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Volumn 144, Issue 1, 2011, Pages 67-78

Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions

Author keywords

CELLBIO; HUMDISEASE

Indexed keywords

AMYLOID; CELL PROTEIN;

EID: 78650963274     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2010.11.050     Document Type: Article
Times cited : (566)

References (49)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • W.E. Balch, R.I. Morimoto, A. Dillin, and J.W. Kelly Adapting proteostasis for disease intervention Science 319 2008 916 919
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 2
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • N.F. Bence, R.M. Sampat, and R.R. Kopito Impairment of the ubiquitin-proteasome system by protein aggregation Science 292 2001 1552 1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 7
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • J. Cox, and M. Mann MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification Nat. Biotechnol. 26 2008 1367 1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 8
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Z. Dosztanyi, V. Csizmok, P. Tompa, and I. Simon IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content Bioinformatics 21 2005 3433 3434
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 10
    • 77950483916 scopus 로고    scopus 로고
    • Functional interplay between chromatin remodeling complexes RSC, SWI/SNF and ISWI in regulation of yeast heat shock genes
    • T.Y. Erkina, Y. Zou, S. Freeling, V.I. Vorobyev, and A.M. Erkine Functional interplay between chromatin remodeling complexes RSC, SWI/SNF and ISWI in regulation of yeast heat shock genes Nucleic Acids Res. 38 2010 1441 1449
    • (2010) Nucleic Acids Res. , vol.38 , pp. 1441-1449
    • Erkina, T.Y.1    Zou, Y.2    Freeling, S.3    Vorobyev, V.I.4    Erkine, A.M.5
  • 11
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • J. Frydman Folding of newly translated proteins in vivo: The role of molecular chaperones Annu. Rev. Biochem. 70 2001 603 647
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 12
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • T. Gidalevitz, A. Ben-Zvi, K.H. Ho, H.R. Brignull, and R.I. Morimoto Progressive disruption of cellular protein folding in models of polyglutamine diseases Science 311 2006 1471 1474
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 13
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • L. Goldschmidt, P.K. Teng, R. Riek, and D. Eisenberg Identifying the amylome, proteins capable of forming amyloid-like fibrils Proc. Natl. Acad. Sci. USA 107 2010 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
  • 14
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • F.U. Hartl, and M. Hayer-Hartl Molecular chaperones in the cytosol: from nascent chain to folded protein Science 295 2002 1852 1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 16
    • 36749078792 scopus 로고    scopus 로고
    • Folding versus aggregation: Polypeptide conformations on competing pathways
    • T.R. Jahn, and S.E. Radford Folding versus aggregation: Polypeptide conformations on competing pathways Arch. Biochem. Biophys. 469 2008 100 117
    • (2008) Arch. Biochem. Biophys. , vol.469 , pp. 100-117
    • Jahn, T.R.1    Radford, S.E.2
  • 17
  • 20
    • 33750449952 scopus 로고    scopus 로고
    • A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide
    • W. Kim, Y. Kim, J. Min, D.J. Kim, Y.T. Chang, and M.H. Hecht A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide ACS Chem. Biol. 1 2006 461 469
    • (2006) ACS Chem. Biol. , vol.1 , pp. 461-469
    • Kim, W.1    Kim, Y.2    Min, J.3    Kim, D.J.4    Chang, Y.T.5    Hecht, M.H.6
  • 21
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • H.A. Lashuel, and P.T. Lansbury Jr. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q. Rev. Biophys. 39 2006 167 201
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury Jr., P.T.2
  • 26
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • R.I. Morimoto Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging Genes Dev. 22 2008 1427 1438
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 30
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • S.E. Ong, and M. Mann A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC) Nat. Protoc. 1 2006 2650 2660
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 31
    • 77949360998 scopus 로고    scopus 로고
    • Modularity of intrinsic disorder in the human proteome
    • M.M. Pentony, and D.T. Jones Modularity of intrinsic disorder in the human proteome Proteins 78 2009 212 221
