메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; CHAPERONE; PRION PROTEIN; SUP35 PROTEIN; UNCLASSIFIED DRUG; PRION; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84904458790     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5383     Document Type: Article
Times cited : (91)

References (70)
  • 1
    • 66249126298 scopus 로고    scopus 로고
    • Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans
    • Arnesen, T. et al. Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans. Proc. Natl Acad. Sci. USA 106, 8157-8162 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 8157-8162
    • Arnesen, T.1
  • 2
    • 79958039807 scopus 로고    scopus 로고
    • Towards a functional understanding of protein N-terminal acetylation
    • Arnesen, T. Towards a functional understanding of protein N-terminal acetylation. PLoS Biol. 9, e1001074 (2011).
    • (2011) PLoS Biol. , vol.9
    • Arnesen, T.1
  • 3
    • 0037462954 scopus 로고    scopus 로고
    • N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins
    • Polevoda, B. & Sherman, F. N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins. J. Mol. Biol. 325, 595-622 (2003).
    • (2003) J. Mol. Biol. , vol.325 , pp. 595-622
    • Polevoda, B.1    Sherman, F.2
  • 4
    • 0022407123 scopus 로고
    • The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways
    • Whiteway, M. & Szostak, J. W. The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways. Cell 43, 483-492 (1985).
    • (1985) Cell , vol.43 , pp. 483-492
    • Whiteway, M.1    Szostak, J.W.2
  • 5
    • 0025900189 scopus 로고
    • Modifiers of position effect are shared between telomeric and silent mating-type loci in S
    • Aparicio, O. M., Billington, B. L. & Gottschling, D. E. Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae. Cell 66, 1279-1287 (1991).
    • (1991) Cerevisiae. Cell , vol.66 , pp. 1279-1287
    • Aparicio, O.M.1    Billington, B.L.2    Gottschling, D.E.3
  • 6
    • 0043234609 scopus 로고    scopus 로고
    • Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin
    • Polevoda, B., Cardillo, T. S., Doyle, T. C., Bedi, G. S. & Sherman, F. Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal acetyltransferase and of actin and tropomyosin. J. Biol. Chem. 278, 30686-30697 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 30686-30697
    • Polevoda, B.1    Cardillo, T.S.2    Doyle, T.C.3    Bedi, G.S.4    Sherman, F.5
  • 7
    • 64049100053 scopus 로고    scopus 로고
    • The NatA acetyltransferase couples Sup35 prion complexes to the [PSI] phenotype
    • Pezza, J. A. et al. The NatA acetyltransferase couples Sup35 prion complexes to the [PSI] phenotype. Mol. Biol. Cell 20, 1068-1080 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1068-1080
    • Pezza, J.A.1
  • 8
    • 84884694093 scopus 로고    scopus 로고
    • N-alpha-terminal acetylation of histone H4 regulates arginine methylation and ribosomal DNA silencing
    • Schiza, V., Molina-Serrano, D., Kyriakou, D., Hadjiantoniou, A. & Kirmizis, A. N-alpha-terminal acetylation of histone H4 regulates arginine methylation and ribosomal DNA silencing. PLoS Genet. 9, e1003805 (2013).
    • (2013) PLoS Genet , vol.9
    • Schiza, V.1    Molina-Serrano, D.2    Kyriakou, D.3    Hadjiantoniou, A.4    Kirmizis, A.5
  • 9
    • 80051550297 scopus 로고    scopus 로고
    • Using VAAST to identify an X-linked disorder resulting in lethality in male infants due to N-terminal acetyltransferase deficiency
    • Rope, A. F. et al. Using VAAST to identify an X-linked disorder resulting in lethality in male infants due to N-terminal acetyltransferase deficiency. Am. J. Hum. Genet. 89, 28-43 (2011).
    • (2011) Am. J. Hum. Genet. , vol.89 , pp. 28-43
    • Rope, A.F.1
  • 10
    • 84904481340 scopus 로고    scopus 로고
    • A Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase Naa10S37P mutant
    • doi: 10.1074/mcp.M113.035402
    • Van Damme, P., Støve, S. I., Glomnes, N., Gevaert, K. & Arnesen, T. A Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase Naa10S37P mutant. Mol. Cell. Proteomics. doi: 10.1074/mcp.M113.035402 (2014).
