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Volumn 110, Issue 17, 2013, Pages

MChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases

Author keywords

Acetylation map; Yeast

Indexed keywords

ACYLTRANSFERASE; HISTONE H4; LYSINE; LYSINE ACETYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 84876885763     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1218515110     Document Type: Article
Times cited : (35)

References (62)
  • 1
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange S, Wagner T, Heinzel T, Krämer OH (2009) Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int J Biochem Cell Biol 41(1):185-198.
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.1 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Krämer, O.H.4
  • 2
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and the bromodomain: A new partnership for signaling
    • Yang XJ (2004) Lysine acetylation and the bromodomain: A new partnership for signaling. Bioessays 26(10):1076-1087.
    • (2004) Bioessays , vol.26 , Issue.10 , pp. 1076-1087
    • Yang, X.J.1
  • 3
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C, et al. (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325(5942):834-840.
    • (2009) Science , vol.325 , Issue.5942 , pp. 834-840
    • Choudhary, C.1
  • 4
    • 84869215170 scopus 로고    scopus 로고
    • Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae
    • Henriksen P, et al. (2012) Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Mol Cell Proteomics 11(11):1510-1522.
    • (2012) Mol Cell Proteomics , vol.11 , Issue.11 , pp. 1510-1522
    • Henriksen, P.1
  • 5
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim SC, et al. (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 23(4):607-618.
    • (2006) Mol Cell , vol.23 , Issue.4 , pp. 607-618
    • Kim, S.C.1
  • 6
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang Q, et al. (2010) Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 327(5968):1004-1007.
    • (2010) Science , vol.327 , Issue.5968 , pp. 1004-1007
    • Wang, Q.1
  • 7
    • 79960797509 scopus 로고    scopus 로고
    • Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation
    • Weinert BT, et al. (2011) Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Sci Signal 4(183):ra48.
    • (2011) Sci Signal , vol.4 , Issue.183
    • Weinert, B.T.1
  • 8
    • 61649089277 scopus 로고    scopus 로고
    • Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli
    • Zhang J, et al. (2009) Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics 8(2):215-225.
    • (2009) Mol Cell Proteomics , vol.8 , Issue.2 , pp. 215-225
    • Zhang, J.1
  • 9
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao S, et al. (2010) Regulation of cellular metabolism by protein lysine acetylation. Science 327(5968):1000-1004.
    • (2010) Science , vol.327 , Issue.5968 , pp. 1000-1004
    • Zhao, S.1
  • 10
    • 84865726581 scopus 로고    scopus 로고
    • Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns
    • Lundby A, et al. (2012) Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Cell Rep 2(2):419-431.
    • (2012) Cell Rep , vol.2 , Issue.2 , pp. 419-431
    • Lundby, A.1
  • 11
    • 80053450838 scopus 로고    scopus 로고
    • Regulation of septin dynamics by the Saccharomyces cerevisiae lysine acetyltransferase NuA4
    • Mitchell L, et al. (2011) Regulation of septin dynamics by the Saccharomyces cerevisiae lysine acetyltransferase NuA4. PLoS ONE 6(10):e25336.
    • (2011) PLoS ONE , vol.6 , Issue.10
    • Mitchell, L.1
  • 12
    • 84860848452 scopus 로고    scopus 로고
    • Exploring the yeast acetylome using functional genomics
    • Kaluarachchi Duffy S, et al. (2012) Exploring the yeast acetylome using functional genomics. Cell 149(4):936-948.
    • (2012) Cell , vol.149 , Issue.4 , pp. 936-948
    • Kaluarachchi Duffy, S.1
  • 13
    • 62149143727 scopus 로고    scopus 로고
    • Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis
    • Lin YY, et al. (2009) Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell 136(6):1073-1084.
    • (2009) Cell , vol.136 , Issue.6 , pp. 1073-1084
    • Lin, Y.Y.1
  • 14
    • 1942439646 scopus 로고    scopus 로고
    • The highly conserved and multifunctional NuA4 HAT complex
    • Doyon Y, Côté J (2004) The highly conserved and multifunctional NuA4 HAT complex. Curr Opin Genet Dev 14(2):147-154.
