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Volumn 462, Issue 7275, 2009, Pages 886-890

The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress

Author keywords

[No Author keywords available]

Indexed keywords

BRCA1 PROTEIN; PROTEIN INHIBITOR OF ACTIVATED STAT; SUMO 1 PROTEIN; SUMO 2 PROTEIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 72449163470     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08593     Document Type: Article
Times cited : (353)

References (50)
  • 1
    • 0033613222 scopus 로고    scopus 로고
    • RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
    • Lorick, K. L. et al. RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Proc. Natl Acad. Sci. USA 96, 11364-11369 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11364-11369
    • Lorick, K.L.1
  • 2
    • 0035805582 scopus 로고    scopus 로고
    • The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation
    • Hashizume, R. et al. The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation. J. Biol. Chem. 276, 14537-14540 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 14537-14540
    • Hashizume, R.1
  • 3
    • 0037610801 scopus 로고    scopus 로고
    • Binding and recognition in the assembly of an active BRCA1/ BARD1 ubiquitin-ligase complex
    • Brzovic, P. S. et al. Binding and recognition in the assembly of an active BRCA1/ BARD1 ubiquitin-ligase complex. Proc. Natl Acad. Sci. USA 100, 5646-5651 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5646-5651
    • Brzovic, P.S.1
  • 4
    • 32144463131 scopus 로고    scopus 로고
    • Genetic analysis of BRCA1 ubiquitin ligase activity and its relationship to breast cancer susceptibility
    • Morris, J. R. et al. Genetic analysis of BRCA1 ubiquitin ligase activity and its relationship to breast cancer susceptibility. Hum. Mol. Genet. 15, 599-606 (2006).
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 599-606
    • Morris, J.R.1
  • 5
    • 1942517849 scopus 로고    scopus 로고
    • BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair
    • Morris, J. R. & Solomon, E. BRCA1: BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair. Hum. Mol. Genet. 13, 807-817 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 807-817
    • Morris, J.R.1    Brcal, S.E.2
  • 7
    • 58549098527 scopus 로고    scopus 로고
    • E3 ligase activity of BRCA1 is not essential for mammalian cell viability or homology-directed repair of double-strand DNA breaks
    • Reid, L. J. et al. E3 ligase activity of BRCA1 is not essential for mammalian cell viability or homology-directed repair of double-strand DNA breaks. Proc. Natl Acad. Sci. USA 105, 20876-20881 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 20876-20881
    • Reid, L.J.1
  • 8
    • 33646808638 scopus 로고    scopus 로고
    • A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites.
    • Polanowska, J., Martin, J. S., Garcia-Muse, T., Petalcorin, M. I. & Boulton, S. J. A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites. EMBO J. 25, 2178-2188 (2006).
    • (2006) EMBO J. , vol.25 , pp. 2178-2188
    • Polanowska, J.1    Martin, J.S.2    Garcia-Muse, T.3    Petalcorin, M.I.4    Boulton, S.J.5
  • 9
    • 33847413700 scopus 로고    scopus 로고
    • A critical role for the ubiquitin-conjugating enzyme Ubc13 in initiating homologous recombination.
    • Zhao, G. Y. et al. A critical role for the ubiquitin-conjugating enzyme Ubc13 in initiating homologous recombination. Mol. Cell 25, 663-675 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 663-675
    • Zhao, G.Y.1
  • 10
    • 59049091728 scopus 로고    scopus 로고
    • RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins.
    • Doil, C. et al. RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 136, 435-446 (2009).
    • (2009) Cell , vol.136 , pp. 435-446
    • Doil, C.1
  • 11
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly.
    • Huen, M. S. et al. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 131, 901-914 (2007).
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.1
  • 12
    • 36749084931 scopus 로고    scopus 로고
    • Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase.
    • Kolas, N. K. et al. Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase. Science 318, 1637-1640 (2007).
    • (2007) Science , vol.318 , pp. 1637-1640
    • Kolas, N.K.1
  • 13
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins.
    • Mailand, N. et al. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 131, 887-900 (2007).
