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Volumn 24, Issue 11, 2017, Pages 1388-1400.e7

Proteome-wide Map of Targets of T790M-EGFR-Directed Covalent Inhibitors

Author keywords

cathepsins; chemical probes; covalent inhibitors; kinases; lysosomal accumulation; proteomics; T790M EGFR

Indexed keywords

AFATINIB; CATHEPSIN; CHECKPOINT KINASE 2; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE INHIBITOR; OSIMERTINIB; PROTEOME; STREPTAVIDIN; 5' NUCLEOTIDASE; CHEK2 PROTEIN, HUMAN; CYSTEINE; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; NT5E PROTEIN, HUMAN; PIPERAZINE DERIVATIVE; PROTEIN KINASE INHIBITOR; RHODAMINE;

EID: 85030723605     PISSN: 24519456     EISSN: 24519448     Source Type: Journal    
DOI: 10.1016/j.chembiol.2017.08.017     Document Type: Article
Times cited : (78)

References (61)
  • 2
    • 85040257501 scopus 로고    scopus 로고
    • 136O: Osimertinib combined with durvalumab in EGFR-mutant non-small cell lung cancer: Results from the TATTON phase Ib trial
    • Ahn, M.J., Yang, J., Yu, H., Saka, H., Ramalingam, S., Goto, K., Kim, S.W., Yang, L., Walding, A., Oxnard, G.R., 136O: Osimertinib combined with durvalumab in EGFR-mutant non-small cell lung cancer: Results from the TATTON phase Ib trial. J. Thorac. Oncol., 11, 2016, S115.
    • (2016) J. Thorac. Oncol. , vol.11 , pp. S115
    • Ahn, M.J.1    Yang, J.2    Yu, H.3    Saka, H.4    Ramalingam, S.5    Goto, K.6    Kim, S.W.7    Yang, L.8    Walding, A.9    Oxnard, G.R.10
  • 3
    • 36448973875 scopus 로고    scopus 로고
    • CHK2 kinase: cancer susceptibility and cancer therapy—two sides of the same coin?
    • Antoni, L., Sodha, N., Collins, I., Garrett, M.D., CHK2 kinase: cancer susceptibility and cancer therapy—two sides of the same coin?. Nat. Rev. Cancer 7 (2007), 925–936.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 925-936
    • Antoni, L.1    Sodha, N.2    Collins, I.3    Garrett, M.D.4
  • 5
    • 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 (2012), 6243–6262.
    • (2012) J. Med. Chem. , vol.55 , pp. 6243-6262
    • Barf, T.1    Kaptein, A.2
  • 7
    • 0034054576 scopus 로고    scopus 로고
    • Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs
    • Bogyo, M., Verhelst, S., Bellingard-Dubouchaud, V., Toba, S., Greenbaum, D., Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs. Chem. Biol. 7 (2000), 27–38.
    • (2000) Chem. Biol. , vol.7 , pp. 27-38
    • Bogyo, M.1    Verhelst, S.2    Bellingard-Dubouchaud, V.3    Toba, S.4    Greenbaum, D.5
  • 8
    • 67649628133 scopus 로고    scopus 로고
    • Cathepsin K inhibitors for osteoporosis and potential off-target effects
    • Bromme, D., Lecaille, F., Cathepsin K inhibitors for osteoporosis and potential off-target effects. Expert Opin. Investig. Drugs 18 (2009), 585–600.
    • (2009) Expert Opin. Investig. Drugs , vol.18 , pp. 585-600
    • Bromme, D.1    Lecaille, F.2
  • 10
    • 84960910347 scopus 로고    scopus 로고
    • Discovery of 1-{(3R,4R)-3-[({5-chloro-2-[(1-methyl-1H-pyrazol-4-yl)amino]-7H-pyrrolo[2,3-d]pyr imidin-4-yl}oxy)methyl]-4-methoxypyrrolidin-1-yl}prop-2-en-1-one (PF-06459988), a potent, WT sparing, irreversible inhibitor of T790M-containing EGFR mutants
    • Cheng, H., Nair, S.K., Murray, B.W., Almaden, C., Bailey, S., Baxi, S., Behenna, D., Cho-Schultz, S., Dalvie, D., Dinh, D.M., et al. Discovery of 1-{(3R,4R)-3-[({5-chloro-2-[(1-methyl-1H-pyrazol-4-yl)amino]-7H-pyrrolo[2,3-d]pyr imidin-4-yl}oxy)methyl]-4-methoxypyrrolidin-1-yl}prop-2-en-1-one (PF-06459988), a potent, WT sparing, irreversible inhibitor of T790M-containing EGFR mutants. J. Med. Chem. 59 (2016), 2005–2024.
    • (2016) J. Med. Chem. , vol.59 , pp. 2005-2024
