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Volumn 16, Issue 4, 2016, Pages 384-396

Metalloprotein inhibitors for the treatment of human diseases

Author keywords

Chelating; Drug design; Drug development; Magnesium; Metalloprotein; Zinc

Indexed keywords

ACETAZOLAMIDE; BENDROFLUMETHIAZIDE; BENZTHIAZIDE; BRINZOLAMIDE; CARBONATE DEHYDRATASE; CHLOROTHIAZIDE; CYCLOTHIAZIDE; DICLOFENAMIDE; DIPEPTIDYL CARBOXYPEPTIDASE; DORZOLAMIDE; ENZYME INHIBITOR; FUROSEMIDE; HISTONE DEACETYLASE; HYDROCHLOROTHIAZIDE; HYDROFLUMETHIAZIDE; INTEGRASE; LIPOXYGENASE; MATRIX METALLOPROTEINASE; METALLOPROTEIN INHIBITOR; METHAZOLAMIDE; METHYCLOTHIAZIDE; QUINETHAZONE; ROMIDEPSIN; STEROL 14ALPHA DEMETHYLASE; TOPIRAMATE; TRICHLORMETHIAZIDE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VORINOSTAT; ZINC ION; ZONISAMIDE; METALLOPROTEIN; PROTEINASE INHIBITOR;

EID: 84979097462     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026615666150813145218     Document Type: Article
Times cited : (34)

References (63)
  • 1
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal? Nat
    • Waldron, K.J.; Robinson, N.J. How do bacterial cells ensure that metalloproteins get the correct metal? Nat. Rev. Microbiol., 2009, 7 (2), 25-35.
    • (2009) Rev. Microbiol. , vol.7 , Issue.2 , pp. 25-35
    • Waldron, K.J.1    Robinson, N.J.2
  • 2
    • 53049093022 scopus 로고    scopus 로고
    • Metallomics and metalloproteomics
    • Shi, W.; Chance, M.R. Metallomics and metalloproteomics. Cell Mol. Life Sci., 2008, 65 (19), 3040-3048.
    • (2008) Cell Mol. Life Sci. , vol.65 , Issue.19 , pp. 3040-3048
    • Shi, W.1    Chance, M.R.2
  • 3
    • 84887128203 scopus 로고    scopus 로고
    • Metalloprotein-inhibitor binding: Human carbonic anhydrase II as a model for probing metal-ligand interactions in a metalloprotein active site
    • Martin, D.P.; Hann, Z.S.; Cohen, S.M. Metalloprotein-inhibitor binding: human carbonic anhydrase II as a model for probing metal-ligand interactions in a metalloprotein active site. Inorg. Chem., 2013, 52 (21), 12207-12215.
    • (2013) Inorg. Chem. , vol.52 , Issue.21 , pp. 12207-12215
    • Martin, D.P.1    Hann, Z.S.2    Cohen, S.M.3
  • 5
    • 47749124645 scopus 로고    scopus 로고
    • Zinc metalloproteins as medicinal targets
    • Anzellotti, A.I.; Farrell, N.P. Zinc metalloproteins as medicinal targets. Chem. Soc. Rev., 2008, 37 (8), 1629-1651.
    • (2008) Chem. Soc. Rev. , vol.37 , Issue.8 , pp. 1629-1651
    • Anzellotti, A.I.1    Farrell, N.P.2
  • 7
    • 24944529911 scopus 로고    scopus 로고
    • Virtual screening against metalloenzymes for inhibitors and substrates
    • Irwin, J.J.; Raushel, F.M.; Shoichet, B.K. Virtual screening against metalloenzymes for inhibitors and substrates. Biochemistry, 2005, 44 (37), 12316-12328.
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12316-12328
    • Irwin, J.J.1    Raushel, F.M.2    Shoichet, B.K.3
  • 8
    • 38849143765 scopus 로고    scopus 로고
    • Carbonic anhydrases: Novel therapeutic applications for inhibitors and activators. Nat
    • Supuran, C.T. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat. Rev. Drug Discov., 2008, 7 (2), 168-181.
