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Volumn 43, Issue 1, 2011, Pages 72-84

Opposing Effects of Glutamine and Asparagine Govern Prion Formation by Intrinsically Disordered Proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; ASPARAGINE; GLUTAMINE; PRION PROTEIN;

EID: 79959882243     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2011.05.013     Document Type: Article
Times cited : (152)

References (79)
  • 1
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S., Halfmann R., King O., Kapila A., Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 2009, 137:146-158.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 2
  • 3
    • 56149086182 scopus 로고    scopus 로고
    • P bodies promote stress granule assembly in Saccharomyces cerevisiae
    • Buchan J.R., Muhlrad D., Parker R. P bodies promote stress granule assembly in Saccharomyces cerevisiae. J. Cell Biol. 2008, 183:441-455.
    • (2008) J. Cell Biol. , vol.183 , pp. 441-455
    • Buchan, J.R.1    Muhlrad, D.2    Parker, R.3
  • 4
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • Chernoff Y.O., Lindquist S.L., Ono B., Inge-Vechtomov S.G., Liebman S.W. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 1995, 268:880-884.
    • (1995) Science , vol.268 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 5
    • 0033500152 scopus 로고    scopus 로고
    • Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion
    • Chernoff Y.O., Newnam G.P., Kumar J., Allen K., Zink A.D. Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion. Mol. Cell. Biol. 1999, 19:8103-8112.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8103-8112
    • Chernoff, Y.O.1    Newnam, G.P.2    Kumar, J.3    Allen, K.4    Zink, A.D.5
  • 6
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • Decker C.J., Teixeira D., Parker R. Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. J. Cell Biol. 2007, 179:437-449.
    • (2007) J. Cell Biol. , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 8
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: the story of [PIN(+)]
    • Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 2001, 106:171-182.
    • (2001) Cell , vol.106 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 9
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K.O., Davies S.W., Bates G.P., Vonsattel J.P., Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997, 277:1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 10
    • 78649824640 scopus 로고    scopus 로고
    • Optical trapping with high forces reveals unexpected behaviors of prion fibrils
    • Dong J., Castro C.E., Boyce M.C., Lang M.J., Lindquist S. Optical trapping with high forces reveals unexpected behaviors of prion fibrils. Nat. Struct. Mol. Biol. 2010, 17:1422-1430.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1422-1430
    • Dong, J.1    Castro, C.E.2    Boyce, M.C.3    Lang, M.J.4    Lindquist, S.5
  • 13
    • 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., Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 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
  • 14
    • 0026019655 scopus 로고
    • Rate of beta-structure formation in polypeptides
    • Finkelstein A.V. Rate of beta-structure formation in polypeptides. Proteins 1991, 9:23-27.
    • (1991) Proteins , vol.9 , pp. 23-27
    • Finkelstein, A.V.1
  • 15
    • 78650441363 scopus 로고    scopus 로고
    • Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins
    • Fiumara F., Fioriti L., Kandel E.R., Hendrickson W.A. Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins. Cell 2010, 143:1121-1135.
    • (2010) Cell , vol.143 , pp. 1121-1135
    • Fiumara, F.1    Fioriti, L.2    Kandel, E.R.3    Hendrickson, W.A.4
  • 17
    • 0030712145 scopus 로고    scopus 로고
    • Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
    • Glover J.R., Kowal A.S., Schirmer E.C., Patino M.M., Liu J.J., Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 1997, 89:811-819.
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1    Kowal, A.S.2    Schirmer, E.C.3    Patino, M.M.4    Liu, J.J.5    Lindquist, S.6
  • 18
    • 1542380028 scopus 로고    scopus 로고
    • The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104
    • Grimminger V., Richter K., Imhof A., Buchner J., Walter S. The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. J. Biol. Chem. 2004, 279:7378-7383.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7378-7383
    • Grimminger, V.1    Richter, K.2    Imhof, A.3    Buchner, J.4    Walter, S.5
  • 19
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: from transcript synthesis to protein degradation
    • Gsponer J., Futschik M.E., Teichmann S.A., Babu M.M. Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science 2008, 322:1365-1368.
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 20
    • 78049361927 scopus 로고    scopus 로고
    • Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits
    • Halfmann R., Lindquist S. Epigenetics in the extreme: prions and the inheritance of environmentally acquired traits. Science 2010, 330:629-632.
    • (2010) Science , vol.330 , pp. 629-632
    • Halfmann, R.1    Lindquist, S.2
  • 21
    • 77249122579 scopus 로고    scopus 로고
    • Prions, protein homeostasis, and phenotypic diversity
    • Halfmann R., Alberti S., Lindquist S. Prions, protein homeostasis, and phenotypic diversity. Trends Cell Biol. 2010, 20:125-133.
