메뉴 건너뛰기




Volumn 20, Issue 2, 2013, Pages 194-201

Sequential primed kinases create a damage-responsive phosphodegron on Eco1

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 4; CELL CYCLE PROTEIN 7; CYCLIN DEPENDENT KINASE 1; FUNGAL PROTEIN; PROTEIN ECO1; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84873571350     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2478     Document Type: Article
Times cited : (63)

References (58)
  • 1
    • 70349546862 scopus 로고    scopus 로고
    • Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution
    • Holt, L.J. et al. Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325, 1682-1686 (2009).
    • (2009) Science , vol.325 , pp. 1682-1686
    • Holt, L.J.1
  • 2
    • 0242300176 scopus 로고    scopus 로고
    • Targets of the cyclin-dependent kinase Cdk1
    • Ubersax, J.A. et al. Targets of the cyclin-dependent kinase Cdk1. Nature 425, 859-864 (2003).
    • (2003) Nature , vol.425 , pp. 859-864
    • Ubersax, J.A.1
  • 3
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski, M.D. & Deshaies, R.J. Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 6, 9-20 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 4
    • 38549086019 scopus 로고    scopus 로고
    • FBW7 ubiquitin ligase: A tumour suppressor at the crossroads of cell division, growth and differentiation
    • Welcker, M. & Clurman, B.E. FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation. Nat. Rev. Cancer 8, 83-93 (2008).
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 83-93
    • Welcker, M.1    Clurman, B.E.2
  • 5
    • 0035969559 scopus 로고    scopus 로고
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
    • Nash, P. et al. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 414, 514-521 (2001).
    • (2001) Nature , vol.414 , pp. 514-521
    • Nash, P.1
  • 6
    • 34047249627 scopus 로고    scopus 로고
    • Structure of a Fbw7-Skp1-Cyclin e Complex: Multisite-Phosphorylated Substrate Recognition by SCF Ubiquitin Ligases
    • Hao, B., Oehlmann, S., Sowa, M.E., Harper, J.W. & Pavletich, N.P. Structure of a Fbw7-Skp1-Cyclin E Complex: Multisite-Phosphorylated Substrate Recognition by SCF Ubiquitin Ligases. Mol. Cell 26, 131-143 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 131-143
    • Hao, B.1    Oehlmann, S.2    Sowa, M.E.3    Harper, J.W.4    Pavletich, N.P.5
  • 7
    • 75649123435 scopus 로고    scopus 로고
    • Multisite phosphorylation of the Saccharomyces cerevisiae filamentous growth regulator Tec1 is required for its recognition by the E3 ubiquitin ligase adaptor Cdc4 and its subsequent destruction in vivo
    • Bao, M.Z., Shock, T.R. & Madhani, H.D. Multisite phosphorylation of the Saccharomyces cerevisiae filamentous growth regulator Tec1 is required for its recognition by the E3 ubiquitin ligase adaptor Cdc4 and its subsequent destruction in vivo. Eukaryot. Cell 9, 31-36 (2010).
    • (2010) Eukaryot. Cell , vol.9 , pp. 31-36
    • Bao, M.Z.1    Shock, T.R.2    Madhani, H.D.3
  • 8
    • 34047255191 scopus 로고    scopus 로고
    • Fbw7/hCDC4 dimerization regulates its substrate interactions
    • Welcker, M. & Clurman, B.E. Fbw7/hCDC4 dimerization regulates its substrate interactions. Cell Div. 2, 7 (2007).
    • (2007) Cell Div , vol.2 , pp. 7
    • Welcker, M.1    Clurman, B.E.2
  • 9
    • 34250017680 scopus 로고    scopus 로고
    • Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination
    • Tang, X. et al. Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination. Cell 129, 1165-1176 (2007).
    • (2007) Cell , vol.129 , pp. 1165-1176
    • Tang, X.1
  • 10
    • 79955514366 scopus 로고    scopus 로고
    • Cdk1-dependent destruction of Eco1 prevents cohesion establishment after S phase
    • Lyons, N.A. & Morgan, D.O. Cdk1-dependent destruction of Eco1 prevents cohesion establishment after S phase. Mol. Cell 42, 378-389 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 378-389
    • Lyons, N.A.1    Morgan, D.O.2
  • 11
    • 48249132443 scopus 로고    scopus 로고
    • Eco1-dependent cohesin acetylation during establishment of sister chromatid cohesion
    • Rolef Ben-Shahar, T. et al. Eco1-dependent cohesin acetylation during establishment of sister chromatid cohesion. Science 321, 563-566 (2008).
