메뉴 건너뛰기




Volumn 13, Issue 5, 2017, Pages 514-521

Structural basis of PROTAC cooperative recognition for selective protein degradation

Author keywords

[No Author keywords available]

Indexed keywords

BRD2 PROTEIN; BRD3 PROTEIN; BRD4 PROTEIN; BROMODOMAIN INHIBITOR; ELONGIN B; ELONGIN C; HISTONE H4; HYPOXIA INDUCIBLE FACTOR 1ALPHA; LYSINE; MZ1 PROTEIN; PENICILLAMINE; PROTEIN; TERNARY COMPLEX FACTOR; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN; AT1 COMPOUND; BRD4 PROTEIN, HUMAN; DIPEPTIDE; ELONGIN; FUSED HETEROCYCLIC RINGS; MOLECULAR LIBRARY; MULTIPROTEIN COMPLEX; MZ1 COMPOUND; NUCLEAR PROTEIN; PROTEIN BINDING; TRANSCRIPTION FACTOR; UBIQUITIN PROTEIN LIGASE; VHL PROTEIN, HUMAN;

EID: 85015018807     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.2329     Document Type: Article
Times cited : (814)

References (42)
  • 1
    • 84963540125 scopus 로고    scopus 로고
    • Drugging the undruggables: Exploring the ubiquitin system for drug development
    • Huang, X., Dixit, V. M. Drugging the undruggables: Exploring the ubiquitin system for drug development. Cell Res. 26, 484-498 (2016).
    • (2016) Cell Res. , vol.26 , pp. 484-498
    • Huang, X.1    Dixit, V.M.2
  • 2
    • 84963542597 scopus 로고    scopus 로고
    • Structural basis of lenalidomide-induced CK1 degradation by the CRL4(CRBN) ubiquitin ligase
    • Petzold, G., Fischer, E. S., Thomä, N. H. Structural basis of lenalidomide-induced CK1 degradation by the CRL4(CRBN) ubiquitin ligase. Nature 532, 127-130 (2016).
    • (2016) Nature , vol.532 , pp. 127-130
    • Petzold, G.1    Fischer, E.S.2    Thomä, N.H.3
  • 3
    • 84978715161 scopus 로고    scopus 로고
    • A novel cereblon modulator recruits GSPT1 to the CRL4(CRBN) ubiquitin ligase
    • Matyskiela, M. E., et al. A novel cereblon modulator recruits GSPT1 to the CRL4(CRBN) ubiquitin ligase. Nature 535, 252-257 (2016).
    • (2016) Nature , vol.535 , pp. 252-257
    • Matyskiela, M.E.1
  • 4
    • 84996848891 scopus 로고    scopus 로고
    • Induced protein degradation: An emerging drug discovery paradigm
    • Lai, A. C., Crews, C. M. Induced protein degradation: An emerging drug discovery paradigm. Nat. Rev. Drug Discov. 16, 101-114 (2016).
    • (2016) Nat. Rev. Drug Discov. , vol.16 , pp. 101-114
    • Lai, A.C.1    Crews, C.M.2
  • 5
    • 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
  • 6
    • 84932634729 scopus 로고    scopus 로고
    • Drug development Phthalimide conjugation as a strategy for in vivo target protein degradation
    • Winter, G. E., et al. Drug development. Phthalimide conjugation as a strategy for in vivo target protein degradation. Science 348, 1376-1381 (2015).
    • (2015) Science , vol.348 , pp. 1376-1381
    • Winter, G.E.1
  • 7
    • 84939788143 scopus 로고    scopus 로고
    • Selective small molecule induced degradation of the BET bromodomain protein BRD4
    • Zengerle, M., Chan, K.-H., Ciulli, A. Selective small molecule induced degradation of the BET bromodomain protein BRD4. ACS Chem. Biol. 10, 1770-1777 (2015).
    • (2015) ACS Chem. Biol. , vol.10 , pp. 1770-1777
    • Zengerle, M.1    Chan, K.-H.2    Ciulli, A.3
  • 8
    • 84931560527 scopus 로고    scopus 로고
    • Hijacking the E3 ubiquitin ligase cereblon to efficiently target BRD4
    • Lu, J., et al. Hijacking the E3 ubiquitin ligase cereblon to efficiently target BRD4. Chem. Biol. 22, 755-763 (2015).
    • (2015) Chem. Biol. , vol.22 , pp. 755-763
    • Lu, J.1
  • 9
    • 84937514576 scopus 로고    scopus 로고
    • Catalytic in vivo protein knockdown by small-molecule PROTACs
