Updated on 2026/03/07

写真a

 
UCHIKOGA NOBUYUKI
 
Organization
Undergraduate School School of Interdisciplinary Mathematical Sciences Associate Professor (non-tenured)
Title
Associate Professor (non-tenured)
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Degree

  • 博士(学術) ( 東京大学 )

Research Interests

  • タンパク質間相互作用予測

Research Areas

  • Informatics / Biological, health, and medical informatics

Education

  • The University of Tokyo

    - 2001

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    Country/Region: Japan

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  • The University of Tokyo

    - 1998

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    Country/Region: Japan

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  • Tokyo University of Science   Faculty of Science and Technology   Physics

    - 1996

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    Country/Region: Japan

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  • 城北学園高等学校

    - 1991

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    Country/Region: Japan

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Research History

  • Meiji University   School of Interdisciplinary Mathematical Sciences   Associate Professor (non-tenured)

    2021.4

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  • Meiji University   School of Interdisciplinary Mathematical Sciences   Assistant Professor (non-tenured)

    2018.10 - 2021.3

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  • Tokyo Institute of Technology

    2017.4 - 2018.3

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  • 立教大学非常勤講師

    2012.4 - 2021

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  • Chuo University   Faculty of Science and Engineering

    2012.4 - 2017.3

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  • Tokyo Institute of Technology   Graduate School of Information Science and Engineering, Department of Computer Science

    2010.4 - 2012.3

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  • (社)バイオ産業情報化コンソーシアム特別研究員(産業技術総合研究所 生命情報工学研究センター共同研究員)

    2006.4 - 2010.3

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  • Prefectural University of Hiroshima   Faculty of Life and Environmental Scienses

    2005.4 - 2014.3

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  • Nagahama Institute of Bio-Science and Technology

    2005.4 - 2006.3

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  • 名古屋大学工学研究科VBL 研究員

    2004.4 - 2006.3

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  • 日本学術振興会 特別研究員(PD) 名古屋大学工学研究科マテリアル理工学専攻応用物理学分野

    2003.4 - 2004.3

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  • 日本学術振興会 特別研究員(PD) 東京農工大学工学部生命工学科

    2001.4 - 2004.3

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Professional Memberships

Committee Memberships

  • Editorial Board : Frontiers in Bioinformatics (Protein Bioinformatics)   Review Editor  

    2022   

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    Committee type:Other

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  • 日本生物物理学会   第41回日本生物物理学会年会実行委員  

    2003   

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    Committee type:Academic society

    日本生物物理学会

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Papers

  • Evaluation of CONSRANK-Like Scoring Functions for Rescoring Ensembles of Protein-Protein Docking Poses Reviewed International journal

    Guillaume Launay, Masahito Ohue, Julia Prieto Santero, Yuri Matsuzaki, Cécile Hilpert, Nobuyuki Uchikoga, Takanori Hayashi, Juliette Martin

    Frontiers in molecular biosciences   7   308 - 559005   2020.10

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    Scoring is a challenging step in protein-protein docking, where typically thousands of solutions are generated. In this study, we ought to investigate the contribution of consensus-rescoring, as introduced by Oliva et al. (2013) with the CONSRANK method, where the set of solutions is used to build statistics in order to identify recurrent solutions. We explore several ways to perform consensus-based rescoring on the ZDOCK decoy set for Benchmark 4. We show that the information of the interface size is critical for successful rescoring in this context, but that consensus rescoring in itself performs less well than traditional physics-based evaluation. The results of physics-based and consensus-based rescoring are partially overlapping, supporting the use of a combination of these approaches.

    DOI: 10.3389/fmolb.2020.559005

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  • Rigid-Docking Approaches to Explore Protein-Protein Interaction Space Reviewed

    Yuri Matsuzaki, Nobuyuki Uchikoga, Masahito Ohue, Yutaka Akiyama

    NETWORK BIOLOGY   160   33 - 55   2017

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    DOI: 10.1007/10_2016_41

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  • Specificity of broad protein interaction surfaces for proteins with multiple binding partners Reviewed

    Uchikoga N, Matsuzaki Y, Ohue M, Akiyama Y

    Biophysics and Physicobiology   13   105 - 115   2016.6

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    Analysis of protein-protein interaction networks has revealed the presence of proteins with multiple interaction ligand proteins, such as hub proteins. For such proteins, multiple ligands would be predicted as interacting partners when predicting all-to-all protein-protein interactions (PPIs). In this work, to obtain a better understanding of PPI mechanisms, we focused on protein interaction surfaces, which differ between protein pairs. We then performed rigid-body docking to obtain information of interfaces of a set of decoy structures, which include many possible interaction surfaces between a certain protein pair. Then, we investigated the specificity of sets of decoy interactions between true binding partners in each case of alpha-chymotrypsin, actin, and cyclin-dependent kinase 2 as test proteins having multiple true binding partners. To observe differences in interaction surfaces of docking decoys, we introduced broad interaction profiles (BIPs), generated by assembling interaction profiles of decoys for each protein pair. After cluster analysis, the specificity of BIPs of true binding partners was observed for each receptor. We used two types of BIPs: those involved in amino acid sequences (BIP-seqs) and those involved in the compositions of interacting amino acid residue pairs (BIP-AAs). The specificity of a BIP was defined as the number of group members including all true binding partners. We found that BIP-AA cases were more specific than BIP-seq cases. These results indicated that the composition of interacting amino acid residue pairs was sufficient for determining the properties of protein interaction surfaces.

