메뉴 건너뛰기




Volumn 6, Issue JAN, 2016, Pages

The rho termination factor of Clostridium botulinum contains a prion-like domain with a highly amyloidogenic core

Author keywords

Amyloid; Bacteria; Clostridium; Prion; Protein aggregation

Indexed keywords

AMYLOID; PRION PROTEIN; RNA BINDING PROTEIN; TRANSCRIPTION TERMINATION FACTOR RHO;

EID: 84957991392     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2015.01516     Document Type: Article
Times cited : (33)

References (100)
  • 1
    • 0032559911 scopus 로고    scopus 로고
    • Spongiform encephalopathies. The prion's perplexing persistence
    • Aguzzi, A., and Weissmann, C. (1998). Spongiform encephalopathies. The prion's perplexing persistence. Nature 392, 763-764. doi: 10.1038/33812.
    • (1998) Nature , vol.392 , pp. 763-764
    • Aguzzi, A.1    Weissmann, C.2
  • 2
    • 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., and Lindquist, S. (2009). A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137, 146-158. doi: 10.1016/j.cell.2009.02.044.
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 3
    • 77349095036 scopus 로고    scopus 로고
    • Novel eukaryotic enzymes modifying cell-surface biopolymers
    • Anantharaman, V., and Aravind, L. (2010). Novel eukaryotic enzymes modifying cell-surface biopolymers. Biol. Direct 5:1. doi: 10.1186/1745-6150-5-1.
    • (2010) Biol. Direct , vol.5 , pp. 1
    • Anantharaman, V.1    Aravind, L.2
  • 4
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid
    • Balbirnie, M., Grothe, R., and Eisenberg, D. S. (2001). An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid. Proc. Natl. Acad. Sci. U.S.A. 98, 2375-2380. doi: 10.1073/pnas.041617698.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 5
    • 33646886355 scopus 로고    scopus 로고
    • Crystal structure of a novel β-lactam-insensitive peptidoglycan transpeptidase
    • Biarrotte-Sorin, S., Hugonnet, J. E., Delfosse, V., Mainardi, J. L., Gutmann, L., Arthur, M., et al. (2006). Crystal structure of a novel β-lactam-insensitive peptidoglycan transpeptidase. J. Mol. Biol. 359, 533-538. doi: 10.1016/j.jmb.2006.03.014.
    • (2006) J. Mol. Biol , vol.359 , pp. 533-538
    • Biarrotte-Sorin, S.1    Hugonnet, J.E.2    Delfosse, V.3    Mainardi, J.L.4    Gutmann, L.5    Arthur, M.6
  • 6
    • 0033120903 scopus 로고    scopus 로고
    • The structural basis for terminator recognition by the rho transcription termination factor
    • Bogden, C. E., Fass, D., Bergman, N., Nichols, M. D., and Berger, J. M. (1999). The structural basis for terminator recognition by the rho transcription termination factor. Mol. Cell. 3, 487-493. doi: 10.1016/S1097-2765(00)80476-1.
    • (1999) Mol. Cell , vol.3 , pp. 487-493
    • Bogden, C.E.1    Fass, D.2    Bergman, N.3    Nichols, M.D.4    Berger, J.M.5
  • 7
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork, P., Sander, C., and Valencia, A. (1992). An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc. Natl. Acad. Sci. U.S.A. 89, 7290-7294. doi: 10.1073/pnas.89.16.7290.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 8
    • 84877054205 scopus 로고    scopus 로고
    • Terminator still moving forward: expanding roles for Rho factor
    • Boudvillain, M., Figueroa-Bossi, N., and Bossi, L. (2013). Terminator still moving forward: expanding roles for Rho factor. Curr. Opin. Microbiol. 16, 118-124. doi: 10.1016/j.mib.2012.12.003.
    • (2013) Curr. Opin. Microbiol , vol.16 , pp. 118-124
    • Boudvillain, M.1    Figueroa-Bossi, N.2    Bossi, L.3
  • 9
    • 84915752004 scopus 로고    scopus 로고
    • Prion-like polymerization as a signaling mechanism
    • Cai, X., and Chen, Z. J. (2014). Prion-like polymerization as a signaling mechanism. Trends Immunol. 35, 622-630. doi: 10.1016/j.it.2014.10.003.
    • (2014) Trends Immunol , vol.35 , pp. 622-630
    • Cai, X.1    Chen, Z.J.2
  • 10
    • 44249091644 scopus 로고    scopus 로고
    • Termination factor rho and its cofactors NusA and NusG silence foreign DNA in E. coli
    • Cardinale, C. J., Washburn, R. S., Tadigotla, V. R., Brown, L. M., Gottesman, M. E., and Nudler, E. (2008). Termination factor rho and its cofactors NusA and NusG silence foreign DNA in E. coli. Science 320, 935-938. doi: 10.1126/science.1152763.
    • (2008) Science , vol.320 , pp. 935-938
    • Cardinale, C.J.1    Washburn, R.S.2    Tadigotla, V.R.3    Brown, L.M.4    Gottesman, M.E.5    Nudler, E.6
  • 11
    • 0035961323 scopus 로고    scopus 로고
    • Prion protein interconversions
    • Caughey, B. (2001). Prion protein interconversions. Philos. Trans. R. Soc. B Biol. Sci. 356, 197-202. doi: 10.1098/rstb.2000.0765.
