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Volumn 1834, Issue 5, 2013, Pages 918-931

Protein disorder, prion propensities, and self-organizing macromolecular collectives

Author keywords

Amyloid; Phase transition; Prion; Protein disorder; Self organization

Indexed keywords

AMYLOID;

EID: 84876288161     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.01.003     Document Type: Review
Times cited : (149)

References (187)
  • 1
    • 39749192575 scopus 로고    scopus 로고
    • Self-organization in cell biology: A brief history, Nature reviews
    • E. Karsenti Self-organization in cell biology: a brief history, Nature reviews Mol. Cell. Biol. 9 2008 255 262
    • (2008) Mol. Cell. Biol. , vol.9 , pp. 255-262
    • Karsenti, E.1
  • 3
    • 47749146582 scopus 로고    scopus 로고
    • Building the cell: Design principles of cellular architecture, Nature reviews
    • S.M. Rafelski, and W.F. Marshall Building the cell: design principles of cellular architecture, Nature reviews Mol. Cell. Biol. 9 2008 593 602
    • (2008) Mol. Cell. Biol. , vol.9 , pp. 593-602
    • Rafelski, S.M.1    Marshall, W.F.2
  • 4
    • 0035889085 scopus 로고    scopus 로고
    • The concept of self-organization in cellular architecture
    • T. Misteli The concept of self-organization in cellular architecture J. Cell Biol. 155 2001 181 185
    • (2001) J. Cell Biol. , vol.155 , pp. 181-185
    • Misteli, T.1
  • 5
    • 41749092312 scopus 로고    scopus 로고
    • Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
    • S. An, R. Kumar, E.D. Sheets, and S.J. Benkovic Reversible compartmentalization of de novo purine biosynthetic complexes in living cells Science 320 2008
    • (2008) Science , vol.320
    • An, S.1    Kumar, R.2    Sheets, E.D.3    Benkovic, S.J.4
  • 8
    • 0031030491 scopus 로고    scopus 로고
    • A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates
    • V.I. Bashkirov, H. Scherthan, J.A. Solinger, J.M. Buerstedde, and W.D. Heyer A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates J. Cell Biol. 136 1997 761 773
    • (1997) J. Cell Biol. , vol.136 , pp. 761-773
    • Bashkirov, V.I.1    Scherthan, H.2    Solinger, J.A.3    Buerstedde, J.M.4    Heyer, W.D.5
  • 10
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • J.R. Buchan, and R. Parker Eukaryotic stress granules: the ins and outs of translation Mol. Cell 36 2009 932 941
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 11
    • 2442566370 scopus 로고    scopus 로고
    • Cytoplasmic foci are sites of mRNA decay in human cells
    • N. Cougot, S. Babajko, and B. Seraphin Cytoplasmic foci are sites of mRNA decay in human cells J. Cell Biol. 165 2004 31 40
    • (2004) J. Cell Biol. , vol.165 , pp. 31-40
    • Cougot, N.1    Babajko, S.2    Seraphin, B.3
  • 13
    • 0029064131 scopus 로고
    • Coiled bodies contain U7 small nuclear RNA and associate with specific DNA sequences in interphase human cells
    • M.R. Frey, and A.G. Matera Coiled bodies contain U7 small nuclear RNA and associate with specific DNA sequences in interphase human cells Proc. Natl. Acad. Sci. U. S. A. 92 1995 5915 5919
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 5915-5919
    • Frey, M.R.1    Matera, A.G.2
  • 14
    • 35348989809 scopus 로고    scopus 로고
    • Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies
    • N.P. Hoyle, L.M. Castelli, S.G. Campbell, L.E. Holmes, and M.P. Ashe Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies J. Cell Biol. 179 2007 65 74
    • (2007) J. Cell Biol. , vol.179 , pp. 65-74
    • Hoyle, N.P.1    Castelli, L.M.2    Campbell, S.G.3    Holmes, L.E.4    Ashe, M.P.5
  • 15
    • 0036909093 scopus 로고    scopus 로고
    • The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
    • D. Ingelfinger, D.J. Arndt-Jovin, R. Luhrmann, and T. Achsel The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci RNA 8 2002 1489 1501
    • (2002) RNA , vol.8 , pp. 1489-1501
    • Ingelfinger, D.1    Arndt-Jovin, D.J.2    Luhrmann, R.3    Achsel, T.4
  • 16
    • 4344705968 scopus 로고    scopus 로고
    • The budding yeast spindle pole body: Structure, duplication, and function
    • S.L. Jaspersen, and M. Winey The budding yeast spindle pole body: structure, duplication, and function Annu. Rev. Cell Dev. Biol. 20 2004 1 28
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 1-28
    • Jaspersen, S.L.1    Winey, M.2
  • 17
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • J.A. Johnston, C.L. Ward, and R.R. Kopito Aggresomes: a cellular response to misfolded proteins J. Cell Biol. 143 1998 1883 1898
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 18
    • 0035674402 scopus 로고    scopus 로고
    • Translational regulation and RNA localization in Drosophila oocytes and embryos
    • O. Johnstone, and P. Lasko Translational regulation and RNA localization in Drosophila oocytes and embryos Annu. Rev. Genet. 35 2001 365 406
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 365-406
    • Johnstone, O.1    Lasko, P.2
  • 19
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • N.L. Kedersha, M. Gupta, W. Li, I. Miller, and P. Anderson RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules J. Cell Biol. 147 1999 1431 1442
    • (1999) J. Cell Biol. , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 21
    • 44649161981 scopus 로고    scopus 로고
    • Reversible cytoplasmic localization of the proteasome in quiescent yeast cells
    • D. Laporte, B. Salin, B. Daignan-Fornier, and I. Sagot Reversible cytoplasmic localization of the proteasome in quiescent yeast cells J. Cell Biol. 181 2008 737 745
    • (2008) J. Cell Biol. , vol.181 , pp. 737-745
    • Laporte, D.1    Salin, B.2    Daignan-Fornier, B.3    Sagot, I.4
  • 22
    • 33644871486 scopus 로고    scopus 로고
    • Dynamic nature of cleavage bodies and their spatial relationship to DDX1 bodies, Cajal bodies, and gems
    • L. Li, K. Roy, S. Katyal, X. Sun, S. Bleoo, and R. Godbout Dynamic nature of cleavage bodies and their spatial relationship to DDX1 bodies, Cajal bodies, and gems Mol. Biol. Cell 17 2006 1126 1140
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1126-1140
    • Li, L.1    Roy, K.2    Katyal, S.3    Sun, X.4    Bleoo, S.5    Godbout, R.6
  • 23
    • 34547461601 scopus 로고    scopus 로고
    • U bodies are cytoplasmic structures that contain uridine-rich small nuclear ribonucleoproteins and associate with P bodies
    • J.L. Liu, and J.G. Gall U bodies are cytoplasmic structures that contain uridine-rich small nuclear ribonucleoproteins and associate with P bodies Proc. Natl. Acad. Sci. U. S. A. 104 2007 11655 11659
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 11655-11659
    • Liu, J.L.1    Gall, J.G.2
  • 25
    • 71849090342 scopus 로고    scopus 로고
    • Nuclear bodies: Random aggregates of sticky proteins or crucibles of macromolecular assembly?
