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Volumn 50, Issue 27, 2011, Pages 5971-5978

Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure

Author keywords

[No Author keywords available]

Indexed keywords

ALBICANS; CANDIDA ALBICANS; CANDIDA GLABRATA; CEREVISIAE; N-TERMINAL DOMAINS; N-TERMINALS; S.CEREVISIAE; SHEET STRUCTURE; SOLID-STATE NUCLEAR MAGNETIC RESONANCE;

EID: 79960007397     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200142x     Document Type: Article
Times cited : (14)

References (64)
  • 1
    • 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 S. cerevisiae Science 264, 566-569 (Pubitemid 24185861)
    • (1994) Science , vol.264 , Issue.5158 , pp. 566-569
    • Wickner, R.B.1
  • 2
    • 0030833388 scopus 로고    scopus 로고
    • +] prion in Saccharomyces cerevisiae
    • Derkatch, I. L., Bradley, M. E., Zhou, P., Chernoff, Y. O., and Liebman, S. W. (1997) Genetic and environmental factors affecting the de novo appearance of the [ PSI +] prion in Saccharomyces cerevisiae Genetics 147, 507-519 (Pubitemid 27418562)
    • (1997) Genetics , vol.147 , Issue.2 , pp. 507-519
    • Derkatch, I.L.1    Bradley, M.E.2    Zhou, P.3    Chernoff, Y.O.4    Liebman, S.W.5
  • 3
    • 0035958585 scopus 로고    scopus 로고
    • +]
    • DOI 10.1016/S0092-8674(01)00427-5
    • Derkatch, I. L., Bradley, M. E., Hong, J. Y., and Liebman, S. W. (2001) Prions affect the appearance of other prions: The story of [PIN] Cell 106, 171-182 (Pubitemid 32772628)
    • (2001) Cell , vol.106 , Issue.2 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 4
    • 41349087784 scopus 로고    scopus 로고
    • Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae
    • DOI 10.1038/ng.112, PII NG112
    • Du, Z., Park, 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 (Pubitemid 351450881)
    • (2008) Nature Genetics , vol.40 , Issue.4 , pp. 460-465
    • Du, Z.1    Park, K.-W.2    Yu, H.3    Fan, Q.4    Li, L.5
  • 5
    • 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
    • (2009) Nat. Cell Biol. , vol.11 , pp. 344-349
    • Patel, B.K.1    Gavin-Smyth, J.2    Liebman, S.W.3
  • 6
    • 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
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 8
    • 0028859540 scopus 로고
    • Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
    • Masison, D. C. and Wickner, R. B. (1995) Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells Science 270, 93-95
    • (1995) Science , vol.270 , pp. 93-95
    • Masison, D.C.1    Wickner, R.B.2
  • 9
    • 0028200770 scopus 로고
    • +] in the yeast Saccharomyces cerevisiae
    • TerAvanesyan, A., Dagkesamanskaya, A. R., Kushnirov, V. V., and Smirnov, V. N. (1994) The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae Genetics 137, 671-676 (Pubitemid 24196460)
    • (1994) Genetics , vol.137 , Issue.3 , pp. 671-676
    • Ter-Avanesyan, M.D.1    Dagkesamanskaya, A.R.2    Kushnirov, V.V.3    Smirnov, V.N.4
  • 10
    • 0037058949 scopus 로고    scopus 로고
    • Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein
    • DOI 10.1073/pnas.162349599
    • Edskes, H. K. and Wickner, R. B. (2002) Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein Proc. Natl. Acad. Sci. U.S.A. 99 (Suppl. 4) 16384-16391 (Pubitemid 35470983)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.SUPPL. 4 , pp. 16384-16391
    • Edskes, H.K.1    Wickner, R.B.2
  • 12
    • 26444520003 scopus 로고    scopus 로고
    • The [URE3] prion is not conserved among Saccharomyces species
    • Talarek, N., Maillet, L., Cullin, C., and Aigle, M. (2005) The [URE3] prion is not conserved among Saccharomyces species Genetics 171, 23-54
    • (2005) Genetics , vol.171 , pp. 23-54
    • Talarek, N.1    Maillet, L.2    Cullin, C.3    Aigle, M.4
  • 13
    • 62549130374 scopus 로고    scopus 로고
    • Prion variants and species barriers among Saccharomyces Ure2 proteins