    • (2008) Rev. Drug Discov. , vol.7 , Issue.2 , pp. 168-181
    • Supuran, C.T.1
  • 9
    • 79961070760 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors and activators for novel therapeutic applications
    • Supuran, C.T. Carbonic anhydrase inhibitors and activators for novel therapeutic applications. Future Med. Chem., 2011, 3 (9), 1165-1180.
    • (2011) Future Med. Chem. , vol.3 , Issue.9 , pp. 1165-1180
    • Supuran, C.T.1
  • 10
    • 80053563164 scopus 로고    scopus 로고
    • Interfering with pH regulation in tumours as a therapeutic strategy
    • Neri, D.; Supuran, C.T. Interfering with pH regulation in tumours as a therapeutic strategy. Nat. Rev. Drug Discov., 2011, 10 (10), 767-777.
    • (2011) Nat. Rev. Drug Discov. , vol.10 , Issue.10 , pp. 767-777
    • Neri, D.1    Supuran, C.T.2
  • 11
    • 78649659788 scopus 로고    scopus 로고
    • PH control mechanisms of tumor survival and growth
    • Parks, S.K.; Chiche, J.; Pouyssegur, J. pH control mechanisms of tumor survival and growth. J. Cell Physiol., 2011, 226 (2), 299-308.
    • (2011) J. Cell Physiol. , vol.226 , Issue.2 , pp. 299-308
    • Parks, S.K.1    Chiche, J.2    Pouyssegur, J.3
  • 13
    • 78751661570 scopus 로고    scopus 로고
    • Identifying chelators for metalloprotein inhibitors using a fragment-based approach
    • Jacobsen, J.A.; Fullagar, J.L.; Miller, M.T.; Cohen, S.M. Identifying chelators for metalloprotein inhibitors using a fragment-based approach. J. Med. Chem., 2011, 54 (2), 591-602.
    • (2011) J. Med. Chem. , vol.54 , Issue.2 , pp. 591-602
    • Jacobsen, J.A.1    Fullagar, J.L.2    Miller, M.T.3    Cohen, S.M.4
  • 14
    • 84866414247 scopus 로고    scopus 로고
    • Neutron diffraction of acetazolamide-bound human carbonic anhydrase II reveals atomic details of drug binding
    • Fisher, S.Z.; Aggarwal, M.; Kovalevsky, A.Y.; Silverman, D.N.; McKenna, R. Neutron diffraction of acetazolamide-bound human carbonic anhydrase II reveals atomic details of drug binding. J. Am. Chem. Soc., 2012, 134 (36), 14726-14729.
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.36 , pp. 14726-14729
    • Fisher, S.Z.1    Aggarwal, M.2    Kovalevsky, A.Y.3    Silverman, D.N.4    McKenna, R.5
  • 16
    • 84864722456 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in the treatment of cancer: Overview and perspectives
    • Giannini, G.; Cabri, W.; Fattorusso, C.; Rodriquez, M. Histone deacetylase inhibitors in the treatment of cancer: overview and perspectives. Future Med. Chem., 2012, 4 (11), 1439-1460.
    • (2012) Future Med. Chem. , vol.4 , Issue.11 , pp. 1439-1460
    • Giannini, G.1    Cabri, W.2    Fattorusso, C.3    Rodriquez, M.4
  • 17
    • 84858685501 scopus 로고    scopus 로고
    • Targeted cancer therapy: Giving histone deacetylase inhibitors all they need to succeed
    • Gryder, B.E.; Sodji, Q.H.; Oyelere, A.K. Targeted cancer therapy: giving histone deacetylase inhibitors all they need to succeed. Future Med. Chem., 2012, 4 (4), 505-524.
    • (2012) Future Med. Chem. , vol.4 , Issue.4 , pp. 505-524
    • Gryder, B.E.1    Sodji, Q.H.2    Oyelere, A.K.3
  • 18
    • 84877834926 scopus 로고    scopus 로고
    • Current trends in the development of histone deacetylase inhibitors: A review of recent patent applications
    • Thaler, F. Current trends in the development of histone deacetylase inhibitors: a review of recent patent applications. Pharm. Pat. Anal., 2012, 1 (1), 75-90.