    • A.G. Matera, M. Izaguire-Sierra, K. Praveen, and T.K. Rajendra Nuclear bodies: random aggregates of sticky proteins or crucibles of macromolecular assembly? Dev. Cell 17 2009 639 647
    • (2009) Dev. Cell , vol.17 , pp. 639-647
    • Matera, A.G.1    Izaguire-Sierra, M.2    Praveen, K.3    Rajendra, T.K.4
  • 26
    • 0037112805 scopus 로고    scopus 로고
    • Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression
    • R. Mazroui, M.E. Huot, S. Tremblay, C. Filion, Y. Labelle, and E.W. Khandjian Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression Hum. Mol. Genet. 11 2002 3007 3017
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 3007-3017
    • Mazroui, R.1    Huot, M.E.2    Tremblay, S.3    Filion, C.4    Labelle, Y.5    Khandjian, E.W.6
  • 27
    • 49749135529 scopus 로고    scopus 로고
    • Maternal mRNAs are regulated by diverse P body-related mRNP granules during early Caenorhabditis elegans development
    • S.L. Noble, B.L. Allen, L.K. Goh, K. Nordick, and T.C. Evans Maternal mRNAs are regulated by diverse P body-related mRNP granules during early Caenorhabditis elegans development J. Cell Biol. 182 2008 559 572
    • (2008) J. Cell Biol. , vol.182 , pp. 559-572
    • Noble, S.L.1    Allen, B.L.2    Goh, L.K.3    Nordick, K.4    Evans, T.C.5
  • 28
    • 77955906574 scopus 로고    scopus 로고
    • Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster
    • C. Noree, B.K. Sato, R.M. Broyer, and J.E. Wilhelm Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster J. Cell Biol. 190 2010 541 551
    • (2010) J. Cell Biol. , vol.190 , pp. 541-551
    • Noree, C.1    Sato, B.K.2    Broyer, R.M.3    Wilhelm, J.E.4
  • 29
    • 0032536858 scopus 로고    scopus 로고
    • Regional and temporal specialization in the nucleus: A transcriptionally-active nuclear domain rich in PTF, Oct1 and PIKA antigens associates with specific chromosomes early in the cell cycle
    • A. Pombo, P. Cuello, W. Schul, J.B. Yoon, R.G. Roeder, P.R. Cook, and S. Murphy Regional and temporal specialization in the nucleus: a transcriptionally-active nuclear domain rich in PTF, Oct1 and PIKA antigens associates with specific chromosomes early in the cell cycle EMBO J. 17 1998 1768 1778
    • (1998) EMBO J. , vol.17 , pp. 1768-1778
    • Pombo, A.1    Cuello, P.2    Schul, W.3    Yoon, J.B.4    Roeder, R.G.5    Cook, P.R.6    Murphy, S.7
  • 30
    • 33750522651 scopus 로고    scopus 로고
    • Actin bodies in yeast quiescent cells: An immediately available actin reserve?
    • I. Sagot, B. Pinson, B. Salin, and B. Daignan-Fornier Actin bodies in yeast quiescent cells: an immediately available actin reserve? Mol. Biol. Cell 17 2006 4645 4655
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4645-4655
    • Sagot, I.1    Pinson, B.2    Salin, B.3    Daignan-Fornier, B.4
  • 31
    • 0032563598 scopus 로고    scopus 로고
    • The human polycomb group complex associates with pericentromeric heterochromatin to form a novel nuclear domain
    • A.J. Saurin, C. Shiels, J. Williamson, D.P. Satijn, A.P. Otte, D. Sheer, and P.S. Freemont The human polycomb group complex associates with pericentromeric heterochromatin to form a novel nuclear domain J. Cell Biol. 142 1998 887 898
    • (1998) J. Cell Biol. , vol.142 , pp. 887-898
    • Saurin, A.J.1    Shiels, C.2    Williamson, J.3    Satijn, D.P.4    Otte, A.P.5    Sheer, D.6    Freemont, P.S.7
  • 32
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • U. Sheth, and R. Parker Decapping and decay of messenger RNA occur in cytoplasmic processing bodies Science 300 2003 805 808
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 34
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • E. van Dijk, N. Cougot, S. Meyer, S. Babajko, E. Wahle, and B. Seraphin Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures EMBO J. 21 2002 6915 6924
    • (2002) EMBO J. , vol.21 , pp. 6915-6924
    • Van Dijk, E.1    Cougot, N.2    Meyer, S.3    Babajko, S.4    Wahle, E.5    Seraphin, B.6
  • 35
    • 0033199695 scopus 로고    scopus 로고
    • Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body
    • T.R. Yeager, A.A. Neumann, A. Englezou, L.I. Huschtscha, J.R. Noble, and R.R. Reddel Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body Cancer Res. 59 1999 4175 4179
    • (1999) Cancer Res. , vol.59 , pp. 4175-4179
    • Yeager, T.R.1    Neumann, A.A.2    Englezou, A.3    Huschtscha, L.I.4    Noble, J.R.5    Reddel, R.R.6
  • 36
    • 84856290771 scopus 로고    scopus 로고
    • The centrosome in cells and organisms
    • M. Bornens The centrosome in cells and organisms Science 335 2012 422 426
    • (2012) Science , vol.335 , pp. 422-426
    • Bornens, M.1
  • 37
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • D. Kaganovich, R. Kopito, and J. Frydman Misfolded proteins partition between two distinct quality control compartments Nature 454 2008 1088 1095
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 38
    • 79960622503 scopus 로고    scopus 로고
    • Biogenesis and function of nuclear bodies
    • Y.S. Mao, B. Zhang, and D.L. Spector Biogenesis and function of nuclear bodies Trends Genet. 27 2011 295 306
    • (2011) Trends Genet. , vol.27 , pp. 295-306
    • Mao, Y.S.1    Zhang, B.2    Spector, D.L.3
  • 40
    • 58149259990 scopus 로고    scopus 로고
    • De novo formation of a subnuclear body
    • T.E. Kaiser, R.V. Intine, and M. Dundr De novo formation of a subnuclear body Science 322 2008 1713 1717
    • (2008) Science , vol.322 , pp. 1713-1717
    • Kaiser, T.E.1    Intine, R.V.2    Dundr, M.3
  • 46
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • R.D. Phair, and T. Misteli High mobility of proteins in the mammalian cell nucleus Nature 404 2000 604 609
