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Volumn 465, Issue 3, 2013, Pages 419-425

Frontiers of protein expression control with conditional degrons

Author keywords

Degron; Expression control; Proteasome; Protein degradation

Indexed keywords

AUXIN; FK 506 BINDING PROTEIN;

EID: 84878863921     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-012-1203-y     Document Type: Review
Times cited : (14)

References (45)
  • 1
    • 36749086400 scopus 로고    scopus 로고
    • An FKBP destabilization domain modulates protein levels in Plasmodium falciparum
    • 10.1038/nmeth1132 17994030 10.1038/nmeth1132 1:CAS:528:DC%2BD2sXhtlKlt7fK
    • Armstrong CM, Goldberg DE (2007) An FKBP destabilization domain modulates protein levels in Plasmodium falciparum. Nat Methods 4:1007-1009. doi: 10.1038/nmeth1132
    • (2007) Nat Methods , vol.4 , pp. 1007-1009
    • Armstrong, C.M.1    Goldberg, D.E.2
  • 2
    • 33748195107 scopus 로고    scopus 로고
    • A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules
    • 10.1016/j.cell.2006.07.025 16959577 10.1016/j.cell.2006.07.025 1:CAS:528:DC%2BD28XpvVKiurs%3D
    • Banaszynski LA, Chen LC, Maynard-Smith LA, Ooi AG, Wandless TJ (2006) A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules. Cell 126:995-1004. doi: 10.1016/j.cell.2006.07.025
    • (2006) Cell , vol.126 , pp. 995-1004
    • Banaszynski, L.A.1    Chen, L.C.2    Maynard-Smith, L.A.3    Ooi, A.G.4    Wandless, T.J.5
  • 3
    • 53549129978 scopus 로고    scopus 로고
    • Chemical control of protein stability and function in living mice
    • 10.1038/nm.1754 18836461 10.1038/nm.1754 1:CAS:528:DC%2BD1cXht1Slu7jI
    • Banaszynski LA, Sellmyer MA, Contag CH, Wandless TJ, Thorne SH (2008) Chemical control of protein stability and function in living mice. Nat Med 14:1123-1127. doi: 10.1038/nm.1754
    • (2008) Nat Med , vol.14 , pp. 1123-1127
    • Banaszynski, L.A.1    Sellmyer, M.A.2    Contag, C.H.3    Wandless, T.J.4    Thorne, S.H.5
  • 4
    • 79960559614 scopus 로고    scopus 로고
    • Small-molecule displacement of a cryptic degron causes conditional protein degradation
    • 10.1038/nchembio.598 21725303 10.1038/nchembio.598 1:CAS:528: DC%2BC3MXotlCkt7k%3D
    • Bonger KM, Chen LC, Liu CW, Wandless TJ (2011) Small-molecule displacement of a cryptic degron causes conditional protein degradation. Nat Chem Biol 7:531-537. doi: 10.1038/nchembio.598
    • (2011) Nat Chem Biol , vol.7 , pp. 531-537
    • Bonger, K.M.1    Chen, L.C.2    Liu, C.W.3    Wandless, T.J.4
  • 5
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms
    • 10.1016/j.molcel.2010.10.001 20965419 10.1016/j.molcel.2010.10.001 1:CAS:528:DC%2BC3cXhtlCjtr7L
    • Buchberger A, Bukau B, Sommer T (2010) Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol Cell 40:238-252. doi: 10.1016/j.molcel.2010.10.001
    • (2010) Mol Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 6
    • 19544379019 scopus 로고    scopus 로고
    • The F-box protein TIR1 is an auxin receptor
    • 10.1038/nature03543 15917797 10.1038/nature03543 1:CAS:528: DC%2BD2MXksVeisrs%3D
    • Dharmasiri N, Dharmasiri S, Estelle M (2005) The F-box protein TIR1 is an auxin receptor. Nature 435:441-445. doi: 10.1038/nature03543
    • (2005) Nature , vol.435 , pp. 441-445
    • Dharmasiri, N.1    Dharmasiri, S.2    Estelle, M.3
  • 7
    • 21344458139 scopus 로고    scopus 로고
    • Plant development is regulated by a family of auxin receptor F box proteins