    • (2008) Science , vol.321 , pp. 563-566
    • Rolef Ben-Shahar, T.1
  • 12
    • 62549149415 scopus 로고    scopus 로고
    • Building sister chromatid cohesion: Smc3 acetylation counteracts an antiestablishment activity
    • Rowland, B.D. et al. Building sister chromatid cohesion: smc3 acetylation counteracts an antiestablishment activity. Mol. Cell 33, 763-774 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 763-774
    • Rowland, B.D.1
  • 13
    • 62549130668 scopus 로고    scopus 로고
    • Budding yeast Wpl1(Rad61)-Pds5 complex counteracts sister chromatid cohesion-establishing reaction
    • Sutani, T., Kawaguchi, T., Kanno, R., Itoh, T. & Shirahige, K. Budding yeast Wpl1(Rad61)-Pds5 complex counteracts sister chromatid cohesion-establishing reaction. Curr. Biol. 19, 492-497 (2009).
    • (2009) Curr. Biol , vol.19 , pp. 492-497
    • Sutani, T.1    Kawaguchi, T.2    Kanno, R.3    Itoh, T.4    Shirahige, K.5
  • 14
    • 48249142388 scopus 로고    scopus 로고
    • A molecular determinant for the establishment of sister chromatid cohesion
    • Unal, E. et al. A molecular determinant for the establishment of sister chromatid cohesion. Science 321, 566-569 (2008).
    • (2008) Science , vol.321 , pp. 566-569
    • Unal, E.1
  • 15
    • 34447549077 scopus 로고    scopus 로고
    • Postreplicative formation of cohesion is required for repair and induced by a single DNA break
    • Ström, L. et al. Postreplicative formation of cohesion is required for repair and induced by a single DNA break. Science 317, 242-245 (2007).
    • (2007) Science , vol.317 , pp. 242-245
    • Ström, L.1
  • 16
    • 10944232673 scopus 로고    scopus 로고
    • Postreplicative recruitment of cohesin to double-strand breaks is required for DNA repair
    • Ström, L., Lindroos, H.B., Shirahige, K. & Sjogren, C. Postreplicative recruitment of cohesin to double-strand breaks is required for DNA repair. Mol. Cell 16, 1003-1015 (2004).
    • (2004) Mol. Cell , vol.16 , pp. 1003-1015
    • Ström, L.1    Lindroos, H.B.2    Shirahige, K.3    Sjogren, C.4
  • 17
    • 34447536708 scopus 로고    scopus 로고
    • DNA double-strand breaks trigger genome-wide sister-chromatid cohesion through Eco1 (Ctf7
    • Unal, E., Heidinger-Pauli, J.M. & Koshland, D. DNA double-strand breaks trigger genome-wide sister-chromatid cohesion through Eco1 (Ctf7). Science 317, 245-248 (2007).
    • (2007) Science , vol.317 , pp. 245-248
    • Unal, E.1    Heidinger-Pauli, J.M.2    Koshland, D.3
  • 18
    • 0035954251 scopus 로고    scopus 로고
    • Sister chromatid cohesion is required for postreplicative double-strand break repair in Saccharomyces cerevisiae
    • Sjögren, C. & Nasmyth, K. Sister chromatid cohesion is required for postreplicative double-strand break repair in Saccharomyces cerevisiae. Curr. Biol. 11, 991-995 (2001).
    • (2001) Curr. Biol , vol.11 , pp. 991-995
    • Sjögren, C.1    Nasmyth, K.2
  • 19
    • 46149118183 scopus 로고    scopus 로고
    • The kleisin subunit of cohesin dictates damage-induced cohesion
    • Heidinger-Pauli, J.M., Unal, E., Guacci, V. & Koshland, D. The kleisin subunit of cohesin dictates damage-induced cohesion. Mol. Cell 31, 47-56 (2008).