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 47
    • 17844371700 scopus 로고    scopus 로고
    • A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
    • M.A. Andrei, D. Ingelfinger, R. Heintzmann, T. Achsel, R. Rivera-Pomar, and R. Luhrmann A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies RNA 11 2005 717 727
    • (2005) RNA , vol.11 , pp. 717-727
    • Andrei, M.A.1    Ingelfinger, D.2    Heintzmann, R.3    Achsel, T.4    Rivera-Pomar, R.5    Luhrmann, R.6
  • 48
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • S.B. Zimmerman, and A.P. Minton Macromolecular crowding: biochemical, biophysical, and physiological consequences Annu. Rev. Biophys. Biomol. Struct. 22 1993 27 65
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 51
    • 0033991735 scopus 로고    scopus 로고
    • Partitioning and concentrating biomaterials in aqueous phase systems
    • G. Johansson, and H. Walter Partitioning and concentrating biomaterials in aqueous phase systems Int. Rev. Cytol. 192 2000 33 60
    • (2000) Int. Rev. Cytol. , vol.192 , pp. 33-60
    • Johansson, G.1    Walter, H.2
  • 52
    • 0033991589 scopus 로고    scopus 로고
    • Compositions and phase diagrams for aqueous systems based on proteins and polysaccharides
    • V. Tolstoguzov Compositions and phase diagrams for aqueous systems based on proteins and polysaccharides Int. Rev. Cytol. 192 2000 3 31
    • (2000) Int. Rev. Cytol. , vol.192 , pp. 3-31
    • Tolstoguzov, V.1
  • 54
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • A.P. Minton The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media J. Biol. Chem. 276 2001 10577 10580
    • (2001) J. Biol. Chem. , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 55
    • 33845295824 scopus 로고    scopus 로고
    • The depletion attraction: An underappreciated force driving cellular organization
    • D. Marenduzzo, K. Finan, and P.R. Cook The depletion attraction: an underappreciated force driving cellular organization J. Cell Biol. 175 2006 681 686
    • (2006) J. Cell Biol. , vol.175 , pp. 681-686
    • Marenduzzo, D.1    Finan, K.2    Cook, P.R.3
  • 56
    • 84856073148 scopus 로고    scopus 로고
    • Macromolecular crowding regulates assembly of mRNA stress granules after osmotic stress: New role for compatible osmolytes
    • O. Bounedjah, L. Hamon, P. Savarin, B. Desforges, P.A. Curmi, and D. Pastre Macromolecular crowding regulates assembly of mRNA stress granules after osmotic stress: new role for compatible osmolytes J. Biol. Chem. 287 2012 2446 2458
    • (2012) J. Biol. Chem. , vol.287 , pp. 2446-2458
    • Bounedjah, O.1    Hamon, L.2    Savarin, P.3    Desforges, B.4    Curmi, P.A.5    Pastre, D.6
  • 57
    • 0028940740 scopus 로고
    • Phase separation in cytoplasm, due to macromolecular crowding, is the basis for microcompartmentation
    • H. Walter, and D.E. Brooks Phase separation in cytoplasm, due to macromolecular crowding, is the basis for microcompartmentation FEBS Lett. 361 1995 135 139
    • (1995) FEBS Lett. , vol.361 , pp. 135-139
    • Walter, H.1    Brooks, D.E.2
  • 58
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • D. Lingwood, and K. Simons Lipid rafts as a membrane-organizing principle Science 327 2010 46 50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 59
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • J. Tyedmers, A. Mogk, and B. Bukau Cellular strategies for controlling protein aggregation Nat. Rev. Mol. Cell Biol. 11 2010 777 788
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 60
    • 79960285739 scopus 로고    scopus 로고
    • Beyond stereospecificity: Liquids and mesoscale organization of cytoplasm
    • A.A. Hyman, and C.P. Brangwynne Beyond stereospecificity: liquids and mesoscale organization of cytoplasm Dev. Cell 21 2011 14 16
    • (2011) Dev. Cell , vol.21 , pp. 14-16
    • Hyman, A.A.1    Brangwynne, C.P.2
  • 61
    • 84865560483 scopus 로고    scopus 로고
    • Beyond oil and water-phase transitions in cells
    • A.A. Hyman, and K. Simons Beyond oil and water-phase transitions in cells Science 337 2012 1047 1049
    • (2012) Science , vol.337 , pp. 1047-1049
    • Hyman, A.A.1    Simons, K.2
  • 64
    • 33747191719 scopus 로고    scopus 로고
    • Prevalent structural disorder in E. coli and S. cerevisiae proteomes
    • P. Tompa, Z. Dosztanyi, and I. Simon Prevalent structural disorder in E. coli and S. cerevisiae proteomes J. Proteome Res. 5 2006 1996 2000
    • (2006) J. Proteome Res. , vol.5 , pp. 1996-2000
    • Tompa, P.1    Dosztanyi, Z.2    Simon, I.3
  • 66
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • J.J. Ward, J.S. Sodhi, L.J. McGuffin, B.F. Buxton, and D.T. Jones Prediction and functional analysis of native disorder in proteins from the three kingdoms of life J. Mol. Biol. 337 2004 635 645
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 68
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions, Nature reviews
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions, Nature reviews Mol. Cell. Biol. 6 2005 197 208
    • (2005) Mol. Cell. Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 69
    • 58149199635 scopus 로고    scopus 로고
    • The 'fuzzy' interactome
    • (author reply 3)
    • G.R. Welch The 'fuzzy' interactome Trends Biochem. Sci. 34 2009 1 2 (author reply 3)
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 1-2
    • Welch, G.R.1
  • 70
    • 84870057622 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: A 10-year recap
    • P. Tompa Intrinsically disordered proteins: a 10-year recap Trends Biochem. Sci. 2012
    • (2012) Trends Biochem. Sci.
