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Volumn 7, Issue 2, 2012, Pages

Structural stability of human protein tyrosine phosphatase ρ catalytic domain: Effect of point mutations

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE RHO; UNCLASSIFIED DRUG;

EID: 84857517538     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0032555     Document Type: Article
Times cited : (15)

References (34)
  • 1
    • 77249128431 scopus 로고    scopus 로고
    • Identification and functional characterization of paxillin as a target of protein tyrosine phosphatase receptor T
    • Zhao Y, Zhang X, Guda K, Lawrence E, Sun Q, et al. (2010) Identification and functional characterization of paxillin as a target of protein tyrosine phosphatase receptor T. Proc Natl Acad Sci U S A 107: 2592-2597.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 2592-2597
    • Zhao, Y.1    Zhang, X.2    Guda, K.3    Lawrence, E.4    Sun, Q.5
  • 3
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: from genes, to function, to disease
    • Tonks NK, (2006) Protein tyrosine phosphatases: from genes, to function, to disease. Nat Rev Mol Cell Biol 7: 833-846.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 4
    • 0036181649 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development
    • Zhang ZY, (2002) Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development. Annu Rev Pharmacol Toxicol 42: 209-234.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 209-234
    • Zhang, Z.Y.1
  • 5
    • 0034785827 scopus 로고    scopus 로고
    • Structural and evolutionary relationships among protein tyrosine phosphatase domains
    • Andersen JN, Mortensen OH, Peters GH, Drake PG, Iversen LF, et al. (2001) Structural and evolutionary relationships among protein tyrosine phosphatase domains. Mol Cell Biol 21: 7117-7136.
    • (2001) Mol Cell Biol , vol.21 , pp. 7117-7136
    • Andersen, J.N.1    Mortensen, O.H.2    Peters, G.H.3    Drake, P.G.4    Iversen, L.F.5
  • 8
    • 58249138122 scopus 로고    scopus 로고
    • Large-scale structural analysis of the classical human protein tyrosine phosphatome
    • Barr AJ, Ugochukwu E, Lee WH, King ON, Filippakopoulos P, et al. (2009) Large-scale structural analysis of the classical human protein tyrosine phosphatome. Cell 136: 352-363.
    • (2009) Cell , vol.136 , pp. 352-363
    • Barr, A.J.1    Ugochukwu, E.2    Lee, W.H.3    King, O.N.4    Filippakopoulos, P.5
  • 9
    • 0026705734 scopus 로고
    • Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase
    • Zheng XM, Wang Y, Pallen CJ, (1992) Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase. Nature 359: 336-339.
    • (1992) Nature , vol.359 , pp. 336-339
    • Zheng, X.M.1    Wang, Y.2    Pallen, C.J.3
  • 10
    • 2442648882 scopus 로고    scopus 로고
    • Mutational analysis of the tyrosine phosphatome in colorectal cancers
    • Wang Z, Shen D, Parsons DW, Bardelli A, Sager J, et al. (2004) Mutational analysis of the tyrosine phosphatome in colorectal cancers. Science 304: 1164-1166.
    • (2004) Science , vol.304 , pp. 1164-1166
    • Wang, Z.1    Shen, D.2    Parsons, D.W.3    Bardelli, A.4    Sager, J.5
  • 11
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • Barford D, Flint AJ, Tonks NK, (1994) Crystal structure of human protein tyrosine phosphatase 1B. Science 263: 1397-1404.
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 12
    • 39149103362 scopus 로고    scopus 로고
    • Human Gene Mutation Database: towards a comprehensive central mutation database
    • Stenson PD, Ball E, Howells K, Phillips A, Mort M, et al. (2008) Human Gene Mutation Database: towards a comprehensive central mutation database. J Med Genet 45: 124-126.
    • (2008) J Med Genet , vol.45 , pp. 124-126