    • (2012) Pharm. Pat. Anal. , vol.1 , Issue.1 , pp. 75-90
    • Thaler, F.1
  • 20
    • 38949086502 scopus 로고    scopus 로고
    • Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy
    • Weichert, W.; Roske, A.; Gekeler, V.; Beckers, T.; Stephan, C.; Jung, K.; Fritzsche, F.R.; Niesporek, S.; Denkert, C.; Dietel, M.; Kristiansen, G. Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy. Br. J. Cancer, 2008, 98 (3), 604-610.
    • (2008) Br. J. Cancer , vol.98 , Issue.3 , pp. 604-610
    • Weichert, W.1    Roske, A.2    Gekeler, V.3    Beckers, T.4    Stephan, C.5    Jung, K.6    Fritzsche, F.R.7    Niesporek, S.8    Denkert, C.9    Dietel, M.10    Kristiansen, G.11
  • 21
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (And more) treatments for cancer
    • Minucci, S.; Pelicci, P.G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer, 2006, 6 (1), 38-51.
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 23
    • 80051599485 scopus 로고    scopus 로고
    • Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases
    • Cole, K.E.; Dowling, D.P.; Boone, M.A.; Phillips, A.J.; Christianson, D.W. Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases. J. Am. Chem. Soc., 2011, 133, (32), 12474-12477.
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.32 , pp. 12474-12477
    • Cole, K.E.1    Dowling, D.P.2    Boone, M.A.3    Phillips, A.J.4    Christianson, D.W.5
  • 26
    • 84907859411 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of 1, 3-disubstituted-pyrazole derivatives as new class I and IIb histone deacetylase inhibitors
    • Yao, Y.W.; Liao, C.H.; Li, Z.; Wang, Z.; Sun, Q.; Liu, C.P.; Yang, Y.; Tu, Z.C.; Jiang, S. Design, synthesis, and biological evaluation of 1, 3-disubstituted-pyrazole derivatives as new class I and IIb histone deacetylase inhibitors. Eur. J. Med. Chem., 2014, 86, 639-652.
    • (2014) Eur. J. Med. Chem. , vol.86 , pp. 639-652
    • Yao, Y.W.1    Liao, C.H.2    Li, Z.3    Wang, Z.4    Sun, Q.5    Liu, C.P.6    Yang, Y.7    Tu, Z.C.8    Jiang, S.9
  • 27
    • 77954386602 scopus 로고    scopus 로고
    • High-resolution crystal structures of Drosophila melanogaster angiotensin-converting enzyme in complex with novel inhibitors and antihypertensive drugs
    • Akif, M.; Georgiadis, D.; Mahajan, A.; Dive, V.; Sturrock, E.D.; Isaac, R.E.; Acharya, K.R. High-resolution crystal structures of Drosophila melanogaster angiotensin-converting enzyme in complex with novel inhibitors and antihypertensive drugs. J. Mol. Biol., 2010, 400 (3), 502-517.
    • (2010) J. Mol. Biol. , vol.400 , Issue.3 , pp. 502-517
    • Akif, M.1    Georgiadis, D.2    Mahajan, A.3    Dive, V.4    Sturrock, E.D.5    Isaac, R.E.6    Acharya, K.R.7
  • 28
    • 72449178934 scopus 로고    scopus 로고
    • The interaction of zinc(II) and hydroxamic acids and a metal-triggered Lossen rearrangement
    • Duchackova, L.; Roithova, J. The interaction of zinc(II) and hydroxamic acids and a metal-triggered Lossen rearrangement. Chemistry, 2009, 15 (48), 13399-13405.
    • (2009) Chemistry , vol.15 , Issue.48 , pp. 13399-13405
    • Duchackova, L.1    Roithova, J.2
  • 29
    • 3042732126 scopus 로고    scopus 로고
    • Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin Iconverting enzyme
    • Natesh, R.; Schwager, S.L.; Evans, H.R.; Sturrock, E.D.; Acharya, K.R. Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin Iconverting enzyme. Biochemistry, 2004, 43 (27), 8718-8724.