    • (2010) Trends Cell Biol. , vol.20 , pp. 125-133
    • Halfmann, R.1    Alberti, S.2    Lindquist, S.3
  • 23
    • 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
    • Harrison P.M., Gerstein M. A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes. Genome Biol. 2003, 4:R40.
    • (2003) Genome Biol. , vol.4
    • Harrison, P.M.1    Gerstein, M.2
  • 25
    • 0035543109 scopus 로고    scopus 로고
    • The architecture of parallel beta-helices and related folds
    • Jenkins J., Pickersgill R. The architecture of parallel beta-helices and related folds. Prog. Biophys. Mol. Biol. 2001, 77:111-175.
    • (2001) Prog. Biophys. Mol. Biol. , vol.77 , pp. 111-175
    • Jenkins, J.1    Pickersgill, R.2
  • 28
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • Kodali R., Wetzel R. Polymorphism in the intermediates and products of amyloid assembly. Curr. Opin. Struct. Biol. 2007, 17:48-57.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 29
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan R., Lindquist S.L. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 2005, 435:765-772.
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 30
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • Krobitsch S., Lindquist S. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc. Natl. Acad. Sci. USA 2000, 97:1589-1594.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 31
    • 1542782213 scopus 로고    scopus 로고
    • Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104
    • Kryndushkin D.S., Alexandrov I.M., Ter-Avanesyan M.D., Kushnirov V.V. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J. Biol. Chem. 2003, 278:49636-49643.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49636-49643
    • Kryndushkin, D.S.1    Alexandrov, I.M.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 32
    • 77749271373 scopus 로고    scopus 로고
    • The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system
    • Lancaster A.K., Bardill J.P., True H.L., Masel J. The spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] system. Genetics 2010, 184:393-400.
    • (2010) Genetics , vol.184 , pp. 393-400
    • Lancaster, A.K.1    Bardill, J.P.2    True, H.L.3    Masel, J.4
  • 34
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 1993, 2:404-410.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1
  • 35
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A., Van Dyke M., Stock J. Predicting coiled coils from protein sequences. Science 1991, 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 36
    • 32144456009 scopus 로고    scopus 로고
    • Paircoil2: improved prediction of coiled coils from sequence
    • McDonnell A.V., Jiang T., Keating A.E., Berger B. Paircoil2: improved prediction of coiled coils from sequence. Bioinformatics 2006, 22:356-358.
    • (2006) Bioinformatics , vol.22 , pp. 356-358
    • McDonnell, A.V.1    Jiang, T.2    Keating, A.E.3    Berger, B.4
  • 37
    • 0037053566 scopus 로고    scopus 로고
    • Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • Meriin A.B., Zhang X., He X., Newnam G.P., Chernoff Y.O., Sherman M.Y. Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J. Cell Biol. 2002, 157:997-1004.
    • (2002) J. Cell Biol. , vol.157 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3    Newnam, G.P.4    Chernoff, Y.O.5    Sherman, M.Y.6
  • 39
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions
    • Michelitsch M.D., Weissman J.S. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. USA 2000, 97:11910-11915.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 40
    • 33847324863 scopus 로고    scopus 로고
    • A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
    • Mukhopadhyay S., Krishnan R., Lemke E.A., Lindquist S., Deniz A.A. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc. Natl. Acad. Sci. USA 2007, 104:2649-2654.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5
  • 41
    • 33645995764 scopus 로고    scopus 로고
    • Recent atomic models of amyloid fibril structure
    • Nelson R., Eisenberg D. Recent atomic models of amyloid fibril structure. Curr. Opin. Struct. Biol. 2006, 16:260-265.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 260-265
    • Nelson, R.1    Eisenberg, D.2
  • 43
    • 36749056299 scopus 로고    scopus 로고
    • A polymer physics perspective on driving forces and mechanisms for protein aggregation
    • Pappu R.V., Wang X., Vitalis A., Crick S.L. A polymer physics perspective on driving forces and mechanisms for protein aggregation. Arch. Biochem. Biophys. 2008, 469:132-141.
    • (2008) Arch. Biochem. Biophys. , vol.469 , pp. 132-141
    • Pappu, R.V.1    Wang, X.2    Vitalis, A.3    Crick, S.L.4
  • 44
    • 61849091420 scopus 로고    scopus 로고
    • The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion
    • Patel B.K., Gavin-Smyth J., Liebman S.W. The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nat. Cell Biol. 2009, 11:344-349.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 344-349
    • Patel, B.K.1    Gavin-Smyth, J.2    Liebman, S.W.3
  • 45
    • 0035849879 scopus 로고    scopus 로고
    • Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats
    • Perutz M.F., Windle A.H. Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats. Nature 2001, 412:143-144.
