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Volumn 3, Issue 10, 2014, Pages 913-923

Global analysis of protein aggregation in yeast during physiological conditions and arsenite stress

Author keywords

Arsenite; Chaperone; Protein aggregation; Protein folding; Translation

Indexed keywords


EID: 84979217605     PISSN: None     EISSN: 20466390     Source Type: Journal    
DOI: 10.1242/bio.20148938     Document Type: Article
Times cited : (34)

References (63)
  • 1
    • 77950573146 scopus 로고    scopus 로고
    • A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis
    • Albanèse, V., Reissmann, S. and Frydman, J. (2010). A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis. J. Cell Biol. 189, 69-81.
    • (2010) J. Cell Biol. , vol.189 , pp. 69-81
    • Albanèse, V.1    Reissmann, S.2    Frydman, J.3
  • 2
    • 84874407643 scopus 로고    scopus 로고
    • The role of metal ions in amyloid formation: General principles from model peptides
    • Alies, B., Hureau, C. and Faller, P. (2013). The role of metal ions in amyloid formation: general principles from model peptides. Metallomics 5, 183-192.
    • (2013) Metallomics , vol.5 , pp. 183-192
    • Alies, B.1    Hureau, C.2    Faller, P.3
  • 4
    • 77949505299 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble proteins in ALS indicates a causal link between nitrative stress and aggregation in pathogenesis
    • Basso, M., Samengo, G., Nardo, G., Massignan, T., D'Alessandro, G., Tartari, S., Cantoni, L., Marino, M., Cheroni, C., De Biasi, S. et al. (2009). Characterization of detergent-insoluble proteins in ALS indicates a causal link between nitrative stress and aggregation in pathogenesis. PLoS ONE 4, e8130.
    • (2009) PLoS ONE , vol.4 , pp. 8130
    • Basso, M.1    Samengo, G.2    Nardo, G.3    Massignan, T.4    D'Alessandro, G.5    Tartari, S.6    Cantoni, L.7    Marino, M.8    Cheroni, C.9    De Biasi, S.10
  • 6
    • 84864760160 scopus 로고    scopus 로고
    • Metal imaging in neurodegenerative diseases
    • Bourassa, M. W. and Miller, L. M. (2012). Metal imaging in neurodegenerative diseases. Metallomics 4, 721-738.
    • (2012) Metallomics , vol.4 , pp. 721-738
    • Bourassa, M.W.1    Miller, L.M.2
  • 7
    • 80455137197 scopus 로고    scopus 로고
    • Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases
    • Breydo, L. and Uversky, V. N. (2011). Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases. Metallomics 3, 1163-1180.
    • (2011) Metallomics , vol.3 , pp. 1163-1180
    • Breydo, L.1    Uversky, V.N.2
  • 8
    • 0031961688 scopus 로고    scopus 로고
    • Regulation of translational initiation during cellular responses to stress
    • Brostrom, C. O. and Brostrom, M. A. (1997). Regulation of translational initiation during cellular responses to stress. Prog. Nucleic Acid Res. Mol. Biol. 58, 79-125.
    • (1997) Prog. Nucleic Acid Res. Mol. Biol , vol.58 , pp. 79-125
    • Brostrom, C.O.1    Brostrom, M.A.2
  • 12
    • 84887606872 scopus 로고    scopus 로고
    • Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins
    • Ciryam, P., Tartaglia, G. G., Morimoto, R. I., Dobson, C. M. and Vendruscolo, M. (2013). Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins. Cell Reports 5, 781-790.
    • (2013) Cell Reports , vol.5 , pp. 781-790
    • Ciryam, P.1    Tartaglia, G.G.2    Morimoto, R.I.3    Dobson, C.M.4    Vendruscolo, M.5
  • 15
    • 0027445111 scopus 로고
    • Transfer of arsenite from glutathione to dithiols: A model of interaction
    • Delnomdedieu, M., Basti, M. M., Otvos, J. D. and Thomas, D. J. (1993). Transfer of arsenite from glutathione to dithiols: a model of interaction. Chem. Res. Toxicol. 6, 598-602.
    • (1993) Chem. Res. Toxicol , vol.6 , pp. 598-602
    • Delnomdedieu, M.1    Basti, M.M.2    Otvos, J.D.3    Thomas, D.J.4
  • 16
    • 70349333227 scopus 로고    scopus 로고