    • 10.1016/j.devcel.2005.05.014 15992545 10.1016/j.devcel.2005.05.014 1:CAS:528:DC%2BD2MXmvVehurg%3D
    • Dharmasiri N, Dharmasiri S, Weijers D, Lechner E, Yamada M, Hobbie L, Ehrismann JS, Jurgens G, Estelle M (2005) Plant development is regulated by a family of auxin receptor F box proteins. Dev Cell 9:109-119. doi: 10.1016/j.devcel.2005.05.014
    • (2005) Dev Cell , vol.9 , pp. 109-119
    • Dharmasiri, N.1    Dharmasiri, S.2    Weijers, D.3    Lechner, E.4    Yamada, M.5    Hobbie, L.6    Ehrismann, J.S.7    Jurgens, G.8    Estelle, M.9
  • 8
    • 28844506010 scopus 로고    scopus 로고
    • Heat-inducible degron and the making of conditional mutants
    • 10.1016/S0076-6879(05)99052-6 16338396 10.1016/S0076-6879(05)99052-6 1:CAS:528:DC%2BD2sXlvFymtbs%3D
    • Dohmen RJ, Varshavsky A (2005) Heat-inducible degron and the making of conditional mutants. Methods Enzymol 399:799-822. doi: 10.1016/S0076-6879(05) 99052-6
    • (2005) Methods Enzymol , vol.399 , pp. 799-822
    • Dohmen, R.J.1    Varshavsky, A.2
  • 9
    • 0028213449 scopus 로고
    • Heat-inducible degron: A method for constructing temperature-sensitive mutants
    • 8122109 10.1126/science.8122109 1:CAS:528:DyaK2cXitFagt7o%3D
    • Dohmen RJ, Wu P, Varshavsky A (1994) Heat-inducible degron: a method for constructing temperature-sensitive mutants. Science 263:1273-1276
    • (1994) Science , vol.263 , pp. 1273-1276
    • Dohmen, R.J.1    Wu, P.2    Varshavsky, A.3
  • 10
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • 10.1038/35078107 11373684 10.1038/35078107 1:CAS:528:DC%2BD3MXkt1ejt7Y%3D
    • Elbashir SM, Harborth J, Lendeckel W, Yalcin A, Weber K, Tuschl T (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411:494-498. doi: 10.1038/35078107
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 11
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • 1319065 10.1073/pnas.89.12.5547 1:CAS:528:DyaK38Xks1equr4%3D
    • Gossen M, Bujard H (1992) Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc Natl Acad Sci USA 89:5547-5551
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 12
    • 0141856295 scopus 로고    scopus 로고
    • Fission yeast Cdc23/Mcm10 functions after pre-replicative complex formation to promote Cdc45 chromatin binding
    • 10.1091/mbc.E03-02-0090 12972571 10.1091/mbc.E03-02-0090 1:CAS:528:DC%2BD3sXnslymt78%3D
    • Gregan J, Lindner K, Brimage L, Franklin R, Namdar M, Hart EA, Aves SJ, Kearsey SE (2003) Fission yeast Cdc23/Mcm10 functions after pre-replicative complex formation to promote Cdc45 chromatin binding. Mol Biol Cell 14:3876-3887. doi: 10.1091/mbc.E03-02-0090
    • (2003) Mol Biol Cell , vol.14 , pp. 3876-3887
    • Gregan, J.1    Lindner, K.2    Brimage, L.3    Franklin, R.4    Namdar, M.5    Hart, E.A.6    Aves, S.J.7    Kearsey, S.E.8
  • 13
    • 23444448243 scopus 로고    scopus 로고
    • Adding value to fusion proteins through covalent labelling
    • 10.1016/j.copbio.2005.06.001 15967656 10.1016/j.copbio.2005.06.001 1:CAS:528:DC%2BD2MXntVCqtbg%3D
    • Gronemeyer T, Godin G, Johnsson K (2005) Adding value to fusion proteins through covalent labelling. Curr Opin Biotechnol 16:453-458. doi: 10.1016/j.copbio.2005.06.001
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 453-458
    • Gronemeyer, T.1    Godin, G.2    Johnsson, K.3
  • 15
    • 77956972260 scopus 로고    scopus 로고
    • A general chemical method to regulate protein stability in the mammalian central nervous system
