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Volumn 10, Issue 4, 2014, Pages 851-861

A proteomic survey of widespread protein aggregation in yeast

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ARSENIC; CHAPERONE; GLUTAMATE AMMONIA LIGASE; GLUTAMINE SYNTHETASE I; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HSP82 PROTEIN, S CEREVISIAE; PHOSPHOGLYCERATE MUTASE; SACCHAROMYCES CEREVISIAE PROTEIN; SSA1 PROTEIN, S CEREVISIAE; SSA3 PROTEIN, S CEREVISIAE;

EID: 84897680356     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/c3mb70508k     Document Type: Article
Times cited : (45)

References (38)
  • 2
    • 77955906574 scopus 로고    scopus 로고
    • Identification of novel filament-forming proteins in Saccharomyces cerevisiae and drosophila melanogaster
    • C. Noree B. K. Sato R. M. Broyer J. E. Wilhelm Identification of novel filament-forming proteins in Saccharomyces cerevisiae and drosophila melanogaster J. Cell Biol. 2010 190 4 541 551
    • (2010) J. Cell Biol. , vol.190 , Issue.4 , pp. 541-551
    • Noree, C.1    Sato, B.K.2    Broyer, R.M.3    Wilhelm, J.E.4
  • 3
    • 55249120532 scopus 로고    scopus 로고
    • Protein quality control: On IPODs and other JUNQ
    • K. Bagola T. Sommer Protein quality control: on IPODs and other JUNQ Curr. Biol. 2008 18 21 R1019 R1021
    • (2008) Curr. Biol. , vol.18 , Issue.21
    • Bagola, K.1    Sommer, T.2
  • 5
    • 77952734418 scopus 로고    scopus 로고
    • Intracellular compartmentation of CTP synthase in Drosophila
    • J.-L. Liu Intracellular compartmentation of CTP synthase in Drosophila J. Genet. Genomics 2010 37 5 281 296
    • (2010) J. Genet. Genomics , vol.37 , Issue.5 , pp. 281-296
    • Liu, J.-L.1
  • 8
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • D. Kaganovich R. Kopito J. Frydman Misfolded proteins partition between two distinct quality control compartments Nature 2008 454 7208 1088 1095
    • (2008) Nature , vol.454 , Issue.7208 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 10
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • J. A. Johnston C. L. Ward R. R. Kopito Aggresomes: a cellular response to misfolded proteins J. Cell Biol. 1998 143 7 1883 1898
    • (1998) J. Cell Biol. , vol.143 , Issue.7 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 12
    • 27144515901 scopus 로고    scopus 로고
    • Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies
    • M. Brengues D. Teixeira R. Parker Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies Science 2005 310 5747 486 489
    • (2005) Science , vol.310 , Issue.5747 , pp. 486-489
    • Brengues, M.1    Teixeira, D.2    Parker, R.3
  • 13
    • 33750522651 scopus 로고    scopus 로고
    • Actin bodies in yeast quiescent cells: An immediately available actin reserve?
    • I. Sagot B. Pinson B. Salin B. Daignan-Fornier Actin bodies in yeast quiescent cells: an immediately available actin reserve? Mol. Biol. Cell 2006 17 11 4645 4655
    • (2006) Mol. Biol. Cell , vol.17 , Issue.11 , pp. 4645-4655
    • Sagot, I.1    Pinson, B.2    Salin, B.3    Daignan-Fornier, B.4
  • 15
    • 34447526217 scopus 로고    scopus 로고
    • Stress and prions: Lessons from the yeast model
    • Y. O. Chernoff Stress and prions: lessons from the yeast model FEBS Lett. 2007 581 19 3695 3701
    • (2007) FEBS Lett. , vol.581 , Issue.19 , pp. 3695-3701
    • Chernoff, Y.O.1
  • 16
    • 48749096008 scopus 로고    scopus 로고
    • Carcinogenic metal compounds: Recent insight into molecular and cellular mechanisms
    • D. Beyersmann A. Hartwig Carcinogenic metal compounds: recent insight into molecular and cellular mechanisms Arch. Toxicol. 2008 82 8 493 512
    • (2008) Arch. Toxicol. , vol.82 , Issue.8 , pp. 493-512
    • Beyersmann, D.1    Hartwig, A.2
  • 21
    • 41749092312 scopus 로고    scopus 로고
    • Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
    • S. An R. Kumar E. D. Sheets S. J. Benkovic Reversible compartmentalization of de novo purine biosynthetic complexes in living cells Science 2008 320 5872 103 106
    • (2008) Science , vol.320 , Issue.5872 , pp. 103-106
    • An, S.1    Kumar, R.2    Sheets, E.D.3    Benkovic, S.J.4
  • 23
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • A.-M. Fernandez-Escamilla F. Rousseau J. Schymkowitz L. Serrano Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins Nat. Biotechnol. 2004 22 10 1302 1306
    • (2004) Nat. Biotechnol. , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 24