    • (2004) Curr Opin Genet Dev , vol.14 , Issue.2 , pp. 147-154
    • Doyon, Y.1    Côté, J.2
  • 15
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransfer-ase complex containing Esa1p and the ATM-related cofactor Tra1p
    • Allard S, et al. (1999) NuA4, an essential transcription adaptor/histone H4 acetyltransfer-ase complex containing Esa1p and the ATM-related cofactor Tra1p. EMBO J 18(18): 5108-5119.
    • (1999) EMBO J , vol.18 , Issue.18 , pp. 5108-5119
    • Allard, S.1
  • 16
    • 66149100528 scopus 로고    scopus 로고
    • A novel proteomics approach for the discovery of chromatin-associated protein networks
    • Lambert JP, Mitchell L, Rudner A, Baetz K, Figeys D (2009) A novel proteomics approach for the discovery of chromatin-associated protein networks. Mol Cell Proteomics 8(4):870-882.
    • (2009) Mol Cell Proteomics , vol.8 , Issue.4 , pp. 870-882
    • Lambert, J.P.1    Mitchell, L.2    Rudner, A.3    Baetz, K.4    Figeys, D.5
  • 17
    • 78650643943 scopus 로고    scopus 로고
    • Defining the budding yeast chromatin-associated interactome
    • Lambert JP, et al. (2010) Defining the budding yeast chromatin-associated interactome. Mol Syst Biol 6:448.
    • (2010) Mol Syst Biol , vol.6 , pp. 448
    • Lambert, J.P.1
  • 18
    • 79952263955 scopus 로고    scopus 로고
    • Srf1 is a novel regulator of phospholipase D activity and is essential to buffer the toxic effects of C16:0 platelet activating factor
    • Kennedy MA, et al. (2011) Srf1 is a novel regulator of phospholipase D activity and is essential to buffer the toxic effects of C16:0 platelet activating factor. PLoS Genet 7 (2):e1001299.
    • (2011) PLoS Genet , vol.7 , Issue.2
    • Kennedy, M.A.1
  • 19
    • 0032965152 scopus 로고    scopus 로고
    • Esa1p is an essential histone acetyltransferase required for cell cycle progression
    • Clarke AS, Lowell JE, Jacobson SJ, Pillus L (1999) Esa1p is an essential histone acetyltransferase required for cell cycle progression. Mol Cell Biol 19(4):2515-2526.
    • (1999) Mol Cell Biol , vol.19 , Issue.4 , pp. 2515-2526
    • Clarke, A.S.1    Lowell, J.E.2    Jacobson, S.J.3    Pillus, L.4
  • 20
    • 41149083933 scopus 로고    scopus 로고
    • Functional dissection of the NuA4 histone acetyltransferase reveals its role as a genetic hub and that Eaf1 is essential for complex integrity
    • Mitchell L, et al. (2008) Functional dissection of the NuA4 histone acetyltransferase reveals its role as a genetic hub and that Eaf1 is essential for complex integrity. Mol Cell Biol 28(7):2244-2256.
    • (2008) Mol Cell Biol , vol.28 , Issue.7 , pp. 2244-2256
    • Mitchell, L.1
  • 21
    • 46949104585 scopus 로고    scopus 로고
    • The interaction network of the chaperonin CCT
    • Dekker C, et al. (2008) The interaction network of the chaperonin CCT. EMBO J 27(13): 1827-1839.
    • (2008) EMBO J , vol.27 , Issue.13 , pp. 1827-1839
    • Dekker, C.1
  • 22
    • 34247565469 scopus 로고    scopus 로고
    • Functional and physical interactions between yeast 14-3-3 proteins, acetyltransferases, and deacetylases in response to DNA replication perturbations
    • Lottersberger F, Panza A, Lucchini G, Longhese MP (2007) Functional and physical interactions between yeast 14-3-3 proteins, acetyltransferases, and deacetylases in response to DNA replication perturbations. Mol Cell Biol 27(9):3266-3281.
