메뉴 건너뛰기




Volumn 12, Issue 11, 2016, Pages 931-936

Inhibition of Mcl-1 through covalent modification of a noncatalytic lysine side chain

Author keywords

[No Author keywords available]

Indexed keywords

BORONIC ACID DERIVATIVE; CARBONYL DERIVATIVE; CASPASE 3; CASPASE 7; LYSINE; PROTEIN MCL 1; STAUROSPORINE; MCL1 PROTEIN, HUMAN;

EID: 84991584281     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.2174     Document Type: Article
Times cited : (150)

References (52)
  • 1
    • 76149109071 scopus 로고    scopus 로고
    • Targeting protein-protein interactions for therapeutic intervention: A challenge for the future
    • Zinzalla, G. & Thurston, D.E. Targeting protein-protein interactions for therapeutic intervention: a challenge for the future. Future Med. Chem. 1, 65-93 (2009).
    • (2009) Future Med. Chem. , vol.1 , pp. 65-93
    • Zinzalla, G.1    Thurston, D.E.2
  • 2
    • 84875436143 scopus 로고    scopus 로고
    • Inhibition of α-helix-mediated protein-protein interactions using designed molecules
    • Azzarito, V., Long, K., Murphy, N.S. & Wilson, A.J. Inhibition of α-helix-mediated protein-protein interactions using designed molecules. Nat. Chem. 5, 161-173 (2013).
    • (2013) Nat. Chem. , vol.5 , pp. 161-173
    • Azzarito, V.1    Long, K.2    Murphy, N.S.3    Wilson, A.J.4
  • 3
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • Arkin, M.R. & Wells, J.A. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat. Rev. Drug Discov. 3, 301-317 (2004).
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 4
    • 33645827371 scopus 로고    scopus 로고
    • Targeting protein-protein interactions by rational design: Mimicry of protein surfaces
    • Fletcher, S. & Hamilton, A.D. Targeting protein-protein interactions by rational design: mimicry of protein surfaces. J. R. Soc. Interface 3, 215-233 (2006).
    • (2006) J. R. Soc. Interface , vol.3 , pp. 215-233
    • Fletcher, S.1    Hamilton, A.D.2
  • 5
    • 84937416706 scopus 로고    scopus 로고
    • The promise and peril of chemical probes
    • Arrowsmith, C.H. et al. The promise and peril of chemical probes. Nat. Chem. Biol. 11, 536-541 (2015).
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 536-541
    • Arrowsmith, C.H.1
  • 6
    • 23944485507 scopus 로고    scopus 로고
    • Protein-protein interactions in drug discovery
    • Fischer, P.M. Protein-protein interactions in drug discovery. Drug Design Reviews Online 2, 179-207 (2005).
    • (2005) Drug Design Reviews Online , vol.2 , pp. 179-207
    • Fischer, P.M.1
  • 7
    • 0033981862 scopus 로고    scopus 로고
    • Covalent modification as a strategy to block protein-protein interactions with small-molecule drugs
    • Way, J.C. Covalent modification as a strategy to block protein-protein interactions with small-molecule drugs. Curr. Opin. Chem. Biol. 4, 40-46 (2000).
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 40-46
    • Way, J.C.1
  • 9
    • 44049103958 scopus 로고    scopus 로고
    • Residence time of receptor-ligand complexes and its effect on biological function
    • Tummino, P.J. & Copeland, R.A. Residence time of receptor-ligand complexes and its effect on biological function. Biochemistry 47, 5481-5492 (2008).
    • (2008) Biochemistry , vol.47 , pp. 5481-5492
    • Tummino, P.J.1    Copeland, R.A.2
  • 10
    • 33845364148 scopus 로고    scopus 로고
    • Fragment-based drug design: How big is too big?
    • Hajduk, P.J. Fragment-based drug design: how big is too big? J. Med. Chem. 49, 6972-6976 (2006).
    • (2006) J. Med. Chem. , vol.49 , pp. 6972-6976
    • Hajduk, P.J.1
  • 12
    • 77952312935 scopus 로고    scopus 로고
    • Determinants of BH3 binding specificity for Mcl-1 versus Bcl-xL
    • Dutta, S. et al. Determinants of BH3 binding specificity for Mcl-1 versus Bcl-xL. J. Mol. Biol. 398, 747-762 (2010).