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  • 2P271 Analysis of properties of protein-protein interaction surface areas involved in more near-native complexes by Re-docking scheme(22A. Bioinformatics:Structural genomics,Poster)

    Uchikoga Nobuyuki, Matsuzaki Yuri, Ohue Masahito, Akiyama Yutaka, Hirokawa Takatsugu

    Seibutsu Butsuri   54 ( 1 )   S240   2014

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    Language:English   Publisher:The Biophysical Society of Japan General Incorporated Association  

    DOI: 10.2142/biophys.54.S240_1

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  • 2P014 MEGADOCK: a high-performance protein-protein interaction prediction tool on supercomputing environments(01A. Protein: Structure,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

    Ohue Masahito, Matsuzaki Yuri, Uchikoga Nobuyuki, Ishida Takashi, Akiyama Yutaka

    Seibutsu Butsuri   54 ( 1 )   S197   2014

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    Language:English   Publisher:The Biophysical Society of Japan General Incorporated Association  

    DOI: 10.2142/biophys.54.S197_2

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  • MEGADOCK: An All-to-All Protein-Protein Interaction Prediction System Using Tertiary Structure Data Reviewed

    Masahito Ohue, Yuri Matsuzaki, Nobuyuki Uchikoga, Takashi Ishida, Yutaka Akiyama

    PROTEIN AND PEPTIDE LETTERS   21 ( 8 )   766 - 778   2014

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  • Protein-protein Interaction Network Prediction by Using Rigid-Body Docking Tools: Application to Bacterial Chemotaxis Reviewed

    Yuri Matsuzaki, Masahito Ohue, Nobuyuki Uchikoga, Yutaka Akiyama

    PROTEIN AND PEPTIDE LETTERS   21 ( 8 )   790 - 798   2014

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  • MEGADOCK 3.0: A high-performance protein-protein interaction prediction software using hybrid parallel computing for petascale supercomputing environments Reviewed

    Yuri Matsuzaki, Nobuyuki Uchikoga, Masahito Ohue, Takehiro Shimoda, Toshiyuki Sato, Takashi Ishida, Yutaka Akiyama

    Source Code for Biology and Medicine   8   18   2013.9

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    DOI: 10.1186/1751-0473-8-18

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  • Re-Docking Scheme for Generating Near-Native Protein Complexes by Assembling Residue Interaction Fingerprints Reviewed

    Nobuyuki Uchikoga, Yuri Matsuzaki, Masahito Ohue, Takatsugu Hirokawa, Yutaka Akiyama

    PLOS ONE   8 ( 7 )   e69365   2013.7

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    DOI: 10.1371/journal.pone.0069365

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  • 2P267 Re-docking scheme for prediction of protein-protein interactions using interaction fingerprints(22A. Bioinformatics: Structural genomics,Poster)

    Uchikoga Nobuyuki, Matsuzaki Yuri, Ohue Masahito, Hirokawa Takatsugu, Akiyama Yutaka

    Seibutsu Butsuri   53 ( 1 )   S203   2013

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    DOI: 10.2142/biophys.53.S203_2

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  • The MEGADOCK project: Ultra-high-speed protein-protein interaction prediction tools on supercomputing environments Reviewed

    Takehiro Shimoda, Masahito Ohue, Yuri Matsuzaki, Takayuki Fujiwara, Nobuyuki Uchikoga, Takashi Ishida, Yutaka Akiyama

    2013 ACM Conference on Bioinformatics, Computational Biology and Biomedical Informatics, ACM-BCB 2013   667   2013

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    DOI: 10.1145/2506583.2506670

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  • 2PT104 Development of re-docking method by obtaining native interaction pattern(The 50th Annual Meeting of the Biophysical Society of Japan)

    Uchikoga Nobuyuki, Matsuzaki Yuri, Ohue Masahito, Akiyama Yutaka, Hirokawa Takatsugu

    Seibutsu Butsuri   52   S122   2012

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    DOI: 10.2142/biophys.52.S122_1

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  • Community-Wide Assessment of Protein-Interface Modeling Suggests Improvements to Design Methodology Reviewed