    • Tompa, P.1
  • 71
    • 84859494186 scopus 로고    scopus 로고
    • Fuzzy complexes: A more stochastic view of protein function
    • M. Fuxreiter, and P. Tompa Fuzzy complexes: a more stochastic view of protein function Adv. Exp. Med. Biol. 725 2012 1 14
    • (2012) Adv. Exp. Med. Biol. , vol.725 , pp. 1-14
    • Fuxreiter, M.1    Tompa, P.2
  • 72
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • P. Tompa, and M. Fuxreiter Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions Trends Biochem. Sci. 33 2008 2 8
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 73
    • 82655180384 scopus 로고    scopus 로고
    • Fuzziness: Linking regulation to protein dynamics
    • M. Fuxreiter Fuzziness: linking regulation to protein dynamics Mol. Biosyst. 8 2012 168 177
    • (2012) Mol. Biosyst. , vol.8 , pp. 168-177
    • Fuxreiter, M.1
  • 74
    • 77956636245 scopus 로고    scopus 로고
    • Computational identification and analysis of protein short linear motifs
    • N.E. Davey, R.J. Edwards, and D.C. Shields Computational identification and analysis of protein short linear motifs Front. Biosci. 15 2010 801 825
    • (2010) Front. Biosci. , vol.15 , pp. 801-825
    • Davey, N.E.1    Edwards, R.J.2    Shields, D.C.3
  • 76
    • 84861327457 scopus 로고    scopus 로고
    • Interactions via intrinsically disordered regions: What kind of motifs?
    • R. Pancsa, and M. Fuxreiter Interactions via intrinsically disordered regions: what kind of motifs? IUBMB Life 64 2012 513 520
    • (2012) IUBMB Life , vol.64 , pp. 513-520
    • Pancsa, R.1    Fuxreiter, M.2
  • 79
    • 84859976535 scopus 로고    scopus 로고
    • Unmasking functional motifs within disordered regions of proteins
    • R.K. Das, A.H. Mao, and R.V. Pappu Unmasking functional motifs within disordered regions of proteins Sci. Signal. 5 2012 e17
    • (2012) Sci. Signal. , vol.5 , pp. 17
    • Das, R.K.1    Mao, A.H.2    Pappu, R.V.3
  • 80
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • M. Fuxreiter, P. Tompa, and I. Simon Local structural disorder imparts plasticity on linear motifs Bioinformatics 23 2007 950 956
    • (2007) Bioinformatics , vol.23 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 81
    • 84863958621 scopus 로고    scopus 로고
    • Protein solubility and protein homeostasis: A generic view of protein misfolding disorders
    • M. Vendruscolo, T.P. Knowles, and C.M. Dobson Protein solubility and protein homeostasis: a generic view of protein misfolding disorders Cold Spring Harb. Perspect. Biol. 3 2011
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Vendruscolo, M.1    Knowles, T.P.2    Dobson, C.M.3
  • 82
    • 33750934185 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions
    • S.L. Crick, M. Jayaraman, C. Frieden, R. Wetzel, and R.V. Pappu Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions Proc. Natl. Acad. Sci. U. S. A. 103 2006 16764 16769
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16764-16769
    • Crick, S.L.1    Jayaraman, M.2    Frieden, C.3    Wetzel, R.4    Pappu, R.V.5
  • 84
    • 33847324863 scopus 로고    scopus 로고
    • A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
    • S. Mukhopadhyay, R. Krishnan, E.A. Lemke, S. Lindquist, and A.A. Deniz A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures Proc. Natl. Acad. Sci. U. S. A. 104 2007 2649 2654
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5
  • 85
    • 34548757409 scopus 로고    scopus 로고
    • Quantitative characterization of intrinsic disorder in polyglutamine: Insights from analysis based on polymer theories
    • A. Vitalis, X. Wang, and R.V. Pappu Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories Biophys. J. 93 2007 1923 1937
    • (2007) Biophys. J. , vol.93 , pp. 1923-1937
    • Vitalis, A.1    Wang, X.2    Pappu, R.V.3
  • 86
    • 70349838220 scopus 로고    scopus 로고
    • Examining polyglutamine peptide length: A connection between collapsed conformations and increased aggregation
    • R.H. Walters, and R.M. Murphy Examining polyglutamine peptide length: a connection between collapsed conformations and increased aggregation J. Mol. Biol. 393 2009 978 992
    • (2009) J. Mol. Biol. , vol.393 , pp. 978-992
    • Walters, R.H.1    Murphy, R.M.2
  • 87
    • 33645281939 scopus 로고    scopus 로고
    • Characterizing the conformational ensemble of monomeric polyglutamine
    • X. Wang, A. Vitalis, M.A. Wyczalkowski, and R.V. Pappu Characterizing the conformational ensemble of monomeric polyglutamine Proteins 63 2006 297 311
    • (2006) Proteins , vol.63 , pp. 297-311
    • Wang, X.1    Vitalis, A.2    Wyczalkowski, M.A.3    Pappu, R.V.4
  • 88
    • 44949262123 scopus 로고    scopus 로고
    • Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins
    • H.T. Tran, A. Mao, and R.V. Pappu Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins J. Am. Chem. Soc. 130 2008 7380 7392
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 7380-7392
    • Tran, H.T.1    Mao, A.2    Pappu, R.V.3
  • 89
    • 80053441923 scopus 로고    scopus 로고
    • Dynamic protein-DNA recognition: Beyond what can be seen
    • M. Fuxreiter, I. Simon, and S. Bondos Dynamic protein-DNA recognition: beyond what can be seen Trends Biochem. Sci. 36 2011 415 423
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 415-423
    • Fuxreiter, M.1    Simon, I.2    Bondos, S.3
  • 90
    • 77952335311 scopus 로고    scopus 로고
    • Net charge per residue modulates conformational ensembles of intrinsically disordered proteins
    • A.H. Mao, S.L. Crick, A. Vitalis, C.L. Chicoine, and R.V. Pappu Net charge per residue modulates conformational ensembles of intrinsically disordered proteins Proc. Natl. Acad. Sci. U. S. A. 107 2010 8183 8188
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 8183-8188
    • Mao, A.H.1    Crick, S.L.2    Vitalis, A.3    Chicoine, C.L.4    Pappu, R.V.5
