| Year |
Citation |
Score |
| 2017 |
Kinjo AR, Bekker GJ, Wako H, Endo S, Tsuchiya Y, Sato H, Nishi H, Kinoshita K, Suzuki H, Kawabata T, Yokochi M, Iwata T, Kobayashi N, Fujiwara T, Kurisu G, et al. New tools and functions in Data-out activities at Protein Data Bank Japan (PDBj). Protein Science : a Publication of the Protein Society. PMID 28815765 DOI: 10.1002/Pro.3273 |
0.422 |
|
| 2017 |
Yamada KD, Omori S, Nishi H, Miyagi M. Identification of the sequence determinants of protein N-terminal acetylation through a decision tree approach. Bmc Bioinformatics. 18: 289. PMID 28578658 DOI: 10.1186/S12859-017-1699-4 |
0.466 |
|
| 2016 |
Hasumi H, Hasumi Y, Baba M, Nishi H, Furuya M, Vocke CD, Lang M, Irie N, Esumi C, Merino MJ, Kawahara T, Isono Y, Makiyama K, Warner AC, Haines DC, et al. H255Y and K508R missense mutations in tumour suppressor folliculin (FLCN) promote kidney cell proliferation. Human Molecular Genetics. PMID 28007907 DOI: 10.1093/Hmg/Ddw392 |
0.34 |
|
| 2016 |
Yamada KD, Nishi H, Nakata J, Kinoshita K. Structural characterization of single nucleotide variants at ligand binding sites and enzyme active sites of human proteins. Biophysics and Physicobiology. 13: 157-163. PMID 27924270 DOI: 10.2142/Biophysico.13.0_157 |
0.508 |
|
| 2016 |
Nishi H, Nakata J, Kinoshita K. Distribution of single-nucleotide variants on protein-protein interaction sites and its relationship with minor allele frequency. Protein Science : a Publication of the Protein Society. 25: 316-21. PMID 26580303 DOI: 10.1002/Pro.2845 |
0.444 |
|
| 2016 |
Nishi H. Structural and Functional Characteristics of Protein Phosphorylation Revealed by Bioinformatic Approaches Seibutsu Butsuri. 56: 207-211. DOI: 10.2142/Biophys.56.207 |
0.486 |
|
| 2015 |
Nishi H, Demir E, Panchenko AR. Crosstalk between signaling pathways provided by single and multiple protein phosphorylation sites. Journal of Molecular Biology. 427: 511-20. PMID 25451034 DOI: 10.1016/J.Jmb.2014.11.001 |
0.666 |
|
| 2014 |
Nishi H, Shaytan A, Panchenko AR. Physicochemical mechanisms of protein regulation by phosphorylation. Frontiers in Genetics. 5: 270. PMID 25147561 DOI: 10.3389/Fgene.2014.00270 |
0.749 |
|
| 2014 |
Nishi H, Kidera A. 3P267 Structural characteristics of phosphorylation sites on disordered binding regions(20. Origin of life & Evolution,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) Biophysics. 54. DOI: 10.2142/Biophys.54.S293_3 |
0.347 |
|
| 2014 |
Shimizu M, Nishi H, Moritsugu K, Kidera A. 1P038 Full-scale conformational sampling of K63 and linear polyubiquitins(01B. Protein : Structure & Function,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) Seibutsu Butsuri. 54. DOI: 10.2142/Biophys.54.S147_2 |
0.333 |
|
| 2013 |
Stefl S, Nishi H, Petukh M, Panchenko AR, Alexov E. Molecular mechanisms of disease-causing missense mutations. Journal of Molecular Biology. 425: 3919-36. PMID 23871686 DOI: 10.1016/J.Jmb.2013.07.014 |
0.641 |
|
| 2013 |
Nishi H, Tyagi M, Teng S, Shoemaker BA, Hashimoto K, Alexov E, Wuchty S, Panchenko AR. Cancer missense mutations alter binding properties of proteins and their interaction networks. Plos One. 8: e66273. PMID 23799087 DOI: 10.1371/Journal.Pone.0066273 |
0.697 |
|
| 2013 |
Nishi H, Hashimoto K, Madej T, Panchenko AR. Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization. Progress in Molecular Biology and Translational Science. 117: 3-24. PMID 23663963 DOI: 10.1016/B978-0-12-386931-9.00001-5 |
0.717 |
|
| 2013 |
Nishi H, Fong JH, Chang C, Teichmann SA, Panchenko AR. Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: analysis of human protein complexes. Molecular Biosystems. 9: 1620-6. PMID 23364837 DOI: 10.1039/C3Mb25514J |
0.707 |
|
| 2013 |
Nishi H, Demir E, Panchenko AR. 1P271 Crosstalk between signaling pathways revealed by database analysis of human phosphorylation sites(22B. Bioinformatics: Functional genomics,Poster) Seibutsu Butsuri. 53. DOI: 10.2142/Biophys.53.S150_6 |
0.582 |
|
| 2011 |
Nishi H, Hashimoto K, Panchenko AR. Phosphorylation in protein-protein binding: effect on stability and function. Structure (London, England : 1993). 19: 1807-15. PMID 22153503 DOI: 10.1016/J.Str.2011.09.021 |
0.724 |
|
| 2011 |
Nishi H, Koike R, Ota M. Cover and spacer insertions: small nonhydrophobic accessories that assist protein oligomerization. Proteins. 79: 2372-9. PMID 21656571 DOI: 10.1002/Prot.23084 |
0.456 |
|
| 2011 |
Hashimoto K, Nishi H, Bryant S, Panchenko AR. Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization. Physical Biology. 8: 035007. PMID 21572178 DOI: 10.1088/1478-3975/8/3/035007 |
0.718 |
|
| 2010 |
Nishi H, Ota M. Amino acid substitutions at protein-protein interfaces that modulate the oligomeris state Proteins: Structure, Function and Bioinformatics. 78: 1563-1574. PMID 20112251 DOI: 10.1002/Prot.22673 |
0.515 |
|
| 2009 |
Nishi H, Ota M. 2TP4-02 Insertion and/or deletion regions on protein-protein interface to alter oligomeric states.(The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49. DOI: 10.2142/Biophys.49.S49_6 |
0.475 |
|
| 2009 |
Nishi H, Ota M. 2P-237 Insertion and/or deletion regions on protein-protein interface to alter oligomeric states(Bioinformatics:Structural genomics,The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49. DOI: 10.2142/Biophys.49.S144_4 |
0.455 |
|
| 2007 |
Nishi H, Ota M. 1P251 Alternation of oligomeric states within protein families(Bioinformatics-structural, functional, and comparative genomics,Oral Presentations) Seibutsu Butsuri. 47. DOI: 10.2142/Biophys.47.S86_2 |
0.371 |
|
| 2006 |
Nishi H, Ota M. 2P434 Emergence of protein-protein interfaces : Insight from amino acid substitutions(48. Bioinformatics, genomics and proteomics (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) Seibutsu Butsuri. 46. DOI: 10.2142/Biophys.46.S404_2 |
0.426 |
|
| 2005 |
Nishi H, Ota M. 2P046 Amino acid substitutions on protein-protein interfaces that will cause the change of oligomeric states Seibutsu Butsuri. 45: S131. DOI: 10.2142/BIOPHYS.45.S131_2 |
0.357 |
|
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