    Sarel J. Fleishman, Timothy A. Whitehead, Eva-Maria Strauch, Jacob E. Corn, Sanbo Qin, Huan-Xiang Zhou, Julie C. Mitchell, Omar N. A. Demerdash, Mayuko Takeda-Shitaka, Genki Terashi, Iain H. Moal, Xiaofan Li, Paul A. Bates, Martin Zacharias, Hahnbeom Park, Jun-su Ko, Hasup Lee, Chaok Seok, Thomas Bourquard, Julie Bernauer, Anne Poupon, Jerome Aze, Seren Soner, Sefik Kerem Ovali, Pemra Ozbek, Nir Ben Tal, Turkan Haliloglu, Howook Hwang, Thom Vreven, Brian G. Pierce, Zhiping Weng, Laura Perez-Cano, Caries Pons, Juan Fernandez-Recio, Fan Jiang, Feng Yang, Xinqi Gong, Libin Cao, Xianjin Xu, Bin Liu, Panwen Wang, Chunhua Li, Cunxin Wang, Charles H. Robert, Mainak Guharoy, Shiyong Liu, Yangyu Huang, Lin Li, Dachuan Guo, Ying Chen, Yi Xiao, Nir London, Zohar Itzhaki, Ora Schueler-Furman, Yuval Inbar, Vladimir Potapov, Mati Cohen, Gideon Schreiber, Yuko Tsuchiya, Eiji Kanamori, Daron M. Standley, Haruki Nakamura, Kengo Kinoshita, Camden M. Driggers, Robert G. Hall, Jessica L. Morgan, Victor L. Hsu, Jian Zhan, Yuedong Yang, Yaoqi Zhou, Panagiotis L. Kastritis, Alexandre M. J. J. Bonvin, Weiyi Zhang, Carlos J. Camacho, Krishna P. Kilambi, Aroop Sircar, Jeffrey J. Gray, Masahito Ohue, Nobuyuki Uchikoga, Yuri Matsuzaki, Takashi Ishida, Yutaka Akiyama, Raed Khashan, Stephen Bush, Denis Fouches, Alexander Tropsha, Juan Esquivel-Rodriguez, Daisuke Kihara, P. Benjamin Stranges, Ron Jacak, Brian Kuhlman, Sheng-You Huang, Xiaoqin Zou, Shoshana J. Wodak, Joel Janin, David Baker

    JOURNAL OF MOLECULAR BIOLOGY   414 ( 2 )   289 - 302   2011.11

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    DOI: 10.1016/j.jmb.2011.09.031

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  • 1E1536 Representative Interaction FingerPrint from decoys generated by rigid-body protein-protein docking(Genome biology, Bioinformatics,The 49th Annual Meeting of the Biophysical Society of Japan)

    Uchikoga Nobuyuki, Matsuzaki Yuri, Ohue Masahito, Hirokawa Takatsugu, Akiyama Yutaka

    Seibutsu Butsuri   51   S41   2011

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    DOI: 10.2142/biophys.51.S41_2

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  • Analysis of protein-protein docking decoys using interaction fingerprints: application to the reconstruction of CaM-ligand complexes Reviewed

    Nobuyuki Uchikoga, Takatsugu Hirokawa

    BMC BIOINFORMATICS   11   236   2010.5

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    DOI: 10.1186/1471-2105-11-236

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  • 3P295 Searching near-native decoys from various types of protein complexes by cluster analysis with Interaction FingerPrint(Bioinformatics: Structural genomics,The 48th Annual Meeting of the Biophysical Society of Japan)

    Uchikoga Nobuyuki, Hirokawa Takatsugu, Akiyama Yutaka

    Seibutsu Butsuri   50 ( 2 )   S197   2010

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    DOI: 10.2142/biophys.50.S197_4

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  • 2TP4-03 Post-docking process for flexible protein docking problems by using interaction fingerprints(The 47th Annual Meeting of the Biophysical Society of Japan)

    Uchikoga Nobuyuki, Hirokawa Takatsugu

    Seibutsu Butsuri   49   S50   2009

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    DOI: 10.2142/biophys.49.S50_1

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  • 2P-284 Protein-protein docking with protein flexibility from bioinformatic approach(Invited Talk for Early Research in Biophysics Award,Early Research in Biophysics Award)(The 46th Annual Meeting of the Biophysical Society of Japan)

    Uchikoga Nobuyuki, Hirokawa Takatsugu

    Seibutsu Butsuri   48   S119   2008

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    DOI: 10.2142/biophys.48.S119_1

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  • 1P488 Analysis of interaction profiles between calmodulin and various target molecules by a protein-protein interaction simulation(23. Bioinformatics, genomics and proteomics (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

    Uchikoga Nobuyuki, Hirokawa Takatsugu

    Seibutsu Butsuri   46 ( 2 )   S268   2006

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    DOI: 10.2142/biophys.46.S268_4

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  • Electric charge balance mechanism of extended soluble proteins Reviewed

    N Uchikoga, SY Takahashi, RC Ke, M Sonoyama, S Mitaku

    PROTEIN SCIENCE   14 ( 1 )   74 - 80   2005.1

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    DOI: 10.1110/ps.04984505

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  • 2E1345 Characteristic ratio of membrane proteins in genomes

    Uchikoga N., Gomi M., Sonoyama M., Mitaku S.