    • (2001) Nature , vol.412 , pp. 143-144
    • Perutz, M.F.1    Windle, A.H.2
  • 46
    • 0037117499 scopus 로고    scopus 로고
    • Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques
    • Perutz M.F., Pope B.J., Owen D., Wanker E.E., Scherzinger E. Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques. Proc. Natl. Acad. Sci. USA 2002, 99:5596-5600.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5596-5600
    • Perutz, M.F.1    Pope, B.J.2    Owen, D.3    Wanker, E.E.4    Scherzinger, E.5
  • 51
    • 33644817188 scopus 로고    scopus 로고
    • Prion domains: sequences, structures and interactions
    • Ross E.D., Minton A., Wickner R.B. Prion domains: sequences, structures and interactions. Nat. Cell Biol. 2005, 7:1039-1044.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1039-1044
    • Ross, E.D.1    Minton, A.2    Wickner, R.B.3
  • 52
    • 74949101025 scopus 로고    scopus 로고
    • Regulation of synaptic Pumilio function by an aggregation-prone domain
    • Salazar A.M., Silverman E.J., Menon K.P., Zinn K. Regulation of synaptic Pumilio function by an aggregation-prone domain. J. Neurosci. 2010, 30:515-522.
    • (2010) J. Neurosci. , vol.30 , pp. 515-522
    • Salazar, A.M.1    Silverman, E.J.2    Menon, K.P.3    Zinn, K.4
  • 55
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter J., Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 2004, 304:1793-1797.
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 56
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • Si K., Lindquist S., Kandel E.R. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 2003, 115:879-891.
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 57
    • 4644370187 scopus 로고    scopus 로고
    • Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum
    • Singh G.P., Chandra B.R., Bhattacharya A., Akhouri R.R., Singh S.K., Sharma A. Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum. Mol. Biochem. Parasitol. 2004, 137:307-319.
    • (2004) Mol. Biochem. Parasitol. , vol.137 , pp. 307-319
    • Singh, G.P.1    Chandra, B.R.2    Bhattacharya, A.3    Akhouri, R.R.4    Singh, S.K.5    Sharma, A.6
  • 58
  • 59
    • 45749102914 scopus 로고    scopus 로고
    • The Zyggregator method for predicting protein aggregation propensities
    • Tartaglia G.G., Vendruscolo M. The Zyggregator method for predicting protein aggregation propensities. Chem. Soc. Rev. 2008, 37:1395-1401.
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1395-1401
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 60
    • 66849099684 scopus 로고    scopus 로고
    • Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]
    • Tessier P.M., Lindquist S. Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]. Nat. Struct. Mol. Biol. 2009, 16:598-605.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 598-605
    • Tessier, P.M.1    Lindquist, S.2
  • 62
    • 73549115633 scopus 로고    scopus 로고
    • Compositional determinants of prion formation in yeast
    • Toombs J.A., McCarty B.R., Ross E.D. Compositional determinants of prion formation in yeast. Mol. Cell. Biol. 2010, 30:319-332.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 319-332
    • Toombs, J.A.1    McCarty, B.R.2    Ross, E.D.3
  • 63
    • 66749115386 scopus 로고    scopus 로고
    • Amyloid deposits: protection against toxic protein species?
    • Treusch S., Cyr D.M., Lindquist S. Amyloid deposits: protection against toxic protein species?. Cell Cycle 2009, 8:1668-1674.
    • (2009) Cell Cycle , vol.8 , pp. 1668-1674
    • Treusch, S.1    Cyr, D.M.2    Lindquist, S.3
  • 64
    • 49349110821 scopus 로고    scopus 로고
    • Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases
    • Truant R., Atwal R.S., Desmond C., Munsie L., Tran T. Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases. FEBS J. 2008, 275:4252-4262.
    • (2008) FEBS J. , vol.275 , pp. 4252-4262
    • Truant, R.1    Atwal, R.S.2    Desmond, C.3    Munsie, L.4    Tran, T.5
  • 65
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • True H.L., Lindquist S.L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 2000, 407:477-483.
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 66
    • 77954217602 scopus 로고    scopus 로고
    • The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation
    • Turoverov K.K., Kuznetsova I.M., Uversky V.N. The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation. Prog. Biophys. Mol. Biol. 2010, 102:73-84.
    • (2010) Prog. Biophys. Mol. Biol. , vol.102 , pp. 73-84
    • Turoverov, K.K.1    Kuznetsova, I.M.2    Uversky, V.N.3
  • 67
    • 77952711519 scopus 로고    scopus 로고
    • Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation
    • Tyedmers J., Treusch S., Dong J., McCaffery J.M., Bevis B., Lindquist S. Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation. Proc. Natl. Acad. Sci. USA 2010, 107:8633-8638.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8633-8638
    • Tyedmers, J.1    Treusch, S.2    Dong, J.3    McCaffery, J.M.4    Bevis, B.5    Lindquist, S.6
  • 68
    • 45449091418 scopus 로고    scopus 로고
    • Amyloidogenesis of natively unfolded proteins
    • Uversky V.N. Amyloidogenesis of natively unfolded proteins. Curr. Alzheimer Res. 2008, 5:260-287.