    • (2004) Biochemistry , vol.43 , Issue.27 , pp. 8718-8724
    • Natesh, R.1    Schwager, S.L.2    Evans, H.R.3    Sturrock, E.D.4    Acharya, K.R.5
  • 31
    • 77954100589 scopus 로고    scopus 로고
    • Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: A theoretical study
    • Liao, C.; Nicklaus, M.C. Tautomerism and magnesium chelation of HIV-1 integrase inhibitors: a theoretical study. ChemMedChem, 2010, 5 (7), 1053-1066.
    • (2010) Chemmedchem , vol.5 , Issue.7 , pp. 1053-1066
    • Liao, C.1    Nicklaus, M.C.2
  • 32
    • 77954667578 scopus 로고    scopus 로고
    • Authentic HIV-1 integrase inhibitors. Future Med
    • Liao, C.; Marchand, C.; Burke, T.R., Jr.; Pommier, Y.; Nicklaus, M.C. Authentic HIV-1 integrase inhibitors. Future Med. Chem., 2010, 2 (7), 1107-1122.
    • (2010) Chem. , vol.2 , Issue.7 , pp. 1107-1122
    • Liao, C.1    Marchand, C.2    Burke, T.R.3    Pommier, Y.4    Nicklaus, M.C.5
  • 34
    • 78650533230 scopus 로고    scopus 로고
    • Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance
    • Hare, S.; Vos, A.M.; Clayton, R.F.; Thuring, J.W.; Cummings, M.D.; Cherepanov, P. Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance. Proc. Natl. Acad. Sci. USA, 2010, 107 (46), 20057-20062.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , Issue.46 , pp. 20057-20062
    • Hare, S.1    Vos, A.M.2    Clayton, R.F.3    Thuring, J.W.4    Cummings, M.D.5    Cherepanov, P.6
  • 35
    • 80052847538 scopus 로고    scopus 로고
    • Structural and functional analyses of the second-generation integrase strand transfer inhibitor dolutegravir (S/GSK1349572)
    • Hare, S.; Smith, S.J.; Metifiot, M.; Jaxa-Chamiec, A.; Pommier, Y.; Hughes, S.H.; Cherepanov, P. Structural and functional analyses of the second-generation integrase strand transfer inhibitor dolutegravir (S/GSK1349572). Mol. Pharmacol., 2011, 80 (4), 565-572.
    • (2011) Mol. Pharmacol. , vol.80 , Issue.4 , pp. 565-572
    • Hare, S.1    Smith, S.J.2    Metifiot, M.3    Jaxa-Chamiec, A.4    Pommier, Y.5    Hughes, S.H.6    Cherepanov, P.7
  • 36
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare, S.; Gupta, S.S.; Valkov, E.; Engelman, A.; Cherepanov, P. Retroviral intasome assembly and inhibition of DNA strand transfer. Nature, 2010, 464 (7286), 232-236.
    • (2010) Nature , vol.464 , Issue.7286 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 37
  • 38
    • 77954682878 scopus 로고    scopus 로고
    • Computer tools in the discovery of HIV-1 integrase inhibitors
    • Liao, C.; Nicklaus, M.C. Computer tools in the discovery of HIV-1 integrase inhibitors. Future Med. Chem., 2010, 2 (7), 1123-1140.
    • (2010) Future Med. Chem. , vol.2 , Issue.7 , pp. 1123-1140
    • Liao, C.1    Nicklaus, M.C.2
  • 40
    • 0039122255 scopus 로고    scopus 로고
    • Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor alpha convertase inhibitors
    • Gomis-Ruth, F.X.; Meyer, E.F.; Kress, L.F.; Politi, V. Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor alpha convertase inhibitors. Protein Sci., 1998, 7 (2), 283-292.