    Seibutsu Butsuri   42 ( 2 )   S111   2002

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    DOI: 10.2142/biophys.42.S111_2

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  • Distribution of Significantly Repetitive Tuples Implying

    Uchikoga Nobuyuki, Suyama Akira

    GI   8   350 - 351   1997

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    We studied the base sequences of tuples frequently occurring in both coding and noncoding regions of several modern genomes classified into the three major biospheres of the phylogenetic tree of life. These significantly repetitive tuples were found to be specific not only to genes but also to the biospheres.

    DOI: 10.11234/gi1990.8.350

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Books

  • バイオ研究がぐんぐん進むコンピュータ活用ガイド

    羊土社  2006.2 

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  • Interaction Surfaces of Proteins Involved in Bacterial Chemotaxis with Rigid-Body Docking Decoys

    Nobuyuki Uchikoga, Yuri Matsuzaki, Masahito Ohue, Yutaka Akiyama

    BIOPHYSICAL JOURNAL   112 ( 3 )   290A - 290A   2017.2

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    DOI: 10.1016/j.bpj.2016.11.1574

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  • A Docking Based Approach to Analyze Interaction Surfaces of Virus-Host Protein-Protein Interactions

    Yuri Matsuzaki, Jaak Simm, Nobuyuki Uchikoga, Yutaka Akiyama

    BIOPHYSICAL JOURNAL   112 ( 3 )   451A - 452A   2017.2

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    DOI: 10.1016/j.bpj.2016.11.2421

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  • Analysis of Physico-Chemical Properties of Protein Docking Decoys Generated by Rigid-Body Docking

    Nobuyuki Uchikoga, Yuri Matsuzaki, Masahito Ohue, Yutaka Akiyama

    BIOPHYSICAL JOURNAL   110 ( 3 )   327A - 327A   2016.2

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    DOI: 10.1016/j.bpj.2015.11.1759

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  • Megadock 4.0. An Ultra-High-Performance Protein-Protein Docking Software for Heterogeneous Supercomputers

    Masahito Ohue, Yuri Matsuzaki, Nobuyuki Uchikoga, Takashi Ishida, Yutaka Akiyama

    BIOPHYSICAL JOURNAL   110 ( 3 )   327A - 327A   2016.2

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    DOI: 10.1016/j.bpj.2015.11.1758

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  • Post-docking analysis by physicochemical properties of protein-protein interactions generated from rigid-body docking processes

    Nobuyuki Uchikoga, Masahito Ohue, Yuri Matsuzaki, Yutaka Akiyama

    PROTEIN SCIENCE   24   253 - 253   2015.10

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  • Analysis of Amino Acid Properties in Interaction Surfaces of Decoys Generated by Re-Docking Scheme

    Nobuyuki Uchikoga, Yuri Matsuzaki, Masahito Ohue, Takatsugu Hirokawa, Yutaka Akiyama

    BIOPHYSICAL JOURNAL   108 ( 2 )   472A - 472A   2015.1

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    DOI: 10.1016/j.bpj.2014.11.2579

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  • Re-Docking Scheme to Explore Docking Search Space by using Interaction Profiles

    Nobuyuki Uchikoga, Yuri Matsuzaki, Masahito Ohue, Takatsugu Hirokawa, Yutaka Akiyama

    BIOPHYSICAL JOURNAL   106 ( 2 )   410A - 410A   2014.1

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    DOI: 10.1016/j.bpj.2013.11.2310

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  • MEGADOCK:構造ドッキング計算を用いたタンパク質間相互作用の大規模予測

    大上雅史, 松崎由理, 内古閑伸之, 石田貴士, 秋山泰

    日本蛋白質科学会年会プログラム・要旨集   13th   63   2013.5

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  • We will Control the Integrated Information Space!

    NEMOTO Wataru, UCHIKOGA Nobuyuki

    Seibutsu Butsuri   52 ( 2 )   110 - 111   2012.3

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    Language:Japanese   Publisher:The Biophysical Society of Japan  

    DOI: 10.2142/biophys.52.110

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  • Docking-calculation-based All-to-all Protein-RNA Interaction Prediction

    OHUE MASAHITO, MATSUZAKI YURI, UCHIKOGA NOBUYUKI, ISHIDA TAKASHI, AKIYAMA YUTAKA

    IEICE technical report. Neurocomputing   111 ( 96 )   169 - 176   2011.6

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    Elucidating protein-RNA interactions (PRIs) is important for understanding cellular systems. We developed a PRI prediction method by using a rigid-body protein-RNA docking calculation with tertiary structure data. We evaluated this method by using 78 protein-RNA complex structures from the Protein Data Bank. We predicted the interactions for pairs in 78x78 combinations. Of these, 78 original complexes were defined as positive pairs, and the other 6,006 complexes were defined as negative pairs; then an F-measure value of 0.465 was obtained with our prediction system.

