메뉴 건너뛰기




Volumn 9, Issue 7, 2014, Pages

Timely activation of budding yeast APCCdh1 involves degradation of its inhibitor, Acm1, by an unconventional proteolytic mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ACM1 PROTEIN; ANAPHASE PROMOTING COMPLEX; CELL CYCLE PROTEIN 20; ENZYME INHIBITOR; POLYUBIQUITIN; PROTEASOME; PROTEIN UBA1; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; UVOMORULIN; ACM1 PROTEIN, S CEREVISIAE; ATP DEPENDENT 26S PROTEASE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CDH1 PROTEIN, S CEREVISIAE; CELL CYCLE PROTEIN; CYCLIN DEPENDENT KINASE; FIZZY RELATED PROTEIN; LEUPEPTIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84904968816     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0103517     Document Type: Article
Times cited : (5)

References (56)
  • 2
    • 70549105793 scopus 로고    scopus 로고
    • Control of cell growth by the SCF and APC/C ubiquitin ligases
    • Skaar JR, Pagano M (2009) Control of cell growth by the SCF and APC/C ubiquitin ligases. Curr Opin Cell Biol 21: 816-824.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 816-824
    • Skaar, J.R.1    Pagano, M.2
  • 3
  • 4
    • 0031772952 scopus 로고    scopus 로고
    • SCF and APC: The yin and yang of cell cycle regulated proteolysis
    • Peters J-M (1998) SCF and APC: the yin and yang of cell cycle regulated proteolysis. Curr Opin Cell Biol 10: 759-768.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 759-768
    • Peters, J.-M.1
  • 5
    • 4544276433 scopus 로고    scopus 로고
    • APC/C and SCF: Controlling each other and the cell cycle
    • Vodermaier HC (2004) APC/C and SCF: Controlling each other and the cell cycle. Curr Biol 14: R787-796.
    • (2004) Curr Biol , vol.14
    • Vodermaier, H.C.1
  • 6
    • 9644273891 scopus 로고    scopus 로고
    • A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
    • DOI 10.1016/j.bbamcr.2004.09.027, PII S0167488904002459, The Ubiquitin-Proteasome System
    • Willems AR, Schwab M, Tyers M (2004) A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. Biochim Biophys Acta 1695: 133-170. (Pubitemid 39574971)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 133-170
    • Willems, A.R.1    Schwab, M.2    Tyers, M.3
  • 7
    • 0036713310 scopus 로고    scopus 로고
    • The anaphase-promoting complex: It's not just for mitosis any more
    • DOI 10.1101/gad.1013102
    • Harper JW, Burton JL, Solomon MJ (2002) The anaphase-promoting complex: it's not just for mitosis any more. Genes Dev 16: 2179-2206. (Pubitemid 35013081)
    • (2002) Genes and Development , vol.16 , Issue.17 , pp. 2179-2206
    • Wade, H.J.1    Burton, J.L.2    Solomon, M.J.3
  • 8
    • 33747589184 scopus 로고    scopus 로고
    • The anaphase promoting complex/cyclosome: A machine designed to destroy
    • Peters JM (2006) The anaphase promoting complex/cyclosome: a machine designed to destroy. Nat Rev Mol Cell Biol 7: 644-656.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 644-656
    • Peters, J.M.1
  • 9
    • 49849098630 scopus 로고    scopus 로고
    • Regulation of APC/C activators in mitosis and meiosis
    • Pesin JA, Orr-Weaver TL (2008) Regulation of APC/C activators in mitosis and meiosis. Annu Rev Cell Dev Biol 24: 475-499.