    • 84860361727 scopus 로고    scopus 로고
    • Segregation of molecules at cell division reveals native protein localization
    • D. Landgraf B. Okumus P. Chien T. A. Baker J. Paulsson Segregation of molecules at cell division reveals native protein localization Nat. Methods 2012 9 5 480 482
    • (2012) Nat. Methods , vol.9 , Issue.5 , pp. 480-482
    • Landgraf, D.1    Okumus, B.2    Chien, P.3    Baker, T.A.4    Paulsson, J.5
  • 26
    • 84897697897 scopus 로고    scopus 로고
    • MRNAs sit out the stress in EGP bodies
    • R. Williams mRNAs sit out the stress in EGP bodies J. Cell Biol. 2007 179 1 2
    • (2007) J. Cell Biol. , vol.179 , Issue.1 , pp. 2
    • Williams, R.1
  • 27
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • E. van Dijk N. Cougot S. Meyer S. Babajko E. Wahle B. Séraphin Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures EMBO J. 2002 21 24 6915 6924
    • (2002) EMBO J. , vol.21 , Issue.24 , pp. 6915-6924
    • Van Dijk, E.1    Cougot, N.2    Meyer, S.3    Babajko, S.4    Wahle, E.5    Séraphin, B.6
  • 28
    • 0015816557 scopus 로고
    • Functional organelles in prokaryotes: Polyhedral inclusions (carboxysomes) of thiobacillus neapolitanus
    • J. M. Shively F. Ball D. H. Brown R. E. Saunders Functional organelles in prokaryotes: polyhedral inclusions (carboxysomes) of thiobacillus neapolitanus Science 1973 182 4112 584 586
    • (1973) Science , vol.182 , Issue.4112 , pp. 584-586
    • Shively, J.M.1    Ball, F.2    Brown, D.H.3    Saunders, R.E.4
  • 29
    • 3142757398 scopus 로고    scopus 로고
    • Cellulosomes: Plant-cell-wall-degrading enzyme complexes
    • R. H. Doi A. Kosugi Cellulosomes: plant-cell-wall-degrading enzyme complexes Nat. Rev. Microbiol. 2004 2 7 541 551
    • (2004) Nat. Rev. Microbiol. , vol.2 , Issue.7 , pp. 541-551
    • Doi, R.H.1    Kosugi, A.2
  • 30
    • 33645958257 scopus 로고    scopus 로고
    • Regulation of the pyruvate dehydrogenase complex
    • M. S. Patel L. G. Korotchkina Regulation of the pyruvate dehydrogenase complex Biochem. Soc. Trans. 2006 34 Pt 2 217 222
    • (2006) Biochem. Soc. Trans. , vol.34 , Issue.PART 2 , pp. 217-222
    • Patel, M.S.1    Korotchkina, L.G.2
  • 33
    • 79959942025 scopus 로고    scopus 로고
    • MSblender: A probabilistic approach for integrating peptide identifications from multiple database search engines
    • T. Kwon H. Choi C. Vogel A. I. Nesvizhskii E. M. Marcotte MSblender: A probabilistic approach for integrating peptide identifications from multiple database search engines J. Proteome Res. 2011 10 7 2949 2958
    • (2011) J. Proteome Res. , vol.10 , Issue.7 , pp. 2949-2958
    • Kwon, T.1    Choi, H.2    Vogel, C.3    Nesvizhskii, A.I.4    Marcotte, E.M.5
  • 34
    • 80052435590 scopus 로고    scopus 로고
    • Faster SEQUEST searching for peptide identification from tandem mass spectra
    • B. J. Diament W. S. Noble Faster SEQUEST searching for peptide identification from tandem mass spectra J. Proteome Res. 2011 10 9 3871 3879
    • (2011) J. Proteome Res. , vol.10 , Issue.9 , pp. 3871-3879
    • Diament, B.J.1    Noble, W.S.2
  • 36
    • 27544511899 scopus 로고    scopus 로고
    • InsPecT: Identification of posttranslationally modified peptides from tandem mass spectra
    • S. Tanner H. Shu A. Frank L.-C. Wang E. Zandi M. Mumby P. A. Pevzner V. Bafna InsPecT: identification of posttranslationally modified peptides from tandem mass spectra Anal. Chem. 2005 77 14 4626 4629
    • (2005) Anal. Chem. , vol.77 , Issue.14 , pp. 4626-4629
    • Tanner, S.1    Shu, H.2    Frank, A.3    Wang, L.-C.4    Zandi, E.5    Mumby, M.6    Pevzner, P.A.7    Bafna, V.8
  • 37
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • P. Lu C. Vogel R. Wang X. Yao E. M. Marcotte Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation Nat. Biotechnol. 2007 25 1 117 124
    • (2007) Nat. Biotechnol. , vol.25 , Issue.1 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 38
    • 42049116064 scopus 로고    scopus 로고
    • Colocalization of fluorescent markers in confocal microscope images of plant cells
    • A. P. French S. Mills R. Swarup M. J. Bennett T. P. Pridmore Colocalization of fluorescent markers in confocal microscope images of plant cells Nat. Protoc. 2008 3 4 619 628
    • (2008) Nat. Protoc. , vol.3 , Issue.4 , pp. 619-628
    • French, A.P.1    Mills, S.2    Swarup, R.3    Bennett, M.J.4    Pridmore, T.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.