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  • Docking-calculation-based All-to-all Protein-RNA Interaction Prediction

    OUE MASAHITO, MATSUZAKI YURI, UCHIKOGA NOBUYUKI, ISHIDA TAKASHI, AKIYAMA YUTAKA

    電子情報通信学会技術研究報告   111 ( 96(NC2011 1-19) )   169 - 176   2011.6

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    Elucidating protein-RNA interactions (PRIs) is important for understanding cellular systems. We developed a PRI prediction method by using a rigid-body protein-RNA docking calculation with tertiary structure data. We evaluated this method by using 78 protein-RNA complex structures from the Protein Data Bank. We predicted the interactions for pairs in 78x78 combinations. Of these, 78 original complexes were defined as positive pairs, and the other 6,006 complexes were defined as negative pairs; then an F-measure value of 0.465 was obtained with our prediction system.

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  • A visualization method and accuracy improvement for protein-protein interaction predictions

    YAMAMOTO KOHEI, OHUE MASAHITO, UCHIKOGA NOBUYUKI, MATSUZAKI YURI, ISHIDA TAKASHI, AKIYAMA YUTAKA

    IEICE technical report. Neurocomputing   111 ( 96 )   177 - 183   2011.6

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    Language:Japanese   Publisher:The Institute of Electronics, Information and Communication Engineers  

    To predict all-to-all the protein-protein interactions (PPIs) from protein monomeric structures, we have been developing a PPI prediction method based on a protein docking calculation. In this study, we developed two methods which visualize complex candidates generated by protein docking calculations. The first method visualizes 3D distribution of the complex candidates in space. And the second one visualizes PPI tendency of each residue by coloring them according to the interaction frequency. By using these visualization methods, we also developed a new score to identify false positives and improved the accuracy of aPPI prediction.

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  • A visualization method and accuracy improvement for protein-protein interaction predictions

    YAMAMOTO KOHEI, OUE MASAHITO, UCHIKOGA NOBUYUKI, MATSUZAKI YURI, ISHIDA TAKASHI, AKIYAMA YUTAKA

    電子情報通信学会技術研究報告   111 ( 96(NC2011 1-19) )   177 - 183   2011.6

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    Language:Japanese   Publisher:The Institute of Electronics, Information and Communication Engineers  

    To predict all-to-all the protein-protein interactions (PPIs) from protein monomeric structures, we have been developing a PPI prediction method based on a protein docking calculation. In this study, we developed two methods which visualize complex candidates generated by protein docking calculations. The first method visualizes 3D distribution of the complex candidates in space. And the second one visualizes PPI tendency of each residue by coloring them according to the interaction frequency. By using these visualization methods, we also developed a new score to identify false positives and improved the accuracy of aPPI prediction.

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  • Post-docking Analysis with Protein-protein Interaction Fingerprints

    UCHIKOGA Nobuyuki, HIROKAWA Takatsugu

    Seibutsu Butsuri   51 ( 1 )   28 - 29   2011.1

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    Language:Japanese   Publisher:The Biophysical Society of Japan  

    DOI: 10.2142/biophys.51.028

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  • タンパク質とRNAの立体構造に基づいた網羅的計算による相互作用予測

    大上雅史, 松崎由理, 内古閑伸之, 石田貴士, 秋山泰

    ハイパフォーマンスコンピューティングと計算科学シンポジウム論文集   2011   56 - 56   2011.1

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  • Exhaustive protein-protein interaction network prediction by using MEGADOCK

    Akiyama, Y, Matsuzaki, Y, Uchikoga, N, Ohue, M

    Biosupercomputing Newsletter   3   p.8   2010.12

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  • MEGADOCKによるタンパク質間相互作用予測~システム生物学への応用~

    松崎由理, 大上雅史, 内古閑伸之, 石田貴士, 秋山泰

    Tsubame e-Sci J   2 ( 2 )   (JA)14-18,(EN)34-37 - 18   2010.11

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  • Computer prediction of protein-protein interaction network using MEGADOCK: application to systems biology

    Tsubame ESJ.   2   34 - 37   2010.11

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  • 相互作用プロファイルによるタンパク質複合体予測のポストドッキング解析

    内古閑伸之, 広川貴次, 秋山泰

    構造活性相関シンポジウム講演要旨集   38th   50 - 51   2010.10

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  • 大きな構造変化を考慮したタンパク質複合体予測構造の相互作用プロファイルを用いたクラスタ解析

    内古閑伸之, 広川貴次

    日本蛋白質科学会年会プログラム・要旨集   9th   136   2009.4

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  • 構造変化を伴うタンパク質間ドッキングシミュレーション

    内古閑伸之, 広川貴次

    日本蛋白質科学会年会プログラム・要旨集   8th   56   2008.5

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  • 1P252 Docking analysis of a large conformational changing protein by using an interaction profile of amino acid residues pairs(Bioinformatics-structural, functional, and comparative genomics,Oral Presentations)

    Uchikoga Nobuyuki, Hirokawa Takatsugu

    Biophysics   47 ( 1 )   S86   2007.11

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    DOI: 10.2142/biophys.47.S86_3

