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Volumn 60, Issue 4, 2017, Pages 1343-1361

Correction to: Discovery of an Inhibitor of the Proteasome Subunit Rpn11 (Journal of Medicinal Chemistry (2017) 60 (1343�-1361) DOI: 10.1021/acs.jmedchem.6b01379));Discovery of an Inhibitor of the Proteasome Subunit Rpn11

Author keywords

[No Author keywords available]

Indexed keywords

8 THIOQUINOLINE; 8,8' DISULFANEDIYLBIS(N (2 (THIAZOL 2 YL)ETHYL)QUINOLINE 3 CARBOXAMIDE); BORTEZOMIB; METALLOPROTEINASE; PROTEASOME; PROTEASOME INHIBITOR; RPN11 PROTEASOME INHIBITOR; RPN11 PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; ZINC ION; PSMD14 PROTEIN, HUMAN; QUINOLINE DERIVATIVE; TRANSACTIVATOR PROTEIN; ZINC;

EID: 85013833905     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.7b00390     Document Type: Erratum
Times cited : (65)

References (54)
  • 1
    • 77249120064 scopus 로고    scopus 로고
    • Treatment of Multiple Myeloma: A Comprehensive Review
    • Kyle, R. A.; Rajkumar, S. V. Treatment of Multiple Myeloma: A Comprehensive Review Clin. Lymphoma Myeloma 2009, 9 ( 4 ) 278-288 10.3816/CLM.2009.n.056
    • (2009) Clin. Lymphoma Myeloma , vol.9 , Issue.4 , pp. 278-288
    • Kyle, R.A.1    Rajkumar, S.V.2
  • 2
    • 85013856889 scopus 로고    scopus 로고
    • American Cancer Society: Atlanta,; (accessed September 16, 2016).
    • Survival Rates by Stage for Multiple Myeloma; American Cancer Society: Atlanta, 2016; http://www.cancer.org/cancer/multiplemyeloma/detailedguide/multiple-myeloma-survival-rates (accessed September 16, 2016).
    • (2016) Survival Rates by Stage for Multiple Myeloma
  • 3
    • 84856373151 scopus 로고    scopus 로고
    • Proteasome Inhibitors: An Expanding Army Attacking a Unique Target
    • Kisselev, A. F.; van der Linden, W. A.; Overkleeft, H. S. Proteasome Inhibitors: An Expanding Army Attacking a Unique Target Chem. Biol. 2012, 19 ( 1 ) 99-115 10.1016/j.chembiol.2012.01.003
    • (2012) Chem. Biol. , vol.19 , Issue.1 , pp. 99-115
    • Kisselev, A.F.1    Van der Linden, W.A.2    Overkleeft, H.S.3
  • 6
    • 84876886990 scopus 로고    scopus 로고
    • Dimerized Linear Mimics of a Natural Cyclopeptide (TMC-95A) Are Potent Noncovalent Inhibitors of the Eukaryotic 20S Proteasome
    • Desvergne, A.; Genin, E.; Marechal, X.; Gallastegui, N.; Dufau, L.; Richy, N.; Groll, M.; Vidal, J.; Reboud-Ravaux, M. Dimerized Linear Mimics of a Natural Cyclopeptide (TMC-95A) Are Potent Noncovalent Inhibitors of the Eukaryotic 20S Proteasome J. Med. Chem. 2013, 56 ( 8 ) 3367-3378 10.1021/jm4002007
    • (2013) J. Med. Chem. , vol.56 , Issue.8 , pp. 3367-3378
    • Desvergne, A.1    Genin, E.2    Marechal, X.3    Gallastegui, N.4    Dufau, L.5    Richy, N.6    Groll, M.7    Vidal, J.8    Reboud-Ravaux, M.9
  • 8
    • 84877697520 scopus 로고    scopus 로고
    • Potent Proteasome Inhibitors Derived from the Unnatural cis-Cyclopropane Isomer of Belactosin A: Synthesis, Biological Activity, and Mode of Action
    • Kawamura, S.; Unno, Y.; List, A.; Mizuno, A.; Tanaka, M.; Sasaki, T.; Arisawa, M.; Asai, A.; Groll, M.; Shuto, S. Potent Proteasome Inhibitors Derived from the Unnatural cis-Cyclopropane Isomer of Belactosin A: Synthesis, Biological Activity, and Mode of Action J. Med. Chem. 2013, 56 ( 9 ) 3689-3700 10.1021/jm4002296
    • (2013) J. Med. Chem. , vol.56 , Issue.9 , pp. 3689-3700
    • Kawamura, S.1    Unno, Y.2    List, A.3    Mizuno, A.4    Tanaka, M.5    Sasaki, T.6    Arisawa, M.7    Asai, A.8    Groll, M.9    Shuto, S.10
  • 10
    • 78049264771 scopus 로고    scopus 로고
    • The 26S proteasome: Assembly and Function of a Destructive Machine