    • (2014) Mol. Cell. Proteomics
    • Van Damme, P.1    Støve, S.I.2    Glomnes, N.3    Gevaert, K.4    Arnesen, T.5
  • 11
    • 84872613178 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases in cancer
    • Kalvik, T. V. & Arnesen, T. Protein N-terminal acetyltransferases in cancer. Oncogene 32, 269-276 (2013).
    • (2013) Oncogene , vol.32 , pp. 269-276
    • Kalvik, T.V.1    Arnesen, T.2
  • 12
    • 84892802083 scopus 로고    scopus 로고
    • The N-terminal methionine of cellular proteins as a degradation signal
    • Kim, H. K. et al. The N-terminal methionine of cellular proteins as a degradation signal. Cell 156, 158-169 (2013).
    • (2013) Cell , vol.156 , pp. 158-169
    • Kim, H.K.1
  • 13
    • 84878195272 scopus 로고    scopus 로고
    • Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway
    • Shemorry, A., Hwang, C. S. & Varshavsky, A. Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway. Mol. Cell 50, 540-551 (2013).
    • (2013) Mol. Cell , vol.50 , pp. 540-551
    • Shemorry, A.1    Hwang, C.S.2    Varshavsky, A.3
  • 14
    • 0024506404 scopus 로고
    • Further studies of the helix dipole model: Effects of a free alpha-NH3 or alpha-COO-group on helix stability
    • Fairman, R., Shoemaker, K. R., York, E. J., Stewart, J. M. & Baldwin, R. L. Further studies of the helix dipole model: Effects of a free alpha-NH3 or alpha-COO-group on helix stability. Proteins 5, 1-7 (1989).
    • (1989) Proteins , vol.5 , pp. 1-7
    • Fairman, R.1    Shoemaker, K.R.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 15
    • 0028289435 scopus 로고
    • Determination of free energies of N-capping in alpha-helices by modification of the Lifson-Roig helix-coil therapy to include N-and C-capping
    • Doig, A. J., Chakrabartty, A., Klingler, T. M. & Baldwin, R. L. Determination of free energies of N-capping in alpha-helices by modification of the Lifson-Roig helix-coil therapy to include N-and C-capping. Biochemistry 33, 3396-3403 (1994).
    • (1994) Biochemistry , vol.33 , pp. 3396-3403
    • Doig, A.J.1    Chakrabartty, A.2    Klingler, T.M.3    Baldwin, R.L.4
  • 16
    • 0023122030 scopus 로고
    • Tests of the helix dipole model for stabilization of alpha-helices
    • Shoemaker, K. R., Kim, P. S., York, E. J., Stewart, J. M. & Baldwin, R. L. Tests of the helix dipole model for stabilization of alpha-helices. Nature 326, 563-567 (1987).
    • (1987) Nature , vol.326 , pp. 563-567
    • Shoemaker, K.R.1    Kim, P.S.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 17
    • 0028855710 scopus 로고
    • Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10
    • Jarvis, J. A., Ryan, M. T., Hoogenraad, N. J., Craik, D. J. & Hoj, P. B. Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10. J. Biol. Chem. 270, 1323-1331 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 1323-1331
    • Jarvis, J.A.1    Ryan, M.T.2    Hoogenraad, N.J.3    Craik, D.J.4    Hoj, P.B.5
  • 18
    • 0027367977 scopus 로고
    • Helix capping propensities in peptides parallel those in proteins
    • Chakrabartty, A., Doig, A. J. & Baldwin, R. L. Helix capping propensities in peptides parallel those in proteins. Proc. Natl Acad. Sci. USA 90, 11332-11336 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11332-11336
    • Chakrabartty, A.1    Doig, A.J.2    Baldwin, R.L.3
  • 19
    • 0028258048 scopus 로고
    • The effect of N-terminal acetylation on the structure of an N-terminal tropomyosin peptide and alpha alpha-tropomyosin
    • Greenfield, N. J., Stafford, W. F. & Hitchcock-DeGregori, S. E. The effect of N-terminal acetylation on the structure of an N-terminal tropomyosin peptide and alpha alpha-tropomyosin. Protein Sci. 3, 402-410 (1994).
