Ota M. and Nishikawa K.
Strong hydrophobic nature of cysteine residues in proteins. FEBS Lett. (1999) 45, 69-71.
Ota M. and Nishikawa K.
Feasibility in the inverse protein folding protocol. Protein Sci. (1999) 8, 1001-1009.
Takano K., Ota M., Ogasahara K., Yamagata Y., Nishikawa K., Yutani K.
Experimental verification of the "Stability Profile of Mutant Protein" (SPMP) data using mutant human lysozymes. Protein Eng. (1999) 12, 663-672.
Isogai Y., Ota M., Fujisawa T., Izuno H., Mukai M., Nakamura H., Iizuka T., Nishikawa K.
Design and synthesis of a globin fold. Biochemistry (1999) 38, 7431-7443.
Kawabata T., Ota M. and Nishikawa K.
The protein mutant database. Nucleic Acids Res. (1999) 27, 355-357.
Nakashima H., Ota M., Nishikawa K. and Ooi T.
Gene from nine genomes are separated into their organisms in the dinucleotide composition space. DNA Res. (1998) 5, 251-259.
Ota M., Isogai Y. and Nishikawa K.
Structural requirement of highly-conserved residues in globins. FEBS Lett. (1997) 415,
129-133.
Ota M. and Nishikawa K.
Assessment of pseudo-energy potential by the best five test. A new use of the three-dimensional profile of proteins. Protein Eng. (1997) 10, 339-351.
Ota M., Kanaya S. and Nishikawa K.
Desk-top analysis of the structural stabilities of various point mutations introduced into ribonuclrease H. J. Mol. Biol. (1995) 248, 733-738.
Ota M. and Miyamoto T.
Optimum particle size distribution in an electrorheorogical fluid. J. Appl. Phys. (1994) 76, 5528-5532.
Miyamoto T. and Ota M.
Mechanism of stress transmission from an electrorheological fluid to the electric plates. Appl. Phys. Lett. (1994) 64, 1165-1167.
Saitô N. and Ota M.
Prediction of Structure of Globular Proteins II. Tertiary Structure. Genome Informatics Workshop IV, (1993) 152-155.
Ota M. and Miyamoto T.
Many-boby effect in the static yield stress of electrorheological fluid. J. Appl. Phys. (1993) 74, 938-941.
宮本哲夫 太田元規
ERFの降伏応力に関する理論的実験的検討 機論B, (1993) 59, 1822-1828.
Ota M. and N. Saitô
Prediction of the Tertiary Structure of Parathypoid-Hormone-Related Protein (Residue 1-34) by the Island Model. J. Prot. Chem. (1992) 11, 623-628.
Saitô N., Kobayashi Y., Ota M. and Mitaku S.
Mechanism of Protein Folding and Its Applications to Structure Prediction of Proteins. Rep. Polym. Phys. Jap. (1992) 35, 1-22.
Aizawa Y., Kikuchi T., Harayama T., Yamamoto K., Ota M. and Tanaka K.
Stagnant Motions in Hamiltonian Systems. Prog. Theor. Phys. (1989) Suppl. 98, 36-82