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  • 1P286 Classification of physicochemical interactions between dumbbell-type proteins and their target proteins

    Uchikoga N, Mitaku S

    Biophysics   45 ( 1 )   S103   2005.10

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    DOI: 10.2142/biophys.45.S103_2

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  • Genome Scale Classification of Extended Proteins by a Predictor SOSUIdumbbell

    Uchikoga Nobuyuki, Rungcong Ke, Akazawa Fumitsugu, Sonoyama Masashi, Mitaku Shigeki

    GI   14   p.524 - 525   2003.12

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    DOI: 10.11234/gi1990.14.524

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  • Prediction to extended-type proteins in a complex molecule from their amino acid sequences

    Uchikoga N, Takahashi T, Ke R, Sonoyama M, Mitaku S

    Biophysics   43 ( 1 )   S212   2003.8

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    DOI: 10.2142/biophys.43.S212_1

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  • ゲノムにおける膜タンパク質の割合に関する解析

    内古閑伸之, 五味雅裕, 園山正史, 美宅成樹

    日本生物物理学会年会講演予稿集   40th   S111   2002.11

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  • DNA Sequence Analysis for RNA Splicing mechanism

    Fujiwara Toyofumi, Uchikoga Nobuyuki, Mitaku Shigeki

    Meeting abstracts of the Physical Society of Japan   57 ( 2 )   251 - 251   2002.8

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  • Prediction System for Dumbbell-Type Proteins: SOSUIdumbbell

    Uchikoga Nobuyuki, Takahashi Shun-ya, Runcong Ke, Akazawa Fumitsugu, Sonoyama Masashi, Mitaku Shigeki

    GI   12   p.328 - 329   2001.12

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    DOI: 10.11234/gi1990.12.328

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  • ゲノム塩基配列全体にみられる統計的有意に多いタプルを用いた遺伝子水平移動の考察

    内古閑伸之, 陶山明

    日本生物物理学会年会講演予稿集   39th   S78   2001.10

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  • Study on horizontal transfer of genes detected by tuples statistically preferred in the whole genome.

    Uchikoga N, Suyama A

    Biophysics   41 ( 1 )   S78   2001.9

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    DOI: 10.2142/biophys.41.S78_1

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  • Evolution of E.coli genome with statistical significant tuples

    Uchikoga N, Suyama A

    Biophysics   40 ( 1 )   S198   2000.8

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    DOI: 10.2142/biophys.40.S198_1

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  • Distances between Completely Matched Tuples in the Modern Gene Sequences

    Uchikoga Nobuyuki, Suyama Akira

    GI   9   p.388 - 351   1999.12

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    DOI: 10.11234/gi1990.10.350

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  • アミノ酸配列に観測されないcoding DNA中の頻出類似配列

    内古閑伸之, 陶山明

    日本分子生物学会年会プログラム・講演要旨集   22nd   764   1999.11

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  • DNA配列中の類似配列の出現頻度による進化的考察

    内古閑伸之, 陶山明

    日本生物物理学会年会講演予稿集   37th   S202   1999.9

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  • Evolutional consideration of DNA sequence using frequency of similar tuples.

    Uchikoga N, Suyama A

    Biophysics   39 ( 1 )   S202   1999.9

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    DOI: 10.2142/biophys.39.S202_1

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  • Statistically significant repetition of short tuples in DNA sequences

    Uchikoga N, Suyama A

    Biophysics   38 ( 2 )   S96   1998.9

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  • DNA配列に頻出する繰り返し配列

    内古閑伸之, 陶山明

    日本生物物理学会年会講演予稿集   36th   S96   1998.9

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  • Gene Has Its Inherent Significantly Repetitive Tuples

    Uchikoga Nobuyuki, Suyama Akira

    GI   8   p.350 - 389   1997.12

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    DOI: 10.11234/gi1990.9.388

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  • Search for the vestiges of primordial genes in modern genomes.

    UCHIKOGA NOBUYUKI, SUYAMA AKIRA

    日本分子生物学会年会プログラム・講演要旨集   20th   666   1997.12

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  • 2T06 Searching for vestiges of primodial words in base sequences of modern genomes

    Uchikoga N, Suyama A

    Biophysics   37 ( 2 )   S129   1997.9

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  • 計算機による原始遺伝子の痕跡の探査

    内古閑伸之, 陶山明

    日本生物物理学会年会講演予稿集   35th   S129   1997.9

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  • Vestiges of Primordial Words in Base Sequences of Modern Genomes

    Uchikoga Nobuyuki, Suyama Akira

    GI   7   p.242 - 243   1996.12

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    Base sequences of genomes were found to consist of a restricted set of homologous short segments when examining base sequences of several genomes classified into different branches of the phylogenetic tree of life. The homologous segments were longer than the triplet codons encoding amino acids, and were observed in both coding and noncoding regions more frequently than the random expectation level. They are thus likely to be the vestiges of the primordial words arisen in the primeval Earth eons ago.