    • (2009) Proteins , vol.78 , pp. 212-221
    • Pentony, M.M.1    Jones, D.T.2
  • 32
    • 65949097958 scopus 로고    scopus 로고
    • The role of intrinsically unstructured proteins in neurodegenerative diseases
    • S. Raychaudhuri, S. Dey, N.P. Bhattacharyya, and D. Mukhopadhyay The role of intrinsically unstructured proteins in neurodegenerative diseases PLoS ONE 4 2009 e5566
    • (2009) PLoS ONE , vol.4 , pp. 5566
    • Raychaudhuri, S.1    Dey, S.2    Bhattacharyya, N.P.3    Mukhopadhyay, D.4
  • 33
    • 0032831760 scopus 로고    scopus 로고
    • Toxicity of protein aggregates in PC12 cells: 3-(4,5-dimethylthiazol-2- yl)-2,5-diphenyltetrazolium bromide assay
    • M.S. Shearman Toxicity of protein aggregates in PC12 cells: 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay Methods Enzymol. 309 1999 716 723
    • (1999) Methods Enzymol. , vol.309 , pp. 716-723
    • Shearman, M.S.1
  • 34
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • M. Stefani, and C.M. Dobson Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution J. Mol. Med. 81 2003 678 699
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 36
    • 0034897667 scopus 로고    scopus 로고
    • Transcriptional activation domains of human heat shock factor 1 recruit human SWI/SNF
    • E.K. Sullivan, C.S. Weirich, J.R. Guyon, S. Sif, and R.E. Kingston Transcriptional activation domains of human heat shock factor 1 recruit human SWI/SNF Mol. Cell. Biol. 21 2001 5826 5837
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5826-5837
    • Sullivan, E.K.1    Weirich, C.S.2    Guyon, J.R.3    Sif, S.4    Kingston, R.E.5
  • 41
    • 0024411246 scopus 로고
    • E1a transactivation of the human HSP70 promoter is mediated through the basal transcriptional complex
    • G.T. Williams, T.K. McClanahan, and R.I. Morimoto E1a transactivation of the human HSP70 promoter is mediated through the basal transcriptional complex Mol. Cell. Biol. 9 1989 2574 2587
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2574-2587
    • Williams, G.T.1    McClanahan, T.K.2    Morimoto, R.I.3
  • 42
    • 38549169530 scopus 로고    scopus 로고
    • The two faces of protein misfolding: Gain- and loss-of-function in neurodegenerative diseases
    • K.F. Winklhofer, J. Tatzelt, and C. Haass The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases EMBO J. 27 2008 336 349
    • (2008) EMBO J. , vol.27 , pp. 336-349
    • Winklhofer, K.F.1    Tatzelt, J.2    Haass, C.3
  • 43
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • J.C. Young, N.J. Hoogenraad, and F.U. Hartl Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70 Cell 112 2003 41 50
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 46
    • 0037424352 scopus 로고    scopus 로고
    • The core of the tetrameric mycobacterial porin MspA is an extremely stable beta-sheet domain
    • Heinz, C., Engelhardt, H., Niederweis, M., Heinz, C., Engelhardt, H., and Niederweis, M. (2003). The core of the tetrameric mycobacterial porin MspA is an extremely stable beta-sheet domain. J. Biol. Chem. 278, 8678-8685.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8678-8685
    • Heinz, C.1    Engelhardt, H.2    Niederweis, M.3    Heinz, C.4    Engelhardt, H.5    Niederweis, M.6
  • 47
    • 33846805944 scopus 로고    scopus 로고
    • Prediction of local structural stabilities of proteins from their amino acid sequences
    • Tartaglia, G.G., Cavalli, A., and Vendruscolo, M. (2007). Prediction of local structural stabilities of proteins from their amino acid sequences. Structure 15, 139-143.
    • (2007) Structure , vol.15 , pp. 139-143
    • Tartaglia, G.G.1    Cavalli, A.2    Vendruscolo, M.3
  • 48
    • 0036308719 scopus 로고    scopus 로고
    • Mutations that reduce aggregation of the Alzheimer's A beta 42 peptide: An unbiased search for the sequence determinants of A beta amyloidogenesis
    • Wurth, C., Guimard, N.K., and Hecht, M.H. (2002). Mutations that reduce aggregation of the Alzheimer's A beta 42 peptide: an unbiased search for the sequence determinants of A beta amyloidogenesis. J. Mol. Biol. 319, 1279-1290.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1279-1290
    • Wurth, C.1    Guimard, N.K.2    Hecht, M.H.3
  • 49
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils
    • Zandomeneghi, G., Krebs, M.R., McCammon, M.G., Fandrich, M. (2004). FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. Protein Sci. 13, 3314-3321.
    • (2004) Protein Sci. , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.2    McCammon, M.G.3    Fandrich, M.4


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