    • Stenson, P.D.1    Ball, E.2    Howells, K.3    Phillips, A.4    Mort, M.5
  • 13
    • 13444266370 scopus 로고    scopus 로고
    • Online Mendelian Inheritance in Man (OMIM), a knowledgebase of human genes and genetic disorders
    • Hamosh A, Scott AF, Amberger JS, Bocchini CA, McKusick VA, (2005) Online Mendelian Inheritance in Man (OMIM), a knowledgebase of human genes and genetic disorders. Nucleic Acids Res 33: D514-517.
    • (2005) Nucleic Acids Res , vol.33
    • Hamosh, A.1    Scott, A.F.2    Amberger, J.S.3    Bocchini, C.A.4    McKusick, V.A.5
  • 14
    • 69549111112 scopus 로고    scopus 로고
    • Correlating protein function and stability through the analysis of single amino acid substitutions
    • Bromberg Y, Rost B, (2009) Correlating protein function and stability through the analysis of single amino acid substitutions. BMC Bioinformatics 10, (Suppl 8): S8.
    • (2009) BMC Bioinformatics , vol.10 , Issue.SUPPL. 8
    • Bromberg, Y.1    Rost, B.2
  • 15
    • 70350668615 scopus 로고    scopus 로고
    • A survey of proteins encoded by non-synonymous single nucleotide polymorphisms reveals a significant fraction with altered stability and activity
    • Allali-Hassani A, Wasney GA, Chau I, Hong BS, Senisterra G, et al. (2009) A survey of proteins encoded by non-synonymous single nucleotide polymorphisms reveals a significant fraction with altered stability and activity. Biochem J 424: 15-26.
    • (2009) Biochem J , vol.424 , pp. 15-26
    • Allali-Hassani, A.1    Wasney, G.A.2    Chau, I.3    Hong, B.S.4    Senisterra, G.5
  • 16
    • 0035065485 scopus 로고    scopus 로고
    • SNPs, protein structure, and disease
    • Wang Z, Moult J, (2001) SNPs, protein structure, and disease. Hum Mutat 17: 263-270.
    • (2001) Hum Mutat , vol.17 , pp. 263-270
    • Wang, Z.1    Moult, J.2
  • 17
    • 25144523127 scopus 로고    scopus 로고
    • Loss of protein structure stability as a major causative factor in monogenic disease
    • Yue P, Li Z, Moult J, (2005) Loss of protein structure stability as a major causative factor in monogenic disease. J Mol Biol 353: 459-473.
    • (2005) J Mol Biol , vol.353 , pp. 459-473
    • Yue, P.1    Li, Z.2    Moult, J.3
  • 18
    • 32044453591 scopus 로고    scopus 로고
    • Identification and analysis of deleterious human SNPs
    • Yue P, Moult J, (2006) Identification and analysis of deleterious human SNPs. J Mol Biol 356: 1263-1274.
    • (2006) J Mol Biol , vol.356 , pp. 1263-1274
    • Yue, P.1    Moult, J.2
  • 19
    • 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
  • 21
    • 48249136625 scopus 로고    scopus 로고
    • Prediction by graph theoretic measures of structural effects in proteins arising from non-synonymous single nucleotide polymorphisms
    • Cheng TM, Lu YE, Vendruscolo M, Lio' P, Blundell TL, (2008) Prediction by graph theoretic measures of structural effects in proteins arising from non-synonymous single nucleotide polymorphisms. PLoS Comput Biol 4: e1000135.
    • (2008) PLoS Comput Biol , vol.4
    • Cheng, T.M.1    Lu, Y.E.2    Vendruscolo, M.3    Lio', P.4    Blundell, T.L.5
  • 22
    • 33747832183 scopus 로고    scopus 로고
    • FASTSNP: an always up-to-date and extendable service for SNP function analysis and prioritization
    • Yuan HY, Chiou JJ, Tseng WH, Liu CH, Liu CK, et al. (2006) FASTSNP: an always up-to-date and extendable service for SNP function analysis and prioritization. Nucleic Acids Res 34: W635-41.
    • (2006) Nucleic Acids Res , vol.34
    • Yuan, H.Y.1    Chiou, J.J.2    Tseng, W.H.3    Liu, C.H.4    Liu, C.K.5
  • 23
    • 78651330430 scopus 로고    scopus 로고
    • COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer
    • Forbes SA, Bindal N, Bamford S, Cole C, Kok CY, et al. (2011) COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer. Nucleic Acids Res 39: D945-50.
