메뉴 건너뛰기




Volumn 33, Issue 2, 2012, Pages 359-363

Protein-protein interaction sites are hot spots for disease-associated nonsynonymous SNPs

Author keywords

Bioinformatics.; Interactome; Nonsynonymous snps; Protein structure

Indexed keywords

SODIUM CHLORIDE; STERICOL;

EID: 84857790275     PISSN: 10597794     EISSN: 10981004     Source Type: Journal    
DOI: 10.1002/humu.21656     Document Type: Article
Times cited : (144)

References (46)
  • 2
    • 79954986866 scopus 로고    scopus 로고
    • A new face and new challenges for Online Mendelian Inheritance in Man (OMIM(R))
    • Amberger J, Bocchini C, Hamosh A. 2011. A new face and new challenges for Online Mendelian Inheritance in Man (OMIM(R)). Hum Mutat 32:564-567.
    • (2011) Hum Mutat , vol.32 , pp. 564-567
    • Amberger, J.1    Bocchini, C.2    Hamosh, A.3
  • 5
    • 0042667013 scopus 로고    scopus 로고
    • Stereospecific interactions of proline residues in protein structures and complexes
    • Bhattacharyya R, Chakrabarti P. 2003. Stereospecific interactions of proline residues in protein structures and complexes. J Mol Biol 331:925-940.
    • (2003) J Mol Biol , vol.331 , pp. 925-940
    • Bhattacharyya, R.1    Chakrabarti, P.2
  • 6
    • 34547100092 scopus 로고    scopus 로고
    • SNAP: predict effect of non-synonymous polymorphisms on function
    • Bromberg Y, Rost B. 2007. SNAP: predict effect of non-synonymous polymorphisms on function. Nucleic Acids Res 35:3823-3835.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3823-3835
    • Bromberg, Y.1    Rost, B.2
  • 10
    • 61449243886 scopus 로고    scopus 로고
    • MatrixDB, a database focused on extracellular protein-protein and protein-carbohydrate interactions
    • Chautard E, Ballut L, Thierry-Mieg N, Ricard-Blum S. 2009. MatrixDB, a database focused on extracellular protein-protein and protein-carbohydrate interactions. Bioinformatics 25:690-691.
    • (2009) Bioinformatics , vol.25 , pp. 690-691
    • Chautard, E.1    Ballut, L.2    Thierry-Mieg, N.3    Ricard-Blum, S.4
  • 14
    • 0027317580 scopus 로고
    • Performance evaluation of amino acid substitution matrices
    • Henikoff S, Henikoff JG. 1993. Performance evaluation of amino acid substitution matrices. Proteins 17:49-61.
    • (1993) Proteins , vol.17 , pp. 49-61
    • Henikoff, S.1    Henikoff, J.G.2
  • 15
    • 77949268302 scopus 로고    scopus 로고
    • Involvement of connexin 43 in the acupuncture effect of improving rat blastocyst implantation
    • Huang GY, Zheng CH, Wu YX, Wang W. 2010. Involvement of connexin 43 in the acupuncture effect of improving rat blastocyst implantation. Fertil Steril 93:1715-1717.
    • (2010) Fertil Steril , vol.93 , pp. 1715-1717
    • Huang, G.Y.1    Zheng, C.H.2    Wu, Y.X.3    Wang, W.4
  • 16
    • 0025938637 scopus 로고
    • Molecular characterization of variant alpha-subunit of electron transfer flavoprotein in three patients with glutaric acidemia type II-and identification of glycine substitution for valine-157 in the sequence of the precursor, producing an unstable mature protein in a patient
    • Indo Y, Glassberg R, Yokota I, Tanaka K. 1991. Molecular characterization of variant alpha-subunit of electron transfer flavoprotein in three patients with glutaric acidemia type II-and identification of glycine substitution for valine-157 in the sequence of the precursor, producing an unstable mature protein in a patient. Am J Hum Genet 49:575-580.
    • (1991) Am J Hum Genet , vol.49 , pp. 575-580
    • Indo, Y.1    Glassberg, R.2    Yokota, I.3    Tanaka, K.4
  • 17
    • 33646757738 scopus 로고    scopus 로고
    • Compound and doublemutations in patients with hypertrophic cardiomyopathy: implications for genetic testing and counselling
    • Ingles J, Doolan A, Chiu C, Seidman J, Seidman C, Semsarian C. 2005. Compound and doublemutations in patients with hypertrophic cardiomyopathy: implications for genetic testing and counselling. J Med Genet 42:e59.
    • (2005) J Med Genet , vol.42