    • Bondeson, D. P., et al. Catalytic in vivo protein knockdown by small-molecule PROTACs. Nat. Chem. Biol. 11, 611-617 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 611-617
    • Bondeson, D.P.1
  • 10
    • 84939552495 scopus 로고    scopus 로고
    • Protein degradation: Prime time for PROTACs
    • Deshaies, R. J. Protein degradation: Prime time for PROTACs. Nat. Chem. Biol. 11, 634-635 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 634-635
    • Deshaies, R.J.1
  • 11
    • 84961285814 scopus 로고    scopus 로고
    • Small-molecule PROTACS: New approaches to protein degradation
    • Toure, M., Crews, C. M. Small-molecule PROTACS: New approaches to protein degradation. Angew. Chem. Int. Edn Engl. 55, 1966-1973 (2016).
    • (2016) Angew. Chem. Int. Edn Engl. , vol.55 , pp. 1966-1973
    • Toure, M.1    Crews, C.M.2
  • 12
    • 84958748153 scopus 로고    scopus 로고
    • Modular PROTAC design for the degradation of oncogenic BCR-ABL
    • Lai, A. C., et al. Modular PROTAC design for the degradation of oncogenic BCR-ABL. Angew. Chem. Int. Edn Engl. 55, 807-810 (2016).
    • (2016) Angew. Chem. Int. Edn Engl. , vol.55 , pp. 807-810
    • Lai, A.C.1
  • 13
    • 78650847770 scopus 로고    scopus 로고
    • Selective inhibition of BET bromodomains
    • Filippakopoulos, P., et al. Selective inhibition of BET bromodomains. Nature 468, 1067-1073 (2010).
    • (2010) Nature , vol.468 , pp. 1067-1073
    • Filippakopoulos, P.1
  • 14
    • 84908373179 scopus 로고    scopus 로고
    • Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von Hippel-Lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities
    • Galdeano, C., et al. Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von Hippel-Lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities. J. Med. Chem. 57, 8657-8663 (2014).
    • (2014) J. Med. Chem. , vol.57 , pp. 8657-8663
    • Galdeano, C.1
  • 15
    • 84994592337 scopus 로고    scopus 로고
    • Potent and selective chemical probe of hypoxic signalling downstream of HIF-hydroxylation via VHL inhibition
    • Frost, J., et al. Potent and selective chemical probe of hypoxic signalling downstream of HIF-hydroxylation via VHL inhibition. Nat. Commun. 7, 13312 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 13312
    • Frost, J.1
  • 16
    • 80055000824 scopus 로고    scopus 로고
    • RNAi screen identifies Brd4 as a therapeutic target in acute myeloid leukaemia
    • Zuber, J., et al. RNAi screen identifies Brd4 as a therapeutic target in acute myeloid leukaemia. Nature 478, 524-528 (2011).
    • (2011) Nature , vol.478 , pp. 524-528
    • Zuber, J.1
  • 17
    • 78650806593 scopus 로고    scopus 로고
    • Suppression of inflammation by a synthetic histone mimic
    • Nicodeme, E., et al. Suppression of inflammation by a synthetic histone mimic. Nature 468, 1119-1123 (2010).
    • (2010) Nature , vol.468 , pp. 1119-1123
    • Nicodeme, E.1
  • 18
    • 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
  • 19
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1alpha-pVHL complex: Hydroxyproline recognition in signaling
    • Min, J.-H., et al. Structure of an HIF-1alpha-pVHL complex: Hydroxyproline recognition in signaling. Science 296, 1886-1889 (2002).
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.-H.1
  • 20
    • 84859181036 scopus 로고    scopus 로고
    • Histone recognition and large-scale structural analysis of the human bromodomain family
    • Filippakopoulos, P., et al. Histone recognition and large-scale structural analysis of the human bromodomain family. Cell 149, 214-231 (2012).