    • (2011) Nucleic Acids Res , vol.39
    • Forbes, S.A.1    Bindal, N.2    Bamford, S.3    Cole, C.4    Kok, C.Y.5
  • 24
    • 34247189533 scopus 로고    scopus 로고
    • Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T
    • Zhang X, Guo A, Yu J, Possemato A, Chen Y, et al. (2007) Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T. Proc Natl Acad Sci U S A 104: 4060-4064.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 4060-4064
    • Zhang, X.1    Guo, A.2    Yu, J.3    Possemato, A.4    Chen, Y.5
  • 25
    • 33644499478 scopus 로고    scopus 로고
    • Monitoring protein aggregation during thermal unfolding in circular dichroism experiments
    • Benjwal S, Verma S, Röhm KH, Gursky O, (2006) Monitoring protein aggregation during thermal unfolding in circular dichroism experiments. Protein Sci 15: 635-639.
    • (2006) Protein Sci , vol.15 , pp. 635-639
    • Benjwal, S.1    Verma, S.2    Röhm, K.H.3    Gursky, O.4
  • 26
    • 0036286323 scopus 로고    scopus 로고
    • What causes hyperfluorescence: folding intermediates or conformationally flexible native states?
    • Ervin J, Larios E, Osváth S, Schulten K, Gruebele M, (2002) What causes hyperfluorescence: folding intermediates or conformationally flexible native states? Biophys J 83: 473-483.
    • (2002) Biophys J , vol.83 , pp. 473-483
    • Ervin, J.1    Larios, E.2    Osváth, S.3    Schulten, K.4    Gruebele, M.5
  • 27
    • 80155133113 scopus 로고    scopus 로고
    • Tumour suppressor function of protein tyrosine phosphatase receptor-T
    • Scott A, Wang Z, (2011) Tumour suppressor function of protein tyrosine phosphatase receptor-T. Biosci Rep 31: 303-307.
    • (2011) Biosci Rep , vol.31 , pp. 303-307
    • Scott, A.1    Wang, Z.2
  • 28
    • 78751490759 scopus 로고    scopus 로고
    • Cancer cells cut homophilic cell adhesion molecules and run
    • Craig SE, Brady-Kalnay SM, (2011) Cancer cells cut homophilic cell adhesion molecules and run. Cancer Res 71: 303-309.
    • (2011) Cancer Res , vol.71 , pp. 303-309
    • Craig, S.E.1    Brady-Kalnay, S.M.2
  • 29
    • 70149096641 scopus 로고    scopus 로고
    • Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration
    • Burgoyne AM, Phillips-Mason PJ, Burden-Gulley SM, Robinson S, Sloan AE, et al. (2009) Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration. Cancer Res 69: 6960-6968.
    • (2009) Cancer Res , vol.69 , pp. 6960-6968
    • Burgoyne, A.M.1    Phillips-Mason, P.J.2    Burden-Gulley, S.M.3    Robinson, S.4    Sloan, A.E.5
  • 31
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink MR, (1994) The use of fluorescence methods to monitor unfolding transitions in proteins Biophys J 66: 482-501.
    • (1994) Biophys J , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 32
    • 0027378450 scopus 로고
    • Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants
    • Royer CA, Mann CJ, Matthews CR, (1993) Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants. Protein Sci 2: 1844-1852.
    • (1993) Protein Sci , vol.2 , pp. 1844-1852
    • Royer, C.A.1    Mann, C.J.2    Matthews, C.R.3
  • 33
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW, (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27: 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 34
    • 77953756428 scopus 로고    scopus 로고
    • Toward classification of BRCA1 missense variants using a biophysical approach
    • Rowling PJ, Cook R, Itzhaki LS, (2010) Toward classification of BRCA1 missense variants using a biophysical approach. J Biol Chem 285: 20080-20087.
    • (2010) J Biol Chem , vol.285 , pp. 20080-20087
    • Rowling, P.J.1    Cook, R.2    Itzhaki, L.S.3


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