    • Ingles, J.1    Doolan, A.2    Chiu, C.3    Seidman, J.4    Seidman, C.5    Semsarian, C.6
  • 18
    • 77955590137 scopus 로고    scopus 로고
    • Humanallelic variation: perspective from protein function, structure, and evolution
    • JordanDM, RamenskyVE, Sunyaev SR. 2010.Humanallelic variation: perspective from protein function, structure, and evolution. Curr Opin Struc Biol 20:342-350.
    • (2010) Curr Opin Struc Biol , vol.20 , pp. 342-350
    • Jordan, D.M.1    Ramensky, V.E.2    Sunyaev, S.R.3
  • 19
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 20
    • 77954759220 scopus 로고    scopus 로고
    • Geometric similarities of protein-protein interfaces at atomic resolution are only observed within homologous families: an exhaustive structural classification study
    • Kinjo AR, Nakamura H. 2010. Geometric similarities of protein-protein interfaces at atomic resolution are only observed within homologous families: an exhaustive structural classification study. J Mol Biol 399:526-540.
    • (2010) J Mol Biol , vol.399 , pp. 526-540
    • Kinjo, A.R.1    Nakamura, H.2
  • 22
    • 69749093207 scopus 로고    scopus 로고
    • Positional conservation and amino acids shape the correct diagnosis and population frequencies of benign and damaging personal amino acid mutations
    • Kumar S, Suleski MP, Markov GJ, Lawrence S, Marco A, Filipski AJ. 2009. Positional conservation and amino acids shape the correct diagnosis and population frequencies of benign and damaging personal amino acid mutations. Genome Res 19:1562-1569.
    • (2009) Genome Res , vol.19 , pp. 1562-1569
    • Kumar, S.1    Suleski, M.P.2    Markov, G.J.3    Lawrence, S.4    Marco, A.5    Filipski, A.J.6
  • 24
    • 0038021436 scopus 로고    scopus 로고
    • Assessment of blind predictions of protein-protein interactions: current status of docking methods
    • Mendez R, Leplae R, De Maria L, Wodak SJ. 2003. Assessment of blind predictions of protein-protein interactions: current status of docking methods. Proteins 52:51-67.
    • (2003) Proteins , vol.52 , pp. 51-67
    • Mendez, R.1    Leplae, R.2    De Maria, L.3    Wodak, S.J.4
  • 25
    • 0027131267 scopus 로고
    • Familial genetic defect in a case of leukocyte adhesion deficiency
    • Ohashi Y, Yambe T, Tsuchiya S, Kikuchi H, Konno T. 1993. Familial genetic defect in a case of leukocyte adhesion deficiency. Hum Mutat 2:458-467.
    • (1993) Hum Mutat , vol.2 , pp. 458-467
    • Ohashi, Y.1    Yambe, T.2    Tsuchiya, S.3    Kikuchi, H.4    Konno, T.5
  • 26
    • 75549085083 scopus 로고    scopus 로고
    • Human protein reference database and human proteinpedia as discovery tools for systems biology
    • Prasad TS, Kandasamy K, Pandey A. 2009. Human protein reference database and human proteinpedia as discovery tools for systems biology. Methods Mol Biol 577:67-79.
    • (2009) Methods Mol Biol , vol.577 , pp. 67-79
    • Prasad, T.S.1    Kandasamy, K.2    Pandey, A.3
  • 29
    • 45949108954 scopus 로고    scopus 로고
    • Protein interactions in human genetic diseases
    • Schuster-Bockler B, Bateman A. 2008. Protein interactions in human genetic diseases. Genome Biol 9:R9.
    • (2008) Genome Biol , vol.9
    • Schuster-Bockler, B.1    Bateman, A.2
  • 32
    • 79953071469 scopus 로고    scopus 로고
    • Three-dimensional modeling of protein interactions and complexes is going 'omics
    • Stein A, Mosca R, Aloy P. 2011. Three-dimensional modeling of protein interactions and complexes is going 'omics. Curr Opin Struc Biol 21:200-208.
    • (2011) Curr Opin Struc Biol , vol.21 , pp. 200-208
    • Stein, A.1    Mosca, R.2    Aloy, P.3
  • 33
    • 79951521421 scopus 로고    scopus 로고
    • Progress and promise of genome-wide association studies for human complex trait genetics
    • Stranger BE, Stahl EA, Raj T. 2011. Progress and promise of genome-wide association studies for human complex trait genetics. Genetics 187:367-383.
    • (2011) Genetics , vol.187 , pp. 367-383
    • Stranger, B.E.1    Stahl, E.A.2    Raj, T.3
  • 34
    • 0037588762 scopus 로고    scopus 로고
    • Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form
    • Takeda S, Yamashita A, Maeda K, Maeda Y. 2003. Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. Nature 424:35-41.
    • (2003) Nature , vol.424 , pp. 35-41
    • Takeda, S.1    Yamashita, A.2    Maeda, K.3    Maeda, Y.4
  • 35
    • 66149102833 scopus 로고    scopus 로고
    • Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
    • Teng S, Madej T, Panchenko A, Alexov E. 2009. Modeling effects of human single nucleotide polymorphisms on protein-protein interactions. Biophys J 96:2178-2188.
    • (2009) Biophys J , vol.96 , pp. 2178-2188
    • Teng, S.1    Madej, T.2    Panchenko, A.3    Alexov, E.4
  • 36
    • 41949118839 scopus 로고    scopus 로고
    • Approaches and resources for prediction of the effects of non-synonymous single nucleotide polymorphism on protein function and interactions
    • Teng S, Michonova-Alexova E, Alexov E. 2008. Approaches and resources for prediction of the effects of non-synonymous single nucleotide polymorphism on protein function and interactions. Curr Pharm Biotechnol 9:123-133.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 123-133
    • Teng, S.1    Michonova-Alexova, E.2    Alexov, E.3
  • 37
    • 3543004682 scopus 로고    scopus 로고
    • Extensive domain motion and electron transfer in the human electron transferring flavoprotein-medium chain Acyl-CoA dehydrogenase complex
    • Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D. 2004. Extensive domain motion and electron transfer in the human electron transferring flavoprotein-medium chain Acyl-CoA dehydrogenase complex. J Biol Chem 279:32904-32912.
    • (2004) J Biol Chem , vol.279 , pp. 32904-32912
    • Toogood, H.S.1    van Thiel, A.2    Basran, J.3    Sutcliffe, M.J.4    Scrutton, N.S.5    Leys, D.6
  • 38
    • 0035065485 scopus 로고    scopus 로고
    • SNPs, protein structure, and disease
    • Wang Z, Moult J. 2001. SNPs, protein structure, and disease. Hum Mut 17:263-270.
    • Hum Mut , vol.17 , pp. 263-270
    • Wang, Z.1    Moult, J.2
  • 40
    • 76349099822 scopus 로고    scopus 로고
    • Structure of an integrin with an alphaI domain, complement receptor type 4
    • Xie C, Zhu J, Chen X, Mi L, Nishida N, Springer TA. 2010. Structure of an integrin with an alphaI domain, complement receptor type 4. EMBO J 29:666-679.
    • (2010) EMBO J , vol.29 , pp. 666-679
    • Xie, C.1    Zhu, J.2    Chen, X.3    Mi, L.4    Nishida, N.5    Springer, T.A.6
  • 41
    • 33751357065 scopus 로고    scopus 로고
    • ProtBuD: a database of biological unit structures of protein families and superfamilies
    • Xu Q, Canutescu A, Obradovic Z, DunbrackRL. 2006. ProtBuD: a database of biological unit structures of protein families and superfamilies. Bioinformatics 22:2876-2882.
    • (2006) Bioinformatics , vol.22 , pp. 2876-2882
    • Xu, Q.1    Canutescu, A.2    Obradovic, Z.3    Dunbrack, R.L.4
  • 44
    • 33645764714 scopus 로고    scopus 로고
    • SNPs3D: candidate gene and SNP selection for association studies
    • Yue P, Melamud E, Moult J. 2006. SNPs3D: candidate gene and SNP selection for association studies. BMC Bioinformatics 7:166.
    • (2006) BMC Bioinformatics , vol.7 , pp. 166
    • Yue, P.1    Melamud, E.2    Moult, J.3
  • 45
    • 32044453591 scopus 로고    scopus 로고
    • Identification and analysis of deleterious human SNPs
    • Yue P, Moult J. 2006. Identification and analysis of deleterious human SNPs. JMol Biol 356:1263-1274.
    • (2006) JMol Biol , vol.356 , pp. 1263-1274
    • Yue, P.1    Moult, J.2
  • 46
    • 77956276773 scopus 로고    scopus 로고
    • Computational analysis of missense mutations causing Snyder-Robinson syndrome
    • Zhang Z, Teng S, Wang L, Schwartz CE, Alexov E. 2010. Computational analysis of missense mutations causing Snyder-Robinson syndrome. Hum Mutat 31:1043-1049.
    • (2010) Hum Mutat , vol.31 , pp. 1043-1049
    • Zhang, Z.1    Teng, S.2    Wang, L.3    Schwartz, C.E.4    Alexov, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.