    • (1994) Protein Sci. , vol.3 , pp. 402-410
    • Greenfield, N.J.1    Stafford, W.F.2    Hitchcock-Degregori, S.E.3
  • 20
    • 0141640821 scopus 로고    scopus 로고
    • The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides
    • Gautschi, M. et al. The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell Biol. 23, 7403-7414 (2003).
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7403-7414
    • Gautschi, M.1
  • 21
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer, W. J. & Hartl, F. U. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature 388, 343-349 (1997).
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 22
    • 84859490749 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases: When the start matters
    • Starheim, K. K., Gevaert, K. & Arnesen, T. Protein N-terminal acetyltransferases: when the start matters. Trends Biochem. Sci. 37, 152-161 (2012).
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 152-161
    • Starheim, K.K.1    Gevaert, K.2    Arnesen, T.3
  • 23
    • 78649417132 scopus 로고    scopus 로고
    • The prion hypothesis: From biological anomaly to basic regulatory mechanism
    • Tuite, M. F. & Serio, T. R. The prion hypothesis: From biological anomaly to basic regulatory mechanism. Nat. Rev. Mol. Cell Biol. 11, 823-833 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 823-833
    • Tuite, M.F.1    Serio, T.R.2
  • 24
    • 0028200770 scopus 로고
    • The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [PSI] in the yeast Saccharomyces cerevisiae
    • Ter-Avanesyan, M. D., Dagkesamanskaya, A. R., Kushnirov, V. V. & Smirnov, V. N. 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 (1994).
    • (1994) Genetics , vol.137 , pp. 671-676
    • Ter-Avanesyan, M.D.1    Dagkesamanskaya, A.R.2    Kushnirov, V.V.3    Smirnov, V.N.4
  • 25
    • 72949111831 scopus 로고    scopus 로고
    • Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster
    • Goetze, S. et al. Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster. PLoS Biol. 7, e1000236 (2009).
    • (2009) PLoS Biol. , vol.7
    • Goetze, S.1
  • 26
    • 24644467295 scopus 로고    scopus 로고
    • Prion protein remodelling confers an immediate phenotypic switch
    • Satpute-Krishnan, P. & Serio, T. R. Prion protein remodelling confers an immediate phenotypic switch. Nature 437, 262-265 (2005).
    • (2005) Nature , vol.437 , pp. 262-265
    • Satpute-Krishnan, P.1    Serio, T.R.2
  • 27
    • 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. 278, 49636-49643 (2003).
    • (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
  • 28
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • Tanaka, M., Collins, S. R., Toyama, B. H. & Weissman, J. S. The physical basis of how prion conformations determine strain phenotypes. Nature 442, 585-589 (2006).
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 29
    • 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 268, 880-884 (1995).
    • (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
  • 30
    • 0033637153 scopus 로고    scopus 로고
    • Genomic expression programs in the response of yeast cells to environmental changes
    • Gasch, A. P. et al. Genomic expression programs in the response of yeast cells to environmental changes. Mol. Biol. Cell 11, 4241-4257 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4241-4257
    • Gasch, A.P.1
  • 31
    • 0035149551 scopus 로고    scopus 로고
    • Remodeling of yeast genome expression in response to environmental changes
    • Causton, H. C. et al. Remodeling of yeast genome expression in response to environmental changes. Mol. Biol. Cell 12, 323-337 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 323-337
    • Causton, H.C.1
  • 32
    • 0032500690 scopus 로고    scopus 로고
    • Transcriptional factor mutations reveal regulatory complexities of heat shock and newly identified stress genes in Saccharomyces cerevisiae
    • Treger, J. M., Schmitt, A. P., Simon, J. R. & McEntee, K. Transcriptional factor mutations reveal regulatory complexities of heat shock and newly identified stress genes in Saccharomyces cerevisiae. J. Biol. Chem. 273, 26875-26879 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 26875-26879
    • Treger, J.M.1    Schmitt, A.P.2    Simon, J.R.3    McEntee, K.4
  • 33
    • 0346736509 scopus 로고    scopus 로고
    • Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae
    • Trotter, E. W. et al. Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae. J. Biol. Chem. 277, 44817-44825 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 44817-44825
    • Trotter, E.W.1
  • 34
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development and lifespan
    • Akerfelt, M., Morimoto, R. I. & Sistonen, L. Heat shock factors: integrators of cell stress, development and lifespan. Nat. Rev. Mol. Cell Biol. 11, 545-555 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 35
    • 0023427519 scopus 로고
    • Purification and characterization of a heat-shock element binding protein from yeast
    • Sorger, P. K. & Pelham, H. R. Purification and characterization of a heat-shock element binding protein from yeast. EMBO J. 6, 3035-3041 (1987).