    • 10.1016/j.chembiol.2010.07.009 20851347 10.1016/j.chembiol.2010.07.009 1:CAS:528:DC%2BC3cXhtFyitL7N
    • Iwamoto M, Bjorklund T, Lundberg C, Kirik D, Wandless TJ (2010) A general chemical method to regulate protein stability in the mammalian central nervous system. Chem Biol 17:981-988. doi: 10.1016/j.chembiol.2010.07.009
    • (2010) Chem Biol , vol.17 , pp. 981-988
    • Iwamoto, M.1    Bjorklund, T.2    Lundberg, C.3    Kirik, D.4    Wandless, T.J.5
  • 16
    • 78650599094 scopus 로고    scopus 로고
    • Targeted protein depletion in Saccharomyces cerevisiae by activation of a bidirectional degron
    • 10.1186/1752-0509-4-176 21190544 10.1186/1752-0509-4-176 1:CAS:528:DC%2BC3MXlvVSguw%3D%3D
    • Jungbluth M, Renicke C, Taxis C (2010) Targeted protein depletion in Saccharomyces cerevisiae by activation of a bidirectional degron. BMC Syst Biol 4:176. doi: 10.1186/1752-0509-4-176
    • (2010) BMC Syst Biol , vol.4 , pp. 176
    • Jungbluth, M.1    Renicke, C.2    Taxis, C.3
  • 17
    • 0038680253 scopus 로고    scopus 로고
    • Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo
    • 10.1038/nature01692 12768207 10.1038/nature01692 1:CAS:528: DC%2BD3sXksV2it7o%3D
    • Kanemaki M, Sanchez-Diaz A, Gambus A, Labib K (2003) Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo. Nature 423:720-724. doi: 10.1038/nature01692
    • (2003) Nature , vol.423 , pp. 720-724
    • Kanemaki, M.1    Sanchez-Diaz, A.2    Gambus, A.3    Labib, K.4
  • 19
    • 68349132121 scopus 로고    scopus 로고
    • Using the DHFR heat-inducible degron for protein inactivation in Schizosaccharomyces pombe
    • 19563124 10.1007/978-1-60327-815-7-27 1:CAS:528:DC%2BD1MXls1ertb0%3D
    • Kearsey SE, Gregan J (2009) Using the DHFR heat-inducible degron for protein inactivation in Schizosaccharomyces pombe. Methods Mol Biol 521:483-492
    • (2009) Methods Mol Biol , vol.521 , pp. 483-492
    • Kearsey, S.E.1    Gregan, J.2
  • 20
    • 0034595448 scopus 로고    scopus 로고
    • Uninterrupted MCM2-7 function required for DNA replication fork progression
    • 10834843 10.1126/science.288.5471.1643 1:CAS:528:DC%2BD3cXjvVGru7k%3D
    • Labib K, Tercero JA, Diffley JF (2000) Uninterrupted MCM2-7 function required for DNA replication fork progression. Science 288:1643-1647
    • (2000) Science , vol.288 , pp. 1643-1647
    • Labib, K.1    Tercero, J.A.2    Diffley, J.F.3
  • 21
    • 0036176135 scopus 로고    scopus 로고
    • Essential role of MCM proteins in premeiotic DNA replication
    • 10.1091/mbc.01-11-0537 11854402 10.1091/mbc.01-11-0537 1:CAS:528:DC%2BD38XivVertrk%3D
    • Lindner K, Gregan J, Montgomery S, Kearsey SE (2002) Essential role of MCM proteins in premeiotic DNA replication. Mol Biol Cell 13:435-444. doi: 10.1091/mbc.01-11-0537
    • (2002) Mol Biol Cell , vol.13 , pp. 435-444
    • Lindner, K.1    Gregan, J.2    Montgomery, S.3    Kearsey, S.E.4
  • 22
    • 34447272975 scopus 로고    scopus 로고
    • The HaloTag: A novel technology for cell imaging and protein analysis
    • 16988404 1:CAS:528:DC%2BD28XhtFOntbbI
    • Los GV, Wood K (2007) The HaloTag: a novel technology for cell imaging and protein analysis. Methods Mol Biol 356:195-208
    • (2007) Methods Mol Biol , vol.356 , pp. 195-208
    • Los, G.V.1    Wood, K.2
  • 23
    • 18744406025 scopus 로고    scopus 로고
    • In vivo protein labeling with trimethoprim conjugates: A flexible chemical tag
    • 10.1038/nmeth749 15782216 10.1038/nmeth749 1:CAS:528:DC%2BD2MXisFejtbk%3D
