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Volumn 11, Issue 8, 2015, Pages 611-617

Catalytic in vivo protein knockdown by small-molecule PROTACs

(29)  Bondeson, Daniel P a   Mares, Alina b   Smith, Ian E D b   Ko, Eunhwa a   Campos, Sebastien b   Miah, Afjal H b   Mulholland, Katie E b   Routly, Natasha b   Buckley, Dennis L a   Gustafson, Jeffrey L a   Zinn, Nico b   Grandi, Paola b   Shimamura, Satoko b   Bergamini, Giovanna b   Faelth Savitski, Maria b   Bantscheff, Marcus b   Cox, Carly a   Gordon, Deborah A c   Willard, Ryan R c   Flanagan, John J c   more..


Author keywords

[No Author keywords available]

Indexed keywords

I KAPPA B KINASE ALPHA; I KAPPA B KINASE BETA; I KAPPA B KINASE GAMMA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; UBIQUITIN PROTEIN LIGASE E3; ANTINEOPLASTIC AGENT; ERRALPHA ESTROGEN-RELATED RECEPTOR; ESTROGEN RECEPTOR; MOLECULAR LIBRARY; PROTEASOME; PROTEIN BINDING; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE 2; RIPK2 PROTEIN, HUMAN; TUMOR PROTEIN; UBIQUITIN; VHL PROTEIN, HUMAN; VON HIPPEL LINDAU PROTEIN;

EID: 84937514576     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1858     Document Type: Article
Times cited : (922)