    • (2001) Philos. Trans. R. Soc. B Biol. Sci , vol.356 , pp. 197-202
    • Caughey, B.1
  • 12
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366. doi: 10.1146/annurev.biochem.75.101304.123901.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 13
    • 33947517558 scopus 로고    scopus 로고
    • AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
    • Conchillo-Solé, O., de Groot, N. S., Avilés, F. X., Vendrell, J., Daura, X., and Ventura, S. (2007). AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC Bioinformatics 8:65. doi: 10.1186/1471-2105-8-65.
    • (2007) BMC Bioinformatics , vol.8 , pp. 65
    • Conchillo-Solé, O.1    de Groot, N.S.2    Avilés, F.X.3    Vendrell, J.4    Daura, X.5    Ventura, S.6
  • 14
    • 33847772827 scopus 로고    scopus 로고
    • Ile-phe dipeptide self-assembly: clues to amyloid formation
    • de Groot, N. S., Parella, T., Aviles, F. X., Vendrell, J., and Ventura, S. (2007). Ile-phe dipeptide self-assembly: clues to amyloid formation. Biophys. J. 92, 1732-1741. doi: 10.1529/biophysj.106.096677.
    • (2007) Biophys. J , vol.92 , pp. 1732-1741
    • de Groot, N.S.1    Parella, T.2    Aviles, F.X.3    Vendrell, J.4    Ventura, S.5
  • 15
    • 84869017593 scopus 로고    scopus 로고
    • Operational plasticity enables Hsp104 to disaggregate diverse amyloid and nonamyloid clients
    • Desantis, M. E., Leung, E. H., Sweeny, E. A., Jackrel, M. E., Cushman-Nick, M., Neuhaus-Follini, A., et al. (2012). Operational plasticity enables Hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell 151, 778-793. doi: 10.1016/j.cell.2012.09.038.
    • (2012) Cell , vol.151 , pp. 778-793
    • Desantis, M.E.1    Leung, E.H.2    Sweeny, E.A.3    Jackrel, M.E.4    Cushman-Nick, M.5    Neuhaus-Follini, A.6
  • 16
    • 0038690113 scopus 로고    scopus 로고
    • Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide
    • Diaz-Avalos, R., Long, C., Fontano, E., Balbirnie, M., Grothe, R., Eisenberg, D., et al. (2003). Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide. J. Mol. Biol. 330, 1165-1175. doi: 10.1016/S0022-2836(03)00659-4.
    • (2003) J. Mol. Biol , vol.330 , pp. 1165-1175
    • Diaz-Avalos, R.1    Long, C.2    Fontano, E.3    Balbirnie, M.4    Grothe, R.5    Eisenberg, D.6
  • 17
    • 29344476196 scopus 로고    scopus 로고
    • The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus
    • Divakaruni, A. V., Loo, R. R., Xie, Y., Loo, J. A., and Gober, J. W. (2005). The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus. Proc. Natl. Acad. Sci. U.S.A. 102, 18602-18607. doi: 10.1073/pnas.0507937102.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 18602-18607
    • Divakaruni, A.V.1    Loo, R.R.2    Xie, Y.3    Loo, J.A.4    Gober, J.W.5
  • 18
    • 0037096832 scopus 로고    scopus 로고
    • Strong aggregation and increased toxicity of polyleucine over polyglutamine stretches in mammalian cells
    • Dorsman, J. C., Pepers, B., Langenberg, D., Kerkdijk, H., Ijszenga, M., den Dunnen, J. T., et al. (2002). Strong aggregation and increased toxicity of polyleucine over polyglutamine stretches in mammalian cells. Hum. Mol. Genet. 11, 1487-1496. doi: 10.1093/hmg/11.13.1487.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 1487-1496
    • Dorsman, J.C.1    Pepers, B.2    Langenberg, D.3    Kerkdijk, H.4    Ijszenga, M.5    den Dunnen, J.T.6
  • 19
    • 41349087784 scopus 로고    scopus 로고
    • Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae
    • Du, Z., Park, K. K.-W., Yu, H., Fan, Q., and Li, L. (2008). Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nat. Genet. 40, 460-465. doi: 10.1038/ng.112.
    • (2008) Nat. Genet , vol.40 , pp. 460-465
    • Du, Z.1    Park, K.K.-W.2    Yu, H.3    Fan, Q.4    Li, L.5
  • 20
    • 79959887638 scopus 로고    scopus 로고
    • A diversity of assembly mechanisms of a generic amyloid fold
    • Eichner, T., and Radford, S. E. (2011). A diversity of assembly mechanisms of a generic amyloid fold. Mol. Cell. 43, 8-18. doi: 10.1016/j.molcel.2011.05.012.
    • (2011) Mol. Cell , vol.43 , pp. 8-18
    • Eichner, T.1    Radford, S.E.2
  • 21
    • 84862610982 scopus 로고    scopus 로고
    • Yeast prions form infectious amyloid inclusion bodies in bacteria
    • Espargaró, A., Villar-Piqué, A., Sabaté, R., and Ventura, S. (2012). Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb. Cell Fact. 11, 89-89. doi: 10.1186/1475-2859-11-89.
    • (2012) Microb. Cell Fact , vol.11 , pp. 89-89
    • Espargaró, A.1    Villar-Piqué, A.2    Sabaté, R.3    Ventura, S.4
  • 22
    • 84905169854 scopus 로고    scopus 로고
    • Botulism outbreaks in natural environments-an update
    • Espelund, M., and Klaveness, D. (2014). Botulism outbreaks in natural environments-an update. Front. Microbiol. 5:287. doi: 10.3389/fmicb.2014.00287.