    • (2012) Cell , vol.149 , pp. 214-231
    • Filippakopoulos, P.1
  • 21
    • 84992313205 scopus 로고    scopus 로고
    • Design and characterization of bivalent BET inhibitors
    • Tanaka, M., et al. Design and characterization of bivalent BET inhibitors. Nat. Chem. Biol. 12, 1089-1096 (2016).
    • (2016) Nat. Chem. Biol. , vol.12 , pp. 1089-1096
    • Tanaka, M.1
  • 22
    • 47649098600 scopus 로고    scopus 로고
    • Cooperativity and biological complexity
    • Whitty, A. Cooperativity and biological complexity. Nat. Chem. Biol. 4, 435-439 (2008).
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 435-439
    • Whitty, A.1
  • 24
    • 85056062287 scopus 로고    scopus 로고
    • The use of AlphaScreen technology in HTS: Current status
    • Eglen, R. M., et al. The use of AlphaScreen technology in HTS: Current status. Curr. Chem. Genomics 1, 2-10 (2008).
    • (2008) Curr. Chem. Genomics , vol.1 , pp. 2-10
    • Eglen, R.M.1
  • 25
    • 84994050174 scopus 로고    scopus 로고
    • A bead-based proximity assay for BRD4 ligand discovery
    • Roberts, J. M., Bradner, J. E. A bead-based proximity assay for BRD4 ligand discovery. Curr. Protoc. Chem. Biol. 7, 263-278 (2015).
    • (2015) Curr. Protoc. Chem. Biol. , vol.7 , pp. 263-278
    • Roberts, J.M.1    Bradner, J.E.2
  • 26
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-elonginc-elongin B complex: Implications for VHL tumor suppressor function
    • Stebbins, C. E., Kaelin, W. G. Jr., Pavletich, N. P. Structure of the VHL-ElonginC-ElonginB complex: Implications for VHL tumor suppressor function. Science 284, 455-461 (1999).
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin, W.G.2    Pavletich, N.P.3
  • 27
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda, D. M., et al. Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation. Cell 134, 995-1006 (2008).
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1
  • 28
    • 84958601201 scopus 로고    scopus 로고
    • Current experimental methods for characterizing protein-protein interactions
    • Zhou, M., Li, Q., Wang, R. Current experimental methods for characterizing protein-protein interactions. ChemMedChem 11, 738-756 (2016).
    • (2016) Chem Med Chem , vol.11 , pp. 738-756
    • Zhou, M.1    Li, Q.2    Wang, R.3
  • 29
    • 84976614642 scopus 로고    scopus 로고
    • PROTAC-induced BET protein degradation as a therapy for castration-resistant prostate cancer
    • Raina, K., et al. PROTAC-induced BET protein degradation as a therapy for castration-resistant prostate cancer. Proc. Natl. Acad. Sci. USA 113, 7124-7129 (2016).
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. 7124-7129
    • Raina, K.1
  • 30
    • 84934901165 scopus 로고    scopus 로고
    • Targeting Cullin-RING E3 ubiquitin ligases for drug discovery: Structure, assembly and small-molecule modulation
    • Bulatov, E., Ciulli, A. Targeting Cullin-RING E3 ubiquitin ligases for drug discovery: Structure, assembly and small-molecule modulation. Biochem. J. 467, 365-386 (2015).
    • (2015) Biochem. J. , vol.467 , pp. 365-386
    • Bulatov, E.1    Ciulli, A.2
  • 31
    • 84905568369 scopus 로고    scopus 로고
    • Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with thalidomide
    • Fischer, E. S., et al. Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with thalidomide. Nature 512, 49-53 (2014).
    • (2014) Nature , vol.512 , pp. 49-53
    • Fischer, E.S.1
  • 33
    • 34247219263 scopus 로고    scopus 로고