References (53)
  • 1
    • 33748652419 scopus 로고    scopus 로고
    • What is the right dose? The elusive optimal biologic dose in phase I clinical trials
    • Adjei, A.A. What is the right dose? The elusive optimal biologic dose in phase I clinical trials. J. Clin. Oncol. 24, 4054-4055 (2006).
    • (2006) J. Clin. Oncol. , vol.24 , pp. 4054-4055
    • Adjei, A.A.1
  • 2
    • 9144247189 scopus 로고    scopus 로고
    • Therapeutic silencing of an endogenous gene by systemic administration of modified siRNAs
    • Soutschek, J. et al. Therapeutic silencing of an endogenous gene by systemic administration of modified siRNAs. Nature 432, 173-178 (2004).
    • (2004) Nature , vol.432 , pp. 173-178
    • Soutschek, J.1
  • 3
    • 33751099034 scopus 로고    scopus 로고
    • RNAi therapeutics: A potential new class of pharmaceutical drugs
    • Bumcrot, D., Manoharan, M., Koteliansky, V. & Sah, D.W. RNAi therapeutics: a potential new class of pharmaceutical drugs. Nat. Chem. Biol. 2, 711-719 (2006).
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 711-719
    • Bumcrot, D.1    Manoharan, M.2    Koteliansky, V.3    Sah, D.W.4
  • 5
    • 84894414494 scopus 로고    scopus 로고
    • Small-molecule control of intracellular protein levels through modulation of the ubiquitin proteasome system
    • Buckley, D.L. & Crews, C.M. Small-molecule control of intracellular protein levels through modulation of the ubiquitin proteasome system. Angew. Chem. Int. Edn. Engl. 53, 2312-2330 (2014).
    • (2014) Angew. Chem. Int. Edn. Engl. , vol.53 , pp. 2312-2330
    • Buckley, D.L.1    Crews, C.M.2
  • 6
    • 0035902475 scopus 로고    scopus 로고
    • Protacs: Chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation
    • Sakamoto, K.M. et al. 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 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8554-8559
    • Sakamoto, K.M.1
  • 7
    • 55549137044 scopus 로고    scopus 로고
    • Targeted intracellular protein degradation induced by a small molecule: En route to chemical proteomics
    • Schneekloth, A.R., Pucheault, M., Tae, H.S. & Crews, C.M. Targeted intracellular protein degradation induced by a small molecule: en route to chemical proteomics. Bioorg. Med. Chem. Lett. 18, 5904-5908 (2008).
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 5904-5908
    • Schneekloth, A.R.1    Pucheault, M.2    Tae, H.S.3    Crews, C.M.4
  • 8
    • 1642343326 scopus 로고    scopus 로고
    • Chemical genetic control of protein levels: Selective in vivo targeted degradation
    • Schneekloth, J.S. Jr. et al. Chemical genetic control of protein levels: selective in vivo targeted degradation. J. Am. Chem. Soc. 126, 3748-3754 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3748-3754
    • Schneekloth, J.S.1
  • 9
    • 84878429220 scopus 로고    scopus 로고
    • Posttranslational protein knockdown coupled to receptor tyrosine kinase activation with phosphoPROTACs
    • Hines, J., Gough, J.D., Corson, T.W. & Crews, C.M. Posttranslational protein knockdown coupled to receptor tyrosine kinase activation with phosphoPROTACs. Proc. Natl. Acad. Sci. USA 110, 8942-8947 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 8942-8947
    • Hines, J.1    Gough, J.D.2    Corson, T.W.3    Crews, C.M.4
  • 10
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1α-pVHL complex: Hydroxyproline recognition in signaling
    • Min, J.H. et al. Structure of an HIF-1α-pVHL complex: hydroxyproline recognition in signaling. Science 296, 1886-1889 (2002).
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.H.1
  • 11
    • 18444368709 scopus 로고    scopus 로고
    • Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL
    • Hon, W.C. et al. Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. Nature 417, 975-978 (2002).
    • (2002) Nature , vol.417 , pp. 975-978
    • Hon, W.C.1
  • 12
    • 57349130557 scopus 로고    scopus 로고
    • Targeting steroid hormone receptors for ubiquitination and degradation in breast and prostate cancer
    • Rodriguez-Gonzalez, A. et al. Targeting steroid hormone receptors for ubiquitination and degradation in breast and prostate cancer. Oncogene 27, 7201-7211 (2008).
    • (2008) Oncogene , vol.27 , pp. 7201-7211
    • Rodriguez-Gonzalez, A.1
  • 13
    • 41149156498 scopus 로고    scopus 로고
    • Development of an aryl hydrocarbon receptor antagonist using the proteolysis-targeting chimeric molecules approach: A potential tool for chemoprevention
    • Puppala, D., Lee, H., Kim, K.B. & Swanson, H.I. Development of an aryl hydrocarbon receptor antagonist using the proteolysis-targeting chimeric molecules approach: a potential tool for chemoprevention. Mol. Pharmacol. 73, 1064-1071 (2008).
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1064-1071