    • Miller LW, Cai Y, Sheetz MP, Cornish VW (2005) In vivo protein labeling with trimethoprim conjugates: a flexible chemical tag. Nat Methods 2:255-257. doi: 10.1038/nmeth749
    • (2005) Nat Methods , vol.2 , pp. 255-257
    • Miller, L.W.1    Cai, Y.2    Sheetz, M.P.3    Cornish, V.W.4
  • 26
    • 73349085934 scopus 로고    scopus 로고
    • An auxin-based degron system for the rapid depletion of proteins in nonplant cells
    • 10.1038/nmeth.1401 19915560 10.1038/nmeth.1401 1:CAS:528: DC%2BD1MXhsVWlsbzM
    • Nishimura K, Fukagawa T, Takisawa H, Kakimoto T, Kanemaki M (2009) An auxin-based degron system for the rapid depletion of proteins in nonplant cells. Nat Methods 6:917-922. doi: 10.1038/nmeth.1401
    • (2009) Nat Methods , vol.6 , pp. 917-922
    • Nishimura, K.1    Fukagawa, T.2    Takisawa, H.3    Kakimoto, T.4    Kanemaki, M.5
  • 27
    • 84934444085 scopus 로고    scopus 로고
    • Design and testing of zinc finger nucleases for use in mammalian cells
    • 10.1007/978-1-59745-232-8-4 18370067 10.1007/978-1-59745-232-8-4 1:CAS:528:DC%2BD2sXhtlerurvO
    • Porteus M (2008) Design and testing of zinc finger nucleases for use in mammalian cells. Methods Mol Biol 435:47-61. doi: 10.1007/978-1-59745-232-8-4
    • (2008) Methods Mol Biol , vol.435 , pp. 47-61
    • Porteus, M.1
  • 28
    • 2442575658 scopus 로고    scopus 로고
    • The N-degron approach to create temperature-sensitive mutants in Schizosaccharomyces pombe
    • 10.1016/j.ymeth.2003.11.015 15157887 10.1016/j.ymeth.2003.11.015 1:CAS:528:DC%2BD2cXkt1CmsLs%3D
    • Rajagopalan S, Liling Z, Liu J, Balasubramanian M (2004) The N-degron approach to create temperature-sensitive mutants in Schizosaccharomyces pombe. Methods 33:206-212. doi: 10.1016/j.ymeth.2003.11.015
    • (2004) Methods , vol.33 , pp. 206-212
    • Rajagopalan, S.1    Liling, Z.2    Liu, J.3    Balasubramanian, M.4
  • 29
    • 80051793721 scopus 로고    scopus 로고
    • Evaluation of FKBP and DHFR based destabilizing domains in Saccharomyces cerevisiae
    • 10.1016/j.bmcl.2011.06.006 21741238 10.1016/j.bmcl.2011.06.006 1:CAS:528:DC%2BC3MXhtVaisL%2FK
    • Rakhit R, Edwards SR, Iwamoto M, Wandless TJ (2011) Evaluation of FKBP and DHFR based destabilizing domains in Saccharomyces cerevisiae. Bioorg Med Chem Lett 21:4965-4968. doi: 10.1016/j.bmcl.2011.06.006
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 4965-4968
    • Rakhit, R.1    Edwards, S.R.2    Iwamoto, M.3    Wandless, T.J.4
  • 30
    • 0035902475 scopus 로고    scopus 로고
    • Protacs: Chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation
    • 10.1073/pnas.141230798 11438690 10.1073/pnas.141230798 1:CAS:528:DC%2BD3MXls1Wisbk%3D
    • Sakamoto KM, Kim KB, Kumagai A, Mercurio F, Crews CM, Deshaies RJ (2001) Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation. Proc Natl Acad Sci USA 98:8554-8559. doi: 10.1073/pnas.141230798
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8554-8559
    • Sakamoto, K.M.1    Kim, K.B.2    Kumagai, A.3    Mercurio, F.4    Crews, C.M.5    Deshaies, R.J.6
  • 31
    • 12144288039 scopus 로고    scopus 로고
    • Rapid depletion of budding yeast proteins by fusion to a heat-inducible degron
    • doi: 10.1126/stke.2232004pl8
    • Sanchez-Diaz A, Kanemaki M, Marchesi V, Labib K (2004) Rapid depletion of budding yeast proteins by fusion to a heat-inducible degron. Sci STKE PL8. doi: 10.1126/stke.2232004pl8
    • (2004) Sci STKE PL8
    • Sanchez-Diaz, A.1    Kanemaki, M.2    Marchesi, V.3    Labib, K.4