    • Mechanism of auxin perception by the TIR1 ubiquitin ligase
    • Tan, X., et al. Mechanism of auxin perception by the TIR1 ubiquitin ligase. Nature 446, 640-645 (2007).
    • (2007) Nature , vol.446 , pp. 640-645
    • Tan, X.1
  • 34
    • 78549274705 scopus 로고    scopus 로고
    • Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-receptor
    • Sheard, L. B., et al. Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-receptor. Nature 468, 400-405 (2010).
    • (2010) Nature , vol.468 , pp. 400-405
    • Sheard, L.B.1
  • 35
    • 77949350034 scopus 로고    scopus 로고
    • Identification of a primary target of thalidomide teratogenicity
    • Ito, T., et al. Identification of a primary target of thalidomide teratogenicity. Science 327, 1345-1350 (2010).
    • (2010) Science , vol.327 , pp. 1345-1350
    • Ito, T.1
  • 36
    • 84892593087 scopus 로고    scopus 로고
    • The myeloma drug lenalidomide promotes the cereblon-dependent destruction of Ikaros proteins
    • Lu, G., et al. The myeloma drug lenalidomide promotes the cereblon-dependent destruction of Ikaros proteins. Science 343, 305-309 (2014).
    • (2014) Science , vol.343 , pp. 305-309
    • Lu, G.1
  • 37
    • 84892576029 scopus 로고    scopus 로고
    • Lenalidomide causes selective degradation of IKZF1 and IKZF3 in multiple myeloma cells
    • Krönke, J., et al. Lenalidomide causes selective degradation of IKZF1 and IKZF3 in multiple myeloma cells. Science 343, 301-305 (2014).
    • (2014) Science , vol.343 , pp. 301-305
    • Krönke, J.1
  • 38
    • 84916880505 scopus 로고    scopus 로고
    • Structure of the human Cereblon-DDB1-lenalidomide complex reveals basis for responsiveness to thalidomide analogs
    • Chamberlain, P. P., et al. Structure of the human Cereblon-DDB1-lenalidomide complex reveals basis for responsiveness to thalidomide analogs. Nat. Struct. Mol. Biol. 21, 803-809 (2014).
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 803-809
    • Chamberlain, P.P.1
  • 39
    • 84855347756 scopus 로고    scopus 로고
    • Interfacial inhibitors: Targeting macromolecular complexes
    • Pommier, Y., Marchand, C. Interfacial inhibitors: Targeting macromolecular complexes. Nat. Rev. Drug Discov. 11, 25-36 (2011).
    • (2011) Nat. Rev. Drug Discov. , vol.11 , pp. 25-36
    • Pommier, Y.1    Marchand, C.2
  • 40
    • 84857509304 scopus 로고    scopus 로고
    • Small-molecule stabilization of protein-protein interactions: An underestimated concept in drug discovery Angew
    • Thiel, P., Kaiser, M., Ottmann, C. Small-molecule stabilization of protein-protein interactions: An underestimated concept in drug discovery Angew. Chem. Int. Edn Engl. 51, 2012-2018 (2012).
    • (2012) Chem. Int. Edn Engl. , vol.51 , pp. 2012-2018
    • Thiel, P.1    Kaiser, M.2    Ottmann, C.3
  • 41
    • 84922949970 scopus 로고    scopus 로고
    • Chemical biology A small-molecule inhibitor of the aberrant transcription factor CBF-SMMHC delays leukemia in mice
    • Illendula, A., et al. Chemical biology. A small-molecule inhibitor of the aberrant transcription factor CBF-SMMHC delays leukemia in mice. Science 347, 779-784 (2015).
    • (2015) Science , vol.347 , pp. 779-784
    • Illendula, A.1
  • 42
    • 84986242046 scopus 로고    scopus 로고
    • Potent and selective bivalent inhibitors of BET bromodomains
    • Waring, M. J., et al. Potent and selective bivalent inhibitors of BET bromodomains. Nat. Chem. Biol. 12, 1097-1104 (2016).
    • (2016) Nat. Chem. Biol. , vol.12 , pp. 1097-1104
    • Waring, M.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.