    • (1987) EMBO J. , vol.6 , pp. 3035-3041
    • Sorger, P.K.1    Pelham, H.R.2
  • 36
    • 0024894102 scopus 로고
    • Expression of members of the Saccharomyces cerevisiae Hsp70 multigene family
    • Werner-Washburne, M. & Craig, E. A. Expression of members of the Saccharomyces cerevisiae Hsp70 multigene family. Genome 31, 684-689 (1989).
    • (1989) Genome , vol.31 , pp. 684-689
    • Werner-Washburne, M.1    Craig, E.A.2
  • 37
    • 0028886503 scopus 로고
    • Mutated yeast heat shock transcription factor exhibits elevated basal transcriptional activation and confers metal resistance
    • Sewell, A. K. et al. Mutated yeast heat shock transcription factor exhibits elevated basal transcriptional activation and confers metal resistance. J. Biol. Chem. 270, 25079-25086 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 25079-25086
    • Sewell, A.K.1
  • 38
    • 0029095916 scopus 로고
    • A heat shock transcription factor with reduced activity suppresses a yeast HSP70 mutant
    • Halladay, J. T. & Craig, E. A. A heat shock transcription factor with reduced activity suppresses a yeast HSP70 mutant. Mol. Cell Biol. 15, 4890-4897 (1995).
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4890-4897
    • Halladay, J.T.1    Craig, E.A.2
  • 39
    • 78049408567 scopus 로고    scopus 로고
    • A size threshold limits prion transmission and establishes phenotypic diversity
    • Derdowski, A., Sindi, S. S., Klaips, C. L., DiSalvo, S. & Serio, T. R. A size threshold limits prion transmission and establishes phenotypic diversity. Science 330, 680-683 (2010).
    • (2010) Science , vol.330 , pp. 680-683
    • Derdowski, A.1    Sindi, S.S.2    Klaips, C.L.3    Disalvo, S.4    Serio, T.R.5
  • 40
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • Albanese, V., Yam, A. Y., Baughman, J., Parnot, C. & Frydman, J. Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell 124, 75-88 (2006).
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanese, V.1    Yam, A.Y.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 41
    • 84878658572 scopus 로고    scopus 로고
    • The nascent polypeptide-associated complex is a key regulator of proteostasis
    • Kirstein-Miles, J., Scior, A., Deuerling, E. & Morimoto, R. I. The nascent polypeptide-associated complex is a key regulator of proteostasis. EMBO J. 32, 1451-1468 (2013).
    • (2013) EMBO J. , vol.32 , pp. 1451-1468
    • Kirstein-Miles, J.1    Scior, A.2    Deuerling, E.3    Morimoto, R.I.4
  • 42
    • 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. 19, 8103-8112 (1999).
    • (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
  • 43
    • 0032951475 scopus 로고    scopus 로고
    • Antagonistic Interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    • Newman, G. P., Wegrzyn, R. D., Lindquist, S. L. & Chernoff, Y. O. Antagonistic Interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell Biol. 19, 1325-1333 (1999).
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1325-1333
    • Newman, G.P.1    Wegrzyn, R.D.2    Lindquist, S.L.3    Chernoff, Y.O.4
  • 44
    • 84904497710 scopus 로고    scopus 로고
    • Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype
    • Pezza, J. A., Villali, J., Sindi, S. & Serio, T. R. Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype. Nat. Commun. 5, 4384 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4384
    • Pezza, J.A.1    Villali, J.2    Sindi, S.3    Serio, T.R.4
  • 45
    • 84883744311 scopus 로고    scopus 로고
    • Nalpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain
    • Yang, D. et al. Nalpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain. Nat. Struct. Mol. Biol. 20, 1116-1118 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1116-1118
    • Yang, D.1
  • 46
    • 84883742201 scopus 로고    scopus 로고
    • The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
    • Arnaudo, N. et al. The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle. Nat. Struct. Mol. Biol. 20, 1119-1121 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1119-1121
    • Arnaudo, N.1
  • 47
    • 0034046081 scopus 로고    scopus 로고
    • Two classes of sir3 mutants enhance the sir1 mutant mating defect and abolish telomeric silencing in Saccharomyces cerevisiae
    • Stone, E. M., Reifsnyder, C., McVey, M., Gazo, B. & Pillus, L. Two classes of sir3 mutants enhance the sir1 mutant mating defect and abolish telomeric silencing in Saccharomyces cerevisiae. Genetics 155, 509-522 (2000).