    • (2010) J. Mol. Biol. , vol.398 , pp. 747-762
    • Dutta, S.1
  • 13
    • 60449094541 scopus 로고    scopus 로고
    • Beyond picomolar affinities: Quantitative aspects of noncovalent and covalent binding of drugs to proteins
    • Smith, A.J.T., Zhang, X., Leach, A.G. & Houk, K.N. Beyond picomolar affinities: quantitative aspects of noncovalent and covalent binding of drugs to proteins. J. Med. Chem. 52, 225-233 (2009).
    • (2009) J. Med. Chem. , vol.52 , pp. 225-233
    • Smith, A.J.T.1    Zhang, X.2    Leach, A.G.3    Houk, K.N.4
  • 14
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • Copeland, R.A., Pompliano, D.L. & Meek, T.D. Drug-target residence time and its implications for lead optimization. Nat. Rev. Drug Discov. 5, 730-739 (2006).
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 15
    • 84887977876 scopus 로고    scopus 로고
    • Discovery of a mutant-selective covalent inhibitor of EGFR that overcomes T790M-mediated resistance in NSCLC
    • Walter, A.O. et al. Discovery of a mutant-selective covalent inhibitor of EGFR that overcomes T790M-mediated resistance in NSCLC. Cancer Discov. 3, 1404-1415 (2013).
    • (2013) Cancer Discov. , vol.3 , pp. 1404-1415
    • Walter, A.O.1
  • 16
    • 84898016210 scopus 로고    scopus 로고
    • Selective inhibition of mutant Ras protein through covalent binding
    • Rudolph, J. & Stokoe, D. Selective inhibition of mutant Ras protein through covalent binding. Angew. Chem. Int. Ed. Engl. 53, 3777-3779 (2014).
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , pp. 3777-3779
    • Rudolph, J.1    Stokoe, D.2
  • 17
    • 84930083960 scopus 로고    scopus 로고
    • Structure-based design and synthesis of covalent-reversible inhibitors to overcome drug resistance in EGFR
    • Basu, D., Richters, A. & Rauh, D. Structure-based design and synthesis of covalent-reversible inhibitors to overcome drug resistance in EGFR. Bioorg. Med. Chem. 23, 2767-2780 (2015).
    • (2015) Bioorg. Med. Chem. , vol.23 , pp. 2767-2780
    • Basu, D.1    Richters, A.2    Rauh, D.3
  • 18
    • 84908371107 scopus 로고    scopus 로고
    • Discovery of a potent and selective EGFR inhibitor (AZD9291) of both sensitizing and T790M resistance mutations that spares the wild type form of the receptor
    • Finlay, M.R.V. et al. Discovery of a potent and selective EGFR inhibitor (AZD9291) of both sensitizing and T790M resistance mutations that spares the wild type form of the receptor. J. Med. Chem. 57, 8249-8267 (2014).
    • (2014) J. Med. Chem. , vol.57 , pp. 8249-8267
    • Finlay, M.R.V.1
  • 19
    • 84864246491 scopus 로고    scopus 로고
    • Irreversible protein kinase inhibitors: Balancing the benefits and risks
    • Barf, T. & Kaptein, A. Irreversible protein kinase inhibitors: balancing the benefits and risks. J. Med. Chem. 55, 6243-6262 (2012).
    • (2012) J. Med. Chem. , vol.55 , pp. 6243-6262
    • Barf, T.1    Kaptein, A.2
  • 20
    • 84865407060 scopus 로고    scopus 로고
    • Reversible covalent inhibition of a protein target
    • Lee, C.U. & Grossmann, T.N. Reversible covalent inhibition of a protein target. Angew. Chem. Int. Ed. Engl. 51, 8699-8700 (2012).
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 8699-8700
    • Lee, C.U.1    Grossmann, T.N.2
  • 21
    • 84859845948 scopus 로고    scopus 로고
    • Reversible targeting of noncatalytic cysteines with chemically tuned electrophiles
    • Serafimova, I.M. et al. Reversible targeting of noncatalytic cysteines with chemically tuned electrophiles. Nat. Chem. Biol. 8, 471-476 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 471-476
    • Serafimova, I.M.1
  • 22
    • 75349104695 scopus 로고    scopus 로고