  • 92
    • 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
  • 94
    • 33644817188 scopus 로고    scopus 로고
    • Prion domains: Sequences, structures and interactions
    • E.D. Ross, A. Minton, and R.B. Wickner Prion domains: sequences, structures and interactions Nat. Cell Biol. 7 2005 1039 1044
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1039-1044
    • Ross, E.D.1    Minton, A.2    Wickner, R.B.3
  • 95
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • J. Shorter, and S. Lindquist Prions as adaptive conduits of memory and inheritance Nat. Rev. 6 2005 435 450
    • (2005) Nat. Rev. , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 96
    • 78649417132 scopus 로고    scopus 로고
    • The prion hypothesis: From biological anomaly to basic regulatory mechanism, Nature reviews
    • M.F. Tuite, and T.R. Serio The prion hypothesis: from biological anomaly to basic regulatory mechanism, Nature reviews Mol. Cell. Biol. 11 2010 823 833
    • (2010) Mol. Cell. Biol. , vol.11 , pp. 823-833
    • Tuite, M.F.1    Serio, T.R.2
  • 97
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • S. Alberti, R. Halfmann, O. King, A. Kapila, and S. Lindquist A systematic survey identifies prions and illuminates sequence features of prionogenic proteins Cell 137 2009 146 158
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 98
    • 0033118934 scopus 로고    scopus 로고
    • Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism
    • S.S. Eaglestone, B.S. Cox, and M.F. Tuite Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism EMBO J. 18 1999 1974 1981
    • (1999) EMBO J. , vol.18 , pp. 1974-1981
    • Eaglestone, S.S.1    Cox, B.S.2    Tuite, M.F.3
  • 100
    • 4544235083 scopus 로고    scopus 로고
    • Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits
    • H.L. True, I. Berlin, and S.L. Lindquist Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits Nature 431 2004 184 187
    • (2004) Nature , vol.431 , pp. 184-187
    • True, H.L.1    Berlin, I.2    Lindquist, S.L.3
  • 101
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • H.L. True, and S.L. Lindquist A yeast prion provides a mechanism for genetic variation and phenotypic diversity Nature 407 2000 477 483
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 102
    • 77249122579 scopus 로고    scopus 로고
    • Prions, protein homeostasis, and phenotypic diversity
    • R. Halfmann, S. Alberti, and S. Lindquist Prions, protein homeostasis, and phenotypic diversity Trends Cell Biol. 20 2010 125 133
    • (2010) Trends Cell Biol. , vol.20 , pp. 125-133
    • Halfmann, R.1    Alberti, S.2    Lindquist, S.3
  • 103
    • 78049361927 scopus 로고    scopus 로고
    • Epigenetics in the extreme: Prions and the inheritance of environmentally acquired traits
    • R. Halfmann, and S. Lindquist Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits Science 330 2010 629 632
    • (2010) Science , vol.330 , pp. 629-632
    • Halfmann, R.1    Lindquist, S.2
  • 105
    • 83755183700 scopus 로고    scopus 로고
    • The yeast prions [PSI +] and [URE3] are molecular degenerative diseases
    • R.B. Wickner, H.K. Edskes, D. Bateman, A.C. Kelly, and A. Gorkovskiy The yeast prions [PSI +] and [URE3] are molecular degenerative diseases Prion 5 2011 258 262
    • (2011) Prion , vol.5 , pp. 258-262
    • Wickner, R.B.1    Edskes, H.K.2    Bateman, D.3    Kelly, A.C.4    Gorkovskiy, A.5
  • 108
    • 73549115633 scopus 로고    scopus 로고
    • Compositional determinants of prion formation in yeast
    • J.A. Toombs, B.R. McCarty, and E.D. Ross Compositional determinants of prion formation in yeast Mol. Cell. Biol. 30 2010 319 332
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 319-332
    • Toombs, J.A.1    McCarty, B.R.2    Ross, E.D.3
  • 109
    • 84867594034 scopus 로고    scopus 로고
    • Prion domain of yeast Ure2 protein adopts a completely disordered structure: A solid-support EPR study
    • S. Ngo, V. Chiang, E. Ho, L. Le, and Z. Guo Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study PLoS One 7 2012 e47248
    • (2012) PLoS One , vol.7 , pp. 47248
    • Ngo, S.1    Chiang, V.2    Ho, E.3    Le, L.4    Guo, Z.5
  • 111
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • R. Krishnan, and S.L. Lindquist Structural insights into a yeast prion illuminate nucleation and strain diversity Nature 435 2005 765 772
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 113
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • M.D. Michelitsch, and J.S. Weissman A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions Proc. Natl. Acad. Sci. U. S. A. 97 2000 11910 11915
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 114
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: An epigenetic modifier of protein function in yeast
    • N. Sondheimer, and S. Lindquist Rnq1: an epigenetic modifier of protein function in yeast Mol. Cell 5 2000 163 172
    • (2000) Mol. Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 115
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • K. Si, S. Lindquist, and E.R. Kandel A neuronal isoform of the aplysia CPEB has prion-like properties Cell 115 2003 879 891
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 116
    • 70349554668 scopus 로고    scopus 로고
    • Amyloids go genomic: Insights regarding the sequence determinants of prion formation from genome-wide studies
    • H.A. Lashuel, and R.V. Pappu Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies ChemBioChem 10 2009 1951 1954
    • (2009) ChemBioChem , vol.10 , pp. 1951-1954
    • Lashuel, H.A.1    Pappu, R.V.2
  • 117
    • 0038576863 scopus 로고    scopus 로고
    • A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes
    • P.M. Harrison, and M. Gerstein A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes Genome Biol. 4 2003 R40