    • (2000) Genetics , vol.155 , pp. 509-522
    • Stone, E.M.1    Reifsnyder, C.2    McVey, M.3    Gazo, B.4    Pillus, L.5
  • 48
    • 48149087568 scopus 로고    scopus 로고
    • Non-functional phosphorylations?
    • Lienhard, G. E. Non-functional phosphorylations? Trends Biochem. Sci. 33, 351-352 (2008).
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 351-352
    • Lienhard, G.E.1
  • 49
    • 34548615995 scopus 로고    scopus 로고
    • The structural basis of yeast prion strain variants
    • Toyama, B. H., Kelly, M. J., Gross, J. D. & Weissman, J. S. The structural basis of yeast prion strain variants. Nature 449, 233-237 (2007).
    • (2007) Nature , vol.449 , pp. 233-237
    • Toyama, B.H.1    Kelly, M.J.2    Gross, J.D.3    Weissman, J.S.4
  • 50
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels, T., Choi, J. G. & Selkoe, D. J. alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477, 107-110 (2011).
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 51
    • 80055020885 scopus 로고    scopus 로고
    • Identification of novel alpha-synuclein isoforms in human brain tissue by using an online nanoLC-ESI-FTICR-MS method
    • Ohrfelt, A. et al. Identification of novel alpha-synuclein isoforms in human brain tissue by using an online nanoLC-ESI-FTICR-MS method. Neurochem. Res. 36, 2029-2042 (2011).
    • (2011) Neurochem. Res. , vol.36 , pp. 2029-2042
    • Ohrfelt, A.1
  • 52
    • 84877130674 scopus 로고    scopus 로고
    • Impairment of mitochondria in adult mouse brain overexpressing predominantly full-length, N-terminally acetylated human alpha-synuclein
    • Sarafian, T. A. et al. Impairment of mitochondria in adult mouse brain overexpressing predominantly full-length, N-terminally acetylated human alpha-synuclein. PLoS One 8, e63557 (2013).
    • (2013) PLoS One , vol.8
    • Sarafian, T.A.1
  • 53
    • 33749570292 scopus 로고    scopus 로고
    • Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease
    • Anderson, J. P. et al. Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. J. Biol. Chem. 281, 29739-29752 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 29739-29752
    • Anderson, J.P.1
  • 54
    • 84884216544 scopus 로고    scopus 로고
    • Mechanistic insight into the relationship between N-terminal acetylation of alpha-synuclein and fibril formation rates by NMR and fluorescence
    • Kang, L., Janowska, M. K., Moriarty, G. M. & Baum, J. Mechanistic insight into the relationship between N-terminal acetylation of alpha-synuclein and fibril formation rates by NMR and fluorescence. PLoS One 8, e75018 (2013).
    • (2013) PLoS One , vol.8
    • Kang, L.1    Janowska, M.K.2    Moriarty, G.M.3    Baum, J.4
  • 55
    • 84862555977 scopus 로고    scopus 로고
    • N-terminal acetylation of alpha-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer
    • Kang, L. et al. N-terminal acetylation of alpha-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer. Protein Sci. 21, 911-917 (2012).
    • (2012) Protein Sci , vol.21 , pp. 911-917
    • Kang, L.1
  • 56
    • 84865249504 scopus 로고    scopus 로고
    • Characterization of semisynthetic and naturally Nalphaacetylated alpha-synuclein in vitro and in intact cells: Implications for aggregation and cellular properties of alpha-synuclein
    • Fauvet, B. et al. Characterization of semisynthetic and naturally Nalphaacetylated alpha-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of alpha-synuclein. J. Biol. Chem. 287, 28243-28262 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 28243-28262
    • Fauvet, B.1
  • 57
    • 80051970600 scopus 로고    scopus 로고
    • Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival
    • Yi, C. H. et al. Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival. Cell 146, 607-620 (2011).