    • (2007) Mol Cell Biol , vol.27 , Issue.9 , pp. 3266-3281
    • Lottersberger, F.1    Panza, A.2    Lucchini, G.3    Longhese, M.P.4
  • 23
    • 4344705968 scopus 로고    scopus 로고
    • The budding yeast spindle pole body: Structure, duplication, and function
    • Jaspersen SL, Winey M (2004) The budding yeast spindle pole body: Structure, duplication, and function. Annu Rev Cell Dev Biol 20:1-28.
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 1-28
    • Jaspersen, S.L.1    Winey, M.2
  • 24
    • 0032536209 scopus 로고    scopus 로고
    • Epsilon-COP is a structural component of coatomer that functions to stabilize alpha-COP
    • Duden R, Kajikawa L, Wuestehube L, Schekman R (1998) Epsilon-COP is a structural component of coatomer that functions to stabilize alpha-COP. EMBO J 17(4):985-995.
    • (1998) EMBO J , vol.17 , Issue.4 , pp. 985-995
    • Duden, R.1    Kajikawa, L.2    Wuestehube, L.3    Schekman, R.4
  • 25
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino JS, Glick BS (2004) The mechanisms of vesicle budding and fusion. Cell 116(2):153-166.
    • (2004) Cell , vol.116 , Issue.2 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 26
    • 77955099645 scopus 로고    scopus 로고
    • Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae
    • Swisher KD, Parker R (2010) Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae. PLoS ONE 5(4):e10006.
    • (2010) PLoS ONE , vol.5 , Issue.4
    • Swisher, K.D.1    Parker, R.2
  • 27
    • 26844433577 scopus 로고    scopus 로고
    • Proteasome-associated proteins: Regulation of a proteolytic machine
    • Schmidt M, Hanna J, Elsasser S, Finley D (2005) Proteasome-associated proteins: Regulation of a proteolytic machine. Biol Chem 386(8):725-737.
    • (2005) Biol Chem , vol.386 , Issue.8 , pp. 725-737
    • Schmidt, M.1    Hanna, J.2    Elsasser, S.3    Finley, D.4
  • 28
    • 84858430267 scopus 로고    scopus 로고
    • The 19S proteasome subcomplex promotes the targeting of NuA4 HAT to the promoters of ribosomal protein genes to facilitate the recruitment of TFIID for transcriptional initiation in vivo
    • Uprety B, et al. (2012) The 19S proteasome subcomplex promotes the targeting of NuA4 HAT to the promoters of ribosomal protein genes to facilitate the recruitment of TFIID for transcriptional initiation in vivo. Nucleic Acids Res 40(5):1969-1983.
    • (2012) Nucleic Acids Res , vol.40 , Issue.5 , pp. 1969-1983
    • Uprety, B.1
  • 29
    • 34547890019 scopus 로고    scopus 로고
    • Functions of site-specific histone acetylation and deacetylation
    • Shahbazian MD, Grunstein M (2007) Functions of site-specific histone acetylation and deacetylation. Annu Rev Biochem 76:75-100.
    • (2007) Annu Rev Biochem , vol.76 , pp. 75-100
    • Shahbazian, M.D.1    Grunstein, M.2
  • 30
    • 69549124552 scopus 로고    scopus 로고
    • Proteome-wide prediction of acetylation substrates
    • Basu A, et al. (2009) Proteome-wide prediction of acetylation substrates. Proc Natl Acad Sci USA 106(33):13785-13790.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.33 , pp. 13785-13790
    • Basu, A.1
  • 31
    • 84855341934 scopus 로고    scopus 로고
    • MYST protein acetyltransferase activity requires active site lysine autoacetylation
    • Yuan H, et al. (2012) MYST protein acetyltransferase activity requires active site lysine autoacetylation. EMBO J 31(1):58-70.
    • (2012) EMBO J , vol.31 , Issue.1 , pp. 58-70
    • Yuan, H.1
  • 32
    • 19344372948 scopus 로고    scopus 로고
    • A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin
    • Kobor MS, et al. (2004) A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin. PLoS Biol 2(5):E131.