    • (2014) Front. Microbiol , vol.5 , pp. 287
    • Espelund, M.1    Klaveness, D.2
  • 23
    • 84896720208 scopus 로고    scopus 로고
    • PrionScan: an online database of predicted prion domains in complete proteomes
    • Espinosa Angarica, V., Angulo, A., Giner, A., Losilla, G., Ventura, S., and Sancho, J. (2014). PrionScan: an online database of predicted prion domains in complete proteomes. BMC Genomics 15:102. doi: 10.1186/1471-2164-15-102.
    • (2014) BMC Genomics , vol.15 , pp. 102
    • Espinosa Angarica, V.1    Angulo, A.2    Giner, A.3    Losilla, G.4    Ventura, S.5    Sancho, J.6
  • 24
    • 84877834389 scopus 로고    scopus 로고
    • Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains
    • Espinosa Angarica, V., Ventura, S., and Sancho, J. (2013). Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains. BMC Genomics 14:316. doi: 10.1186/1471-2164-14-316.
    • (2013) BMC Genomics , vol.14 , pp. 316
    • Espinosa Angarica, V.1    Ventura, S.2    Sancho, J.3
  • 25
    • 28044457195 scopus 로고    scopus 로고
    • The amyloid stretch hypothesis: recruiting proteins toward the dark side
    • Esteras-Chopo, A., Serrano, L., and López de la Paz, M. (2005). The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc. Natl. Acad. Sci. U.S.A. 102, 16672-16677. doi: 10.1073/pnas.0505905102.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 16672-16677
    • Esteras-Chopo, A.1    Serrano, L.2    López de la Paz, M.3
  • 26
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich, M., and Dobson, C. M. (2002). The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21, 5682-5690. doi: 10.1093/emboj/cdf573.
    • (2002) EMBO J , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 27
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla, A.-M., Rousseau, F., Schymkowitz, J., and Serrano, L. (2004). Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 22, 1302-1306. doi: 10.1038/nbt1012.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 28
    • 34247899121 scopus 로고    scopus 로고
    • Functional amyloid-from bacteria to humans
    • Fowler, D. M., Koulov, A. V., Balch, W. E., and Kelly, J. W. (2007). Functional amyloid-from bacteria to humans. Trends Biochem. Sci. 32, 217-224. doi: 10.1016/j.tibs.2007.03.003.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 217-224
    • Fowler, D.M.1    Koulov, A.V.2    Balch, W.E.3    Kelly, J.W.4
  • 29
    • 84877324483 scopus 로고    scopus 로고
    • Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases
    • Furukawa, Y., and Nukina, N. (2013). Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases. Biochim. Biophys. Acta 1832, 1271-1278. doi: 10.1016/j.bbadis.2013.04.011.
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 1271-1278
    • Furukawa, Y.1    Nukina, N.2
  • 30
    • 82655180384 scopus 로고    scopus 로고
    • Fuzziness: linking regulation to protein dynamics
    • Fuxreiter, M. (2012). Fuzziness: linking regulation to protein dynamics. Mol. BioSyst. 8, 168-177. doi: 10.1039/c1mb05234a.
    • (2012) Mol. BioSyst , vol.8 , pp. 168-177
    • Fuxreiter, M.1
  • 31
    • 77949532822 scopus 로고    scopus 로고
    • FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence
    • Garbuzynskiy, S. O., Lobanov, M. Y., and Galzitskaya, O. V. (2010). FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence. Bioinformatics 26, 326-332. doi: 10.1093/bioinformatics/btp691.
    • (2010) Bioinformatics , vol.26 , pp. 326-332
    • Garbuzynskiy, S.O.1    Lobanov, M.Y.2    Galzitskaya, O.V.3
  • 33
    • 0027250342 scopus 로고
    • A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho
    • Geiselmann, J., Wang, Y., Seifried, S. E., and von Hippel, P. H. (1993). A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho. Proc. Natl. Acad. Sci. U.S.A. 90, 7754-7758. doi: 10.1073/pnas.90.16.7754.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 7754-7758
    • Geiselmann, J.1    Wang, Y.2    Seifried, S.E.3    von Hippel, P.H.4
  • 35
    • 84898605418 scopus 로고    scopus 로고
    • N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case
    • Graña-Montes, R., Marinelli, P., Reverter, D., and Ventura, S. (2014). N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case. Biomacromolecules 15, 1194-1203. doi: 10.1021/bm401776z.
    • (2014) Biomacromolecules , vol.15 , pp. 1194-1203
    • Graña-Montes, R.1    Marinelli, P.2    Reverter, D.3    Ventura, S.4
  • 36
    • 79958008649 scopus 로고    scopus 로고
    • The stb operon balances the requirements for vegetative stability and conjugative transfer of plasmid R388
    • Guynet, C., Cuevas, A., Moncalián, G., and de la Cruz, F. (2011). The stb operon balances the requirements for vegetative stability and conjugative transfer of plasmid R388. PLoS Genet. 7:e1002073. doi: 10.1371/journal.pgen.1002073.