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1
  • 14
    • 36749025467 scopus 로고    scopus 로고
    • Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage
    • Wang, B. & Elledge, S. J. Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage. Proc. Natl Acad. Sci. USA 104, 20759-20763 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 20759-20763
    • Wang, B.1    Elledge, S.J.2
  • 15
    • 34547655427 scopus 로고    scopus 로고
    • CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response
    • DOI 10.1038/nsmb1277, PII NSMB1277
    • Kim, H., Huang, J. & Chen, J. CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response. Nature Struct. Mol. Biol. 14, 710-715 (2007). (Pubitemid 47220062)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.8 , pp. 710-715
    • Kim, H.1    Huang, J.2    Chen, J.3
  • 16
    • 34249950879 scopus 로고    scopus 로고
    • Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response
    • DOI 10.1126/science.1139621
    • Kim, H., Chen, J. & Yu, X. Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response. Science 316, 1202-1205 (2007). (Pubitemid 46877484)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1202-1205
    • Kim, H.1    Chen, J.2    Yu, X.3
  • 17
    • 34547662882 scopus 로고    scopus 로고
    • CCDC98 targets BRCA1 to DNA damage sites
    • Liu, Z., Wu, J. & Yu, X. CCDC98 targets BRCA1 to DNA damage sites. Nature Struct. Mol. Biol. 14, 716-720 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 716-720
    • Liu, Z.1    Wu, J.2    Yu, X.3
  • 18
    • 34249949779 scopus 로고    scopus 로고
    • RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites.
    • Sobhian, B. et al. RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites. Science 316, 1198-1202 (2007).
    • (2007) Science , vol.316 , pp. 1198-1202
    • Sobhian, B.1
  • 19
    • 34249946686 scopus 로고    scopus 로고
    • Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response.
    • Wang, B. et al. Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response. Science 316, 1194-1198 (2007).
    • (2007) Science , vol.316 , pp. 1194-1198
    • Wang, B.1
  • 20
    • 34547120473 scopus 로고    scopus 로고
    • The ubiquitin-interacting motif containing protein RAP80 interacts with BRCA1 and functions in DNA damage repair response.
    • Yan, J. et al. The ubiquitin-interacting motif containing protein RAP80 interacts with BRCA1 and functions in DNA damage repair response. Cancer Res. 67, 6647-6656 (2007).
    • (2007) Cancer Res. , vol.67 , pp. 6647-6656
    • Yan, J.1
  • 21
    • 59049103900 scopus 로고    scopus 로고
    • The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage.
    • Stewart, G. S. et al. The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell 136, 420-434 (2009).
    • (2009) Cell , vol.136 , pp. 420-434
    • Stewart, G.S.1
  • 22
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification.
    • Hay, R. T. SUMO: a history of modification. Mol. Cell 18, 1-12 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 23
    • 16544390672 scopus 로고    scopus 로고
    • Overexpression of a dominant-negative mutant Ubc9 is associated with increased sensitivity to anticancer drugs.
    • Mo, Y. Y., Yu, Y., Ee, P. L. & Beck, W. T. Overexpression of a dominant-negative mutant Ubc9 is associated with increased sensitivity to anticancer drugs. Cancer Res. 64, 2793-2798 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 2793-2798
    • Mo, Y.Y.1    Yu, Y.2    Ee, P.L.3    Beck, W.T.4
  • 24
    • 16344370926 scopus 로고    scopus 로고
    • SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
    • Zhao, X. & Blobel, G. A. SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc. Natl Acad. Sci. USA 102, 4777-4782 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4777-4782
    • Zhao, X.1    Blobel, G.A.2
  • 25
    • 23344442009 scopus 로고    scopus 로고
    • Human MMS21/NSE2 is a SUMO ligase required for DNA repair
    • Potts, P. R. & Yu, H. Human MMS21/NSE2 is a SUMO ligase required for DNA repair. Mol. Cell. Biol. 25, 7021-7032 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7021-7032
    • Potts, P.R.1    Yu, H.2
  • 26
    • 33748188499 scopus 로고    scopus 로고
    • PIASy mediates NEMO sumoylation and NF-kB activation in response to genotoxic stress.
    • Mabb, A. M., Wuerzberger-Davis, S. M. & Miyamoto, S. PIASy mediates NEMO sumoylation and NF-kB activation in response to genotoxic stress. Nature Cell Biol. 8, 986-993 (2006).