    • Edskes, H. K., McCann, L. M., Hebert, A. M., and Wickner, R. B. (2009) Prion variants and species barriers among Saccharomyces Ure2 proteins Genetics 181, 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
  • 14
    • 78651492351 scopus 로고    scopus 로고
    • Yeast prions: Could they be exaptations? the URE2/ [URE3] system in Kluyveromyces lactis
    • Safadi, R. A., Talarek, N., Jacques, N., and Aigle, M. (2011) Yeast prions: could they be exaptations? The URE2/ [URE3] system in Kluyveromyces lactis FEMS Yeast Res. 11, 151-153
    • (2011) FEMS Yeast Res. , vol.11 , pp. 151-153
    • Safadi, R.A.1    Talarek, N.2    Jacques, N.3    Aigle, M.4
  • 15
    • 0141866883 scopus 로고    scopus 로고
    • Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation
    • DOI 10.1074/jbc.C300300200
    • Hosoda, N., Kobayashii, T., Uchida, N., Funakoshi, Y., Kikuchi, Y., Hoshino, S., and Katada, T. (2003) Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation J. Biol. Chem. 278, 38287-38291 (Pubitemid 37221719)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 38287-38291
    • Hosoda, N.1    Kobayashi, T.2    Uchida, N.3    Funakoshi, Y.4    Kikuchi, Y.5    Hoshino, S.6    Katada, T.7
  • 16
    • 0033962765 scopus 로고    scopus 로고
    • Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein
    • DOI 10.1046/j.1365-2958.2000.01761.x
    • Chernoff, Y. O., Galkin, A. P., Lewitin, E., Chernova, T. A., Newnam, G. P., and Belenkiy, S. M. (2000) Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein Mol. Microbiol. 35, 865-876 (Pubitemid 30107537)
    • (2000) Molecular Microbiology , vol.35 , Issue.4 , pp. 865-876
    • Chernoff, Y.O.1    Galkin, A.P.2    Lewitin, E.3    Chernova, T.A.4    Newnam, G.P.5    Belenkiy, S.M.6
  • 18
    • 0034695569 scopus 로고    scopus 로고
    • Molecular basis of a yeast prion species barrier
    • Santoso, A., Chien, P., Osherovich, L. Z., and Weissman, J. S. (2000) Molecular basis of a yeast prion species barrier Cell 100, 277-288 (Pubitemid 30064915)
    • (2000) Cell , vol.100 , Issue.2 , pp. 277-288
    • Santoso, A.1    Chien, P.2    Osherovich, L.Z.3    Weissman, J.S.4
  • 22
    • 0034462603 scopus 로고    scopus 로고
    • [URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • DOI 10.1128/MCB.20.23.8916-8922.2000
    • Moriyama, H., Edskes, H. K., and Wickner, R. B. (2000) [URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p Mol. Cell. Biol. 20, 8916-8922 (Pubitemid 32245922)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.23 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 23
    • 0141455115 scopus 로고    scopus 로고
    • +] prion in yeast
    • Cox, B. S., Ness, F., and Tuite, M. F. (2003) Analysis of the generation and segregation of propagons: Entities that propagate the [PSI+] prion in yeast Genetics 165, 23-33 (Pubitemid 37204053)
    • (2003) Genetics , vol.165 , Issue.1 , pp. 23-33
    • Cox, B.1    Ness, F.2    Tuite, M.3
  • 24
    • 32944457631 scopus 로고    scopus 로고
    • +] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans
    • DOI 10.1128/EC.5.2.217-225.2006
    • Zenthon, J. F., Ness, F., Cox, B., and Tuite, M. F. (2006) The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans Eukaryotic Cell 5, 217-225 (Pubitemid 43262009)
    • (2006) Eukaryotic Cell , vol.5 , Issue.2 , pp. 217-225
    • Zenthon, J.F.1    Ness, F.2    Cox, B.3    Tuite, M.F.4
  • 25
    • 1642617641 scopus 로고    scopus 로고
    • Protein-only transmission of three yeast prion strains
    • DOI 10.1038/nature02391
    • King, C. Y. and Diaz-Avalos, R. (2004) Protein-only transmission of three yeast prion strains Nature 428, 319-323 (Pubitemid 38418802)
    • (2004) Nature , vol.428 , Issue.6980 , pp. 319-323
    • King, C.-Y.1    Diaz-Avalos, R.2
  • 26
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • DOI 10.1038/nature02392
    • Tanaka, M., Chien, P., Naber, N., Cooke, R., and Weissman, J. S. (2004) Conformational variations in an infectious protein determine prion strain differences Nature 428, 323-328 (Pubitemid 38418803)