  • 32
    • 43149091910 scopus 로고    scopus 로고
    • Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast
    • 10.1038/ncb1701 18344988 10.1038/ncb1701 1:CAS:528:DC%2BD1cXktVGqsLY%3D
    • Sanchez-Diaz A, Marchesi V, Murray S, Jones R, Pereira G, Edmondson R, Allen T, Labib K (2008) Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast. Nat Cell Biol 10:395-406. doi: 10.1038/ncb1701
    • (2008) Nat Cell Biol , vol.10 , pp. 395-406
    • Sanchez-Diaz, A.1    Marchesi, V.2    Murray, S.3    Jones, R.4    Pereira, G.5    Edmondson, R.6    Allen, T.7    Labib, K.8
  • 33
    • 0024041732 scopus 로고
    • Site-specific DNA recombination in mammalian cells by the Cre recombinase of bacteriophage P1
    • 2839833 10.1073/pnas.85.14.5166 1:CAS:528:DyaL1cXltVGrtro%3D
    • Sauer B, Henderson N (1988) Site-specific DNA recombination in mammalian cells by the Cre recombinase of bacteriophage P1. Proc Natl Acad Sci USA 85:5166-5170
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5166-5170
    • Sauer, B.1    Henderson, N.2
  • 34
    • 1642343326 scopus 로고    scopus 로고
    • Chemical genetic control of protein levels: Selective in vivo targeted degradation
    • 10.1021/ja039025z 15038727 10.1021/ja039025z 1:CAS:528: DC%2BD2cXhvVegur0%3D
    • Schneekloth JS Jr, Fonseca FN, Koldobskiy M, Mandal A, Deshaies R, Sakamoto K, Crews CM (2004) Chemical genetic control of protein levels: selective in vivo targeted degradation. J Am Chem Soc 126:3748-3754. doi: 10.1021/ja039025z
    • (2004) J Am Chem Soc , vol.126 , pp. 3748-3754
    • Schneekloth, Jr.J.S.1    Fonseca, F.N.2    Koldobskiy, M.3    Mandal, A.4    Deshaies, R.5    Sakamoto, K.6    Crews, C.M.7
  • 35
    • 80054958053 scopus 로고    scopus 로고
    • The N-end rule pathway: Emerging functions and molecular principles of substrate recognition
    • 10.1038/nrm3217 22016057 10.1038/nrm3217 1:CAS:528:DC%2BC3MXhtlGhtbjM
    • Sriram SM, Kim BY, Kwon YT (2011) The N-end rule pathway: emerging functions and molecular principles of substrate recognition. Nat Rev Mol Cell Biol 12:735-747. doi: 10.1038/nrm3217
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 735-747
    • Sriram, S.M.1    Kim, B.Y.2    Kwon, Y.T.3
  • 36
    • 53549087771 scopus 로고    scopus 로고
    • Cell-cycle coordination between DNA replication and recombination revealed by a vertebrate N-end rule degron-Rad51
    • 10.1038/nsmb.1490 18794841 10.1038/nsmb.1490 1:CAS:528:DC%2BD1cXht1Sisb7L
    • Su X, Bernal JA, Venkitaraman AR (2008) Cell-cycle coordination between DNA replication and recombination revealed by a vertebrate N-end rule degron-Rad51. Nat Struct Mol Biol 15:1049-1058. doi: 10.1038/nsmb.1490
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1049-1058
    • Su, X.1    Bernal, J.A.2    Venkitaraman, A.R.3
  • 37
    • 0033231281 scopus 로고    scopus 로고
    • Degradation signals in the lysine-asparagine sequence space
    • 10.1093/emboj/18.21.6017 10545113 10.1093/emboj/18.21.6017 1:CAS:528:DyaK1MXns1entr0%3D
    • Suzuki T, Varshavsky A (1999) Degradation signals in the lysine-asparagine sequence space. EMBO J 18:6017-6026. doi: 10.1093/emboj/18.21. 6017
    • (1999) EMBO J , vol.18 , pp. 6017-6026
    • Suzuki, T.1    Varshavsky, A.2
  • 38
    • 34247219263 scopus 로고    scopus 로고
    • Mechanism of auxin perception by the TIR1 ubiquitin ligase
    • 10.1038/nature05731 17410169 10.1038/nature05731 1:CAS:528: DC%2BD2sXjslOlsbc%3D