    • Cheng, H.1    Nair, S.K.2    Murray, B.W.3    Almaden, C.4    Bailey, S.5    Baxi, S.6    Behenna, D.7    Cho-Schultz, S.8    Dalvie, D.9    Dinh, D.M.10
  • 12
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: from enzyme chemistry to proteomic chemistry
    • Cravatt, B.F., Wright, A.T., Kozarich, J.W., Activity-based protein profiling: from enzyme chemistry to proteomic chemistry. Annu. Rev. Biochem. 77 (2008), 383–414.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 17
    • 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., Anderton, M., Ashton, S., Ballard, P., Bethel, P.A., Box, M.R., Bradbury, R.H., Brown, S.J., Butterworth, S., Campbell, A., 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 (2014), 8249–8267.
    • (2014) J. Med. Chem. , vol.57 , pp. 8249-8267
    • Finlay, M.R.1    Anderton, M.2    Ashton, S.3    Ballard, P.4    Bethel, P.A.5    Box, M.R.6    Bradbury, R.H.7    Brown, S.J.8    Butterworth, S.9    Campbell, A.10
  • 20
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum, D., Medzihradszky, K.F., Burlingame, A., Bogyo, M., Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem. Biol. 7 (2000), 569–581.
    • (2000) Chem. Biol. , vol.7 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 25
    • 77953631133 scopus 로고    scopus 로고
    • Strategies for discovering and derisking covalent, irreversible enzyme inhibitors
    • Johnson, D.S., Weerapana, E., Cravatt, B.F., Strategies for discovering and derisking covalent, irreversible enzyme inhibitors. Future Med. Chem. 2 (2010), 949–964.
    • (2010) Future Med. Chem. , vol.2 , pp. 949-964
    • Johnson, D.S.1    Weerapana, E.2    Cravatt, B.F.3
  • 28
    • 36049026281 scopus 로고    scopus 로고
    • Chemical genomic and proteomic methods for determining kinase inhibitor selectivity
    • Krishnamurty, R., Maly, D.J., Chemical genomic and proteomic methods for determining kinase inhibitor selectivity. Comb. Chem. High Throughput Screen. 10 (2007), 652–666.
    • (2007) Comb. Chem. High Throughput Screen. , vol.10 , pp. 652-666
    • Krishnamurty, R.1    Maly, D.J.2
  • 30
    • 84896950653 scopus 로고    scopus 로고
    • Small-molecule probes elucidate global enzyme activity in a proteomic context
    • Lee, J.S., Yoo, Y.H., Yoon, C.N., Small-molecule probes elucidate global enzyme activity in a proteomic context. BMB Rep. 47 (2014), 149–157.
    • (2014) BMB Rep. , vol.47 , pp. 149-157
    • Lee, J.S.1    Yoo, Y.H.2    Yoon, C.N.3
  • 31
    • 85034077031 scopus 로고    scopus 로고
    • Heterocyclic compounds and uses thereof. Google Patents.
    • Lee, K., Niu, D., Petter, R.C., Baevsky, M.F., and Singh, J. (2015). Heterocyclic compounds and uses thereof. Google Patents.
    • (2015)
    • Lee, K.1    Niu, D.2    Petter, R.C.3    Baevsky, M.F.4    Singh, J.5
  • 32
    • 79952269716 scopus 로고    scopus 로고
    • Cysteine mapping in conformationally distinct kinase nucleotide binding sites: application to the design of selective covalent inhibitors
    • Leproult, E., Barluenga, S., Moras, D., Wurtz, J.M., Winssinger, N., Cysteine mapping in conformationally distinct kinase nucleotide binding sites: application to the design of selective covalent inhibitors. J. Med. Chem. 54 (2011), 1347–1355.
    • (2011) J. Med. Chem. , vol.54 , pp. 1347-1355
    • Leproult, E.1    Barluenga, S.2    Moras, D.3    Wurtz, J.M.4    Winssinger, N.5
  • 33
    • 84978153612 scopus 로고    scopus 로고
    • Dimethyl fumarate in multiple sclerosis: latest developments, evidence and place in therapy
    • Linker, R.A., Haghikia, A., Dimethyl fumarate in multiple sclerosis: latest developments, evidence and place in therapy. Ther. Adv. Chronic Dis. 7 (2016), 198–207.