    • (2004) Nature , vol.428 , Issue.6980 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 27
    • 27144451227 scopus 로고    scopus 로고
    • Prion generation in vitro: Amyloid of Ure2p is infectious
    • DOI 10.1038/sj.emboj.7600772, PII 7600772
    • Brachmann, A., Baxa, U., and Wickner, R. B. (2005) Prion generation in vitro: Amyloid of Ure2p is infectious EMBO J. 24, 3082-3092 (Pubitemid 41486344)
    • (2005) EMBO Journal , vol.24 , Issue.17 , pp. 3082-3092
    • Brachmann, A.1    Baxa, U.2    Wickner, R.B.3
  • 28
    • 33845605514 scopus 로고    scopus 로고
    • +]
    • DOI 10.1016/j.jmb.2006.10.069, PII S0022283606014495
    • Patel, B. K. and Liebman, S. W. (2007) "Prion proof" for [PIN+]: Infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+] J. Mol. Biol. 365, 773-782 (Pubitemid 44960370)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.3 , pp. 773-782
    • Patel, B.K.1    Liebman, S.W.2
  • 30
    • 36048969163 scopus 로고    scopus 로고
    • 1-89 yeast prion fibrils by solid-state nuclear magnetic resonance
    • DOI 10.1021/bi700826b
    • Baxa, U., Wickner, R. B., Steven, A. C., Anderson, D., Marekov, L., Yau, W.-M., and Tycko, R. (2007) Characterization of β-sheet structure in Ure2p1-89 yeast prion fibrils by solid state nuclear magnetic resonance Biochemistry 46, 13149-13162 (Pubitemid 350086233)
    • (2007) Biochemistry , vol.46 , Issue.45 , pp. 13149-13162
    • Baxa, U.1    Wickner, R.B.2    Steven, A.C.3    Anderson, D.E.4    Marekov, L.N.5    Yau, W.-M.6    Tycko, R.7
  • 32
  • 34
    • 70149087962 scopus 로고    scopus 로고
    • Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy
    • Chen, B., Thurber, K. R., Shewmaker, F., Wickner, R. B., and Tycko, R. (2009) Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy Proc. Natl. Acad. Sci. U.S.A. 106, 14339-14344
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 14339-14344
    • Chen, B.1    Thurber, K.R.2    Shewmaker, F.3    Wickner, R.B.4    Tycko, R.5
  • 35
    • 3543022080 scopus 로고    scopus 로고
    • Scrambled prion domains form prions and amyloid
    • DOI 10.1128/MCB.24.16.7206-7213.2004
    • Ross, E. D., Baxa, U., and Wickner, R. B. (2004) Scrambled prion domains form prions and amyloid Mol. Cell. Biol. 24, 7206-7213 (Pubitemid 39014446)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.16 , pp. 7206-7213
    • Ross, E.D.1    Baxa, U.2    Wickner, R.B.3
  • 37
    • 33644817188 scopus 로고    scopus 로고
    • Prion domains: Sequences, structures and interactions
    • Ross, E. D., Minton, A. P., and Wickner, R. B. (2005) Prion domains: Sequences, structures and interactions Nat. Cell Biol. 7, 1039-1044
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1039-1044
    • Ross, E.D.1    Minton, A.P.2    Wickner, R.B.3
  • 38
    • 53149116688 scopus 로고    scopus 로고
    • Protein inheritance (prions) based on parallel in-register β-sheet amyloid structures
    • Wickner, R. B., Shewmaker, F., Kryndushkin, D., and Edskes, H. K. (2008) Protein inheritance (prions) based on parallel in-register β-sheet amyloid structures BioEssays 30, 955-964
    • (2008) BioEssays , vol.30 , pp. 955-964
    • Wickner, R.B.1    Shewmaker, F.2    Kryndushkin, D.3    Edskes, H.K.4
  • 41
    • 33745585095 scopus 로고    scopus 로고
    • Reporter assay systems for [URE3] detection and analysis
    • DOI 10.1016/j.ymeth.2006.04.008, PII S1046202306000545
    • Brachmann, A., Toombs, J. A., and Ross, E. D. (2006) Reporter assay systems for [URE3] detection and analysis Methods 39, 35-42 (Pubitemid 43994491)
    • (2006) Methods , vol.39 , Issue.1 , pp. 35-42
    • Brachmann, A.1    Toombs, J.A.2    Ross, E.D.3
  • 43
    • 0031627465 scopus 로고    scopus 로고
    • An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli
    • Cai, M. L., Huang, Y., Sakaguchi, K., Clore, G. M., Gronenborn, A. M., and Craigie, R. (1998) An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli J. Biomol. NMR 11, 97-102 (Pubitemid 128510229)