    • (2011) PLoS Genet , vol.7
    • Guynet, C.1    Cuevas, A.2    Moncalián, G.3    de la Cruz, F.4
  • 37
    • 79959882243 scopus 로고    scopus 로고
    • Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins
    • Halfmann, R., Alberti, S., Krishnan, R., Lyle, N., O'Donnell, C. W., King, O. D., et al. (2011). Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Mol. Cell 43, 72-84. doi: 10.1016/j.molcel.2011.05.013.
    • (2011) Mol. Cell , vol.43 , pp. 72-84
    • Halfmann, R.1    Alberti, S.2    Krishnan, R.3    Lyle, N.4    O'Donnell, C.W.5    King, O.D.6
  • 38
    • 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., and Gerstein, M. (2003). 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, R40-R40. doi: 10.1186/gb-2003-4-6-r40.
    • (2003) Genome Biol , vol.4 , pp. R40-R40
    • Harrison, P.M.1    Gerstein, M.2
  • 39
    • 79952578947 scopus 로고    scopus 로고
    • Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB)
    • Heinrich, S. U., and Lindquist, S. (2011). Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB). Proc. Natl. Acad. Sci. U.S.A. 108, 2999-3004. doi: 10.1073/pnas.1019368108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 2999-3004
    • Heinrich, S.U.1    Lindquist, S.2
  • 40
    • 34047157022 scopus 로고    scopus 로고
    • Hydrophobic cooperativity as a mechanism for amyloid nucleation
    • Hills, R. D., and Brooks, C. L. (2007). Hydrophobic cooperativity as a mechanism for amyloid nucleation. J. Mol. Biol. 368, 894-901. doi: 10.1016/j.jmb.2007.02.043.
    • (2007) J. Mol. Biol , vol.368 , pp. 894-901
    • Hills, R.D.1    Brooks, C.L.2
  • 41
    • 84940541696 scopus 로고    scopus 로고
    • The phenotypic signature of adaptation to thermal stress in Escherichia coli
    • Hug, S. M., and Gaut, B. S. (2015). The phenotypic signature of adaptation to thermal stress in Escherichia coli. BMC Evol. Biol. 15:177. doi: 10.1186/s12862-015-0457-3.
    • (2015) BMC Evol. Biol , vol.15 , pp. 177
    • Hug, S.M.1    Gaut, B.S.2
  • 42
    • 84946827128 scopus 로고    scopus 로고
    • Computational analysis of candidate prion-like proteins in bacteria and their role
    • Iglesias, V., de Groot, N. S., and Ventura, S. (2015). Computational analysis of candidate prion-like proteins in bacteria and their role. Front. Microbiol. 6:1123. doi: 10.3389/fmicb.2015.01123.
    • (2015) Front. Microbiol , vol.6 , pp. 1123
    • Iglesias, V.1    de Groot, N.S.2    Ventura, S.3
  • 43
    • 0027006436 scopus 로고
    • Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB
    • Jarrett, J. T., and Lansbury, P. T. (1992). Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry 31, 12345-12352. doi: 10.1021/bi00164a008.
    • (1992) Biochemistry , vol.31 , pp. 12345-12352
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 44
    • 84875605133 scopus 로고    scopus 로고
    • Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
    • Kim, H. J., Kim, N. C., Wang, Y. D., Scarborough, E. A., Moore, J., Diaz, Z., et al. (2013). Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 495, 467-473. doi: 10.1038/nature11922.
    • (2013) Nature , vol.495 , pp. 467-473
    • Kim, H.J.1    Kim, N.C.2    Wang, Y.D.3    Scarborough, E.A.4    Moore, J.5    Diaz, Z.6
  • 45
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King, O. D., Gitler, A. D., and Shorter, J. (2012). The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res. 1462, 61-80. doi: 10.1016/j.brainres.2012.01.016.
    • (2012) Brain Res , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 46
    • 0024352110 scopus 로고
    • Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk, W. E., Pettegrew, J. W., and Abraham, D. J. (1989). Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 37, 1273-1281. doi: 10.1177/37.8.2666510.
    • (1989) J. Histochem. Cytochem , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 47
    • 84871946865 scopus 로고    scopus 로고
    • Rho-dependent transcription termination is essential to prevent excessive genome-wide R-loops in Escherichia coli
    • Krishna Leela, J., Syeda, A. H., Anupama, K., and Gowrishankar, J. (2013). Rho-dependent transcription termination is essential to prevent excessive genome-wide R-loops in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 110, 258-263. doi: 10.1073/pnas.1213123110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 258-263
    • Krishna Leela, J.1    Syeda, A.H.2    Anupama, K.3    Gowrishankar, J.4
  • 48
    • 58549116147 scopus 로고    scopus 로고
    • Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation
    • Kumaran, D., Eswaramoorthy, S., Furey, W., Navaza, J., Sax, M., and Swaminathan, S. (2009). Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation. J. Mol. Biol. 386, 233-245. doi: 10.1016/j.jmb.2008.12.027.
    • (2009) J. Mol. Biol , vol.386 , pp. 233-245
    • Kumaran, D.1    Eswaramoorthy, S.2    Furey, W.3    Navaza, J.4    Sax, M.5    Swaminathan, S.6
  • 49
    • 84907029459 scopus 로고    scopus 로고
    • PLAAC: a web and command-line application to identify proteins with Prion-Like Amino Acid Composition
    • Lancaster, A. K., Nutter-Upham, A., Lindquist, S., and King, O. D. (2014). PLAAC: a web and command-line application to identify proteins with Prion-Like Amino Acid Composition. Bioinformatics 30, 2-3. doi: 10.1093/bioinformatics/btu310.