    • (2016) Ther. Adv. Chronic Dis. , vol.7 , pp. 198-207
    • Linker, R.A.1    Haghikia, A.2
  • 35
    • 84893055506 scopus 로고    scopus 로고
    • The nutrient-responsive transcription factor TFE3 promotes autophagy, lysosomal biogenesis, and clearance of cellular debris
    • Martina, J.A., Diab, H.I., Lishu, L., Jeong, A.L., Patange, S., Raben, N., Puertollano, R., The nutrient-responsive transcription factor TFE3 promotes autophagy, lysosomal biogenesis, and clearance of cellular debris. Sci. Signal., 7, 2014, ra9.
    • (2014) Sci. Signal. , vol.7 , pp. ra9
    • Martina, J.A.1    Diab, H.I.2    Lishu, L.3    Jeong, A.L.4    Patange, S.5    Raben, N.6    Puertollano, R.7
  • 37
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S.E., Blagoev, B., Kratchmarova, I., Kristensen, D.B., Steen, H., Pandey, A., Mann, M., Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics 1 (2002), 376–386.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 38
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong, S.E., Foster, L.J., Mann, M., Mass spectrometric-based approaches in quantitative proteomics. Methods 29 (2003), 124–130.
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 40
    • 85017666129 scopus 로고    scopus 로고
    • Discovery of N-((3R,4R)-4-fluoro-1-(6-((3-methoxy-1-methyl-1H-pyrazol-4-yl)amino)-9-methyl-9H- purin-2-yl)pyrrolidine-3-yl)acrylamide (PF-06747775) through structure-based drug design: a high affinity irreversible inhibitor targeting oncogenic EGFR mutants with selectivity over wild-type EGFR
    • Planken, S., Behenna, D.C., Nair, S.K., Johnson, T.O., Nagata, A., Almaden, C., Bailey, S., Ballard, T.E., Bernier, L., Cheng, H., et al. Discovery of N-((3R,4R)-4-fluoro-1-(6-((3-methoxy-1-methyl-1H-pyrazol-4-yl)amino)-9-methyl-9H- purin-2-yl)pyrrolidine-3-yl)acrylamide (PF-06747775) through structure-based drug design: a high affinity irreversible inhibitor targeting oncogenic EGFR mutants with selectivity over wild-type EGFR. J. Med. Chem. 60 (2017), 3002–3019.
    • (2017) J. Med. Chem. , vol.60 , pp. 3002-3019
    • Planken, S.1    Behenna, D.C.2    Nair, S.K.3    Johnson, T.O.4    Nagata, A.5    Almaden, C.6    Bailey, S.7    Ballard, T.E.8    Bernier, L.9    Cheng, H.10
  • 41
    • 64349093749 scopus 로고    scopus 로고
    • Covalent modifiers: an orthogonal approach to drug design
    • Potashman, M.H., Duggan, M.E., Covalent modifiers: an orthogonal approach to drug design. J. Med. Chem. 52 (2009), 1231–1246.
    • (2009) J. Med. Chem. , vol.52 , pp. 1231-1246
    • Potashman, M.H.1    Duggan, M.E.2
  • 43
    • 84878926653 scopus 로고    scopus 로고
    • Functional interrogation of kinases and other nucleotide-binding proteins
    • Rosenblum, J.S., Nomanbhoy, T.K., Kozarich, J.W., Functional interrogation of kinases and other nucleotide-binding proteins. FEBS Lett. 587 (2013), 1870–1877.
    • (2013) FEBS Lett. , vol.587 , pp. 1870-1877
    • Rosenblum, J.S.1    Nomanbhoy, T.K.2    Kozarich, J.W.3
  • 44
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective “ligation” of azides and terminal alkynes
    • Rostovtsev, V.V., Green, L.G., Fokin, V.V., Sharpless, K.B., A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective “ligation” of azides and terminal alkynes. Angew. Chem. Int. Ed. 41 (2002), 2596–2599.
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 45
    • 84902181290 scopus 로고    scopus 로고
    • Activity-based profiling of proteases
    • Sanman, L.E., Bogyo, M., Activity-based profiling of proteases. Annu. Rev. Biochem. 83 (2014), 249–273.
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 249-273
    • Sanman, L.E.1    Bogyo, M.2
  • 47