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 475-499
    • Pesin, J.A.1    Orr-Weaver, T.L.2
  • 10
    • 34247135912 scopus 로고    scopus 로고
    • Cdh1 activity by Cdh1/Acm1/Bmh1 ternary complex formation
    • DOI 10.1074/jbc.M606589200
    • Dial JM, Petrotchenko EV, Borchers CH (2007) Inhibition of APCCdh1 activity by Cdh1/Acm1/Bmh1 ternary complex formation. J Biol Chem 282: 5237-5248. (Pubitemid 47093786)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5237-5248
    • Dial, J.M.1    Petrotchenko, E.V.2    Borchers, C.H.3
  • 11
    • 33845448198 scopus 로고    scopus 로고
    • Acm1 is a negative regulator of the Cdh1-dependent anaphase-promoting complex/cyclosome in budding yeast
    • DOI 10.1128/MCB.00603-06
    • Martinez JS, Jeong DE, Choi E, Billings BM, Hall MC (2006) Acm1 is a negative regulator of the Cdh1-dependent anaphase-promoting complex/cyclosome in budding yeast. Mol Cell Biol 26: 9162-9176. (Pubitemid 44904413)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.24 , pp. 9162-9176
    • Martinez, J.S.1    Jeong, D.-E.2    Choi, E.3    Billings, B.M.4    Hall, M.C.5
  • 12
    • 84856112461 scopus 로고    scopus 로고
    • Acm1 contributes to nuclear positioning by inhibiting Cdh1-substrate interactions
    • Martinez JS, Hall H, Bartolowits MD, Hall MC (2012) Acm1 contributes to nuclear positioning by inhibiting Cdh1-substrate interactions. Cell Cycle 11: 384-394.
    • (2012) Cell Cycle , vol.11 , pp. 384-394
    • Martinez, J.S.1    Hall, H.2    Bartolowits, M.D.3    Hall, M.C.4
  • 13
    • 43449139689 scopus 로고    scopus 로고
    • Modulation of the Mitotic Regulatory Network by APC-Dependent Destruction of the Cdh1 Inhibitor Acm1
    • DOI 10.1016/j.molcel.2008.04.004, PII S1097276508002645
    • Enquist-Newman M, Sullivan M, Morgan DO (2008) Modulation of the mitotic regulatory network by APC-dependent destruction of the Cdh1 inhibitor Acm1. Mol Cell 30: 437-446. (Pubitemid 351672373)
    • (2008) Molecular Cell , vol.30 , Issue.4 , pp. 437-446
    • Enquist-Newman, M.1    Sullivan, M.2    Morgan, D.O.3
  • 15
    • 44449087798 scopus 로고    scopus 로고
    • Cdc28 and Cdc14 Control Stability of the Anaphase-promoting Complex Inhibitor Acm1
    • Hall MC, Jeong DE, Henderson JT, Choi E, Bremmer SC, et al. (2008) Cdc28 and Cdc14 Control Stability of the Anaphase-promoting Complex Inhibitor Acm1. J Biol Chem 283: 10396-10407.
    • (2008) J Biol Chem , vol.283 , pp. 10396-10407
    • Hall, M.C.1    Jeong, D.E.2    Henderson, J.T.3    Choi, E.4    Bremmer, S.C.5
  • 16
    • 47949105016 scopus 로고    scopus 로고
    • Pseudosubstrate inhibition of the anaphase-promoting complex by Acm1: Regulation by proteolysis and Cdc28 phosphorylation
    • Ostapenko D, Burton JL, Wang R, Solomon MJ (2008) Pseudosubstrate inhibition of the anaphase-promoting complex by Acm1: regulation by proteolysis and Cdc28 phosphorylation. Mol Cell Biol 28: 4653-4664.