    • (2014) Bioinformatics , vol.30 , pp. 2-3
    • Lancaster, A.K.1    Nutter-Upham, A.2    Lindquist, S.3    King, O.D.4
  • 50
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine, H. (1993). Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2, 404-410. doi: 10.1002/pro.5560020312.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine, H.1
  • 51
    • 84961287878 scopus 로고    scopus 로고
    • Distinct amino acid compositional requirements for formation and maintenance of the [\n PSI\n +\n] Prion in Yeast
    • MacLea, K. S., Paul, K. R., Ben-Musa, Z., Waechter, A., Shattuck, J. E., Gruca, M., et al. (2015). Distinct amino acid compositional requirements for formation and maintenance of the [\n PSI\n +\n] Prion in Yeast. Mol. Cell. Biol. 35, 899-911. doi: 10.1128/MCB.01020-14.
    • (2015) Mol. Cell. Biol , vol.35 , pp. 899-911
    • MacLea, K.S.1    Paul, K.R.2    Ben-Musa, Z.3    Waechter, A.4    Shattuck, J.E.5    Gruca, M.6
  • 52
    • 34250305970 scopus 로고    scopus 로고
    • Specificity of L, D-transpeptidases from gram-positive bacteria producing different peptidoglycan chemotypes
    • Magnet, S., Arbeloa, A., Mainardi, J. L., Hugonnet, J. E., Fourgeaud, M., Dubost, L., et al. (2007). Specificity of L, D-transpeptidases from gram-positive bacteria producing different peptidoglycan chemotypes. J. Biol. Chem. 282, 13151-13159. doi: 10.1074/jbc. M610911200.
    • (2007) J. Biol. Chem , vol.282 , pp. 13151-13159
    • Magnet, S.1    Arbeloa, A.2    Mainardi, J.L.3    Hugonnet, J.E.4    Fourgeaud, M.5    Dubost, L.6
  • 53
    • 67650809307 scopus 로고    scopus 로고
    • Functional amyloids as natural storage of peptide hormones in pituitary secretory granules
    • Maji, S. K., Perrin, M. H., Sawaya, M. R., Jessberger, S., Vadodaria, K., Rissman, R. A., et al. (2009). Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325, 328-332. doi: 10.1126/science.1173155.
    • (2009) Science , vol.325 , pp. 328-332
    • Maji, S.K.1    Perrin, M.H.2    Sawaya, M.R.3    Jessberger, S.4    Vadodaria, K.5    Rissman, R.A.6
  • 54
    • 84862776939 scopus 로고    scopus 로고
    • Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memory
    • Majumdar, A., Cesario, W. C., White-Grindley, E., Jiang, H., Ren, F., Khan, M. R., et al. (2012). Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memory. Cell 148, 515-529. doi: 10.1016/j.cell.2012.01.004.
    • (2012) Cell , vol.148 , pp. 515-529
    • Majumdar, A.1    Cesario, W.C.2    White-Grindley, E.3    Jiang, H.4    Ren, F.5    Khan, M.R.6
  • 55
    • 84876288161 scopus 로고    scopus 로고
    • Protein disorder, prion propensities, and self-organizing macromolecular collectives
    • Malinovska, L., Kroschwald, S., and Alberti, S. (2013). Protein disorder, prion propensities, and self-organizing macromolecular collectives. Biochim. Biophys. Acta 1834, 918-931. doi: 10.1016/j.bbapap.2013.01.003.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 918-931
    • Malinovska, L.1    Kroschwald, S.2    Alberti, S.3
  • 56
    • 0141499226 scopus 로고    scopus 로고
    • The role of alpha-synuclein in Parkinson's disease: insights from animal models
    • Maries, E., Dass, B., Collier, T. J., Kordower, J. H., and Steece-Collier, K. (2003). The role of alpha-synuclein in Parkinson's disease: insights from animal models. Nat. Rev. Neurosci. 4, 727-738. doi: 10.1038/nrn1199.
    • (2003) Nat. Rev. Neurosci , vol.4 , pp. 727-738
    • Maries, E.1    Dass, B.2    Collier, T.J.3    Kordower, J.H.4    Steece-Collier, K.5
  • 57
    • 84883433978 scopus 로고    scopus 로고
    • Transcription termination controls prophage maintenance in Escherichia coli genomes
    • Menouni, R., Champ, S., Espinosa, L., Boudvillain, M., and Ansaldi, M. (2013). Transcription termination controls prophage maintenance in Escherichia coli genomes. Proc. Natl. Acad. Sci. U.S.A. 110, 14414-14419. doi: 10.1073/pnas.1303400110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 14414-14419
    • Menouni, R.1    Champ, S.2    Espinosa, L.3    Boudvillain, M.4    Ansaldi, M.5
  • 58
    • 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., and Weissman, J. S. (2000). 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, 11910-11915. doi: 10.1073/pnas.97.22.11910.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 59
    • 84936864678 scopus 로고    scopus 로고
    • The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria
    • Navarro, S., Marinelli, P., Diaz-Caballero, M., and Ventura, S. (2015). The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria. Microb. Cell Fact. 14, 102-102. doi: 10.1186/s12934-015-0284-7.