    • (1998) Protein Sci. , vol.7 , Issue.2 , pp. 283-292
    • Gomis-Ruth, F.X.1    Meyer, E.F.2    Kress, L.F.3    Politi, V.4
  • 41
    • 79955851447 scopus 로고    scopus 로고
    • Structural characterization of three novel hydroxamate-based zinc chelating inhibitors of the Clostridium botulinum serotype A neurotoxin light chain metalloprotease reveals a compact binding site resulting from 60/70 loop flexibility
    • Thompson, A.A.; Jiao, G.S.; Kim, S.; Thai, A.; Cregar-Hernandez, L.; Margosiak, S.A.; Johnson, A.T.; Han, G.W.; O'Malley, S.; Stevens, R.C. Structural characterization of three novel hydroxamate-based zinc chelating inhibitors of the Clostridium botulinum serotype A neurotoxin light chain metalloprotease reveals a compact binding site resulting from 60/70 loop flexibility. Biochemistry, 2011, 50 (19), 4019-4028.
    • (2011) Biochemistry , vol.50 , Issue.19 , pp. 4019-4028
    • Thompson, A.A.1    Jiao, G.S.2    Kim, S.3    Thai, A.4    Cregar-Hernandez, L.5    Margosiak, S.A.6    Johnson, A.T.7    Han, G.W.8    O'malley, S.9    Stevens, R.C.10
  • 43
    • 2642568535 scopus 로고    scopus 로고
    • Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity
    • Reid, T.S.; Beese, L.S. Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity. Biochemistry, 2004, 43 (22), 6877-6884.
    • (2004) Biochemistry , vol.43 , Issue.22 , pp. 6877-6884
    • Reid, T.S.1    Beese, L.S.2
  • 44
    • 33646584823 scopus 로고    scopus 로고
    • Recent advances in MMP inhibitor design
    • Fisher, J.F.; Mobashery, S. Recent advances in MMP inhibitor design. Cancer Metastasis Rev., 2006, 25 (1), 115-136.
    • (2006) Cancer Metastasis Rev. , vol.25 , Issue.1 , pp. 115-136
    • Fisher, J.F.1    Mobashery, S.2
  • 45
    • 84923244141 scopus 로고    scopus 로고
    • Discovery of novel, highly potent, and selective quinazoline-2-carboxamide-based matrix metalloproteinase (MMP)-13 inhibitors without a zinc binding group using a structure-based design approach
    • Nara, H.; Sato, K.; Naito, T.; Mototani, H.; Oki, H.; Yamamoto, Y.; Kuno, H.; Santou, T.; Kanzaki, N.; Terauchi, J.; Uchikawa, O.; Kori, M. Discovery of novel, highly potent, and selective quinazoline-2-carboxamide-based matrix metalloproteinase (MMP)-13 inhibitors without a zinc binding group using a structure-based design approach. J. Med. Chem., 2014, 57 (21), 8886-8902.
    • (2014) J. Med. Chem. , vol.57 , Issue.21 , pp. 8886-8902
    • Nara, H.1    Sato, K.2    Naito, T.3    Mototani, H.4    Oki, H.5    Yamamoto, Y.6    Kuno, H.7    Santou, T.8    Kanzaki, N.9    Terauchi, J.10    Uchikawa, O.11    Kori, M.12
  • 46
    • 65249115262 scopus 로고    scopus 로고
    • Biotin-tagged probes for MMP expression and activation: Design, synthesis, and binding properties
    • Dragoni, E.; Calderone, V.; Fragai, M.; Jaiswal, R.; Luchinat, C.; Nativi, C. Biotin-tagged probes for MMP expression and activation: design, synthesis, and binding properties. Bioconjug Chem., 2009, 20 (4), 719-727.
    • (2009) Bioconjug Chem. , vol.20 , Issue.4 , pp. 719-727
    • Dragoni, E.1    Calderone, V.2    Fragai, M.3    Jaiswal, R.4    Luchinat, C.5    Nativi, C.6
  • 47
    • 34250371374 scopus 로고    scopus 로고
    • Protonation patterns in tetracycline:Tet repressor recognition: Simulations and experiments
    • Aleksandrov, A.; Proft, J.; Hinrichs, W.; Simonson, T. Protonation patterns in tetracycline:tet repressor recognition: simulations and experiments. Chembiochem, 2007, 8 (6), 675-685.