    • (2008) Mol. Cell , vol.31 , pp. 47-56
    • Heidinger-Pauli, J.M.1    Unal, E.2    Guacci, V.3    Koshland, D.4
  • 20
    • 65549132836 scopus 로고    scopus 로고
    • Distinct targets of the Eco1 acetyltransferase modulate cohesion in S phase and in response to DNA damage
    • Heidinger-Pauli, J.M., Unal, E. & Koshland, D. Distinct targets of the Eco1 acetyltransferase modulate cohesion in S phase and in response to DNA damage. Mol. Cell 34, 311-321 (2009).
    • (2009) Mol. Cell , vol.34 , pp. 311-321
    • Heidinger-Pauli, J.M.1    Unal, E.2    Koshland, D.3
  • 22
    • 33746849859 scopus 로고    scopus 로고
    • CDC7 kinase phosphorylates serine residues adjacent to acidic amino acids in the minichromosome maintenance 2 protein
    • Cho, W.H., Lee, Y.J., Kong, S.I., Hurwitz, J. & Lee, J.K. CDC7 kinase phosphorylates serine residues adjacent to acidic amino acids in the minichromosome maintenance 2 protein. Proc. Natl. Acad. Sci. USA 103, 11521-11526 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11521-11526
    • Cho, W.H.1    Lee, Y.J.2    Kong, S.I.3    Hurwitz, J.4    Lee, J.K.5
  • 23
    • 0034666016 scopus 로고    scopus 로고
    • Human Cdc7-related kinase complex. in vitro phosphorylation of MCM by concerted actions of Cdks and Cdc7 and that of a criticial threonine residue of Cdc7 by Cdks
    • Masai, H. et al. Human Cdc7-related kinase complex. In vitro phosphorylation of MCM by concerted actions of Cdks and Cdc7 and that of a criticial threonine residue of Cdc7 bY Cdks. J. Biol. Chem. 275, 29042-29052 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 29042-29052
    • Masai, H.1
  • 24
    • 77952986553 scopus 로고    scopus 로고
    • Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs
    • Mok, J. et al. Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs. Sci. Signal. 3, ra12 (2010).
    • (2010) Sci. Signal , vol.3
    • Mok, J.1
  • 25
    • 78149462002 scopus 로고    scopus 로고
    • Mec1 is one of multiple kinases that prime the Mcm2-7 helicase for phosphorylation by Cdc7
    • Randell, J.C. et al. Mec1 is one of multiple kinases that prime the Mcm2-7 helicase for phosphorylation by Cdc7. Mol. Cell 40, 353-363 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 353-363
    • Randell, J.C.1
  • 26
    • 0032997267 scopus 로고    scopus 로고
    • Cell cycle control of Cdc7p kinase activity through regulation of Dbf4p stability
    • Oshiro, G., Owens, J.C., Shellman, Y., Sclafani, R.A. & Li, J.J. Cell cycle control of Cdc7p kinase activity through regulation of Dbf4p stability. Mol. Cell. Biol. 19, 4888-4896 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 4888-4896
    • Oshiro, G.1    Owens, J.C.2    Shellman, Y.3    Sclafani, R.A.4    Li, J.J.5
  • 27
    • 50249127246 scopus 로고    scopus 로고
    • Cyclin-specific control of ribosomal DNA segregation
    • Sullivan, M., Holt, L. & Morgan, D.O. Cyclin-specific control of ribosomal DNA segregation. Mol. Cell. Biol. 28, 5328-5336 (2008).
    • (2008) Mol. Cell. Biol , vol.28 , pp. 5328-5336
    • Sullivan, M.1    Holt, L.2    Morgan, D.O.3
  • 28
    • 77953954908 scopus 로고    scopus 로고
    • How do Cdc7 and cyclin-dependent kinases trigger the initiation of chromosome replication in eukaryotic cells?
    • Labib, K. How do Cdc7 and cyclin-dependent kinases trigger the initiation of chromosome replication in eukaryotic cells? Genes Dev. 24, 1208-1219 (2010).
    • (2010) Genes Dev , vol.24 , pp. 1208-1219
    • Labib, K.1
  • 29
    • 58349100708 scopus 로고    scopus 로고
    • DDK is not just for replication
    • Marston, A.L. Meiosis: DDK is not just for replication. Curr. Biol. 19, R74-R76 (2009).