    • (2011) Cell , vol.146 , pp. 607-620
    • Yi, C.H.1
  • 58
    • 84874644124 scopus 로고    scopus 로고
    • Linking post-translational modifications and variation of phenotypic traits
    • Albertin, W. et al. Linking post-translational modifications and variation of phenotypic traits. Mol. Cell Proteomics 12, 720-735 (2013).
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 720-735
    • Albertin, W.1
  • 59
    • 84878701862 scopus 로고    scopus 로고
    • Potential involvement of N-terminal acetylation in the quantitative regulation of the epsilon subunit of chloroplast ATP synthase under drought stress
    • Hoshiyasu, S. et al. Potential involvement of N-terminal acetylation in the quantitative regulation of the epsilon subunit of chloroplast ATP synthase under drought stress. Biosci. Biotechnol. Biochem. 77, 998-1007 (2013).
    • (2013) Biosci. Biotechnol. Biochem. , vol.77 , pp. 998-1007
    • Hoshiyasu, S.1
  • 60
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S. & Hieter, P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27 (1989).
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 61
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., Pohlmann, R. & Philippsen, P. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10, 1793-1808 (1994).
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 62
    • 0036270928 scopus 로고    scopus 로고
    • LacZ assays in yeast
    • Rupp, S. LacZ assays in yeast. Methods Enzymol. 350, 112-131 (2002).
    • (2002) Methods Enzymol. , vol.350 , pp. 112-131
    • Rupp, S.1
  • 63
    • 79953789286 scopus 로고    scopus 로고
    • Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation
    • DiSalvo, S., Derdowski, A., Pezza, J. A. & Serio, T. R. Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation. Nat. Struct. Mol. Biol. 18, 486-492 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 486-492
    • Disalvo, S.1    Derdowski, A.2    Pezza, J.A.3    Serio, T.R.4
  • 64
    • 58149199563 scopus 로고    scopus 로고
    • Implementation of genepattern within the stanford microarray database
    • Hubble, J. et al. Implementation of GenePattern within the Stanford Microarray Database. Nucleic Acids Res. 37, D898-D901 (2009).
    • (2009) Nucleic Acids Res. , vol.37
    • Hubble, J.1
  • 65
    • 0035162698 scopus 로고    scopus 로고
    • Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p
    • Gasch, A. P. et al. Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p. Mol. Biol. Cell 12, 2987-3003 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2987-3003
    • Gasch, A.P.1
  • 66
    • 0021355377 scopus 로고
    • Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae
    • Adams, A. E. & Pringle, J. R. Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae. J. Cell Biol. 98, 934-945 (1984).
    • (1984) J. Cell Biol. , vol.98 , pp. 934-945
    • Adams, A.E.1    Pringle, J.R.2
  • 67
    • 46849090661 scopus 로고    scopus 로고
    • Extent of N-terminal modifications in cytosolic proteins from eukaryotes
    • Martinez, A. et al. Extent of N-terminal modifications in cytosolic proteins from eukaryotes. Proteomics 8, 2809-2831 (2008).
    • (2008) Proteomics , vol.8 , pp. 2809-2831
    • Martinez, A.1
  • 68
    • 79958027934 scopus 로고    scopus 로고
    • N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum
    • Forte, G. M., Pool, M. R. & Stirling, C. J. N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum. PLoS Biol. 9, e1001073 (2011).
    • (2011) PLoS Biol , vol.9
    • Forte, G.M.1    Pool, M.R.2    Stirling, C.J.3
  • 69
    • 84855184716 scopus 로고    scopus 로고
    • SPINE-D: Accurate prediction of short and long disordered regions by a single neural-network based method
    • Zhang, T. et al. SPINE-D: accurate prediction of short and long disordered regions by a single neural-network based method. J. Biomol. Struct. Dyn. 29, 799-813 (2012).
    • (2012) J. Biomol. Struct. Dyn. , vol.29 , pp. 799-813
    • Zhang, T.1
  • 70
    • 34247500374 scopus 로고    scopus 로고
    • Python for scientific computing
    • Oliphant, T. E. Python for scientific computing. Comput. Sci. Eng. 9, 10-20 (2007).
    • (2007) Comput. Sci. Eng. , vol.9 , pp. 10-20
    • Oliphant, T.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.