    • (2007) Chembiochem , vol.8 , Issue.6 , pp. 675-685
    • Aleksandrov, A.1    Proft, J.2    Hinrichs, W.3    Simonson, T.4
  • 48
    • 84908691597 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of IMP-1 metallo-beta-lactamase complexed with a 3-aminophthalic acid derivative, structure-based drug design, and synthesis of 3,6-disubstituted phthalic acid derivative inhibitors
    • Hiraiwa, Y.; Saito, J.; Watanabe, T.; Yamada, M.; Morinaka, A.; Fukushima, T.; Kudo, T. X-ray crystallographic analysis of IMP-1 metallo-beta-lactamase complexed with a 3-aminophthalic acid derivative, structure-based drug design, and synthesis of 3,6-disubstituted phthalic acid derivative inhibitors. Bioorg. Med. Chem. Lett., 2014, 24 (20), 4891-4894.
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , Issue.20 , pp. 4891-4894
    • Hiraiwa, Y.1    Saito, J.2    Watanabe, T.3    Yamada, M.4    Morinaka, A.5    Fukushima, T.6    Kudo, T.7
  • 50
    • 84897030265 scopus 로고    scopus 로고
    • Efficacy and safety of LCZ696, a first-in-class angiotensin receptor neprilysin inhibitor, in Asian patients with hypertension: A randomized, double-blind, placebo-controlled study
    • Kario, K.; Sun, N.; Chiang, F.T.; Supasyndh, O.; Baek, S.H.; Inubushi-Molessa, A.; Zhang, Y.; Gotou, H.; Lefkowitz, M.; Zhang, J. Efficacy and safety of LCZ696, a first-in-class angiotensin receptor neprilysin inhibitor, in Asian patients with hypertension: a randomized, double-blind, placebo-controlled study. Hypertension, 2014, 63 (4), 698-705.
    • (2014) Hypertension , vol.63 , Issue.4 , pp. 698-705
    • Kario, K.1    Sun, N.2    Chiang, F.T.3    Supasyndh, O.4    Baek, S.H.5    Inubushi-Molessa, A.6    Zhang, Y.7    Gotou, H.8    Lefkowitz, M.9    Zhang, J.10
  • 51
    • 4644350946 scopus 로고    scopus 로고
    • Structural analysis of neprilysin with various specific and potent inhibitors
    • Oefner, C.; Roques, B.P.; Fournie-Zaluski, M.C.; Dale, G.E. Structural analysis of neprilysin with various specific and potent inhibitors. Acta Crystallogr D., 2004, 60, 392-396.
    • (2004) Acta Crystallogr D. , vol.60 , pp. 392-396
    • Oefner, C.1    Roques, B.P.2    Fournie-Zaluski, M.C.3    Dale, G.E.4
  • 52
    • 34147105872 scopus 로고    scopus 로고
    • ADAMs in cancer cell proliferation and progression
    • Mochizuki, S.; Okada, Y. ADAMs in cancer cell proliferation and progression. Cancer Sci., 2007, 98 (5), 621-628.
    • (2007) Cancer Sci. , vol.98 , Issue.5 , pp. 621-628
    • Mochizuki, S.1    Okada, Y.2
  • 53
    • 36048938454 scopus 로고    scopus 로고
    • TACE: A new target in epidermal growth factor receptor dependent tumors
    • Kenny, P.A. TACE: a new target in epidermal growth factor receptor dependent tumors. Differentiation, 2007, 75 (9), 800-808.
    • (2007) Differentiation , vol.75 , Issue.9 , pp. 800-808
    • Kenny, P.A.1
  • 56
    • 84911396858 scopus 로고    scopus 로고
    • Crystal structure of a lipoxygenase in complex with substrate: The arachidonic acid-binding site of 8Rlipoxygenase
    • Neau, D.B.; Bender, G.; Boeglin, W.E.; Bartlett, S.G.; Brash, A.R.; Newcomer, M.E. Crystal structure of a lipoxygenase in complex with substrate: the arachidonic acid-binding site of 8Rlipoxygenase. J. Biol. Chem., 2014, 289, (46), 31905-31913.