    • (2004) PLoS Biol , vol.2 , Issue.5
    • Kobor, M.S.1
  • 33
    • 48749114997 scopus 로고    scopus 로고
    • A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation
    • Lin YY, et al. (2008) A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation. Genes Dev 22(15):2062-2074.
    • (2008) Genes Dev , vol.22 , Issue.15 , pp. 2062-2074
    • Lin, Y.Y.1
  • 34
    • 0037179692 scopus 로고    scopus 로고
    • Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair
    • Bird AW, et al. (2002) Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair. Nature 419(6905):411-415.
    • (2002) Nature , vol.419 , Issue.6905 , pp. 411-415
    • Bird, A.W.1
  • 35
    • 33846374117 scopus 로고    scopus 로고
    • Catalytic mechanism of a MYST family histone acetyltransferase
    • Berndsen CE, Albaugh BN, Tan S, Denu JM (2007) Catalytic mechanism of a MYST family histone acetyltransferase. Biochemistry 46(3):623-629.
    • (2007) Biochemistry , vol.46 , Issue.3 , pp. 623-629
    • Berndsen, C.E.1    Albaugh, B.N.2    Tan, S.3    Denu, J.M.4
  • 36
    • 0038284360 scopus 로고    scopus 로고
    • Yeast enhancer of polycomb defines global Esa1-dependent acetylation of chromatin
    • Boudreault AA, et al. (2003) Yeast enhancer of polycomb defines global Esa1-dependent acetylation of chromatin. Genes Dev 17(11):1415-1428.
    • (2003) Genes Dev , vol.17 , Issue.11 , pp. 1415-1428
    • Boudreault, A.A.1
  • 37
    • 20744445493 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes
    • Selleck W, Fortin I, Sermwittayawong D, Côté J, Tan S (2005) The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes. Mol Cell Biol 25(13):5535-5542.
    • (2005) Mol Cell Biol , vol.25 , Issue.13 , pp. 5535-5542
    • Selleck, W.1    Fortin, I.2    Sermwittayawong, D.3    Côté, J.4    Tan, S.5
  • 38
    • 67649921732 scopus 로고    scopus 로고
    • Regulation of centrosome separation in yeast and vertebrates: Common threads
    • Lim HH, Zhang T, Surana U (2009) Regulation of centrosome separation in yeast and vertebrates: Common threads. Trends Cell Biol 19(7):325-333.
    • (2009) Trends Cell Biol , vol.19 , Issue.7 , pp. 325-333
    • Lim, H.H.1    Zhang, T.2    Surana, U.3
  • 39
    • 4544262211 scopus 로고    scopus 로고
    • Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4
    • Krogan NJ, et al. (2004) Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4. Proc Natl Acad Sci USA 101(37):13513-13518.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.37 , pp. 13513-13518
    • Krogan, N.J.1
  • 40
    • 56049104028 scopus 로고    scopus 로고
    • The essential function of Swc4p - A protein shared by two chromatin-modifying complexes of the yeast Saccharomyces cerevisiae-resides within its N-terminal part
    • Miciałkiewicz A, Chełstowska A (2008) The essential function of Swc4p-a protein shared by two chromatin-modifying complexes of the yeast Saccharomyces cerevisiae-resides within its N-terminal part. Acta Biochim Pol 55(3):603-612.
    • (2008) Acta Biochim Pol , vol.55 , Issue.3 , pp. 603-612
    • Miciałkiewicz, A.1    Chełstowska, A.2
  • 41
    • 76049127469 scopus 로고    scopus 로고
    • Asf1-like structure of the conserved Yaf9 YEATS domain and role in H2A.Z deposition and acetylation
    • Wang AY, et al. (2009) Asf1-like structure of the conserved Yaf9 YEATS domain and role in H2A.Z deposition and acetylation. Proc Natl Acad Sci USA 106(51):21573-21578.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.51 , pp. 21573-21578
    • Wang, A.Y.1
  • 42
    • 0042470632 scopus 로고    scopus 로고
    • Yaf9, a novel NuA4 histone acetyltransferase subunit, is required for the cellular response to spindle stress in yeast
    • Le Masson I, et al. (2003) Yaf9, a novel NuA4 histone acetyltransferase subunit, is required for the cellular response to spindle stress in yeast. Mol Cell Biol 23(17):6086-6102.