    • Gallastegui, N.; Groll, M. The 26S proteasome: Assembly and Function of a Destructive Machine Trends Biochem. Sci. 2010, 35 ( 11 ) 634-642 10.1016/j.tibs.2010.05.005
    • (2010) Trends Biochem. Sci. , vol.35 , Issue.11 , pp. 634-642
    • Gallastegui, N.1    Groll, M.2
  • 11
    • 84859827831 scopus 로고    scopus 로고
    • The Proteasome: Molecular Machinery and Pathophysiological Roles
    • Tanaka, K.; Mizushima, T.; Saeki, Y. The Proteasome: Molecular Machinery and Pathophysiological Roles Biol. Chem. 2012, 393 ( 4 ) 217-234 10.1515/hsz-2011-0285
    • (2012) Biol. Chem. , vol.393 , Issue.4 , pp. 217-234
    • Tanaka, K.1    Mizushima, T.2    Saeki, Y.3
  • 12
    • 65249186662 scopus 로고    scopus 로고
    • Polyubiquitin Binding and Disassembly By Deubiquitinating Enzymes
    • Reyes-Turcu, F. E.; Wilkinson, K. D. Polyubiquitin Binding and Disassembly By Deubiquitinating Enzymes Chem. Rev. 2009, 109 ( 4 ) 1495-1508 10.1021/cr800470j
    • (2009) Chem. Rev. , vol.109 , Issue.4 , pp. 1495-1508
    • Reyes-Turcu, F.E.1    Wilkinson, K.D.2
  • 13
    • 41649091606 scopus 로고    scopus 로고
    • Relative Structural and Functional Roles of Multiple Deubiquitylating Proteins Associated With Mammalian 26S Proteasome
    • Koulich, E.; Li, X. H.; DeMartino, G. N. Relative Structural and Functional Roles of Multiple Deubiquitylating Proteins Associated With Mammalian 26S Proteasome Mol. Biol. Cell 2008, 19 ( 3 ) 1072-1082 10.1091/mbc.E07-10-1040
    • (2008) Mol. Biol. Cell , vol.19 , Issue.3 , pp. 1072-1082
    • Koulich, E.1    Li, X.H.2    DeMartino, G.N.3
  • 14
    • 0347087494 scopus 로고    scopus 로고
    • Complementary Roles for Rpn11 and Ubp6 in Deubiquitination and Proteolysis by the Proteasome
    • Guterman, A.; Glickman, M. H. Complementary Roles for Rpn11 and Ubp6 in Deubiquitination and Proteolysis by the Proteasome J. Biol. Chem. 2004, 279 ( 3 ) 1729-1738 10.1074/jbc.M307050200
    • (2004) J. Biol. Chem. , vol.279 , Issue.3 , pp. 1729-1738
    • Guterman, A.1    Glickman, M.H.2
  • 15
    • 84868324284 scopus 로고    scopus 로고
    • Pivotal Advance: Protein Synthesis Modulates Responsiveness of Differentiating and Malignant Plasma Cells to Proteasome Inhibitors
    • Cenci, S.; Oliva, L.; Cerruti, F.; Milan, E.; Bianchi, G.; Raule, M.; Mezghrani, A.; Pasqualetto, E.; Sitia, R.; Cascio, P. Pivotal Advance: Protein Synthesis Modulates Responsiveness of Differentiating and Malignant Plasma Cells to Proteasome Inhibitors J. Leukocyte Biol. 2012, 92 ( 5 ) 921-931 10.1189/jlb.1011497
    • (2012) J. Leukocyte Biol. , vol.92 , Issue.5 , pp. 921-931
    • Cenci, S.1    Oliva, L.2    Cerruti, F.3    Milan, E.4    Bianchi, G.5    Raule, M.6    Mezghrani, A.7    Pasqualetto, E.8    Sitia, R.9    Cascio, P.10
  • 16
    • 84920861391 scopus 로고    scopus 로고
    • Proteotoxic Crisis, the Ubiquitin-Proteasome System, and Cancer Therapy
    • Deshaies, R. J. Proteotoxic Crisis, the Ubiquitin-Proteasome System, and Cancer Therapy BMC Biol. 2014, 12, 94 10.1186/s12915-014-0094-0
    • (2014) BMC Biol. , vol.12 , pp. 94
    • Deshaies, R.J.1
  • 17
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an Endosome-Associated Ubiquitin Isopeptidase
    • McCullough, J.; Clague, M. J.; Urbe, S. AMSH is an Endosome-Associated Ubiquitin Isopeptidase J. Cell Biol. 2004, 166 ( 4 ) 487-492 10.1083/jcb.200401141
    • (2004) J. Cell Biol. , vol.166 , Issue.4 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 19
    • 34547730282 scopus 로고    scopus 로고
    • A Histone H2A Deubiquitinase Complex Coordinating Histone Acetylation and H1 Dissociation in Transcriptional Regulation