    • (2003) Genome Biol. , vol.4 , pp. 40
    • Harrison, P.M.1    Gerstein, M.2
  • 121
    • 62549130374 scopus 로고    scopus 로고
    • Prion variants and species barriers among Saccharomyces Ure2 proteins
    • H.K. Edskes, L.M. McCann, A.M. Hebert, and R.B. Wickner Prion variants and species barriers among Saccharomyces Ure2 proteins Genetics 181 2009 1159 1167
    • (2009) Genetics , vol.181 , pp. 1159-1167
    • Edskes, H.K.1    McCann, L.M.2    Hebert, A.M.3    Wickner, R.B.4
  • 122
    • 78651492351 scopus 로고    scopus 로고
    • Yeast prions: Could they be exaptations? the URE2/[URE3] system in Kluyveromyces lactis
    • R.A. Safadi, N. Talarek, N. Jacques, and M. Aigle Yeast prions: could they be exaptations? The URE2/[URE3] system in Kluyveromyces lactis FEMS Yeast Res. 11 2011 151 153
    • (2011) FEMS Yeast Res. , vol.11 , pp. 151-153
    • Safadi, R.A.1    Talarek, N.2    Jacques, N.3    Aigle, M.4
  • 123
    • 0141866883 scopus 로고    scopus 로고
    • Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation
    • N. Hosoda, T. Kobayashi, N. Uchida, Y. Funakoshi, Y. Kikuchi, S. Hoshino, and T. Katada Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation J. Biol. Chem. 278 2003 38287 38291
    • (2003) J. Biol. Chem. , vol.278 , pp. 38287-38291
    • Hosoda, N.1    Kobayashi, T.2    Uchida, N.3    Funakoshi, Y.4    Kikuchi, Y.5    Hoshino, S.6    Katada, T.7
  • 124
    • 36849079370 scopus 로고    scopus 로고
    • Mechanism of mRNA deadenylation: Evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases
    • Y. Funakoshi, Y. Doi, N. Hosoda, N. Uchida, M. Osawa, I. Shimada, M. Tsujimoto, T. Suzuki, T. Katada, and S. Hoshino Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases Genes Dev. 21 2007 3135 3148
    • (2007) Genes Dev. , vol.21 , pp. 3135-3148
    • Funakoshi, Y.1    Doi, Y.2    Hosoda, N.3    Uchida, N.4    Osawa, M.5    Shimada, I.6    Tsujimoto, M.7    Suzuki, T.8    Katada, T.9    Hoshino, S.10
  • 125
    • 34547136725 scopus 로고    scopus 로고
    • Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae
    • F. Shewmaker, L. Mull, T. Nakayashiki, D.C. Masison, and R.B. Wickner Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae Genetics 176 2007 1557 1565
    • (2007) Genetics , vol.176 , pp. 1557-1565
    • Shewmaker, F.1    Mull, L.2    Nakayashiki, T.3    Masison, D.C.4    Wickner, R.B.5
  • 126
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • O.D. King, A.D. Gitler, and J. Shorter The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease Brain Res. 1462 2012 61 80
    • (2012) Brain Res. , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 130
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • S. Frey, and D. Gorlich A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes Cell 130 2007 512 523
    • (2007) Cell , vol.130 , pp. 512-523
    • Frey, S.1    Gorlich, D.2
  • 131
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • S. Frey, R.P. Richter, and D. Gorlich FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties Science 314 2006 815 817
    • (2006) Science , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Gorlich, D.3
  • 133
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • K. Ribbeck, and D. Gorlich The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion EMBO J. 21 2002 2664 2671
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Gorlich, D.2
  • 134
    • 79955497151 scopus 로고    scopus 로고
    • P granules extend the nuclear pore complex environment in the C. elegans germ line
    • D.L. Updike, S.J. Hachey, J. Kreher, and S. Strome P granules extend the nuclear pore complex environment in the C. elegans germ line J. Cell Biol. 192 2011 939 948
    • (2011) J. Cell Biol. , vol.192 , pp. 939-948
    • Updike, D.L.1    Hachey, S.J.2    Kreher, J.3    Strome, S.4
  • 135
    • 34547595082 scopus 로고    scopus 로고
    • The nuclear pore complex: Oily spaghetti or gummy bear?
    • K. Weis The nuclear pore complex: oily spaghetti or gummy bear? Cell 130 2007 405 407
    • (2007) Cell , vol.130 , pp. 405-407
    • Weis, K.1
  • 136
    • 84861964894 scopus 로고    scopus 로고
    • Getting RNA and protein in phase
    • S.C. Weber, and C.P. Brangwynne Getting RNA and protein in phase Cell 149 2012 1188 1191
    • (2012) Cell , vol.149 , pp. 1188-1191
    • Weber, S.C.1    Brangwynne, C.P.2
  • 137
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
    • D.P. Denning, S.S. Patel, V. Uversky, A.L. Fink, and M. Rexach Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded Proc. Natl. Acad. Sci. U. S. A. 100 2003 2450 2455
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 138
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • S.S. Patel, B.J. Belmont, J.M. Sante, and M.F. Rexach Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex Cell 129 2007 83 96
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 139
    • 39049094665 scopus 로고    scopus 로고
    • Discovering novel interactions at the nuclear pore complex using bead halo: A rapid method for detecting molecular interactions of high and low affinity at equilibrium
    • S.S. Patel, and M.F. Rexach Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium Mol. Cell Proteomics 7 2008 121 131
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 121-131
    • Patel, S.S.1    Rexach, M.F.2
  • 141
    • 84859502161 scopus 로고    scopus 로고
    • Structural disorder and protein elasticity
    • S. Rauscher, and R. Pomes Structural disorder and protein elasticity Adv. Exp. Med. Biol. 725 2012 159 183
    • (2012) Adv. Exp. Med. Biol. , vol.725 , pp. 159-183
    • Rauscher, S.1    Pomes, R.2
  • 142
    • 1542619619 scopus 로고    scopus 로고
    • Spectroscopic evidence revealing polyproline II structure in hydrophobic, putatively elastomeric sequences encoded by specific exons of human tropoelastin