    • (2008) Mol Cell Biol , vol.28 , pp. 4653-4664
    • Ostapenko, D.1    Burton, J.L.2    Wang, R.3    Solomon, M.J.4
  • 17
    • 0344668551 scopus 로고    scopus 로고
    • Securin and B-cyclin/CDK are the only essential targets of the APC
    • DOI 10.1038/ncb1066
    • Thornton BR, Toczyski DP (2003) Securin and B-cyclin/CDK are the only essential targets of the APC. Nat Cell Biol 5: 1090-1094. (Pubitemid 37509116)
    • (2003) Nature Cell Biology , vol.5 , Issue.12 , pp. 1090-1094
    • Thornton, B.R.1    Toczyski, D.P.2
  • 18
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex- linked Ring10 gene, codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins
    • Heinemeyer W, Gruhler A, Möhrle V, Mahé Y, Wolf DH (1993) PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins. Journal of Biological Chemistry 268: 5115-5120. (Pubitemid 23081638)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.7 , pp. 5115-5120
    • Heinemeyer, W.1    Cruhler, A.2    Mohrle, V.3    Mahe, Y.4    Wolf, D.H.5
  • 19
    • 0027444947 scopus 로고
    • S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase
    • DOI 10.1038/366358a0
    • Ghislain M, Udvardy A, Mann C (1993) S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature 366: 358-362. (Pubitemid 23349365)
    • (1993) Nature , vol.366 , Issue.6453 , pp. 358-362
    • Ghislain, M.1    Udvardy, A.2    Mann, C.3
  • 20
    • 34248180045 scopus 로고    scopus 로고
    • A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome
    • DOI 10.1091/mbc.E06-10-0965
    • Ghaboosi N, Deshaies RJ (2007) A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome. Mol Biol Cell 18: 1953-1963. (Pubitemid 46717574)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.5 , pp. 1953-1963
    • Ghaboosi, N.1    Deshaies, R.J.2
  • 21
    • 11244337377 scopus 로고    scopus 로고
    • Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme
    • DOI 10.1038/sj.emboj.7600473
    • Palanimurugan R, Scheel H, Hofmann K, Dohmen RJ (2004) Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme. EMBO J 23: 4857-4867. (Pubitemid 40069715)
    • (2004) EMBO Journal , vol.23 , Issue.24 , pp. 4857-4867
    • Palanimurugan, R.1    Scheel, H.2    Hofmann, K.3    Dohmen, R.J.4
  • 22
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell J, Shih S, Dunn R, Hicke L (1998) A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol Cell 1: 193-202. (Pubitemid 128378660)
    • (1998) Molecular Cell , vol.1 , Issue.2 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 23
    • 53049108497 scopus 로고    scopus 로고
    • Unique D box and KEN box sequences limit ubiquitination of Acm1 and promote pseudosubstrate inhibition of the anaphase-promoting complex
    • Choi E, Dial JM, Jeong D-E, Hall MC (2008) Unique D box and KEN box sequences limit ubiquitination of Acm1 and promote pseudosubstrate inhibition of the anaphase-promoting complex. J Biol Chem 283: 23701-23710.
    • (2008) J Biol Chem , vol.283 , pp. 23701-23710
    • Choi, E.1    Dial, J.M.2    Jeong, D.-E.3    Hall, M.C.4
  • 24
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • DOI 10.1146/annurev.biochem.68.1.1015
    • Voges D, Zwickl P, Baumeister W (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 68: 1015-1068. (Pubitemid 29449214)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 25
    • 9644300915 scopus 로고    scopus 로고
    • The proteasome: A proteolytic nanomachine of cell regulation and waste disposal
    • DOI 10.1016/j.bbamcr.2004.10.007, PII S0167488904002587, The Ubiquitin-Proteasome System
    • Wolf DH, Hilt W (2004) The proteasome: a proteolytic nanomachine of cell regulation and waste disposal. Biochim Biophys Acta 1695: 19-31. (Pubitemid 39574965)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 19-31
    • Wolf, D.H.1    Hilt, W.2
  • 26
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • DOI 10.1016/S0092-8674(94)90462-6
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, et al. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78: 761-771. (Pubitemid 24294452)
    • (1994) Cell , vol.78 , Issue.5 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 28
    • 56249108370 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of proteins by the proteasome
    • Jariel-Encontre I, Bossis G, Piechaczyk M (2008) Ubiquitin-independent degradation of proteins by the proteasome. Biochim Biophys Acta 1786: 153-177.