    • (2003) Mol Cell Biol , vol.23 , Issue.17 , pp. 6086-6102
    • Le Masson, I.1
  • 43
    • 34250640741 scopus 로고    scopus 로고
    • Actin-related protein Arp4 functions in kinetochore assembly
    • Ogiwara H, et al. (2007) Actin-related protein Arp4 functions in kinetochore assembly. Nucleic Acids Res 35(9):3109-3117.
    • (2007) Nucleic Acids Res , vol.35 , Issue.9 , pp. 3109-3117
    • Ogiwara, H.1
  • 44
    • 45149109211 scopus 로고    scopus 로고
    • Catalytic-site mutations in the MYST family histone acetyltransferase Esa1
    • Decker PV, Yu DY, Iizuka M, Qiu Q, Smith MM (2008) Catalytic-site mutations in the MYST family histone acetyltransferase Esa1. Genetics 178(3):1209-1220.
    • (2008) Genetics , vol.178 , Issue.3 , pp. 1209-1220
    • Decker, P.V.1    Yu, D.Y.2    Iizuka, M.3    Qiu, Q.4    Smith, M.M.5
  • 45
    • 33644778778 scopus 로고    scopus 로고
    • A DNA integrity network in the yeast Saccharomyces cerevisiae
    • Pan X, et al. (2006) A DNA integrity network in the yeast Saccharomyces cerevisiae. Cell 124(5):1069-1081.
    • (2006) Cell , vol.124 , Issue.5 , pp. 1069-1081
    • Pan, X.1
  • 46
    • 75649111192 scopus 로고    scopus 로고
    • The genetic landscape of a cell
    • Costanzo M, et al. (2010) The genetic landscape of a cell. Science 327(5964):425-431.
    • (2010) Science , vol.327 , Issue.5964 , pp. 425-431
    • Costanzo, M.1
  • 47
    • 75749095658 scopus 로고    scopus 로고
    • Integrating high-throughput genetic interaction mapping and high-content screening to explore yeast spindle morphogenesis
    • Vizeacoumar FJ, et al. (2010) Integrating high-throughput genetic interaction mapping and high-content screening to explore yeast spindle morphogenesis. J Cell Biol 188(1):69-81.
    • (2010) J Cell Biol , vol.188 , Issue.1 , pp. 69-81
    • Vizeacoumar, F.J.1
  • 48
    • 33644555054 scopus 로고    scopus 로고
    • Proteome survey reveals modularity of the yeast cell machinery
    • Gavin AC, et al. (2006) Proteome survey reveals modularity of the yeast cell machinery. Nature 440(7084):631-636.
    • (2006) Nature , vol.440 , Issue.7084 , pp. 631-636
    • Gavin, A.C.1
  • 49
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y, et al. (2002) Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415(6868):180-183.
    • (2002) Nature , vol.415 , Issue.6868 , pp. 180-183
    • Ho, Y.1
  • 50
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan NJ, et al. (2006) Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440(7084):637-643.
    • (2006) Nature , vol.440 , Issue.7084 , pp. 637-643
    • Krogan, N.J.1
  • 51
    • 71949105211 scopus 로고    scopus 로고
    • NuA4 lysine acetyltransferase Esa1 is targeted to coding regions and stimulates transcription elongation with Gcn5
    • Ginsburg DS, Govind CK, Hinnebusch AG (2009) NuA4 lysine acetyltransferase Esa1 is targeted to coding regions and stimulates transcription elongation with Gcn5. Mol Cell Biol 29(24):6473-6487.