    • B. Bochicchio, A. Ait-Ali, A.M. Tamburro, and A.J. Alix Spectroscopic evidence revealing polyproline II structure in hydrophobic, putatively elastomeric sequences encoded by specific exons of human tropoelastin Biopolymers 73 2004 484 493
    • (2004) Biopolymers , vol.73 , pp. 484-493
    • Bochicchio, B.1    Ait-Ali, A.2    Tamburro, A.M.3    Alix, A.J.4
  • 143
    • 0016168148 scopus 로고
    • The elastic properties of elastin
    • C.A. Hoeve, and P.J. Flory The elastic properties of elastin Biopolymers 13 1974 677 686
    • (1974) Biopolymers , vol.13 , pp. 677-686
    • Hoeve, C.A.1    Flory, P.J.2
  • 144
    • 1542319866 scopus 로고    scopus 로고
    • Quantitative observation of backbone disorder in native elastin
    • M.S. Pometun, E.Y. Chekmenev, and R.J. Wittebort Quantitative observation of backbone disorder in native elastin J. Biol. Chem. 279 2004 7982 7987
    • (2004) J. Biol. Chem. , vol.279 , pp. 7982-7987
    • Pometun, M.S.1    Chekmenev, E.Y.2    Wittebort, R.J.3
  • 145
    • 13244275209 scopus 로고    scopus 로고
    • Supramolecular amyloid-like assembly of the polypeptide sequence coded by exon 30 of human tropoelastin
    • A.M. Tamburro, A. Pepe, B. Bochicchio, D. Quaglino, and I.P. Ronchetti Supramolecular amyloid-like assembly of the polypeptide sequence coded by exon 30 of human tropoelastin J. Biol. Chem. 280 2005 2682 2690
    • (2005) J. Biol. Chem. , vol.280 , pp. 2682-2690
    • Tamburro, A.M.1    Pepe, A.2    Bochicchio, B.3    Quaglino, D.4    Ronchetti, I.P.5
  • 146
    • 0019405590 scopus 로고
    • Conformation characterization of cyclopentapeptide, L.Val-L.Pro-Gly-L. Val-Gly: A repeating analogue of elastin
    • M.A. Khaled, C.M. Venkatachalam, H. Sugano, and D.W. Urry Conformation characterization of cyclopentapeptide, L.Val-L.Pro-Gly-L.Val-Gly: a repeating analogue of elastin Int. J. Pept. Protein Res. 17 1981 23 33
    • (1981) Int. J. Pept. Protein Res. , vol.17 , pp. 23-33
    • Khaled, M.A.1    Venkatachalam, C.M.2    Sugano, H.3    Urry, D.W.4
  • 147
    • 77950618150 scopus 로고    scopus 로고
    • Molecular simulations of protein disorder
    • S. Rauscher, and R. Pomes Molecular simulations of protein disorder Biochem. Cell Biol. 88 2010 269 290
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 269-290
    • Rauscher, S.1    Pomes, R.2
  • 148
    • 0036151987 scopus 로고    scopus 로고
    • Solid-state (13)C NMR reveals effects of temperature and hydration on elastin
    • A. Perry, M.P. Stypa, B.K. Tenn, and K.K. Kumashiro Solid-state (13)C NMR reveals effects of temperature and hydration on elastin Biophys. J. 82 2002 1086 1095
    • (2002) Biophys. J. , vol.82 , pp. 1086-1095
    • Perry, A.1    Stypa, M.P.2    Tenn, B.K.3    Kumashiro, K.K.4
  • 151
    • 0035131438 scopus 로고    scopus 로고
    • Roles of partly unfolded conformations in macromolecular self-assembly
    • K. Namba Roles of partly unfolded conformations in macromolecular self-assembly Genes Cells 6 2001 1 12
    • (2001) Genes Cells , vol.6 , pp. 1-12
    • Namba, K.1
  • 152
    • 38149063767 scopus 로고    scopus 로고
    • Structural disorder promotes assembly of protein complexes
    • H. Hegyi, E. Schad, and P. Tompa Structural disorder promotes assembly of protein complexes BMC Struct. Biol. 7 2007 65
    • (2007) BMC Struct. Biol. , vol.7 , pp. 65
    • Hegyi, H.1    Schad, E.2    Tompa, P.3
  • 154
  • 157
    • 33749258375 scopus 로고    scopus 로고
    • The yeast actin cytoskeleton: From cellular function to biochemical mechanism
    • J.B. Moseley, and B.L. Goode The yeast actin cytoskeleton: from cellular function to biochemical mechanism Microbiol. Mol. Biol. Rev. 70 2006 605 645
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 605-645
    • Moseley, J.B.1    Goode, B.L.2
  • 158
    • 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
  • 159
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging
    • A. Ben-Zvi, E.A. Miller, and R.I. Morimoto Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging Proc. Natl. Acad. Sci. U. S. A. 106 2009 14914 14919
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 14914-14919
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 163
    • 84865277422 scopus 로고    scopus 로고
    • Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates
    • L. Malinovska, S. Kroschwald, M.C. Munder, D. Richter, and S. Alberti Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates Mol. Biol. Cell 23 2012 3041 3056
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3041-3056
    • Malinovska, L.1    Kroschwald, S.2    Munder, M.C.3    Richter, D.4    Alberti, S.5
  • 164
    • 84868149498 scopus 로고    scopus 로고
    • Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast
    • R. Spokoini, O. Moldavski, Y. Nahmias, J.L. England, M. Schuldiner, and D. Kaganovich Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast Cell Rep. 2 2012 738 747
    • (2012) Cell Rep. , vol.2 , pp. 738-747
    • Spokoini, R.1    Moldavski, O.2    Nahmias, Y.3    England, J.L.4    Schuldiner, M.5    Kaganovich, D.6
  • 165
    • 84869807432 scopus 로고    scopus 로고
    • Molecular mechanisms of spatial protein quality control
    • S. Alberti Molecular mechanisms of spatial protein quality control Prion 7 2012
    • (2012) Prion , vol.7
    • Alberti, S.1
  • 166
    • 79951659192 scopus 로고    scopus 로고
    • Flexible nets of malleable guardians: Intrinsically disordered chaperones in neurodegenerative diseases
    • V.N. Uversky Flexible nets of malleable guardians: intrinsically disordered chaperones in neurodegenerative diseases Chem. Rev. 111 2011 1134 1166
    • (2011) Chem. Rev. , vol.111 , pp. 1134-1166
    • Uversky, V.N.1
  • 167
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • P. Tompa, and P. Csermely The role of structural disorder in the function of RNA and protein chaperones FASEB J. 18 2004 1169 1175