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 260-287
    • Uversky, V.N.1
  • 69
    • 67649635978 scopus 로고    scopus 로고
    • Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity
    • Vavouri T., Semple J.I., Garcia-Verdugo R., Lehner B. Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell 2009, 138:198-208.
    • (2009) Cell , vol.138 , pp. 198-208
    • Vavouri, T.1    Semple, J.I.2    Garcia-Verdugo, R.3    Lehner, B.4
  • 70
    • 68949127591 scopus 로고    scopus 로고
    • Thermodynamics of beta-sheet formation in polyglutamine
    • Vitalis A., Lyle N., Pappu R.V. Thermodynamics of beta-sheet formation in polyglutamine. Biophys. J. 2009, 97:303-311.
    • (2009) Biophys. J. , vol.97 , pp. 303-311
    • Vitalis, A.1    Lyle, N.2    Pappu, R.V.3
  • 71
    • 34548757409 scopus 로고    scopus 로고
    • Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories
    • Vitalis A., Wang X., Pappu R.V. Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories. Biophys. J. 2007, 93:1923-1937.
    • (2007) Biophys. J. , vol.93 , pp. 1923-1937
    • Vitalis, A.1    Wang, X.2    Pappu, R.V.3
  • 72
    • 54249132105 scopus 로고    scopus 로고
    • Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization
    • Vitalis A., Wang X., Pappu R.V. Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization. J. Mol. Biol. 2008, 384:279-297.
    • (2008) J. Mol. Biol. , vol.384 , pp. 279-297
    • Vitalis, A.1    Wang, X.2    Pappu, R.V.3
  • 73
    • 70349838220 scopus 로고    scopus 로고
    • Examining polyglutamine peptide length: a connection between collapsed conformations and increased aggregation
    • Walters R.H., Murphy R.M. Examining polyglutamine peptide length: a connection between collapsed conformations and increased aggregation. J. Mol. Biol. 2009, 393:978-992.
    • (2009) J. Mol. Biol. , vol.393 , pp. 978-992
    • Walters, R.H.1    Murphy, R.M.2
  • 74
    • 33645281939 scopus 로고    scopus 로고
    • Characterizing the conformational ensemble of monomeric polyglutamine
    • Wang X., Vitalis A., Wyczalkowski M.A., Pappu R.V. Characterizing the conformational ensemble of monomeric polyglutamine. Proteins 2006, 63:297-311.
    • (2006) Proteins , vol.63 , pp. 297-311
    • Wang, X.1    Vitalis, A.2    Wyczalkowski, M.A.3    Pappu, R.V.4
  • 75
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
    • Wasmer C., Lange A., Van Melckebeke H., Siemer A.B., Riek R., Meier B.H. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 2008, 319:1523-1526.
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 76
    • 6344277430 scopus 로고    scopus 로고
    • Reduced amino acid alphabet is sufficient to accurately recognize intrinsically disordered protein
    • Weathers E.A., Paulaitis M.E., Woolf T.B., Hoh J.H. Reduced amino acid alphabet is sufficient to accurately recognize intrinsically disordered protein. FEBS Lett. 2004, 576:348-352.
    • (2004) FEBS Lett. , vol.576 , pp. 348-352
    • Weathers, E.A.1    Paulaitis, M.E.2    Woolf, T.B.3    Hoh, J.H.4
  • 77
    • 77649271684 scopus 로고    scopus 로고
    • Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin
    • Williamson T.E., Vitalis A., Crick S.L., Pappu R.V. Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin. J. Mol. Biol. 2010, 396:1295-1309.
    • (2010) J. Mol. Biol. , vol.396 , pp. 1295-1309
    • Williamson, T.E.1    Vitalis, A.2    Crick, S.L.3    Pappu, R.V.4
  • 78
    • 0032483427 scopus 로고    scopus 로고
    • Glutamine-rich domains activate transcription in yeast Saccharomyces cerevisiae
    • Xiao H., Jeang K.T. Glutamine-rich domains activate transcription in yeast Saccharomyces cerevisiae. J. Biol. Chem. 1998, 273:22873-22876.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22873-22876
    • Xiao, H.1    Jeang, K.T.2
  • 79
    • 58749109622 scopus 로고    scopus 로고
    • Simulations of nucleation and elongation of amyloid fibrils
    • Zhang J., Muthukumar M. Simulations of nucleation and elongation of amyloid fibrils. J. Chem. Phys. 2009, 130:035102.
    • (2009) J. Chem. Phys. , vol.130 , pp. 035102
    • Zhang, J.1    Muthukumar, M.2


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