    • Chemoselective small molecules that covalently modify one lysine in a non-enzyme protein in plasma
    • Choi, S., Connelly, S., Reixach, N., Wilson, I.A. & Kelly, J.W. Chemoselective small molecules that covalently modify one lysine in a non-enzyme protein in plasma. Nat. Chem. Biol. 6, 133-139 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 133-139
    • Choi, S.1    Connelly, S.2    Reixach, N.3    Wilson, I.A.4    Kelly, J.W.5
  • 23
    • 84941933056 scopus 로고    scopus 로고
    • Identification and characterization of an irreversible inhibitor of CDK2
    • Anscombe, E. et al. Identification and characterization of an irreversible inhibitor of CDK2. Chem. Biol. 22, 1159-1164 (2015).
    • (2015) Chem. Biol. , vol.22 , pp. 1159-1164
    • Anscombe, E.1
  • 24
    • 84862525703 scopus 로고    scopus 로고
    • Iminoboronates: A new strategy for reversible protein modification
    • Cal, P.M.S.D. et al. Iminoboronates: a new strategy for reversible protein modification. J. Am. Chem. Soc. 134, 10299-10305 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 10299-10305
    • Cal, P.M.S.D.1
  • 25
    • 84924560303 scopus 로고    scopus 로고
    • Targeting bacteria via iminoboronate chemistry of amine-presenting lipids
    • Bandyopadhyay, A., McCarthy, K.A., Kelly, M.A. & Gao, J. Targeting bacteria via iminoboronate chemistry of amine-presenting lipids. Nat. Commun. 6, 6561 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 6561
    • Bandyopadhyay, A.1    McCarthy, K.A.2    Kelly, M.A.3    Gao, J.4
  • 26
    • 37549040575 scopus 로고    scopus 로고
    • The challenge of drugging undruggable targets in cancer: Lessons learned from targeting BCL-2 family members
    • Verdine, G.L. & Walensky, L.D. The challenge of drugging undruggable targets in cancer: lessons learned from targeting BCL-2 family members. Clin. Cancer Res. 13, 7264-7270 (2007).
    • (2007) Clin. Cancer Res. , vol.13 , pp. 7264-7270
    • Verdine, G.L.1    Walensky, L.D.2
  • 27
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory, S. & Adams, J.M. The Bcl2 family: regulators of the cellular life-or-death switch. Nat. Rev. Cancer 2, 647-656 (2002).
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 28
    • 84890909335 scopus 로고    scopus 로고
    • Control of apoptosis by the BCL-2 protein family: Implications for physiology and therapy
    • Czabotar, P.E., Lessene, G., Strasser, A. & Adams, J.M. Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy. Nat. Rev. Mol. Cell Biol. 15, 49-63 (2014).
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 49-63
    • Czabotar, P.E.1    Lessene, G.2    Strasser, A.3    Adams, J.M.4
  • 29
    • 77249119762 scopus 로고    scopus 로고
    • The landscape of somatic copy-number alteration across human cancers
    • Beroukhim, R. et al. The landscape of somatic copy-number alteration across human cancers. Nature 463, 899-905 (2010).
    • (2010) Nature , vol.463 , pp. 899-905
    • Beroukhim, R.1
  • 30
    • 84859825629 scopus 로고    scopus 로고
    • Chemical genomics identifies small-molecule MCL1 repressors and BCL-xL as a predictor of MCL1 dependency
    • Wei, G. et al. Chemical genomics identifies small-molecule MCL1 repressors and BCL-xL as a predictor of MCL1 dependency. Cancer Cell 21, 547-562 (2012).
    • (2012) Cancer Cell , vol.21 , pp. 547-562
    • Wei, G.1
  • 31
    • 84878907241 scopus 로고    scopus 로고
    • MCL1 is deregulated in subgroups of diffuse large B-cell lymphoma
    • Wenzel, S.S. et al. MCL1 is deregulated in subgroups of diffuse large B-cell lymphoma. Leukemia 27, 1381-1390 (2013).
    • (2013) Leukemia , vol.27 , pp. 1381-1390
    • Wenzel, S.S.1
  • 32
    • 84883546687 scopus 로고    scopus 로고
    • BAD dephosphorylation and decreased expression of MCL-1 induce rapid apoptosis in prostate cancer cells