    DOI: 10.11234/gi1990.7.242

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Presentations

  • Re-docking by analyzing the profile of protein-protein interaction

    CBI学会2016年大会  2016 

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  • Analysis of Physico-chemical properties of protein docking decoys generated by rigid-body docking

    Biophysical society 60th annual meeting  2016 

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  • Biophysical view of protein interaction surfaces

    低分子化合物とタンパク質の情報解析  2016 

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  • MEGADOCK 4.0: an ultra-high-performance protein-protein docking software for heterogeneous supercomputers

    Biophysical society 60h annual meeting  2016 

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  • MEGADOCK: A high-performance protein-protein interaction prediction software for petascale super-computing environments

    Supercomputational Life Science 2015 (SCLS2015)  2015 

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  • アミノ酸プロファイルによるタンパク質ペプチド複合体のポストドッキング解析

    第53回日本生物物理学会年会  2015 

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  • タンパク質C末端に存在する機能未知配列に関する研究

    第15回日本蛋白質科学会年会  2015 

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  • MEGADOCK: A high-performance protein-protein interaction prediction software for petascale supercomputing environments

    3rd IIT Madras-Tokyo Tech Joint Symposium on Algorithms and Applications of Bioinformatics  2015 

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  • Analysis of protein docking decoys in terms of physicochemical properties of protein interaction surfaces using rigid-body docking process

    3rd IIT Madras - Tokyo Tech Joint Symposium on Algorithms and Applications of Bioinformatics  2015 

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  • 剛体アンサンブルドッキングによって得られた候補構造群における相互作用残基ペアの特徴の解析

    第53回日本生物物理学会年会  2015 

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  • タンパク質間相互作用残基の物理化学的性質による単純化プロファイルを用いたポストドッキング解析

    第15回日本蛋白質科学会年会  2015 

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  • Analysis of properties of protein-protein interaction surface areas involved in more near-native complexes by Re-docking scheme

    日本生物物理学会第52回年会  2014 

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  • MEGADOCK: a high-performance protein-protein interaction prediction tool on supercomputing environments

    日本生物物理学会第52回年会  2014 

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  • Re-docking scheme to explore docking search space by using interaction profiles

    Biophysical Society  2014 

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  • Protein-protein interacting prediction by using amino acids interaction pattern in rigid-body docking process.

    Biophysical Society 57th annual meeting  2013 

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  • Re-docking scheme of protein-protein interactions for generating near-native interaction patterns in difficult docking cases. (Invited)

    2nd IIT Madras - Tokyo Tech joint symposium on Techniques and Applications of Bioinformatics  2013 

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  • Re-docking scheme for prediction of protein-protein interactions using interaction fingerprints.

    The Biophysical Society of Japan  2013 

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  • Development of re-docking method by using native interaction patterns.

    第50回日本生物物理学会年会  2012 

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  • Exhaustive protein-protein interaction network prediction by MEGADOCK

    Asia Hub for e-Drug Discovery Symposium 2010/Yonsei University  2011 

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  • Representative interaction fingerprint from decoy generated by rigid-body docking

    第48回日本生物物理学会年会予稿集/日本生物物理学会  2011 

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  • Analysis for generating representative interaction fingerprints of protein-protein decoys (Invited)

    IIT Madras-Tokyo Tech Joint Workshop on Bioinformatics and Large Scale Data Analysis/IIT Madras  2011 

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  • 相互作用プロファイルによるタンパク質複合体予測のポストドッキング解析

    第38回構造活性相関シンポジウム講演要旨集/日本薬学会  2010 

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  • Post-docking process for flexible protein docking problems by using intearction fingerprints

    第47回日本生物物理学会年会予稿集/日本生物物理学会  2009 

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  • べん毛モーターの熱反応性

    第47回日本生物物理学会年会予稿集/日本生物物理学会  2009 

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  • タンパク質の揺らぎを考慮したタンパク質間ドッキングシミュレーション (若手奨励賞選考会 若手招待講演)

    第46回日本生物物理学会年会予稿集/日本生物物理学会  2008 

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  • 構造変化の大きなタンパク質におけるアミノ酸残基間の相互作用プロファイルを利用した複合体形成シミュレーション解析

    第45回日本生物物理学会年会予稿集/日本生物物理学会  2007 

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  • Analysis of interaction profiles between calmodulin and various target molecules by a protein-protein interaction simulation

    第44回日本生物物理学会年会予稿集/日本生物物理学会  2006 

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  • ダンベル型タンパク質―標的分子複合体における物理化学的相互作用の解析

    第43回日本生物物理学会年会予稿集/日本生物物理学会  2005 

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  • 複合体における伸びた形をしたタンパク質のアミノ酸配列による予測

    第41回日本生物物理学会年会予稿集/日本生物物理学会  2003 

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  • ゲノムにおける膜タンパク質の割合に関する解析

    第40回日本生物物理学会年会予稿集/日本生物物理学会  2002 

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  • ゲノム塩基配列全体にみられる統計的有意に多いタプルを用いた遺伝子水平移動の考察