    • (1998) Journal of Biomolecular NMR , vol.11 , Issue.1 , pp. 97-102
    • Cai, M.1    Huang, Y.2    Sakaguchi, K.3    Clore, G.M.4    Gronenborn, A.M.5    Craigie, R.6
  • 44
    • 36849106840 scopus 로고
    • Proton-Enhanced NMR of Dilute Spins in Solids
    • Pines, A., Gibby, M. G., and Waugh, J. S. (1973) Proton-Enhanced NMR of Dilute Spins in Solids J. Chem. Phys. 59, 569-590
    • (1973) J. Chem. Phys. , vol.59 , pp. 569-590
    • Pines, A.1    Gibby, M.G.2    Waugh, J.S.3
  • 46
    • 33847064253 scopus 로고    scopus 로고
    • Symmetry-based constant-time homonuclear dipolar recoupling in solid-state NMR
    • Tycko, R. (2007) Symmetry-based constant-time homonuclear dipolar recoupling in solid-state NMR J. Chem. Phys. 126, 064506
    • (2007) J. Chem. Phys. , vol.126 , pp. 064506
    • Tycko, R.1
  • 47
    • 0036018851 scopus 로고    scopus 로고
    • Sensitivity enhancement in structural measurements by solid state NMR through pulsed spin locking
    • Petkova, A. T. and Tycko, R. (2002) Sensitivity enhancement in structural measurements by solid state NMR through pulsed spin locking J. Magn. Reson. 155, 293-299
    • (2002) J. Magn. Reson. , vol.155 , pp. 293-299
    • Petkova, A.T.1    Tycko, R.2
  • 48
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on Unix pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on Unix pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 49
    • 0037094434 scopus 로고    scopus 로고
    • Nitrogen regulation in Saccharomyces cerevisiae
    • DOI 10.1016/S0378-1119(02)00558-9, PII S0378111902005589
    • Magasanik, B. and Kaiser, C. A. (2002) Nitrogen regulation in Saccharomyces cerevisiae Gene 290, 1-18 (Pubitemid 34615905)
    • (2002) Gene , vol.290 , Issue.1-2 , pp. 1-18
    • Magasanik, B.1    Kaiser, C.A.2
  • 50
    • 0036024577 scopus 로고    scopus 로고
    • Transmitting the signal of excess nitrogen in Saccharomyces cerevisiae from the Tor proteins to th GATA factors: Connecting the dots
    • Cooper, T. G. (2002) Transmitting the signal of excess nitrogen in Saccharomyces cerevisiae from the Tor proteins to th GATA factors: Connecting the dots FEMS Microbiol. Rev. 26, 223-238
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 223-238
    • Cooper, T.G.1
  • 51
    • 0023387946 scopus 로고
    • Transcriptional regulation of the DAL5 gene in Saccharomyces cerevisiae
    • Rai, R., Genbauffe, F., Lea, H. Z., and Cooper, T. G. (1987) Transcriptional regulation of the DAL5 gene in Saccharomyces cerevisiae J. Bacteriol. 169, 3521-3524
    • (1987) J. Bacteriol. , vol.169 , pp. 3521-3524
    • Rai, R.1    Genbauffe, F.2    Lea, H.Z.3    Cooper, T.G.4
  • 52
    • 0034808029 scopus 로고    scopus 로고
    • Induction of distinct [URE3] yeast prion strains
    • DOI 10.1128/MCB.21.20.7035-7046.2001
    • Schlumpberger, M., Prusiner, S. B., and Herskowitz, I. (2001) Induction of distinct [URE3] yeast prion strains Mol. Cell. Biol. 21, 7035-7046 (Pubitemid 32911263)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.20 , pp. 7035-7046
    • Schlumpberger, M.1    Prusiner, S.B.2    Herskowitz, I.3
  • 53
    • 0037162510 scopus 로고    scopus 로고
    • Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance
    • DOI 10.1073/pnas.152333299
    • Jung, G., Jones, G., and Masison, D. C. (2002) Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance Proc. Natl. Acad. Sci. U.S.A. 99, 9936-9941 (Pubitemid 34831151)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.15 , pp. 9936-9941
    • Jung, G.1    Jones, G.2    Masison, D.C.3
  • 54
    • 67049087912 scopus 로고    scopus 로고
    • Two prion variants of Sup35p have in-register β-sheet structures, independent of hydration
    • Shewmaker, F., Kryndushkin, D., Chen, B., Tycko, R., and Wickner, R. B. (2009) Two prion variants of Sup35p have in-register β-sheet structures, independent of hydration Biochemistry 48, 5074-5082