    • (2004) FASEB J. , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 170
    • 0034724559 scopus 로고    scopus 로고
    • Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
    • D.A. Haley, M.P. Bova, Q.L. Huang, H.S. McHaourab, and P.L. Stewart Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies J. Mol. Biol. 298 2000 261 272
    • (2000) J. Mol. Biol. , vol.298 , pp. 261-272
    • Haley, D.A.1    Bova, M.P.2    Huang, Q.L.3    McHaourab, H.S.4    Stewart, P.L.5
  • 171
    • 0031561418 scopus 로고    scopus 로고
    • Functional elements in molecular chaperone alpha-crystallin: Identification of binding sites in alpha B-crystallin
    • K.K. Sharma, H. Kaur, and K. Kester Functional elements in molecular chaperone alpha-crystallin: identification of binding sites in alpha B-crystallin Biochem. Biophys. Res. Commun. 239 1997 217 222
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 217-222
    • Sharma, K.K.1    Kaur, H.2    Kester, K.3
  • 173
    • 81355149538 scopus 로고    scopus 로고
    • Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
    • S. Specht, S.B. Miller, A. Mogk, and B. Bukau Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae J. Cell Biol. 195 2011 617 629
    • (2011) J. Cell Biol. , vol.195 , pp. 617-629
    • Specht, S.1    Miller, S.B.2    Mogk, A.3    Bukau, B.4
  • 175
    • 84865658810 scopus 로고    scopus 로고
    • P-bodies and stress granules: Possible roles in the control of translation and mRNA degradation
    • C.J. Decker, and R. Parker P-bodies and stress granules: possible roles in the control of translation and mRNA degradation Cold Spring Harb. Perspect. Biol. 4 2012 a012286
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. 012286
    • Decker, C.J.1    Parker, R.2
  • 176
    • 77952628837 scopus 로고    scopus 로고
    • Regulation of translation by stress granules and processing bodies
    • N. Kedersha, and P. Anderson Regulation of translation by stress granules and processing bodies Prog. Mol. Biol. Transl. Sci. 90 2009 155 185
    • (2009) Prog. Mol. Biol. Transl. Sci. , vol.90 , pp. 155-185
    • Kedersha, N.1    Anderson, P.2
  • 177
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: Post-transcriptional and epigenetic modulators of gene expression, Nature reviews
    • P. Anderson, and N. Kedersha RNA granules: post-transcriptional and epigenetic modulators of gene expression, Nature reviews Mol. Cell. Biol. 10 2009 430 436
    • (2009) Mol. Cell. Biol. , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 178
    • 84871744570 scopus 로고    scopus 로고
    • Processing body and stress granule assembly occur by independent and differentially regulated pathways in Saccharomyces cerevisiae
    • K.H. Shah, B. Zhang, V. Ramachandran, and P.K. Herman Processing body and stress granule assembly occur by independent and differentially regulated pathways in Saccharomyces cerevisiae Genetics 193 2013 109 123
    • (2013) Genetics , vol.193 , pp. 109-123
    • Shah, K.H.1    Zhang, B.2    Ramachandran, V.3    Herman, P.K.4
  • 179
    • 70350367745 scopus 로고    scopus 로고
    • Unravelling the ultrastructure of stress granules and associated P-bodies in human cells
    • S. Souquere, S. Mollet, M. Kress, F. Dautry, G. Pierron, and D. Weil Unravelling the ultrastructure of stress granules and associated P-bodies in human cells J. Cell Sci. 122 2009 3619 3626
    • (2009) J. Cell Sci. , vol.122 , pp. 3619-3626
    • Souquere, S.1    Mollet, S.2    Kress, M.3    Dautry, F.4    Pierron, G.5    Weil, D.6
  • 180
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • C.J. Decker, D. Teixeira, and R. Parker Edc3p and a glutamine/asparagine- rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae J. Cell Biol. 179 2007 437 449
    • (2007) J. Cell Biol. , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 182
    • 50249131374 scopus 로고    scopus 로고
    • A role for Q/N-rich aggregation-prone regions in P-body localization
    • M.A. Reijns, R.D. Alexander, M.P. Spiller, and J.D. Beggs A role for Q/N-rich aggregation-prone regions in P-body localization J. Cell Sci. 121 2008 2463 2472
    • (2008) J. Cell Sci. , vol.121 , pp. 2463-2472
    • Reijns, M.A.1    Alexander, R.D.2    Spiller, M.P.3    Beggs, J.D.4
  • 184
    • 62449148425 scopus 로고    scopus 로고
    • The peculiar interaction between mammalian prion protein and RNA
    • M.P. Gomes, Y. Cordeiro, and J.L. Silva The peculiar interaction between mammalian prion protein and RNA Prion 2 2008 64 66
    • (2008) Prion , vol.2 , pp. 64-66
    • Gomes, M.P.1    Cordeiro, Y.2    Silva, J.L.3
  • 185
    • 15444379718 scopus 로고    scopus 로고
    • Processing bodies require RNA for assembly and contain nontranslating mRNAs
    • D. Teixeira, U. Sheth, M.A. Valencia-Sanchez, M. Brengues, and R. Parker Processing bodies require RNA for assembly and contain nontranslating mRNAs RNA 11 2005 371 382
    • (2005) RNA , vol.11 , pp. 371-382
    • Teixeira, D.1    Sheth, U.2    Valencia-Sanchez, M.A.3    Brengues, M.4    Parker, R.5
  • 186
    • 79551593011 scopus 로고    scopus 로고
    • Nucleation of nuclear bodies by RNA
    • S.P. Shevtsov, and M. Dundr Nucleation of nuclear bodies by RNA Nat. Cell Biol. 13 2011 167 173
    • (2011) Nat. Cell Biol. , vol.13 , pp. 167-173
    • Shevtsov, S.P.1    Dundr, M.2
  • 187
    • 78650511795 scopus 로고    scopus 로고
    • Direct visualization of the co-transcriptional assembly of a nuclear body by noncoding RNAs
    • Y.S. Mao, H. Sunwoo, B. Zhang, and D.L. Spector Direct visualization of the co-transcriptional assembly of a nuclear body by noncoding RNAs Nat. Cell
    • (2011) Nat. Cell Biol. , vol.13 , pp. 95-101
    • Mao, Y.S.1    Sunwoo, H.2    Zhang, B.3    Spector, D.L.4


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