    • Tan X, Calderon-Villalobos LI, Sharon M, Zheng C, Robinson CV, Estelle M, Zheng N (2007) Mechanism of auxin perception by the TIR1 ubiquitin ligase. Nature 446:640-645. doi: 10.1038/nature05731
    • (2007) Nature , vol.446 , pp. 640-645
    • Tan, X.1    Calderon-Villalobos, L.I.2    Sharon, M.3    Zheng, C.4    Robinson, C.V.5    Estelle, M.6    Zheng, N.7
  • 39
    • 84858189214 scopus 로고    scopus 로고
    • TIPI: TEV protease-mediated induction of protein instability
    • 10.1007/978-1-61779-474-2-43 22350916 10.1007/978-1-61779-474-2-43 1:CAS:528:DC%2BC38XhtlansLzE
    • Taxis C, Knop M (2012) TIPI: TEV protease-mediated induction of protein instability. Methods Mol Biol 832:611-626. doi: 10.1007/978-1-61779-474-2-43
    • (2012) Methods Mol Biol , vol.832 , pp. 611-626
    • Taxis, C.1    Knop, M.2
  • 40
    • 66249103970 scopus 로고    scopus 로고
    • Efficient protein depletion by genetically controlled deprotection of a dormant N-degron
    • 10.1038/msb.2009.25 19401679 10.1038/msb.2009.25
    • Taxis C, Stier G, Spadaccini R, Knop M (2009) Efficient protein depletion by genetically controlled deprotection of a dormant N-degron. Mol Syst Biol 5:267. doi: 10.1038/msb.2009.25
    • (2009) Mol Syst Biol , vol.5 , pp. 267
    • Taxis, C.1    Stier, G.2    Spadaccini, R.3    Knop, M.4
  • 41
    • 77955867185 scopus 로고    scopus 로고
    • Genome editing with engineered zinc finger nucleases
    • 10.1038/nrg2842 20717154 10.1038/nrg2842 1:CAS:528:DC%2BC3cXhtVCnurzE
    • Urnov FD, Rebar EJ, Holmes MC, Zhang HS, Gregory PD (2010) Genome editing with engineered zinc finger nucleases. Nat Rev Genet 11:636-646. doi: 10.1038/nrg2842
    • (2010) Nat Rev Genet , vol.11 , pp. 636-646
    • Urnov, F.D.1    Rebar, E.J.2    Holmes, M.C.3    Zhang, H.S.4    Gregory, P.D.5
  • 42
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • 8901547 10.1073/pnas.93.22.12142 1:CAS:528:DyaK28Xms1Gjsrg%3D
    • Varshavsky A (1996) The N-end rule: functions, mysteries, uses. Proc Natl Acad Sci USA 93:12142-12149
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 43
    • 84857370681 scopus 로고    scopus 로고
    • Mcm10 plays a role in functioning of the eukaryotic replicative DNA helicase, Cdc45-Mcm-GINS
    • 10.1016/j.cub.2012.01.023 22285032 10.1016/j.cub.2012.01.023 1:CAS:528:DC%2BC38XhsVeisrs%3D
    • Watase G, Takisawa H, Kanemaki MT (2012) Mcm10 plays a role in functioning of the eukaryotic replicative DNA helicase, Cdc45-Mcm-GINS. Curr Biol 22:343-349. doi: 10.1016/j.cub.2012.01.023
    • (2012) Curr Biol , vol.22 , pp. 343-349
    • Watase, G.1    Takisawa, H.2    Kanemaki, M.T.3
  • 44
    • 13444263620 scopus 로고    scopus 로고
    • Targeted protein degradation
    • 10.1016/j.cbpa.2004.10.012 15701453 10.1016/j.cbpa.2004.10.012 1:CAS:528:DC%2BD2MXhtV2ksrg%3D
    • Zhou P (2005) Targeted protein degradation. Curr Opin Chem Biol 9:51-55. doi: 10.1016/j.cbpa.2004.10.012
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 51-55
    • Zhou, P.1
  • 45
    • 0033638333 scopus 로고    scopus 로고
    • Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins
    • 11030355 10.1016/S1097-2765(00)00074-5 1:CAS:528:DC%2BD3cXntVyhsbk%3D
    • Zhou P, Bogacki R, McReynolds L, Howley PM (2000) Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins. Mol Cell 6:751-756
    • (2000) Mol Cell , vol.6 , pp. 751-756
    • Zhou, P.1    Bogacki, R.2    McReynolds, L.3    Howley, P.M.4


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