    • (2006) Nature Cell Biol. , vol.8 , pp. 986-993
    • Mabb, A.M.1    Wuerzberger-Davis, S.M.2    Miyamoto, S.3
  • 27
    • 10044250110 scopus 로고    scopus 로고
    • DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus formation
    • Ishiai, M. et al. DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus formation. Mol. Cell. Biol. 24, 10733-10741 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10733-10741
    • Ishiai, M.1
  • 28
    • 0346335800 scopus 로고    scopus 로고
    • BRCA1/BARD1 orthologs required for DNA repair in Caenorhabditis elegans
    • Boulton, S. J. et al. BRCA1/BARD1 orthologs required for DNA repair in Caenorhabditis elegans. Curr. Biol. 14, 33-39 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 33-39
    • Boulton, S.J.1
  • 29
    • 38349096713 scopus 로고    scopus 로고
    • SUMO1 negatively regulates BRCA1-mediated transcription, via modulation of promoter occupancy.
    • Park, M. A., Seok, Y. J., Jeong, G. & Lee, J. S. SUMO1 negatively regulates BRCA1-mediated transcription, via modulation of promoter occupancy. Nucleic Acids Res. 36, 263-283 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 263-283
    • Park, M.A.1    Seok, Y.J.2    Jeong, G.3    Lee, J.S.4
  • 30
    • 1842715882 scopus 로고    scopus 로고
    • Imaging molecular interactions by multiphoton FLIM.
    • Peter, M. & Ameer-Beg, S. M. Imaging molecular interactions by multiphoton FLIM. Biol. Cell 96, 231-236 (2004).
    • (2004) Biol. Cell , vol.96 , pp. 231-236
    • Peter, M.1    Ameer-Beg, S.M.2
  • 31
    • 21244478918 scopus 로고    scopus 로고
    • Multiphoton-FLIM quantification of the EGFP-mRFP1 FRET pair for localization of membrane receptor-kinase interactions.
    • Peter, M. et al. Multiphoton-FLIM quantification of the EGFP-mRFP1 FRET pair for localization of membrane receptor-kinase interactions. Biophys. J. 88, 1224-1237 (2005).
    • (2005) Biophys. J. , vol.88 , pp. 1224-1237
    • Peter, M.1
  • 32
    • 0033605542 scopus 로고    scopus 로고
    • Imaging protein kinase Ca activation in cells.
    • Ng, T. et al. Imaging protein kinase Ca activation in cells. Science 283, 2085-2089 (1999).
    • (1999) Science , vol.283 , pp. 2085-2089
    • Ng, T.1
  • 33
    • 33645233077 scopus 로고    scopus 로고
    • A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Forster resonance energy transfer with GFP
    • Ganesan, S., Ameer-Beg, S. M., Ng, T. T., Vojnovic, B. & Wouters, F. S. A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Forster resonance energy transfer with GFP. Proc. Natl Acad. Sci. USA 103, 4089-4094 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4089-4094
    • Ganesan, S.1    Ameer-Beg, S.M.2    Ng, T.T.3    Vojnovic, B.4    Wouters, F.S.5
  • 34
    • 33845914340 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase 1B by sumoylation.
    • Dadke, S. et al. Regulation of protein tyrosine phosphatase 1B by sumoylation. Nature Cell Biol. 9, 80-85 (2007).
    • (2007) Nature Cell Biol. , vol.9 , pp. 80-85
    • Dadke, S.1
  • 35
    • 31544432283 scopus 로고    scopus 로고
    • Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes.
    • Bossis, G. & Melchior, F. Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes. Mol. Cell 21, 349-357 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 349-357
    • Bossis, G.1    Melchior, F.2
  • 36
    • 0346100493 scopus 로고    scopus 로고
    • PIAS/SUMO: New partners in transcriptional regulation
    • Schmidt, D. & Muller, S. PIAS/SUMO: new partners in transcriptional regulation. Cell. Mol. Life Sci. 60, 2561-2574 (2003).
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2561-2574
    • Schmidt, D.1    Muller, S.2
  • 37
    • 10044250116 scopus 로고    scopus 로고
    • PIAS-1 is a checkpoint regulator which affects exit from G1 and G2 by sumoylation of p73
    • Munarriz, E. et al. PIAS-1 is a checkpoint regulator which affects exit from G1 and G2 by sumoylation of p73. Mol. Cell. Biol. 24, 10593-10610 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10593-10610
    • Munarriz, E.1
  • 38
    • 50449098473 scopus 로고    scopus 로고
    • New players in the BRCA1-mediated DNA damage responsive pathway.
    • Kim, H. & Chen, J. New players in the BRCA1-mediated DNA damage responsive pathway. Mol. Cells 25, 457-461 (2008).
    • (2008) Mol. Cells , vol.25 , pp. 457-461
    • Kim, H.1    Chen, J.2
  • 39
    • 15244346738 scopus 로고    scopus 로고
    • Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase.
    • Nishikawa, H., Ooka, S., Sato, K., Arima, K., Okamoto, J., Klevit, R. E., Fukuda, M. & Ohta, T. Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase. J Biol Chem, (2003).
    • (2003) J Biol Chem
    • Nishikawa, H.1    Ooka, S.2    Sato, K.3    Arima, K.4    Okamoto, J.5    Klevit, R.E.6    Fukuda, M.7    Ohta, T.8
  • 40
    • 0042317328 scopus 로고    scopus 로고
    • The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin
    • Wu-Baer, F., Lagrazon, K., Yuan, W. & Baer, R. The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J. Biol. Chem. 278, 34743-34746 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 34743-34746
    • Wu-Baer, F.1    Lagrazon, K.2    Yuan, W.3    Baer, R.4
  • 41
    • 0037122004 scopus 로고    scopus 로고
    • Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains.
    • Mallery, D. L.,Vandenberg, C. J. & Hiom, K. Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains. EMBO J. 21, 6755-6762 (2002).
    • (2002) EMBO J. , vol.21 , pp. 6755-6762
    • Mallery, L.1    Vandenberg, C.J.2    Hiom, K.3
  • 42
    • 34948848684 scopus 로고    scopus 로고
    • E2-BRCA1 RING interactions dictate synthesis of mono-or specific polyubiquitin chain linkages
    • Christensen, D. E., Brzovic, P. S. & Klevit, R. E. E2-BRCA1 RING interactions dictate synthesis of mono-or specific polyubiquitin chain linkages. Nature Struct. Mol. Biol. 14, 941-948 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 941-948
    • Christensen, D.E.1    Brzovic, P.S.2    Klevit, R.E.3
  • 43
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting.
    • Manke, I. A., Lowery, D. M., Nguyen, A. & Yaffe, M. B. BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science 302, 636-639 (2003).
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 44
    • 29044446803 scopus 로고    scopus 로고
    • Detection of modification by ubiquitin-like proteins.
    • Jaffray, E. G. & Hay, R. T. Detection of modification by ubiquitin-like proteins. Methods 38, 35-38 (2006).
    • (2006) Methods , vol.38 , pp. 35-38
    • Jaffray, E.G.1    Hay, R.T.2
  • 45
    • 34547760739 scopus 로고    scopus 로고
    • Activated ezrin promotes cell migration through recruitment of the GEF Dbl to lipid rafts and preferential downstream activation of Cdc42
    • Prag, S. et al. Activated ezrin promotes cell migration through recruitment of the GEF Dbl to lipid rafts and preferential downstream activation of Cdc42. Mol. Biol. Cell 18, 2935-2948 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2935-2948
    • Prag, S.1
  • 46
    • 21844451881 scopus 로고    scopus 로고
    • Global and pixel kinetic data analysis for FRET detection by multi-photon time-domain FLIM.
    • Barber, P. R., Ameer-Beg, S. M., Gilbey, J. D., Edens, R. J., Ezike, I. & Vojnovic, B. Global and pixel kinetic data analysis for FRET detection by multi-photon time-domain FLIM. Proc. SPIE 5700, 171-181 (2005).
    • (2005) Proc. SPIE , vol.5700 , pp. 171-181
    • Barber, P.R.1    Ameer-Beg, S.M.2    Gilbey, J.D.3    Edens, R.J.4    Ezike, I.5    Vojnovic, B.6
  • 47
    • 46249131123 scopus 로고    scopus 로고
    • Alternative-NHEJ is a mechanistically distinct pathway of mammalian chromosome break repair.
    • Bennardo, N., Cheng, A., Huang, N. & Stark, J. M. Alternative-NHEJ is a mechanistically distinct pathway of mammalian chromosome break repair. PLoS Genet. 4, e1000110 (2008).
    • (2008) PLoS Genet. , vol.4
    • Bennardo, N.1    Cheng, A.2    Huang, N.3    Stark, J.M.4
  • 48
    • 0042709466 scopus 로고    scopus 로고
    • PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0.
    • Boutell, C., Orr, A. & Everett, R. D. PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0. J. Virol. 77, 8686-8694 (2003).
    • (2003) J. Virol. , vol.77 , pp. 8686-8694
    • Boutell, C.1    Orr, A.2    Everett, R.D.3
  • 49
    • 0036138854 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro.
    • Boutell, C., Sadis, S. & Everett, R. D. Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol. 76, 841-850 (2002).
    • (2002) J. Virol. , vol.76 , pp. 841-850
    • Boutell, C.1    Sadis, S.2    Everett, R.D.3
  • 50
    • 84946384873 scopus 로고
    • The toxicity of poisons applied jointly
    • Bliss, C. I. The toxicity of poisons applied jointly. Ann. Appl. Biol. 26, 585-615 (1939).
    • (1939) Ann. Appl. Biol. , vol.26 , pp. 585-615
    • Bliss, C.I.1


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