    • (2015) Microb. Cell Fact , vol.14 , pp. 102-102
    • Navarro, S.1    Marinelli, P.2    Diaz-Caballero, M.3    Ventura, S.4
  • 60
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-beta spine of amyloid-like fibrils
    • Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., et al. (2005). Structure of the cross-beta spine of amyloid-like fibrils. Nature 435, 773-778. doi: 10.1038/nature03680.
    • (2005) Nature , vol.435 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.Ø.4    Riekel, C.5    Grothe, R.6
  • 61
    • 84878136082 scopus 로고    scopus 로고
    • Blessings in disguise: biological benefits of prion-like mechanisms
    • Newby, G. A., and Lindquist, S. (2013). Blessings in disguise: biological benefits of prion-like mechanisms. Trends Cell Biol. 23, 251-259. doi: 10.1016/j.tcb.2013.01.007.
    • (2013) Trends Cell Biol , vol.23 , pp. 251-259
    • Newby, G.A.1    Lindquist, S.2
  • 62
    • 51649129503 scopus 로고    scopus 로고
    • Hacking the code of amyloid formation: the amyloid stretch hypothesis
    • Pastor, M. T., Esteras-Chopo, A., and Serrano, L. (2007). Hacking the code of amyloid formation: the amyloid stretch hypothesis. Prion 1, 9-14. doi: 10.4161/pri.1.1.4100.
    • (2007) Prion , vol.1 , pp. 9-14
    • Pastor, M.T.1    Esteras-Chopo, A.2    Serrano, L.3
  • 63
    • 61849091420 scopus 로고    scopus 로고
    • The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion
    • Patel, B. K., Gavin-Smyth, J., and Liebman, S. W. (2009). The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nat. Cell Biol. 11, 344-349. doi: 10.1038/ncb1843.
    • (2009) Nat. Cell Biol , vol.11 , pp. 344-349
    • Patel, B.K.1    Gavin-Smyth, J.2    Liebman, S.W.3
  • 64
    • 24044515001 scopus 로고    scopus 로고
    • FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded
    • Prilusky, J., Felder, C. E., Zeev-Ben-Mordehai, T., Rydberg, E. H., Man, O., and Beckmann, J. S. (2005). FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 21, 3435-3438. doi: 10.1093/bioinformatics/bti537.
    • (2005) Bioinformatics , vol.21 , pp. 3435-3438
    • Prilusky, J.1    Felder, C.E.2    Zeev-Ben-Mordehai, T.3    Rydberg, E.H.4    Man, O.5    Beckmann, J.S.6
  • 65
    • 0025318262 scopus 로고
    • Rho-dependent transcription termination
    • Richardson, J. P. (1990). Rho-dependent transcription termination. Biochim. Biophys. Acta 1048, 127-138. doi: 10.1016/0167-4781(90)90048-7.
    • (1990) Biochim. Biophys. Acta , vol.1048 , pp. 127-138
    • Richardson, J.P.1
  • 66
    • 0030053611 scopus 로고    scopus 로고
    • Structural organization of transcription termination factor Rho
    • Richardson, J. P. (1996). Structural organization of transcription termination factor Rho. J. Biol. Chem. 271, 1251-1254. doi: 10.1074/jbc.271.3.1251.
    • (1996) J. Biol. Chem , vol.271 , pp. 1251-1254
    • Richardson, J.P.1
  • 68
    • 77953767980 scopus 로고    scopus 로고
    • Non-Mendelian determinant [ISP+] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1
    • Rogoza, T., Goginashvili, A., Rodionova, S., Ivanov, M., Viktorovskaya, O., Rubel, A., et al. (2010). Non-Mendelian determinant [ISP+] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1. Proc. Natl. Acad. Sci. U.S.A. 107, 10573-10577. doi: 10.1073/pnas.1005949107.
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 10573-10577
    • Rogoza, T.1    Goginashvili, A.2    Rodionova, S.3    Ivanov, M.4    Viktorovskaya, O.5    Rubel, A.6
  • 69
    • 84907247168 scopus 로고    scopus 로고
    • Functional amyloids in bacteria
    • Romero, D., and Kolter, R. (2014). Functional amyloids in bacteria. Int. Microbiol. 17, 65-73. doi: 10.2436/20.1501.01.208.
    • (2014) Int. Microbiol , vol.17 , pp. 65-73
    • Romero, D.1    Kolter, R.2
  • 70
    • 84904510042 scopus 로고    scopus 로고
    • Botulinum neurotoxins: genetic, structural and mechanistic insights
    • Rossetto, O., Pirazzini, M., and Montecucco, C. (2014). Botulinum neurotoxins: genetic, structural and mechanistic insights. Nat. Rev. Microbiol. 12, 535-549. doi: 10.1038/nrmicro3295.
    • (2014) Nat. Rev. Microbiol , vol.12 , pp. 535-549
    • Rossetto, O.1    Pirazzini, M.2    Montecucco, C.3
  • 71
    • 84862141774 scopus 로고    scopus 로고
    • Native structure protects SUMO proteins from aggregation into amyloid fibrils
    • Sabate, R., Espargaro, A., Graña-Montes, R., Reverter, D., and Ventura, S. (2012). Native structure protects SUMO proteins from aggregation into amyloid fibrils. Biomacromolecules 13, 1916-1926. doi: 10.1021/bm3004385.