    • (2008) Biochim Biophys Acta , vol.1786 , pp. 153-177
    • Jariel-Encontre, I.1    Bossis, G.2    Piechaczyk, M.3
  • 29
    • 0037834898 scopus 로고    scopus 로고
    • Ubiquitin-independent proteolytic functions of the proteasome
    • DOI 10.1016/S0003-9861(03)00197-8
    • Orlowski M, Wilk S (2003) Ubiquitin-independent proteolytic functions of the proteasome. Arch Biochem Biophys 415: 1-5. (Pubitemid 36687910)
    • (2003) Archives of Biochemistry and Biophysics , vol.415 , Issue.1 , pp. 1-5
    • Orlowski, M.1    Wilk, S.2
  • 30
    • 59649115172 scopus 로고    scopus 로고
    • Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination
    • Baugh JM, Viktorova EG, Pilipenko EV (2009) Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination. J Mol Biol 386: 814-827.
    • (2009) J Mol Biol , vol.386 , pp. 814-827
    • Baugh, J.M.1    Viktorova, E.G.2    Pilipenko, E.V.3
  • 31
    • 33748922985 scopus 로고    scopus 로고
    • 20S proteasomes and protein degradation "by default"
    • DOI 10.1002/bies.20447
    • Asher G, Reuven N, Shaul Y (2006) 20S proteasomes and protein degradation "by default". BioEssays 28: 844-849. (Pubitemid 44433746)
    • (2006) BioEssays , vol.28 , Issue.8 , pp. 844-849
    • Asher, G.1    Reuven, N.2    Shaul, Y.3
  • 32
    • 0036299065 scopus 로고    scopus 로고
    • Degradation of ornithine decarboxylase in Saccharomyces cerevisiae is ubiquitin independent
    • DOI 10.1016/S0006-291X(02)00194-8, PII S0006291X02001948
    • Gandre S, Kahana C (2002) Degradation of ornithine decarboxylase in Saccharomyces cerevisiae is ubiquitin independent. Biochem Biophys Res Commun 293: 139-144. (Pubitemid 34694182)
    • (2002) Biochemical and Biophysical Research Communications , vol.293 , Issue.1 , pp. 139-144
    • Gandre, S.1    Kahana, C.2
  • 34
    • 0035291218 scopus 로고    scopus 로고
    • Regulation of cellular polyamines by antizyme
    • Coffino P (2001) Regulation of cellular polyamines by antizyme. Nat Rev Mol Cell Biol 2: 188-194.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 188-194
    • Coffino, P.1
  • 35
    • 0027512650 scopus 로고
    • Degradation of ornithine decarboxylase: Exposure of the C-terminal target by a polyamine-inducible inhibitory protein
    • Li X, Coffino P (1993) Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein. Mol Cell Biol 13: 2377-2383. (Pubitemid 23097716)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.4 , pp. 2377-2383
    • Li, X.1    Coffino, P.2
  • 36
    • 0345701307 scopus 로고    scopus 로고
    • Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate
    • DOI 10.1093/emboj/cdg158
    • Zhang M, Pickart CM, Coffino P (2003) Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate. EMBO J 22: 1488-1496. (Pubitemid 36417398)
    • (2003) EMBO Journal , vol.22 , Issue.7 , pp. 1488-1496
    • Zhang, M.1    Pickart, C.M.2    Coffino, P.3
  • 38
    • 35348851301 scopus 로고    scopus 로고
    • Antizyme1 mediates AURKAIP1-dependent degradation of Aurora-A
    • DOI 10.1038/sj.onc.1210482, PII 1210482
    • Lim SK, Gopalan G (2007) Antizyme1 mediates AURKAIP1-dependent degradation of Aurora-A. Oncogene 26: 6593-6603. (Pubitemid 47573681)
    • (2007) Oncogene , vol.26 , Issue.46 , pp. 6593-6603
    • Lim, S.K.1    Gopalan, G.2
  • 39
    • 13244275245 scopus 로고    scopus 로고
    • A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73
    • DOI 10.1101/gad.319905
    • Asher G, Tsvetkov P, Kahana C, Shaul Y (2005) A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73. Genes Dev 19: 316-321. (Pubitemid 40189294)