    • (2009) Curr. Biol , vol.19
    • Marston, A.L.1    Meiosis2
  • 30
    • 0027192941 scopus 로고
    • Cell cycle regulation of the yeast Cdc7 protein kinase by association with the Dbf4 protein
    • Jackson, A.L., Pahl, P.M., Harrison, K., Rosamond, J. & Sclafani, R.A. Cell cycle regulation of the yeast Cdc7 protein kinase by association with the Dbf4 protein. Mol. Cell. Biol. 13, 2899-2908 (1993).
    • (1993) Mol. Cell. Biol , vol.13 , pp. 2899-2908
    • Jackson, A.L.1    Pahl, P.M.2    Harrison, K.3    Rosamond, J.4    Sclafani, R.A.5
  • 31
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3 tricks of the trade for a multi-tasking kinase
    • Doble, B.W. & Woodgett, J.R. GSK-3: tricks of the trade for a multi-tasking kinase. J. Cell Sci. 116, 1175-1186 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 32
    • 0023656594 scopus 로고
    • Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3
    • Fiol, C.J., Mahrenholz, A.M., Wang, Y., Roeske, R.W. & Roach, P.J. Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3. J. Biol. Chem. 262, 14042-14048 (1987).
    • (1987) J. Biol. Chem , vol.262 , pp. 14042-14048
    • Fiol, C.J.1    Mahrenholz, A.M.2    Wang, Y.3    Roeske, R.W.4    Roach, P.J.5
  • 33
    • 74849138924 scopus 로고    scopus 로고
    • Regulation of protein stability by GSK3 mediated phosphorylation
    • Xu, C., Kim, N.G. & Gumbiner, B.M. Regulation of protein stability by GSK3 mediated phosphorylation. Cell Cycle 8, 4032-4039 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 4032-4039
    • Xu, C.1    Kim, N.G.2    Gumbiner, B.M.3
  • 35
    • 0035282915 scopus 로고    scopus 로고
    • GSK-3 kinase Mck1 and calcineurin coordinately mediate Hsl1 down-regulation by Ca2+ in budding yeast
    • Mizunuma, M., Hirata, D., Miyaoka, R. & Miyakawa, T. GSK-3 kinase Mck1 and calcineurin coordinately mediate Hsl1 down-regulation by Ca2+ in budding yeast. EMBO J. 20, 1074-1085 (2001).
    • (2001) EMBO J , vol.20 , pp. 1074-1085
    • Mizunuma, M.1    Hirata, D.2    Miyaoka, R.3    Miyakawa, T.4
  • 36
    • 36849020875 scopus 로고    scopus 로고
    • The SCFCdc4 ubiquitin ligase regulates calcineurin signaling through degradation of phosphorylated Rcn1, an inhibitor of calcineurin
    • Kishi, T., Ikeda, A., Nagao, R. & Koyama, N. The SCFCdc4 ubiquitin ligase regulates calcineurin signaling through degradation of phosphorylated Rcn1, an inhibitor of calcineurin. Proc. Natl. Acad. Sci. USA 104, 17418-17423 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17418-17423
    • Kishi, T.1    Ikeda, A.2    Nagao, R.3    Koyama, N.4
  • 37
    • 84872020666 scopus 로고    scopus 로고
    • A yeast GSK-3 kinase Mck1 promotes Cdc6 degradation to inhibit DNA re-replication
    • Ikui, A.E., Rossio, V., Schroeder, L. & Yoshida, S. A yeast GSK-3 kinase Mck1 promotes Cdc6 degradation to inhibit DNA re-replication. PLoS Genet. 8, e1003099 (2012).
    • (2012) PLoS Genet , vol.8
    • Ikui, A.E.1    Rossio, V.2    Schroeder, L.3    Yoshida, S.4
  • 38
    • 82555205273 scopus 로고    scopus 로고
    • Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phase
    • Kõivomägi, M. et al. Cascades of multisite phosphorylation control Sic1 destruction at the onset of S phase. Nature 480, 128-131 (2011).
    • (2011) Nature , vol.480 , pp. 128-131
    • Kõivomägi, M.1
  • 39
    • 84857698871 scopus 로고    scopus 로고
    • Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase
    • Tang, X. et al. Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase. Proc. Natl. Acad. Sci. USA 109, 3287-3292 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 3287-3292
    • Tang, X.1
  • 40
    • 78751531102 scopus 로고    scopus 로고
    • SCFCdc4 enables mating type switching in yeast by cyclin-dependent kinase-mediated elimination of the Ash1 transcriptional repressor
    • Liu, Q. et al. SCFCdc4 enables mating type switching in yeast by cyclin-dependent kinase-mediated elimination of the Ash1 transcriptional repressor. Mol. Cell. Biol. 31, 584-598 (2011).