    • The evolutionary consequences of erroneous protein synthesis
    • Drummond, D. A. and Wilke, C. O. (2009). The evolutionary consequences of erroneous protein synthesis. Nat. Rev. Genet. 10, 715-724.
    • (2009) Nat. Rev. Genet , vol.10 , pp. 715-724
    • Drummond, D.A.1    Wilke, C.O.2
  • 17
    • 0042848693 scopus 로고    scopus 로고
    • A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein
    • Du, H. N., Tang, L., Luo, X. Y., Li, H. T., Hu, J., Zhou, J. W. and Hu, H. Y. (2003). A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein. Biochemistry 42, 8870-8878.
    • (2003) Biochemistry , vol.42 , pp. 8870-8878
    • Du, H.N.1    Tang, L.2    Luo, X.Y.3    Li, H.T.4    Hu, J.5    Zhou, J.W.6    Hu, H.Y.7
  • 18
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla, A. M., Rousseau, F., Schymkowitz, J. and Serrano, L. (2004). Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 22, 1302-1306.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 19
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman, D. and Argos, P. (1995). Knowledge-based protein secondary structure assignment. Proteins 23, 566-579.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 20
    • 0030931336 scopus 로고    scopus 로고
    • Seventy-five percent accuracy in protein secondary structure prediction
    • Frishman, D. and Argos, P. (1997). Seventy-five percent accuracy in protein secondary structure prediction. Proteins 27, 329-335.
    • (1997) Proteins , vol.27 , pp. 329-335
    • Frishman, D.1    Argos, P.2
  • 21
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D. J. and Robson, B. (1978). Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 24
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt, L., Teng, P. K., Riek, R. and Eisenberg, D. (2010). Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc. Natl. Acad. Sci. USA 107, 3487-3492.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 25
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: Implications to protein folding pathways in the cell
    • Gong, Y., Kakihara, Y., Krogan, N., Greenblatt, J., Emili, A., Zhang, Z. and Houry, W. A. (2009). An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol. Syst. Biol. 5, 275.
    • (2009) Mol. Syst. Biol , vol.5 , pp. 275
    • Gong, Y.1    Kakihara, Y.2    Krogan, N.3    Greenblatt, J.4    Emili, A.5    Zhang, Z.6    Houry, W.A.7
  • 26
    • 84870427355 scopus 로고    scopus 로고
    • Cellular strategies for regulating functional and nonfunctional protein aggregation
    • Gsponer, J. and Babu, M. M. (2012). Cellular strategies for regulating functional and nonfunctional protein aggregation. Cell Reports 2, 1425-1437.
    • (2012) Cell Reports , vol.2 , pp. 1425-1437
    • Gsponer, J.1    Babu, M.M.2
  • 27
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A. and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 29
    • 0036469888 scopus 로고    scopus 로고
    • Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains
    • Jäkel, S., Mingot, J. M., Schwarzmaier, P., Hartmann, E. and Görlich, D. (2002). Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains. EMBO J. 21, 377-386.
    • (2002) EMBO J , vol.21 , pp. 377-386
    • Jäkel, S.1    Mingot, J.M.2    Schwarzmaier, P.3    Hartmann, E.4    Görlich, D.5
  • 32
    • 77950562866 scopus 로고    scopus 로고
    • A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes
    • Koplin, A., Preissler, S., Ilina, Y., Koch, M., Scior, A., Erhardt, M. and Deuerling, E. (2010). A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes. J. Cell Biol. 189, 57-68.
    • (2010) J. Cell Biol. , vol.189 , pp. 57-68
    • Koplin, A.1    Preissler, S.2    Ilina, Y.3    Koch, M.4    Scior, A.5    Erhardt, M.6    Deuerling, E.7
  • 35
    • 84873467908 scopus 로고    scopus 로고
    • Cotranslational response to proteotoxic stress by elongation pausing of ribosomes