    • (2005) Genes and Development , vol.19 , Issue.3 , pp. 316-321
    • Asher, G.1    Tsvetkov, P.2    Kahana, C.3    Shaul, Y.4
  • 40
    • 34250342888 scopus 로고    scopus 로고
    • Ubiquitin-Independent Degradation of Cell-Cycle Inhibitors by the REGgamma Proteasome
    • DOI 10.1016/j.molcel.2007.05.022, PII S1097276507003231
    • Chen X, Barton LF, Chi Y, Clurman BE, Roberts JM (2007) Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome. Mol Cell 26: 843-852. (Pubitemid 46921008)
    • (2007) Molecular Cell , vol.26 , Issue.6 , pp. 843-852
    • Chen, X.1    Barton, L.F.2    Chi, Y.3    Clurman, B.E.4    Roberts, J.M.5
  • 42
    • 34250339984 scopus 로고    scopus 로고
    • Ubiquitin- and ATP-Independent Proteolytic Turnover of p21 by the REGgamma-Proteasome Pathway
    • DOI 10.1016/j.molcel.2007.05.028, PII S1097276507003292
    • Li X, Amazit L, Long W, Lonard DM, Monaco JJ, et al. (2007) Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway. Mol Cell 26: 831-842. (Pubitemid 46921009)
    • (2007) Molecular Cell , vol.26 , Issue.6 , pp. 831-842
    • Li, X.1    Amazit, L.2    Long, W.3    Lonard, D.M.4    Monaco, J.J.5    O'Malley, B.W.6
  • 44
    • 0037452979 scopus 로고    scopus 로고
    • Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein
    • DOI 10.1073/pnas.0538058100
    • Kalejta RF, Shenk T (2003) Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein. Proceedings of the National Academy of Sciences of the United States of America 100: 3263-3268. (Pubitemid 36356571)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.6 , pp. 3263-3268
    • Kalejta, R.F.1    Shenk, T.2
  • 45
    • 28444437051 scopus 로고    scopus 로고
    • MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein
    • DOI 10.1016/j.molcel.2005.10.017, PII S1097276505016874
    • Sdek P, Ying H, Chang DL, Qiu W, Zheng H, et al. (2005) MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein. Mol Cell 20: 699-708. (Pubitemid 41740692)
    • (2005) Molecular Cell , vol.20 , Issue.5 , pp. 699-708
    • Sdek, P.1    Ying, H.2    Chang, D.L.F.3    Qiu, W.4    Zheng, H.5    Touitou, R.6    Allday, M.J.7    Jim, X.Z.-X.8
  • 46
    • 0037435037 scopus 로고    scopus 로고
    • The structural determinants responsible for c-Fos protein proteasomal degradation differ according to the conditions of expression
    • DOI 10.1038/sj.onc.1206266
    • Ferrara P, Andermarcher E, Bossis G, Acquaviva C, Brockly F, et al. (2003) The structural determinants responsible for c-Fos protein proteasomal degradation differ according to the conditions of expression. Oncogene 22: 1461-1474. (Pubitemid 36390595)
    • (2003) Oncogene , vol.22 , Issue.10 , pp. 1461-1474
    • Ferrara, P.1    Andermarcher, E.2    Bossis, G.3    Acquaviva, C.4    Brockly, F.5    Jariel-Encontre, I.6    Piechaczyk, M.7
  • 47
    • 0142250763 scopus 로고    scopus 로고
    • Proteasome degradation: Enter the substrate
    • DOI 10.1016/j.tcb.2003.09.001
    • Forster A, Hill CP (2003) Proteasome degradation: enter the substrate. Trends Cell Biol 13: 550-553. (Pubitemid 37311393)
    • (2003) Trends in Cell Biology , vol.13 , Issue.11 , pp. 550-553
    • Forster, A.1    Hill, C.P.2
  • 48
    • 84875130745 scopus 로고    scopus 로고
    • Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs
    • Peth A, Kukushkin N, Bosse M, Goldberg AL (2013) Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs. J Biol Chem 288: 7781-7790.