    • (2012) Biomacromolecules , vol.13 , pp. 1916-1926
    • Sabate, R.1    Espargaro, A.2    Graña-Montes, R.3    Reverter, D.4    Ventura, S.5
  • 72
    • 71149094496 scopus 로고    scopus 로고
    • Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion
    • Sabaté, R., Espargaró, A., Saupe, S. J., and Ventura, S. (2009). Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion. Microb. Cell Fact. 8, 56-56. doi: 10.1186/1475-2859-8-56.
    • (2009) Microb. Cell Fact , vol.8 , pp. 56-56
    • Sabaté, R.1    Espargaró, A.2    Saupe, S.J.3    Ventura, S.4
  • 73
    • 84878642986 scopus 로고    scopus 로고
    • Thioflavin-T excimer formation upon interaction with amyloid fibers
    • Sabate, R., Rodriguez-Santiago, L., Sodupe, M., Saupe, S. J., and Ventura, S. (2013). Thioflavin-T excimer formation upon interaction with amyloid fibers. Chem. Commun. 49, 5745-5745. doi: 10.1039/c3cc42040j.
    • (2013) Chem. Commun , vol.49 , pp. 5745-5745
    • Sabate, R.1    Rodriguez-Santiago, L.2    Sodupe, M.3    Saupe, S.J.4    Ventura, S.5
  • 77
    • 84866403056 scopus 로고    scopus 로고
    • Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression
    • Santner, A. A., Croy, C. H., Vasanwala, F. H., Uversky, V. N., Van, Y. Y., and Dunker, A. K. (2012). Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression. Biochemistry 51, 7250-7262. doi: 10.1021/bi300653m.
    • (2012) Biochemistry , vol.51 , pp. 7250-7262
    • Santner, A.A.1    Croy, C.H.2    Vasanwala, F.H.3    Uversky, V.N.4    Van, Y.Y.5    Dunker, A.K.6
  • 78
    • 84947276177 scopus 로고    scopus 로고
    • Prions: what are they good for?
    • Si, K. (2015). Prions: what are they good for? Annu. Rev. Cell Dev. Biol. 31, 149-169. doi: 10.1146/annurev-cellbio-100913-013409.
    • (2015) Annu. Rev. Cell Dev. Biol , vol.31 , pp. 149-169
    • Si, K.1
  • 79
    • 84907478561 scopus 로고    scopus 로고
    • Plasmidome interchange between Clostridium botulinum, Clostridium novyi and Clostridium haemolyticum converts strains of independent lineages into distinctly different pathogens
    • Skarin, H., and Segerman, B. (2014). Plasmidome interchange between Clostridium botulinum, Clostridium novyi and Clostridium haemolyticum converts strains of independent lineages into distinctly different pathogens. PLoS ONE 9:e107777. doi: 10.1371/journal.pone.0107777.
    • (2014) PLoS ONE , vol.9
    • Skarin, H.1    Segerman, B.2
  • 81
    • 84908584357 scopus 로고    scopus 로고
    • Functional dissection of the Clostridium botulinum type B hemagglutinin complex: identification of the carbohydrate and E-cadherin binding sites
    • Sugawara, Y., Yutani, M., Amatsu, S., Matsumura, T., and Fujinaga, Y. (2014). Functional dissection of the Clostridium botulinum type B hemagglutinin complex: identification of the carbohydrate and E-cadherin binding sites. PLoS ONE 9:e111170. doi: 10.1371/journal.pone.0111170.
    • (2014) PLoS ONE , vol.9
    • Sugawara, Y.1    Yutani, M.2    Amatsu, S.3    Matsumura, T.4    Fujinaga, Y.5
  • 82
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • Swaminathan, S., and Eswaramoorthy, S. (2000). Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat. Struct. Biol. 7, 693-699. doi: 10.1186/1741-7015-7-14.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 83
    • 84878369223 scopus 로고    scopus 로고
    • Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior
    • Tariq, M., Wegrzyn, R., Anwar, S., Bukau, B., and Paro, R. (2013). Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior. BMC Genomics 14:374. doi: 10.1186/1471-2164-14-374.
    • (2013) BMC Genomics , vol.14 , pp. 374
    • Tariq, M.1    Wegrzyn, R.2    Anwar, S.3    Bukau, B.4    Paro, R.5
  • 84
    • 84949058405 scopus 로고    scopus 로고
    • MreC and MreD proteins are not required for growth of Staphylococcus aureus
    • Tavares, A. C., Fernandes, P. B., Carballido-Lopez, R., and Pinho, M. G. (2015). MreC and MreD proteins are not required for growth of Staphylococcus aureus. PLoS ONE 10:e0140523. doi: 10.1371/journal.pone.0140523.
    • (2015) PLoS ONE , vol.10
    • Tavares, A.C.1    Fernandes, P.B.2    Carballido-Lopez, R.3    Pinho, M.G.4
  • 86
    • 73549115633 scopus 로고    scopus 로고
    • Compositional determinants of prion formation in yeast
    • Toombs, J. A., McCarty, B. R., and Ross, E. D. (2010). Compositional determinants of prion formation in yeast. Mol. Cell. Biol. 30, 319-332. doi: 10.1128/MCB.01140-09.
    • (2010) Mol. Cell. Biol , vol.30 , pp. 319-332
    • Toombs, J.A.1    McCarty, B.R.2    Ross, E.D.3
  • 88
    • 84878899241 scopus 로고    scopus 로고
    • The most important thing is the tail: multitudinous functionalities of intrinsically disordered protein termini
    • Uversky, V. N. (2013). The most important thing is the tail: multitudinous functionalities of intrinsically disordered protein termini. FEBS Lett. 587, 1891-1901. doi: 10.1016/j.febslet.2013.04.042.