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers, A.E., Cravatt, B.F., Profiling enzyme activities in vivo using click chemistry methods. Chem. Biol. 11 (2004), 535–546.
    • (2004) Chem. Biol. , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 48
    • 79952704441 scopus 로고    scopus 로고
    • EGFR inhibitors in non-small cell lung cancer (NSCLC): the emerging role of the dual irreversible EGFR/HER2 inhibitor BIBW 2992
    • Spicer, J.F., Rudman, S.M., EGFR inhibitors in non-small cell lung cancer (NSCLC): the emerging role of the dual irreversible EGFR/HER2 inhibitor BIBW 2992. Target Oncol. 5 (2010), 245–255.
    • (2010) Target Oncol. , vol.5 , pp. 245-255
    • Spicer, J.F.1    Rudman, S.M.2
  • 49
    • 84982085544 scopus 로고    scopus 로고
    • Focusing on probe-modified peptides: a quick and effective method for target identification
    • Sun, H., Ren, Y., Hou, W., Li, L., Zeng, F., Li, S., Ma, Y., Liu, X., Chen, S., Zhang, Z., Focusing on probe-modified peptides: a quick and effective method for target identification. Chem. Commun. (Camb) 52 (2016), 10225–10228.
    • (2016) Chem. Commun. (Camb) , vol.52 , pp. 10225-10228
    • Sun, H.1    Ren, Y.2    Hou, W.3    Li, L.4    Zeng, F.5    Li, S.6    Ma, Y.7    Liu, X.8    Chen, S.9    Zhang, Z.10
  • 53
    • 84894619225 scopus 로고    scopus 로고
    • A chemoproteomic platform to quantitatively map targets of lipid-derived electrophiles
    • Wang, C., Weerapana, E., Blewett, M.M., Cravatt, B.F., A chemoproteomic platform to quantitatively map targets of lipid-derived electrophiles. Nat. Methods 11 (2014), 79–85.
    • (2014) Nat. Methods , vol.11 , pp. 79-85
    • Wang, C.1    Weerapana, E.2    Blewett, M.M.3    Cravatt, B.F.4
  • 54
    • 85007524757 scopus 로고    scopus 로고
    • Third-generation inhibitors targeting EGFR T790M mutation in advanced non-small cell lung cancer
    • Wang, S., Cang, S., Liu, D., Third-generation inhibitors targeting EGFR T790M mutation in advanced non-small cell lung cancer. J. Hematol. Oncol., 9, 2016, 34.
    • (2016) J. Hematol. Oncol. , vol.9 , pp. 34
    • Wang, S.1    Cang, S.2    Liu, D.3
  • 56
    • 84879577175 scopus 로고    scopus 로고
    • Quantitative comparison of the fasted and re-fed mouse liver phosphoproteomes using lower pH reductive dimethylation
    • Wilson-Grady, J.T., Haas, W., Gygi, S.P., Quantitative comparison of the fasted and re-fed mouse liver phosphoproteomes using lower pH reductive dimethylation. Methods 61 (2013), 277–286.
    • (2013) Methods , vol.61 , pp. 277-286
    • Wilson-Grady, J.T.1    Haas, W.2    Gygi, S.P.3
  • 57
    • 84856877017 scopus 로고    scopus 로고
    • PCI-32765: a novel Bruton's tyrosine kinase inhibitor for the treatment of lymphoid malignancies
    • Winer, E.S., Ingham, R.R., Castillo, J.J., PCI-32765: a novel Bruton's tyrosine kinase inhibitor for the treatment of lymphoid malignancies. Expert Opin. Investig. Drugs 21 (2012), 355–361.
    • (2012) Expert Opin. Investig. Drugs , vol.21 , pp. 355-361
    • Winer, E.S.1    Ingham, R.R.2    Castillo, J.J.3
  • 59
    • 84922430793 scopus 로고    scopus 로고
    • CHK2 kinase in the DNA damage response and beyond
    • Zannini, L., Delia, D., Buscemi, G., CHK2 kinase in the DNA damage response and beyond. J. Mol. Cell Biol. 6 (2014), 442–457.
    • (2014) J. Mol. Cell Biol. , vol.6 , pp. 442-457
    • Zannini, L.1    Delia, D.2    Buscemi, G.3
  • 60
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang, J., Yang, P.L., Gray, N.S., Targeting cancer with small molecule kinase inhibitors. Nat. Rev. Cancer 9 (2009), 28–39.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3


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