    • Yancey, D. et al. BAD dephosphorylation and decreased expression of MCL-1 induce rapid apoptosis in prostate cancer cells. PLoS One 8, e74561 (2013).
    • (2013) PLoS One , vol.8 , pp. e74561
    • Yancey, D.1
  • 33
    • 84913554608 scopus 로고    scopus 로고
    • Overexpression of Mcl-1L splice variant is associated with poor prognosis and chemoresistance in oral cancers
    • Palve, V., Mallick, S., Ghaisas, G., Kannan, S. & Teni, T. Overexpression of Mcl-1L splice variant is associated with poor prognosis and chemoresistance in oral cancers. PLoS One 9, e111927 (2014).
    • (2014) PLoS One , vol.9 , pp. e111927
    • Palve, V.1    Mallick, S.2    Ghaisas, G.3    Kannan, S.4    Teni, T.5
  • 34
    • 84924229796 scopus 로고    scopus 로고
    • Bcl-2 family proteins in breast development and cancer: Could Mcl-1 targeting overcome therapeutic resistance?
    • Williams, M.M. & Cook, R.S. Bcl-2 family proteins in breast development and cancer: could Mcl-1 targeting overcome therapeutic resistance? Oncotarget 6, 3519-3530 (2015).
    • (2015) Oncotarget , vol.6 , pp. 3519-3530
    • Williams, M.M.1    Cook, R.S.2
  • 35
    • 57049155399 scopus 로고    scopus 로고
    • Directing cancer cells to self-destruct with pro-apoptotic receptor agonists
    • Ashkenazi, A. Directing cancer cells to self-destruct with pro-apoptotic receptor agonists. Nat. Rev. Drug Discov. 7, 1001-1012 (2008).
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 1001-1012
    • Ashkenazi, A.1
  • 36
    • 28044468839 scopus 로고    scopus 로고
    • A novel antisense oligonucleotide inhibiting several antiapoptotic Bcl-2 family members induces apoptosis and enhances chemosensitivity in androgen-independent human prostate cancer PC3 cells
    • Yamanaka, K. et al. A novel antisense oligonucleotide inhibiting several antiapoptotic Bcl-2 family members induces apoptosis and enhances chemosensitivity in androgen-independent human prostate cancer PC3 cells. Mol. Cancer Ther. 4, 1689-1698 (2005).
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1689-1698
    • Yamanaka, K.1
  • 37
    • 84866654914 scopus 로고    scopus 로고
    • A competitive stapled peptide screen identifies a selective small molecule that overcomes MCL-1-dependent leukemia cell survival
    • Cohen, N.A. et al. A competitive stapled peptide screen identifies a selective small molecule that overcomes MCL-1-dependent leukemia cell survival. Chem. Biol. 19, 1175-1186 (2012).
    • (2012) Chem. Biol. , vol.19 , pp. 1175-1186
    • Cohen, N.A.1
  • 38
    • 84866419568 scopus 로고    scopus 로고
    • Rational design of proteolytically stable, cell-permeable peptide-based selective Mcl-1 inhibitors
    • Muppidi, A. et al. Rational design of proteolytically stable, cell-permeable peptide-based selective Mcl-1 inhibitors. J. Am. Chem. Soc. 134, 14734-14737 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 14734-14737
    • Muppidi, A.1
  • 39
    • 84890465064 scopus 로고    scopus 로고
    • Discovery of potent Mcl-1/Bcl-xL dual inhibitors by using a hybridization strategy based on structural analysis of target proteins
    • Tanaka, Y. et al. Discovery of potent Mcl-1/Bcl-xL dual inhibitors by using a hybridization strategy based on structural analysis of target proteins. J. Med. Chem. 56, 9635-9645 (2013).
    • (2013) J. Med. Chem. , vol.56 , pp. 9635-9645
    • Tanaka, Y.1
  • 40
    • 84872301920 scopus 로고    scopus 로고
    • Discovery of potent myeloid cell leukemia 1 (Mcl-1) inhibitors using fragment-based methods and structure-based design
    • Friberg, A. et al. Discovery of potent myeloid cell leukemia 1 (Mcl-1) inhibitors using fragment-based methods and structure-based design. J. Med. Chem. 56, 15-30 (2013).
    • (2013) J. Med. Chem. , vol.56 , pp. 15-30