    第39回日本生物物理学会年会予稿集/日本生物物理学会  2001 

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  • 頻出する短い配列によるE.coliゲノムの進化的考察

    第38回日本生物物理学会年会予稿集/日本生物物理学会  2000 

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  • アミノ酸配列に観測されないcoding DNA中の頻出類似配列

    第22回日本分子生物学会年会予稿集/日本分子生物学会  1999 

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  • DNA配列中の類似配列の出現頻度による進化的考察

    第47回日本生物物理学会年会予稿集/日本生物物理学会  1999 

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  • DNA配列に頻出する繰り返し配列 「シンポジウム ゲノム・プロテオームの文法構造を探る」

    第36回日本生物物理学会年会予稿集/日本生物物理学会  1998 

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  • 計算機による原始遺伝子の痕跡の探索

    第35回日本生物物理学会年会予稿集/日本生物物理学会  1997 

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  • 現代ゲノムにおける原始遺伝子の痕跡の探査 「ワークショップ 生物進化と生体ネオシステム」

    第20回日本分子生物学会年会予稿集/日本分子生物学会  1996 

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Works

  • 網羅的ドッキングを用いた熱帯病関連タンパク質間相互作用解析

    2016.4

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  • アミノ酸残基レベルの相互作用プロファイルを用いたタンパク質相互作用予測法の開発

    2015.4

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  • アミノ酸配列からのタンパク質複合体形成の予測

    2001.4

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Research Projects

  • Tropical diseases-related protein-protein interaction analysis by using exhaustive docking

    Grant number:16K00388  2016.4 - 2019.3

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

    Matsuzaki Yuri, Shimu Yaku, Marutan Jurietto, Renei Giyomu

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    Grant amount:\4420000 ( Direct Cost: \3400000 、 Indirect Cost:\1020000 )

    We have developed a computational method of protein-protein interaction (PPI) prediction by using interaction profile analysis of rigid-docking decoys. By combining originially developed interaction fingerprint representation of docking decoys and an extended machine learning (extra-trees) method, we have successfully improved prediction performance of conventional docking based prediction methods. We applied this PPI prediction method on predicting i) PPIs of Trypanosoma cruzi and ii) interactions of dengue virus and human proteins and obtained in total 67 novel PPI candidates. Two candidate pairs of high prediction score were tested by immunoprecipitation experiments and one was confirmed to have affinity. We have also conducted comparison analysis of virus-human and human-human protein interactions in terms of interaction fingerprints of docking decoy set.

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  • アミノ酸残基レベルの相互作用プロファイルを用いたタンパク質間相互作用予測法の開発

    2015.4 - 2018.3

    日本学術振興会  科研費 基盤研究(C) 

    内古閑 伸之

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  • プロファイル法によるタンパク質間相互作用予測

    2006

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  • アミノ酸配列からのタンパク質複合体形成の予測

    Grant number:01J60033  2001.4 - 2004.3

    日本学術振興会  特別研究員奨励費  特別研究員奨励費

    内古閑 伸之

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    Authorship:Principal investigator  Grant type:Competitive

    タンパク質の立体構造や複合体形成はアミノ酸残基の物理化学的相互作用によるメカニズムによって理解できる。複合体形成のメカニズムを考える基礎固めとして、アミノ酸残基間の静電相互作用に着目し、アミノ酸配列情報から伸びた形をしたタンパク質(伸長型タンパク質)の予測を行ってきた。伸長型タンパク質の立体構造の特徴はN末端側とC末端側のドメインが構造上、離れていることである。立体構造情報から得られた典型的な伸長形タンパク質はカルモジュリン、トロポニンCなどであった。また、典型的な伸長型タンパク質のアミノ酸配列から、この構造の形成メカニズムとして静電相互作用による斥力が支配的であると考えられる。
    実際に立体構造データベース(PDB)のアミノ酸配列による予測からカルモジュリン、トロポニンCが得られ、さらにDNA結合タンパク質も得られた。カルモジュリンやトロポニンCのアミノ酸配列は負電荷をもつアミノ酸残基を多く持っており、正電荷を多く持つペプチド分子と結合しやすい。一方でDNA結合タンパク質は正電荷を多く持ち、負に帯電しているDNA分子と結合しやすい。
    また、75種の生物ゲノムについてこの原理を適用し予測した。典型的な伸長型タンパク質であるカルモジュリンやトロポニンCはゲノム内にそれほど多くなく、伸長型タンパク質として予測された機能既知遺伝子情報の半分以上はDNA結合タンパク質であった。また、機能未知で伸長型と予測されたタンパク質は正電荷を多く持ちDNA結合タンパク質の性質を有していた。ヒトゲノムにおいては伸長型タンパク質が予測対象の75種の生物の中で最も多く予測され、機能未知でDNA結合タンパク質の性質を有している遺伝子も最も多く発見できた。以上の成果から、一般的なタンパク質の立体構造形成の相互作用をアミノ酸配列情報から考えるための方向性が見いだせた。

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