    • Puppala, D.1    Lee, H.2    Kim, K.B.3    Swanson, H.I.4
  • 14
    • 84862170982 scopus 로고    scopus 로고
    • Double protein knockdown of cIAP1 and CRABP-II using a hybrid molecule consisting of ATRA and IAPs antagonist
    • Itoh, Y. et al. Double protein knockdown of cIAP1 and CRABP-II using a hybrid molecule consisting of ATRA and IAPs antagonist. Bioorg. Med. Chem. Lett. 22, 4453-4457 (2012).
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 4453-4457
    • Itoh, Y.1
  • 15
    • 84886786805 scopus 로고    scopus 로고
    • Development of hybrid small molecules that induce degradation of estrogen receptor-alpha and necrotic cell death in breast cancer cells
    • Okuhira, K. et al. Development of hybrid small molecules that induce degradation of estrogen receptor-alpha and necrotic cell death in breast cancer cells. Cancer Sci. 104, 1492-1498 (2013).
    • (2013) Cancer Sci. , vol.104 , pp. 1492-1498
    • Okuhira, K.1
  • 16
    • 44049087791 scopus 로고    scopus 로고
    • Small molecules destabilize cIAP1 by activating autoubiquitylation
    • Sekine, K. et al. Small molecules destabilize cIAP1 by activating autoubiquitylation. J. Biol. Chem. 283, 8961-8968 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 8961-8968
    • Sekine, K.1
  • 17
    • 84858201095 scopus 로고    scopus 로고
    • Targeting the von Hippel-Lindau E3 ubiquitin ligase using small molecules to disrupt the VHL/HIF-1alpha interaction
    • Buckley, D.L. et al. Targeting the von Hippel-Lindau E3 ubiquitin ligase using small molecules to disrupt the VHL/HIF-1alpha interaction. J. Am. Chem. Soc. 134, 4465-4468 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 4465-4468
    • Buckley, D.L.1
  • 18
    • 84937534394 scopus 로고    scopus 로고
    • Compounds and methods for the inhibition of vcb e3 ubiquitin ligase
    • Patent
    • Crews, C.M. et al. Compounds and methods for the inhibition of vcb e3 ubiquitin ligase. Patent PCT/US2013/021141 (2013).
    • (2013)
    • Crews, C.M.1
  • 19
    • 84868522211 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the interaction between the E3 ligase VHL and HIF1alpha
    • Buckley, D.L. et al. Small-molecule inhibitors of the interaction between the E3 ligase VHL and HIF1alpha. Angew. Chem. Int. Edn Engl. 51, 11463-11467 (2012).
    • (2012) Angew. Chem. Int. Edn Engl. , vol.51 , pp. 11463-11467
    • Buckley, D.L.1
  • 20
    • 79957944105 scopus 로고    scopus 로고
    • Estrogen related receptors (ERRs): A new dawn in transcriptional control of mitochondrial gene networks
    • Eichner, L.J. & Giguere, V. Estrogen related receptors (ERRs): a new dawn in transcriptional control of mitochondrial gene networks. Mitochondrion 11, 544-552 (2011).
    • (2011) Mitochondrion , vol.11 , pp. 544-552
    • Eichner, L.J.1    Giguere, V.2
  • 21
    • 79851480621 scopus 로고    scopus 로고
    • Identification of diaryl ether-based ligands for estrogen-related receptor α as potential antidiabetic agents
    • Patch, R.J. et al. Identification of diaryl ether-based ligands for estrogen-related receptor α as potential antidiabetic agents. J. Med. Chem. 54, 788-808 (2011).
    • (2011) J. Med. Chem. , vol.54 , pp. 788-808
    • Patch, R.J.1
  • 22
    • 84961289586 scopus 로고    scopus 로고
    • RIP kinases: Key decision makers in cell death and innate immunity
    • Humphries, F., Yang, S., Wang, B. & Moynagh, P.N. RIP kinases: key decision makers in cell death and innate immunity. Cell Death Differ. 22, 225-236 (2015).
    • (2015) Cell Death Differ. , vol.22 , pp. 225-236
    • Humphries, F.1    Yang, S.2    Wang, B.3    Moynagh, P.N.4
  • 23
    • 17944372335 scopus 로고    scopus 로고
    • CARD15 mutations in Blau syndrome
    • Miceli-Richard, C. et al. CARD15 mutations in Blau syndrome. Nat. Genet. 29, 19-20 (2001).
    • (2001) Nat. Genet. , vol.29 , pp. 19-20
    • Miceli-Richard, C.1
  • 24
    • 19944431022 scopus 로고    scopus 로고
    • Early-onset sarcoidosis and CARD15 mutations with constitutive nuclear factor-kappaB activation: Common genetic etiology with Blau syndrome
    • Kanazawa, N. et al. Early-onset sarcoidosis and CARD15 mutations with constitutive nuclear factor-kappaB activation: common genetic etiology with Blau syndrome. Blood 105, 1195-1197 (2005).
    • (2005) Blood , vol.105 , pp. 1195-1197
    • Kanazawa, N.1
  • 25
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng, L. et al. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA 96, 10403-10408 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10403-10408
    • Meng, L.1
  • 26
    • 34249826059 scopus 로고    scopus 로고
    • Molecular mechanisms involved in the regulation of cytokine production by muramyl dipeptide