    • (2009) Mol Cell Biol , vol.29 , Issue.24 , pp. 6473-6487
    • Ginsburg, D.S.1    Govind, C.K.2    Hinnebusch, A.G.3
  • 52
    • 1642499365 scopus 로고    scopus 로고
    • The ctf13-30/CTF13 genomic haploinsufficiency modifier screen identifies the yeast chromatin remodeling complex RSC, which is required for the establishment of sister chromatid cohesion
    • Baetz KK, Krogan NJ, Emili A, Greenblatt J, Hieter P (2004) The ctf13-30/CTF13 genomic haploinsufficiency modifier screen identifies the yeast chromatin remodeling complex RSC, which is required for the establishment of sister chromatid cohesion. Mol Cell Biol 24(3):1232-1244.
    • (2004) Mol Cell Biol , vol.24 , Issue.3 , pp. 1232-1244
    • Baetz, K.K.1    Krogan, N.J.2    Emili, A.3    Greenblatt, J.4    Hieter, P.5
  • 53
    • 0034699391 scopus 로고    scopus 로고
    • Chromodomains are protein-RNA interaction modules
    • Akhtar A, Zink D, Becker PB (2000) Chromodomains are protein-RNA interaction modules. Nature 407(6802):405-409.
    • (2000) Nature , vol.407 , Issue.6802 , pp. 405-409
    • Akhtar, A.1    Zink, D.2    Becker, P.B.3
  • 54
    • 77954310096 scopus 로고    scopus 로고
    • Structure of coatomer cage proteins and the relationship among COPI
    • Lee C, Goldberg J (2010) Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats. Cell 142(1):123-132.
    • (2010) COPII, and Clathrin Vesicle Coats. Cell , vol.142 , Issue.1 , pp. 123-132
    • Lee, C.1    Goldberg, J.2
  • 55
    • 49749106279 scopus 로고    scopus 로고
    • Linking the kinome and phosphorylome-A comprehensive review of approaches to find kinase targets
    • Sopko R, Andrews BJ (2008) Linking the kinome and phosphorylome-A comprehensive review of approaches to find kinase targets. Mol Biosyst 4(9):920-933.
    • (2008) Mol Biosyst , vol.4 , Issue.9 , pp. 920-933
    • Sopko, R.1    Andrews, B.J.2
  • 56
    • 84864213113 scopus 로고    scopus 로고
    • Systematic functional prioritization of protein posttranslational modifications
    • Beltrao P, et al. (2012) Systematic functional prioritization of protein posttranslational modifications. Cell 150(2):413-425.
    • (2012) Cell , vol.150 , Issue.2 , pp. 413-425
    • Beltrao, P.1
  • 57
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine MS, et al. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14(10):953-961.
    • (1998) Yeast , vol.14 , Issue.10 , pp. 953-961
    • Longtine, M.S.1
  • 58
    • 71949107814 scopus 로고    scopus 로고
    • Analysis of low-abundance proteins using the proteomic reactor with pH fractionation
    • Zhou H, Hou W, Lambert JP, Tian R, Figeys D (2010) Analysis of low-abundance proteins using the proteomic reactor with pH fractionation. Talanta 80(4):1526-1531.
    • (2010) Talanta , vol.80 , Issue.4 , pp. 1526-1531
    • Zhou, H.1    Hou, W.2    Lambert, J.P.3    Tian, R.4    Figeys, D.5
  • 59
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm M, et al. (1996) Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379(6564):466-469.
    • (1996) Nature , vol.379 , Issue.6564 , pp. 466-469
    • Wilm, M.1
  • 61
    • 40849098073 scopus 로고    scopus 로고
    • Chromatin-associated genes protect the yeast genome from Ty1 insertional mutagenesis
    • Nyswaner KM, Checkley MA, Yi M, Stephens RM, Garfinkel DJ (2008) Chromatin-associated genes protect the yeast genome from Ty1 insertional mutagenesis. Genetics 178(1):197-214.
    • (2008) Genetics , vol.178 , Issue.1 , pp. 197-214
    • Nyswaner, K.M.1    Checkley, M.A.2    Yi, M.3    Stephens, R.M.4    Garfinkel, D.J.5
  • 62
    • 0142184341 scopus 로고    scopus 로고
    • Global analysis of protein localization in budding yeast
    • Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-691.
    • (2003) Nature , vol.425 , Issue.6959 , pp. 686-691
    • Huh, W.K.1


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