    • (2011) Mol. Cell. Biol , vol.31 , pp. 584-598
    • Liu, Q.1
  • 41
    • 0034634576 scopus 로고    scopus 로고
    • Characterization of the yeast Cdc7p/Dbf4p complex purified from insect cells. Its protein kinase activity is regulated by Rad53p
    • Kihara, M. et al. Characterization of the yeast Cdc7p/Dbf4p complex purified from insect cells. Its protein kinase activity is regulated by Rad53p. J. Biol. Chem. 275, 35051-35062 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 35051-35062
    • Kihara, M.1
  • 42
    • 0033215306 scopus 로고    scopus 로고
    • Cdc7p-Dbf4p kinase binds to chromatin during S phase and is regulated by both the APC and the RAD53 checkpoint pathway
    • Weinreich, M. & Stillman, B. Cdc7p-Dbf4p kinase binds to chromatin during S phase and is regulated by both the APC and the RAD53 checkpoint pathway. EMBO J. 18, 5334-5346 (1999).
    • (1999) EMBO J , vol.18 , pp. 5334-5346
    • Weinreich, M.1    Stillman, B.2
  • 43
    • 0031435940 scopus 로고    scopus 로고
    • Mcm2 is a target of regulation by Cdc7-Dbf4 during the initiation of DNA synthesis
    • Lei, M. et al. Mcm2 is a target of regulation by Cdc7-Dbf4 during the initiation of DNA synthesis. Genes Dev. 11, 3365-3374 (1997).
    • (1997) Genes Dev , vol.11 , pp. 3365-3374
    • Lei, M.1
  • 44
    • 33745338567 scopus 로고    scopus 로고
    • A Dbf4p BRCA1 C-terminal-like domain required for the response to replication fork arrest in budding yeast
    • Gabrielse, C. et al. A Dbf4p BRCA1 C-terminal-like domain required for the response to replication fork arrest in budding yeast. Genetics 173, 541-555 (2006).
    • (2006) Genetics , vol.173 , pp. 541-555
    • Gabrielse, C.1
  • 45
    • 0034765174 scopus 로고    scopus 로고
    • Regulation of initiation of S phase, replication checkpoint signaling, and maintenance of mitotic chromosome structures during S phase by Hsk1 kinase in the fission yeast
    • Takeda, T. et al. Regulation of initiation of S phase, replication checkpoint signaling, and maintenance of mitotic chromosome structures during S phase by Hsk1 kinase in the fission yeast. Mol. Biol. Cell 12, 1257-1274 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1257-1274
    • Takeda, T.1
  • 46
    • 77957144885 scopus 로고    scopus 로고
    • Damage-induced phosphorylation of Sld3 is important to block late origin firing
    • Lopez-Mosqueda, J. et al. Damage-induced phosphorylation of Sld3 is important to block late origin firing. Nature 467, 479-483 (2010).
    • (2010) Nature , vol.467 , pp. 479-483
    • Lopez-Mosqueda, J.1
  • 47
    • 77957149919 scopus 로고    scopus 로고
    • Checkpoint-dependent inhibition of DNA replication initiation by Sld3 and Dbf4 phosphorylation
    • Zegerman, P. & Diffley, J.F. Checkpoint-dependent inhibition of DNA replication initiation by Sld3 and Dbf4 phosphorylation. Nature 467, 474-478 (2010).
    • (2010) Nature , vol.467 , pp. 474-478
    • Zegerman, P.1    Diffley, J.F.2
  • 48
    • 82455164158 scopus 로고    scopus 로고
    • Limiting replication initiation factors execute the temporal programme of origin firing in budding yeast
    • Mantiero, D., Mackenzie, A., Donaldson, A. & Zegerman, P. Limiting replication initiation factors execute the temporal programme of origin firing in budding yeast. EMBO J. 30, 4805-4814 (2011).