    • Windheim, M., Lang, C., Peggie, M., Plater, L.A. & Cohen, P. Molecular mechanisms involved in the regulation of cytokine production by muramyl dipeptide. Biochem. J. 404, 179-190 (2007).
    • (2007) Biochem. J. , vol.404 , pp. 179-190
    • Windheim, M.1    Lang, C.2    Peggie, M.3    Plater, L.A.4    Cohen, P.5
  • 27
    • 79956322553 scopus 로고    scopus 로고
    • Global quantification of mammalian gene expression control
    • Schwanhäusser, B. et al. Global quantification of mammalian gene expression control. Nature 473, 337-342 (2011).
    • (2011) Nature , vol.473 , pp. 337-342
    • Schwanhäusser, B.1
  • 29
    • 0034641615 scopus 로고    scopus 로고
    • Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex
    • Kamura, T. et al. Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex. Proc. Natl. Acad. Sci. USA 97, 10430-10435 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10430-10435
    • Kamura, T.1
  • 30
    • 0033607291 scopus 로고    scopus 로고
    • Identification of the von Hippel-Lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex
    • Iwai, K. et al. Identification of the von Hippel-Lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex. Proc. Natl. Acad. Sci. USA 96, 12436-12441 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12436-12441
    • Iwai, K.1
  • 31
    • 35349008456 scopus 로고    scopus 로고
    • Potentiation of ICI182,780 (Fulvestrant)-induced estrogen receptor-alpha degradation by the estrogen receptor-related receptor-alpha inverse agonist XCT790
    • Lanvin, O., Bianco, S., Kersual, N., Chalbos, D. & Vanacker, J.M. Potentiation of ICI182,780 (Fulvestrant)-induced estrogen receptor-alpha degradation by the estrogen receptor-related receptor-alpha inverse agonist XCT790. J. Biol. Chem. 282, 28328-28334 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 28328-28334
    • Lanvin, O.1    Bianco, S.2    Kersual, N.3    Chalbos, D.4    Vanacker, J.M.5
  • 32
    • 77949874846 scopus 로고    scopus 로고
    • Potent and selective photo-inactivation of proteins with peptoid-ruthenium conjugates
    • Lee, J., Udugamasooriya, D.G., Lim, H.S. & Kodadek, T. Potent and selective photo-inactivation of proteins with peptoid-ruthenium conjugates. Nat. Chem. Biol. 6, 258-260 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 258-260
    • Lee, J.1    Udugamasooriya, D.G.2    Lim, H.S.3    Kodadek, T.4
  • 33
    • 0035347260 scopus 로고    scopus 로고
    • Induction of HIF-1a in response to hypoxia is instantaneous
    • Jewell, U.R. Induction of HIF-1a in response to hypoxia is instantaneous. FASEB J. 15, 1312-1314 (2001).
    • (2001) FASEB J. , vol.15 , pp. 1312-1314
    • Jewell, U.R.1
  • 34
    • 84892188402 scopus 로고    scopus 로고
    • Structural basis for hijacking CBF-β and CUL5 E3 ligase complex by HIV-1 Vif
    • Guo, Y. et al. Structural basis for hijacking CBF-β and CUL5 E3 ligase complex by HIV-1 Vif. Nature 505, 229-233 (2014).
    • (2014) Nature , vol.505 , pp. 229-233
    • Guo, Y.1
  • 35
    • 84877615286 scopus 로고    scopus 로고
    • A call to ARMs: The promise of immunomodulatory small molecules
    • Spiegel, D.A. A call to ARMs: the promise of immunomodulatory small molecules. Expert Rev. Clin. Pharmacol. 6, 223-225 (2013).
    • (2013) Expert Rev. Clin. Pharmacol. , vol.6 , pp. 223-225
    • Spiegel, D.A.1
  • 36
    • 69249218864 scopus 로고    scopus 로고
    • Design, synthesis and selection of DNA-encoded small-molecule libraries
    • Clark, M.A. et al. Design, synthesis and selection of DNA-encoded small-molecule libraries. Nat. Chem. Biol. 5, 647-654 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 647-654
    • Clark, M.A.1
  • 37
    • 84871581868 scopus 로고    scopus 로고
    • A HaloTag-based small molecule microarray screening methodology with increased sensitivity and multiplex capabilities
    • Noblin, D.J. et al. A HaloTag-based small molecule microarray screening methodology with increased sensitivity and multiplex capabilities. ACS Chem. Biol. 7, 2055-2063 (2012).
    • (2012) ACS Chem. Biol. , vol.7 , pp. 2055-2063
    • Noblin, D.J.1
  • 38
    • 33646587681 scopus 로고    scopus 로고
    • A robust small-molecule microarray platform for screening cell lysates
    • Bradner, J.E. et al. A robust small-molecule microarray platform for screening cell lysates. Chem. Biol. 13, 493-504 (2006).
    • (2006) Chem. Biol. , vol.13 , pp. 493-504
    • Bradner, J.E.1
  • 39
    • 34948875686 scopus 로고    scopus 로고
    • Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors
    • Bantscheff, M. et al. Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors. Nat. Biotechnol. 25, 1035-1044 (2007).
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1035-1044
    • Bantscheff, M.1
  • 40
    • 79952396960 scopus 로고    scopus 로고
    • Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes
    • Bantscheff, M. et al. Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes. Nat. Biotechnol. 29, 255-265 (2011).
    • (2011) Nat. Biotechnol. , vol.29 , pp. 255-265
    • Bantscheff, M.1
  • 41
    • 84906260520 scopus 로고    scopus 로고
    • Chemoproteomics reveals time-dependent binding of histone deacetylase inhibitors to endogenous repressor complexes
    • Becher, I. et al. Chemoproteomics reveals time-dependent binding of histone deacetylase inhibitors to endogenous repressor complexes. ACS Chem. Biol. 9, 1736-1746 (2014).
    • (2014) ACS Chem. Biol. , vol.9 , pp. 1736-1746
    • Becher, I.1
  • 42
    • 84861329091 scopus 로고    scopus 로고
    • A selective inhibitor reveals PI3Kγ dependence of TH17 cell differentiation
    • Bergamini, G. et al. A selective inhibitor reveals PI3Kγ dependence of TH17 cell differentiation. Nat. Chem. Biol. 8, 576-582 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 576-582
    • Bergamini, G.1
  • 43
    • 84865454296 scopus 로고    scopus 로고
    • High-resolution enabled TMT 8-plexing
    • Werner, T. et al. High-resolution enabled TMT 8-plexing. Anal. Chem. 84, 7188-7194 (2012).
    • (2012) Anal. Chem. , vol.84 , pp. 7188-7194
    • Werner, T.1
  • 44
    • 78651340521 scopus 로고    scopus 로고
    • Chemoproteomics-based kinome profiling and target deconvolution of clinical multi-kinase inhibitors in primary chronic lymphocytic leukemia cells
    • Kruse, U. et al. Chemoproteomics-based kinome profiling and target deconvolution of clinical multi-kinase inhibitors in primary chronic lymphocytic leukemia cells. Leukemia 25, 89-100 (2011).
    • (2011) Leukemia , vol.25 , pp. 89-100
    • Kruse, U.1
  • 45
    • 84897508532 scopus 로고    scopus 로고
    • Ion coalescence of neutron encoded TMT 10-plex reporter ions
    • Werner, T. et al. Ion coalescence of neutron encoded TMT 10-plex reporter ions. Anal. Chem. 86, 3594-3601 (2014).
    • (2014) Anal. Chem. , vol.86 , pp. 3594-3601
    • Werner, T.1
  • 46
    • 82555185589 scopus 로고    scopus 로고
    • Delayed fragmentation and optimized isolation width settings for improvement of protein identification and accuracy of isobaric mass tag quantification on Orbitrap-type mass spectrometers
    • Savitski, M.M. et al. Delayed fragmentation and optimized isolation width settings for improvement of protein identification and accuracy of isobaric mass tag quantification on Orbitrap-type mass spectrometers. Anal. Chem. 83, 8959-8967 (2011).
    • (2011) Anal. Chem. , vol.83 , pp. 8959-8967
    • Savitski, M.M.1
  • 47
    • 77956836941 scopus 로고    scopus 로고
    • Targeted data acquisition for improved reproducibility and robustness of proteomic mass spectrometry assays
    • Savitski, M.M. et al. Targeted data acquisition for improved reproducibility and robustness of proteomic mass spectrometry assays. J. Am. Soc. Mass Spectrom. 21, 1668-1679 (2010).
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1668-1679
    • Savitski, M.M.1
  • 48
    • 84881163875 scopus 로고    scopus 로고
    • Measuring and managing ratio compression for accurate iTRAQ/TMT quantification
    • Savitski, M.M. et al. Measuring and managing ratio compression for accurate iTRAQ/TMT quantification. J. Proteome Res. 12, 3586-3598 (2013).
    • (2013) J. Proteome Res. , vol.12 , pp. 3586-3598
    • Savitski, M.M.1
  • 49
    • 70349624519 scopus 로고    scopus 로고
    • Proteomics strategy for quantitative protein interaction profiling in cell extracts
    • Sharma, K. et al. Proteomics strategy for quantitative protein interaction profiling in cell extracts. Nat. Methods 6, 741-744 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 741-744
    • Sharma, K.1
  • 50
    • 77954660028 scopus 로고    scopus 로고
    • Implementation and evaluation of relative and absolute quantification in shotgun proteomics with label-free methods
    • Grossmann, J. et al. Implementation and evaluation of relative and absolute quantification in shotgun proteomics with label-free methods. J. Proteomics 73, 1740-1746 (2010).
    • (2010) J. Proteomics , vol.73 , pp. 1740-1746
    • Grossmann, J.1
  • 52
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372 (2008).
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 53
    • 0035829361 scopus 로고    scopus 로고
    • Controlling the false discovery rate in behavior genetics research
    • Benjamini, Y., Drai, D., Elmer, G., Kafkafi, N. & Golani, I. Controlling the false discovery rate in behavior genetics research. Behav. Brain Res. 125, 279-284 (2001).
    • (2001) Behav. Brain Res. , vol.125 , pp. 279-284
    • Benjamini, Y.1    Drai, D.2    Elmer, G.3    Kafkafi, N.4    Golani, I.5


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