    • (2013) J Biol Chem , vol.288 , pp. 7781-7790
    • Peth, A.1    Kukushkin, N.2    Bosse, M.3    Goldberg, A.L.4
  • 49
    • 0037011124 scopus 로고    scopus 로고
    • Cell cycle-dependent nuclear export of Cdh1p may contribute to the inactivation of APC/C (Cdh1)
    • Jaquenoud M, van Drogen F, Peter M (2002) Cell cycle-dependent nuclear export of Cdh1p may contribute to the inactivation of APC/C (Cdh1). EMBO J 21: 6515-6526.
    • (2002) EMBO J , vol.21 , pp. 6515-6526
    • Jaquenoud, M.1    Van Drogen, F.2    Peter, M.3
  • 50
    • 77949432153 scopus 로고    scopus 로고
    • Requirements and reasons for effective inhibition of the anaphase promoting complex activator CDH1
    • Robbins JA, Cross FR (2010) Requirements and reasons for effective inhibition of the anaphase promoting complex activator CDH1. Mol Biol Cell 21: 914-925.
    • (2010) Mol Biol Cell , vol.21 , pp. 914-925
    • Robbins, J.A.1    Cross, F.R.2
  • 52
    • 33644807842 scopus 로고    scopus 로고
    • Synthetic genetic array analysis in Saccharomyces cerevisiae
    • Tong AH, Boone C (2006) Synthetic genetic array analysis in Saccharomyces cerevisiae. Methods Mol Biol 313: 171-192.
    • (2006) Methods Mol Biol , vol.313 , pp. 171-192
    • Tong, A.H.1    Boone, C.2
  • 53
    • 34247574716 scopus 로고    scopus 로고
    • Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells
    • Liu C, Apodaca J, Davis LE, Rao H (2007) Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells. Biotechniques 42: 158, 160, 162.
    • (2007) Biotechniques , vol.42
    • Liu, C.1    Apodaca, J.2    Davis, L.E.3    Rao, H.4
  • 54
    • 20344370277 scopus 로고    scopus 로고
    • Purification of proteasomes, proteasome subcomplexes, and proteasome-associated proteins from budding yeast
    • Leggett DS, Glickman MH, Finley D (2005) Purification of proteasomes, proteasome subcomplexes, and proteasome-associated proteins from budding yeast. Methods Mol Biol 301: 57-70.
    • (2005) Methods Mol Biol , vol.301 , pp. 57-70
    • Leggett, D.S.1    Glickman, M.H.2    Finley, D.3
  • 55
    • 27644518292 scopus 로고    scopus 로고
    • Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates
    • DOI 10.1016/S0076-6879(05)98030-0, PII S0076687905980300, Ubiquitin and Protein Degradation (Part A)
    • Kisselev AF, Goldberg AL (2005) Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates. Methods Enzymol 398: 364-378. (Pubitemid 41578898)
    • (2005) Methods in Enzymology , vol.398 , pp. 364-378
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 56
    • 84855829744 scopus 로고    scopus 로고
    • Cdc14 Phosphatases Preferentially Dephosphorylate a Subset of Cyclin-dependent kinase (Cdk) Sites Containing Phosphoserine
    • Bremmer SC, Hall H, Martinez JS, Eissler CL, Hinrichsen TH, et al. (2012) Cdc14 Phosphatases Preferentially Dephosphorylate a Subset of Cyclin-dependent kinase (Cdk) Sites Containing Phosphoserine. J Biol Chem 287: 1662-1669.
    • (2012) J Biol Chem , vol.287 , pp. 1662-1669
    • Bremmer, S.C.1    Hall, H.2    Martinez, J.S.3    Eissler, C.L.4    Hinrichsen, T.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.