    • Liu, B., Han, Y. and Qian, S. B. (2013). Cotranslational response to proteotoxic stress by elongation pausing of ribosomes. Mol. Cell 49, 453-463.
    • (2013) Mol. Cell , vol.49 , pp. 453-463
    • Liu, B.1    Han, Y.2    Qian, S.B.3
  • 36
    • 77956146939 scopus 로고    scopus 로고
    • Characterization of surface-exposed reactive cysteine residues in Saccharomyces cerevisiae
    • Marino, S. M., Li, Y., Fomenko, D. E., Agisheva, N., Cerny, R. L. and Gladyshev, V. N. (2010). Characterization of surface-exposed reactive cysteine residues in Saccharomyces cerevisiae. Biochemistry 49, 7709-7721.
    • (2010) Biochemistry , vol.49 , pp. 7709-7721
    • Marino, S.M.1    Li, Y.2    Fomenko, D.E.3    Agisheva, N.4    Cerny, R.L.5    Gladyshev, V.N.6
  • 42
    • 30044436319 scopus 로고    scopus 로고
    • The thioredoxin system protects ribosomes against stress-induced aggregation
    • Rand, J. D. and Grant, C. M. (2006). The thioredoxin system protects ribosomes against stress-induced aggregation. Mol. Biol. Cell 17, 387-401.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 387-401
    • Rand, J.D.1    Grant, C.M.2
  • 43
    • 84878034899 scopus 로고    scopus 로고
    • Untangling amyloid-b, tau, and metals in Alzheimer's disease
    • Savelieff, M. G., Lee, S., Liu, Y. and Lim, M. H. (2013). Untangling amyloid-b, tau, and metals in Alzheimer's disease. ACS Chem. Biol. 8, 856-865.
    • (2013) ACS Chem. Biol , vol.8 , pp. 856-865
    • Savelieff, M.G.1    Lee, S.2    Liu, Y.3    Lim, M.H.4
  • 44
    • 34548555911 scopus 로고    scopus 로고
    • OMA Browser -exploring orthologous relations across 352 complete genomes
    • Schneider, A., Dessimoz, C. and Gonnet, G. H. (2007). OMA Browser -exploring orthologous relations across 352 complete genomes. Bioinformatics 23, 2180-2182.
    • (2007) Bioinformatics , vol.23 , pp. 2180-2182
    • Schneider, A.1    Dessimoz, C.2    Gonnet, G.H.3
  • 46
    • 0023650543 scopus 로고
    • The codon Adaptation Index - A measure of directional synonymous codon usage bias, and its potential applications
    • Sharp, P. M. and Li, W. H. (1987). The codon Adaptation Index - a measure of directional synonymous codon usage bias, and its potential applications. Nucleic Acids Res. 15, 1281-1295.
    • (1987) Nucleic Acids Res , vol.15 , pp. 1281-1295
    • Sharp, P.M.1    Li, W.H.2
  • 47
    • 84864393542 scopus 로고    scopus 로고
    • Adaptation to stress in yeast: To translate or not? Biochem
    • Simpson, C. E. and Ashe, M. P. (2012). Adaptation to stress in yeast: to translate or not? Biochem. Soc. Trans. 40, 794-799.
    • (2012) Soc. Trans , vol.40 , pp. 794-799
    • Simpson, C.E.1    Ashe, M.P.2
  • 49
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M. and Dobson, C. M. (2003). Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. (Berl) 81, 678-699.
    • (2003) J. Mol. Med.Berl , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 50
    • 84929151464 scopus 로고    scopus 로고
    • Heavy metals and metalloids as a cause for protein misfolding and aggregation
    • Tamás, M. J., Sharma, S. K., Ibstedt, S., Jacobson, T. and Christen, P. (2014). Heavy metals and metalloids as a cause for protein misfolding and aggregation. Biomolecules 4, 252-267.
    • (2014) Biomolecules , vol.4 , pp. 252-267
    • Tamás, M.J.1    Sharma, S.K.2    Ibstedt, S.3    Jacobson, T.4    Christen, P.5
  • 51
    • 45749102914 scopus 로고    scopus 로고
    • The Zyggregator method for predicting protein aggregation propensities
    • Tartaglia, G. G. and Vendruscolo, M. (2008). The Zyggregator method for predicting protein aggregation propensities. Chem. Soc. Rev. 37, 1395-1401.
    • (2008) Chem. Soc. Rev , vol.37 , pp. 1395-1401
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 52
    • 34247882072 scopus 로고    scopus 로고