    • Friberg, A.1
  • 43
    • 84924674523 scopus 로고    scopus 로고
    • Structure-guided design of a series of MCL-1 inhibitors with high affinity and selectivity
    • Bruncko, M. et al. Structure-guided design of a series of MCL-1 inhibitors with high affinity and selectivity. J. Med. Chem. 58, 2180-2194 (2015).
    • (2015) J. Med. Chem. , vol.58 , pp. 2180-2194
    • Bruncko, M.1
  • 44
    • 84992101172 scopus 로고    scopus 로고
    • Evaluation of Mcl-1 inhibitors in preclinical models of multiple myeloma
    • Belmonte, M.A. et al. Evaluation of Mcl-1 inhibitors in preclinical models of multiple myeloma. Blood 124, 3428 (2014).
    • (2014) Blood , vol.124 , pp. 3428
    • Belmonte, M.A.1
  • 45
    • 84959374954 scopus 로고    scopus 로고
    • BH3 profiling identifies heterogeneous dependency on Bcl-2 family members in multiple myeloma and predicts sensitivity to BH3 mimetics
    • Touzeau, C. et al. BH3 profiling identifies heterogeneous dependency on Bcl-2 family members in multiple myeloma and predicts sensitivity to BH3 mimetics. Leukemia 30, 761-764 (2016).
    • (2016) Leukemia , vol.30 , pp. 761-764
    • Touzeau, C.1
  • 46
    • 84907841902 scopus 로고    scopus 로고
    • MCL1 and BCL-xL levels in solid tumors are predictive of dinaciclib-induced apoptosis
    • Booher, R.N. et al. MCL1 and BCL-xL levels in solid tumors are predictive of dinaciclib-induced apoptosis. PLoS One 9, e108371 (2014).
    • (2014) PLoS One , vol.9 , pp. e108371
    • Booher, R.N.1
  • 47
    • 84929340720 scopus 로고    scopus 로고
    • Reversible lysine modification on proteins by using functionalized boronic acids
    • Cal, P.M.S.D., Frade, R.F.M., Cordeiro, C. & Gois, P.M.P. Reversible lysine modification on proteins by using functionalized boronic acids. Chemistry 21, 8182-8187 (2015).
    • (2015) Chemistry , vol.21 , pp. 8182-8187
    • Cal, P.M.S.D.1    Frade, R.F.M.2    Cordeiro, C.3    Gois, P.M.P.4
  • 48
    • 84891496533 scopus 로고    scopus 로고
    • Drug discovery considerations in the development of covalent inhibitors
    • Mah, R., Thomas, J.R. & Shafer, C.M. Drug discovery considerations in the development of covalent inhibitors. Bioorg. Med. Chem. Lett. 24, 33-39 (2014).
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 33-39
    • Mah, R.1    Thomas, J.R.2    Shafer, C.M.3
  • 49
    • 84918821230 scopus 로고    scopus 로고
    • Small molecule Mcl-1 inhibitors for the treatment of cancer
    • Belmar, J. & Fesik, S.W. Small molecule Mcl-1 inhibitors for the treatment of cancer. Pharmacol. Ther. 145, 76-84 (2015).
    • (2015) Pharmacol. Ther. , vol.145 , pp. 76-84
    • Belmar, J.1    Fesik, S.W.2
  • 50
    • 84925356890 scopus 로고    scopus 로고
    • Interactions of the natural product (+)-avrainvillamide with nucleophosmin and exportin-1 mediate the cellular localization of nucleophosmin and its AML-associated mutants
    • Mukherjee, H. et al. Interactions of the natural product (+)-avrainvillamide with nucleophosmin and exportin-1 mediate the cellular localization of nucleophosmin and its AML-associated mutants. ACS Chem. Biol. 10, 855-863 (2015).
    • (2015) ACS Chem. Biol. , vol.10 , pp. 855-863
    • Mukherjee, H.1
  • 51
    • 85016377807 scopus 로고    scopus 로고
    • Structure modification in chemical databases
    • (ed., T.I. Oprea) Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, FRG)
    • Kenny, P.W. & Sadowski, J. Structure modification in chemical databases. in Chemoinformatics in Drug Discovery (ed., T.I. Oprea) Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, FRG) 271-285 (2005).
    • (2005) Chemoinformatics in Drug Discovery , pp. 271-285
    • Kenny, P.W.1    Sadowski, J.2
  • 52


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.