    • (2011) EMBO J , vol.30 , pp. 4805-4814
    • Mantiero, D.1    MacKenzie, A.2    Donaldson, A.3    Zegerman, P.4
  • 49
    • 84155171119 scopus 로고    scopus 로고
    • Origin association of Sld3, Sld7, and Cdc45 proteins is a key step for determination of origin-firing timing
    • Tanaka, S., Nakato, R., Katou, Y., Shirahige, K. & Araki, H. Origin association of Sld3, Sld7, and Cdc45 proteins is a key step for determination of origin-firing timing. Curr. Biol. 21, 2055-2063 (2011).
    • (2011) Curr. Biol , vol.21 , pp. 2055-2063
    • Tanaka, S.1    Nakato, R.2    Katou, Y.3    Shirahige, K.4    Araki, H.5
  • 50
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S. et al. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961 (1998).
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1
  • 51
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D.A., Washburn, M.P. & Yates, J.R. III. An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 73, 5683-5690 (2001).
    • (2001) Anal. Chem , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates Iii., J.R.3
  • 52
    • 84860636838 scopus 로고    scopus 로고
    • Single-step inline hydroxyapatite enrichment facilitates identification and quantitation of phosphopeptides from mass-limited proteomes with MudPIT
    • Fonslow, B.R. et al. Single-step inline hydroxyapatite enrichment facilitates identification and quantitation of phosphopeptides from mass-limited proteomes with MudPIT. J. Proteome Res. 11, 2697-2709 (2012).
    • (2012) J. Proteome Res , vol.11 , pp. 2697-2709
    • Fonslow, B.R.1
  • 53
    • 67449100431 scopus 로고    scopus 로고
    • Validation of tandem mass spectrometry database search results using DTASelect
    • Unit 13
    • Cociorva, D., Tabb, D.L. & Yates, J.R. Validation of tandem mass spectrometry database search results using DTASelect. Curr Protoc Bioinformatics Chapter 13, Unit 13 4 (2007).
    • (2007) Curr Protoc Bioinformatics Chapter 13 , pp. 4
    • Cociorva, D.1    Tabb, D.L.2    Yates, J.R.3
  • 54
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D.L., McDonald, W.H. & Yates, J.R. III. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 1, 21-26 (2002).
    • (2002) J. Proteome Res , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates Iii., J.R.3
  • 55
    • 3042824849 scopus 로고    scopus 로고
    • A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry
    • Schroeder, M.J., Shabanowitz, J., Schwartz, J.C., Hunt, D.F. & Coon, J.J. A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry. Anal. Chem. 76, 3590-3598 (2004).
    • (2004) Anal. Chem , vol.76 , pp. 3590-3598
    • Schroeder, M.J.1    Shabanowitz, J.2    Schwartz, J.C.3    Hunt, D.F.4    Coon, J.J.5
  • 56
    • 0038034116 scopus 로고    scopus 로고
    • Cleavage N-terminal to proline: Analysis of a database of peptide tandem mass spectra
    • Breci, L.A., Tabb, D.L., Yates, J.R. III & Wysocki, V.H. Cleavage N-terminal to proline: analysis of a database of peptide tandem mass spectra. Anal. Chem. 75, 1963-1971 (2003).
    • (2003) Anal. Chem , vol.75 , pp. 1963-1971
    • Breci, L.A.1    Tabb, D.L.2    Yates Iii., J.R.3    Wysocki, V.H.4
  • 57
    • 84863615204 scopus 로고    scopus 로고
    • Occurrence and detection of phosphopeptide isomers in large-scale phosphoproteomics experiments
    • Courcelles, M., Bridon, G., Lemieux, S. & Thibault, P. Occurrence and detection of phosphopeptide isomers in large-scale phosphoproteomics experiments. J. Proteome Res. 11, 3753-3765 (2012).
    • (2012) J. Proteome Res , vol.11 , pp. 3753-3765
    • Courcelles, M.1    Bridon, G.2    Lemieux, S.3    Thibault, P.4
  • 58
    • 14544270984 scopus 로고    scopus 로고
    • Cyclin specificity in the phosphorylation of cyclin-dependent kinase substrates
    • Loog, M. & Morgan, D.O. Cyclin specificity in the phosphorylation of cyclin-dependent kinase substrates. Nature 434, 104-108 (2005).
    • (2005) Nature , vol.434 , pp. 104-108
    • Loog, M.1    Morgan, D.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.