    • Life on the edge: A link between gene expression levels and aggregation rates of human proteins
    • Tartaglia, G. G., Pechmann, S., Dobson, C. M. and Vendruscolo, M. (2007). Life on the edge: a link between gene expression levels and aggregation rates of human proteins. Trends Biochem. Sci. 32, 204-206.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 204-206
    • Tartaglia, G.G.1    Pechmann, S.2    Dobson, C.M.3    Vendruscolo, M.4
  • 53
    • 70349218068 scopus 로고    scopus 로고
    • Short protein segments can drive a non-fibrillizing protein into the amyloid state
    • Teng, P. K. and Eisenberg, D. (2009). Short protein segments can drive a non-fibrillizing protein into the amyloid state. Protein Eng. Des. Sel. 22, 531-536.
    • (2009) Protein Eng. Des. Sel , vol.22 , pp. 531-536
    • Teng, P.K.1    Eisenberg, D.2
  • 54
    • 34447279050 scopus 로고    scopus 로고
    • Quantitative transcriptome, proteome, and sulfur metabolite profiling of the Saccharomyces cerevisiae response to arsenite
    • Thorsen, M., Lagniel, G., Kristiansson, E., Junot, C., Nerman, O., Labarre, J. and Tamás, M. J. (2007). Quantitative transcriptome, proteome, and sulfur metabolite profiling of the Saccharomyces cerevisiae response to arsenite. Physiol. Genomics 30, 35-43.
    • (2007) Physiol. Genomics , vol.30 , pp. 35-43
    • Thorsen, M.1    Lagniel, G.2    Kristiansson, E.3    Junot, C.4    Nerman, O.5    Labarre, J.6    Tamás, M.J.7
  • 56
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers, J., Mogk, A. and Bukau, B. (2010). Cellular strategies for controlling protein aggregation. Nat. Rev. Mol. Cell Biol. 11, 777-788.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 57
    • 84861763129 scopus 로고    scopus 로고
    • Proteome folding and aggregation
    • Vendruscolo, M. (2012). Proteome folding and aggregation. Curr. Opin. Struct. Biol. 22, 138-143.
    • (2012) Curr. Opin. Struct. Biol , vol.22 , pp. 138-143
    • Vendruscolo, M.1
  • 58
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • Wang, Q., Woltjer, R. L., Cimino, P. J., Pan, C., Montine, K. S., Zhang, J. and Montine, T. J. (2005). Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J. 19, 869-871.
    • (2005) FASEB J , vol.19 , pp. 869-871
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3    Pan, C.4    Montine, K.S.5    Zhang, J.6    Montine, T.J.7
  • 59
    • 0033229970 scopus 로고    scopus 로고
    • The economics of ribosome biosynthesis in yeast
    • Warner, J. R. (1999). The economics of ribosome biosynthesis in yeast. Trends Biochem. Sci. 24, 437-440.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 437-440
    • Warner, J.R.1
  • 60
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D. and Yates, J. R., III. (2001). Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 61
    • 84872577837 scopus 로고    scopus 로고
    • The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis
    • Willmund, F., del Alamo, M., Pechmann, S., Chen, T., Albanèse, V., Dammer, E. B., Peng, J. and Frydman, J. (2013). The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis. Cell 152, 196-209.
    • (2013) Cell , vol.152 , pp. 196-209
    • Willmund, F.1    Del Alamo, M.2    Pechmann, S.3    Chen, T.4    Albanèse, V.5    Dammer, E.B.6    Peng, J.7    Frydman, J.8
  • 62
    • 77649293067 scopus 로고    scopus 로고
    • Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing
    • Winkler, J., Seybert, A., König, L., Pruggnaller, S., Haselmann, U., Sourjik, V., Weiss, M., Frangakis, A. S., Mogk, A. and Bukau, B. (2010). Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing. EMBO J. 29, 910-923.
    • (2010) EMBO J , vol.29 , pp. 910-923
    • Winkler, J.1    Seybert, A.2    König, L.3    Pruggnaller, S.4    Haselmann, U.5    Sourjik, V.6    Weiss, M.7    Frangakis, A.S.8    Mogk, A.9    Bukau, B.10


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