    • (2013) FEBS Lett , vol.587 , pp. 1891-1901
    • Uversky, V.N.1
  • 89
    • 84926374330 scopus 로고    scopus 로고
    • Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders
    • Uversky, V. N. (2015). Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders. Front. Aging Neurosci. 7:18. doi: 10.3389/fnagi.2015.00018.
    • (2015) Front. Aging Neurosci , vol.7 , pp. 18
    • Uversky, V.N.1
  • 90
    • 33747799315 scopus 로고    scopus 로고
    • Dynamic nuclear polarization of amyloidogenic peptide nanocrystals
    • van Der Wel, P. C., Hu, K. N., Lewandowski, J., and Griffin, R. G. (2006). Dynamic nuclear polarization of amyloidogenic peptide nanocrystals. J. Am. Chem. Soc. 128, 10840-10846. doi: 10.1021/ja0626685.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10840-10846
    • van Der Wel, P.C.1    Hu, K.N.2    Lewandowski, J.3    Griffin, R.G.4
  • 91
    • 2442553006 scopus 로고    scopus 로고
    • Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case
    • Ventura, S., Zurdo, J., Narayanan, S., Parreño, M., Mangues, R., Reif, B., et al. (2004). Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. Proc. Natl. Acad. Sci. U.S.A. 101, 7258-7263. doi: 10.1073/pnas.0308249101.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 7258-7263
    • Ventura, S.1    Zurdo, J.2    Narayanan, S.3    Parreño, M.4    Mangues, R.5    Reif, B.6
  • 92
    • 79551674938 scopus 로고    scopus 로고
    • Transcription termination maintains chromosome integrity
    • Washburn, R. S., and Gottesman, M. E. (2011). Transcription termination maintains chromosome integrity. Proc. Natl. Acad. Sci. U.S.A. 108, 792-797. doi: 10.1073/pnas.1009564108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 792-797
    • Washburn, R.S.1    Gottesman, M.E.2
  • 93
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner, R. B. (1994). [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264, 566-569. doi: 10.1126/science.7909170.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 95
    • 0025896984 scopus 로고
    • A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences
    • Wren, B. W. (1991). A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Mol. Microbiol. 5, 797-803. doi: 10.1111/j.1365-2958.1991.tb00752.x.
    • (1991) Mol. Microbiol , vol.5 , pp. 797-803
    • Wren, B.W.1
  • 96
    • 84934290549 scopus 로고    scopus 로고
    • Prion propagation can occur in a prokaryote and requires the ClpB chaperone
    • Yuan, A. H., Garrity, S. J., Nako, E., and Hochschild, A. (2014). Prion propagation can occur in a prokaryote and requires the ClpB chaperone. eLife 3, 1-19. doi: 10.7554/eLife.02949.
    • (2014) eLife , vol.3 , pp. 1-19
    • Yuan, A.H.1    Garrity, S.J.2    Nako, E.3    Hochschild, A.4
  • 97
    • 84964334339 scopus 로고    scopus 로고
    • PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores
    • Zambrano, R., O'Conchillo-Sole, Iglesias, V., Illa, R., Rousseau, F., and Schymkowitz, J. (2015). PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores. Nucleic Acids Res. 43, W331-W337. doi: 10.1093/nar/gkv490.
    • (2015) Nucleic Acids Res , vol.43 , pp. W331-W337
    • Zambrano, R.1    O'Conchillo-Sole Iglesias, V.2    Illa, R.3    Rousseau, F.4    Schymkowitz, J.5
  • 98
    • 33751170680 scopus 로고    scopus 로고
    • Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure
    • Zheng, J., Ma, B., and Nussinov, R. (2006). Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Phys. Biol. 3, 1-1. doi: 10.1088/1478-3975/3/3/P01.
    • (2006) Phys. Biol , vol.3 , pp. 1-1
    • Zheng, J.1    Ma, B.2    Nussinov, R.3
  • 99
    • 84867430805 scopus 로고    scopus 로고
    • Promiscuous cross-seeding between bacterial amyloids promotes interspecies biofilms
    • Zhou, Y., Smith, D., Leong, B. J., Brännström, K., Almqvist, F., and Chapman, M. R. (2012). Promiscuous cross-seeding between bacterial amyloids promotes interspecies biofilms. J. Biol. Chem. 287, 35092-35103. doi: 10.1074/jbc. M112.383737.
    • (2012) J. Biol. Chem , vol.287 , pp. 35092-35103
    • Zhou, Y.1    Smith, D.2    Leong, B.J.3    Brännström, K.4    Almqvist, F.5    Chapman, M.R.6
  • 100
    • 0032938366 scopus 로고    scopus 로고
    • Assembly requirements and role of CotH during spore coat formation in Bacillus subtilis
    • Zilhao, R., Naclerio, G., Henriques, A. O., Baccigalupi, L., Moran, C. P., and Ricca, E. (1999). Assembly requirements and role of CotH during spore coat formation in Bacillus subtilis. J. Bacteriol. 181, 2631-2633.
    • (1999) J. Bacteriol , vol.181 , pp. 2631-2633
    • Zilhao, R.1    Naclerio, G.2    Henriques, A.O.3    Baccigalupi, L.4    Moran, C.P.5    Ricca, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.