    • (2014) J. Biol. Chem. , vol.289 , Issue.46 , pp. 31905-31913
    • Neau, D.B.1    Bender, G.2    Boeglin, W.E.3    Bartlett, S.G.4    Brash, A.R.5    Newcomer, M.E.6
  • 57
    • 84899821420 scopus 로고    scopus 로고
    • Recent Progress in the Research of Small Molecule HIV-1 RNase H Inhibitors
    • Cao, L.L.; Song, W.G.; De Clercq, E.; Zhan, P.; Liu, X.Y. Recent Progress in the Research of Small Molecule HIV-1 RNase H Inhibitors. Curr. Med. Chem., 2014, 21 (17), 1956-1967.
    • (2014) Curr. Med. Chem. , vol.21 , Issue.17 , pp. 1956-1967
    • Cao, L.L.1    Song, W.G.2    De Clercq, E.3    Zhan, P.4    Liu, X.Y.5
  • 58
    • 84921450614 scopus 로고    scopus 로고
    • Design, Synthesis, Biochemical, and Antiviral Evaluations of C6 Benzyl and C6 Biarylmethyl Substituted 2-Hydroxylisoquinoline-1,3-diones: Dual Inhibition against HIV Reverse Transcriptase-Associated RNase H and Polymerase with Antiviral Activities
    • Vernekar, S.K.; Liu, Z.; Nagy, E.; Miller, L.; Kirby, K.A.; Wilson, D.J.; Kankanala, J.; Sarafianos, S.G.; Parniak, M.A.; Wang, Z. Design, Synthesis, Biochemical, and Antiviral Evaluations of C6 Benzyl and C6 Biarylmethyl Substituted 2-Hydroxylisoquinoline-1,3-diones: Dual Inhibition against HIV Reverse Transcriptase-Associated RNase H and Polymerase with Antiviral Activities. J. Med. Chem., 2015, 58(2):651-64.
    • (2015) J. Med. Chem. , vol.58 , Issue.2 , pp. 651-664
    • Vernekar, S.K.1    Liu, Z.2    Nagy, E.3    Miller, L.4    Kirby, K.A.5    Wilson, D.J.6    Kankanala, J.7    Sarafianos, S.G.8    Parniak, M.A.9    Wang, Z.10
  • 60
    • 77952358375 scopus 로고    scopus 로고
    • Structural Characterization of CYP51 from Trypanosoma cruzi and Trypanosoma brucei Bound to the Antifungal Drugs Posaconazole and Fluconazole
    • Chen, C.K.; Leung, S.S.F.; Guilbert, C.; Jacobson, M.P.; McKerrow, J.H.; Podust, L.M. Structural Characterization of CYP51 from Trypanosoma cruzi and Trypanosoma brucei Bound to the Antifungal Drugs Posaconazole and Fluconazole. Plos Negl. Trop. D., 2010, 4 (4), e651.
    • (2010) Plos Negl. Trop. D. , vol.4 , Issue.4 , pp. e651
    • Chen, C.K.1    Leung, S.S.F.2    Guilbert, C.3    Jacobson, M.P.4    McKerrow, J.H.5    Podust, L.M.6
  • 62
    • 79960638515 scopus 로고    scopus 로고
    • MetLigDB: A web-based database for the identification of chemical groups to design metalloprotein inhibitors
    • Choi, H.; Kang, H.; Park, H. MetLigDB: a web-based database for the identification of chemical groups to design metalloprotein inhibitors. J. Appl. Crystallogr., 2011, 44, 878-881.
    • (2011) J. Appl. Crystallogr. , vol.44 , pp. 878-881
    • Choi, H.1    Kang, H.2    Park, H.3
  • 63
    • 84885654692 scopus 로고    scopus 로고
    • Diversity evolution and jump of Polo-like kinase 1 inhibitors
    • Liao, C.Z.; Yao, R.S. Diversity evolution and jump of Polo-like kinase 1 inhibitors. Sci. China Chem., 2013, 56 (10), 1392-1401.
    • (2013) Sci. China Chem. , vol.56 , Issue.10 , pp. 1392-1401
    • Liao, C.Z.1    Yao, R.S.2


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