    • (2009) Biochemistry , vol.48 , pp. 5074-5082
    • Shewmaker, F.1    Kryndushkin, D.2    Chen, B.3    Tycko, R.4    Wickner, R.B.5
  • 55
    • 0029181728 scopus 로고
    • H-1, C-13 and N-15 Random Coil NMR Chemical-Shifts of the Common Amino-Acids. 1. Investigations of Nearest-Neighbor Effects
    • Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., and Sykes, B. D. (1995) H-1, C-13 and N-15 Random Coil NMR Chemical-Shifts of the Common Amino-Acids. 1. Investigations of Nearest-Neighbor Effects J. Biomol. NMR 5, 67-81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 57
    • 0034700129 scopus 로고    scopus 로고
    • Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimers β-amyloid fibrils
    • Antzutkin, O. N., Balbach, J. J., Leapman, R. D., Rizzo, N. W., Reed, J., and Tycko, R. (2000) Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimers β-amyloid fibrils Proc. Natl. Acad. Sci. U.S.A. 97, 13045-13050
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13045-13050
    • Antzutkin, O.N.1    Balbach, J.J.2    Leapman, R.D.3    Rizzo, N.W.4    Reed, J.5    Tycko, R.6
  • 58
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • DOI 10.1017/S0033583506004173, PII S0033583506004173
    • Tycko, R. (2006) Molecular structure of amyloid fibrils: Insights from solid-state NMR Q. Rev. Biophys. 1, 1-55 (Pubitemid 44566373)
    • (2006) Quarterly Reviews of Biophysics , vol.39 , Issue.1 , pp. 1-55
    • Tycko, R.1
  • 59
    • 33947390044 scopus 로고    scopus 로고
    • Evolution of Budding Yeast Prion-determinant Sequences Across Diverse Fungi
    • DOI 10.1016/j.jmb.2007.01.070, PII S0022283607001350
    • Harrison, L. B., Yu, Z., Stajich, J. E., Dietrich, F. S., and Harrison, P. M. (2007) Evolution of budding yeast prion-determinant sequences across diverse fungi J. Mol. Biol. 368, 273-282 (Pubitemid 46442850)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.1 , pp. 273-282
    • Harrison, L.B.1    Yu, Z.2    Stajich, J.E.3    Dietrich, F.S.4    Harrison, P.M.5
  • 60
    • 34547136725 scopus 로고    scopus 로고
    • Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae
    • DOI 10.1534/genetics.107.074153
    • Shewmaker, F., Mull, L., Nakayashiki, T., Masison, D. C., and Wickner, R. B. (2007) Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae Genetics 176, 1557-1565 (Pubitemid 47105217)
    • (2007) Genetics , vol.176 , Issue.3 , pp. 1557-1565
    • Shewmaker, F.1    Mull, L.2    Nakayashiki, T.3    Masison, D.C.4    Wickner, R.B.5
  • 61
    • 0041563922 scopus 로고    scopus 로고
    • Prion protein gene polymorphisms in Saccharomyces cerevisiae
    • DOI 10.1046/j.1365-2958.2003.03608.x
    • Resende, C. G., Outeiro, T. F., Sands, L., Lindquist, S., and Tuite, M. F. (2003) Prion protein gene polymorphisms in Saccharomyces cerevisiae Mol. Microbiol. 49, 1005-1017 (Pubitemid 36981345)
    • (2003) Molecular Microbiology , vol.49 , Issue.4 , pp. 1005-1017
    • Resende, C.G.1    Outeiro, T.F.2    Sands, L.3    Lindquist, S.4    Tuite, M.F.5
  • 62
    • 0033786333 scopus 로고    scopus 로고
    • A role for cytosolic Hsp70 in yeast [PSI+] prion propagation and [PSI+] as a cellular stress
    • Jung, G., Jones, G., Wegrzyn, R. D., and Masison, D. C. (2000) A role for cytosolic Hsp70 in yeast [PSI+] prion propagation and [PSI+] as a cellular stress Genetics 156, 559-570
    • (2000) Genetics , vol.156 , pp. 559-570
    • Jung, G.1    Jones, G.2    Wegrzyn, R.D.3    Masison, D.C.4
  • 63
    • 0036096777 scopus 로고    scopus 로고
    • +] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p
    • DOI 10.1128/MCB.22.11.3590-3598.2002
    • Schwimmer, C. and Masison, D. C. (2002) Antagonistic interactions between yeast [PSI+] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p Mol. Cell. Biol. 22, 3590-3598 (Pubitemid 34525203)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.11 , pp. 3590-3598
    • Schwimmer, C.1    Masison, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.