    • Zhu, P.; Zhou, W. L.; Wang, J. X.; Puc, J.; Ohgi, K. A.; Erdjument-Bromage, H.; Tempst, P.; Glass, C. K.; Rosenfeld, M. G. A Histone H2A Deubiquitinase Complex Coordinating Histone Acetylation and H1 Dissociation in Transcriptional Regulation Mol. Cell 2007, 27 ( 4 ) 609-621 10.1016/j.molcel.2007.07.024
    • (2007) Mol. Cell , vol.27 , Issue.4 , pp. 609-621
    • Zhu, P.1    Zhou, W.L.2    Wang, J.X.3    Puc, J.4    Ohgi, K.A.5    Erdjument-Bromage, H.6    Tempst, P.7    Glass, C.K.8    Rosenfeld, M.G.9
  • 20
    • 19344364762 scopus 로고    scopus 로고
    • JAMM: A Metalloprotease-like Zinc Site in the Proteasome and Signalosome
    • Ambroggio, X. I.; Rees, D. C.; Deshaies, R. J. JAMM: A Metalloprotease-like Zinc Site in the Proteasome and Signalosome PLoS Biol. 2003, 2 ( 1 ) e2 10.1371/journal.pbio.0020002
    • (2003) PLoS Biol. , vol.2 , Issue.1 , pp. e2
    • Ambroggio, X.I.1    Rees, D.C.2    Deshaies, R.J.3
  • 22
    • 0037131242 scopus 로고    scopus 로고
    • Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 From Cul1
    • Cope, G. A.; Suh, G. S. B.; Aravind, L.; Schwarz, S. E.; Zipursky, S. L.; Koonin, E. V.; Deshaies, R. J. Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 From Cul1 Science 2002, 298 ( 5593 ) 608-611 10.1126/science.1075901
    • (2002) Science , vol.298 , Issue.5593 , pp. 608-611
    • Cope, G.A.1    Suh, G.S.B.2    Aravind, L.3    Schwarz, S.E.4    Zipursky, S.L.5    Koonin, E.V.6    Deshaies, R.J.7
  • 24
    • 84901020323 scopus 로고    scopus 로고
    • Insights into the Mechanism of Deubiquitination by JAMM Deubiquitinases from Cocrystal Structures of the Enzyme with the Substrate and Product
    • Shrestha, R. K.; Ronau, J. A.; Davies, C. W.; Guenette, R. G.; Strieter, E. R.; Paul, L. N.; Das, C. Insights into the Mechanism of Deubiquitination by JAMM Deubiquitinases from Cocrystal Structures of the Enzyme with the Substrate and Product Biochemistry 2014, 53 ( 19 ) 3199-3217 10.1021/bi5003162
    • (2014) Biochemistry , vol.53 , Issue.19 , pp. 3199-3217
    • Shrestha, R.K.1    Ronau, J.A.2    Davies, C.W.3    Guenette, R.G.4    Strieter, E.R.5    Paul, L.N.6    Das, C.7
  • 26
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome Inhibitors: From Research Tools to Drug Candidates
    • Kisselev, A. F.; Goldberg, A. L. Proteasome Inhibitors: From Research Tools to Drug Candidates Chem. Biol. 2001, 8 ( 8 ) 739-758 10.1016/S1074-5521(01)00056-4
    • (2001) Chem. Biol. , vol.8 , Issue.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 27
    • 2342667387 scopus 로고    scopus 로고
    • The Development of Proteasome Inhibitors as Anticancer Drugs
    • Adams, J. The Development of Proteasome Inhibitors as Anticancer Drugs Cancer Cell 2004, 5 ( 5 ) 417-421 10.1016/S1535-6108(04)00120-5
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 417-421
    • Adams, J.1
  • 28
    • 79956366646 scopus 로고    scopus 로고
    • Proteasome Inhibitors in Cancer Therapy
    • Crawford, L. J.; Walker, B.; Irvine, A. E. Proteasome Inhibitors in Cancer Therapy J. Cell Commun. Signal. 2011, 5 ( 2 ) 101-110 10.1007/s12079-011-0121-7
    • (2011) J. Cell Commun. Signal. , vol.5 , Issue.2 , pp. 101-110
    • Crawford, L.J.1    Walker, B.2    Irvine, A.E.3
  • 29
    • 34347208609 scopus 로고    scopus 로고
    • Identification of a Peptoid Inhibitor of the Proteasome 19S Regulatory Particle
    • Lim, H. S.; Archer, C. T.; Kodadek, T. Identification of a Peptoid Inhibitor of the Proteasome 19S Regulatory Particle J. Am. Chem. Soc. 2007, 129 ( 25 ) 7750-7751 10.1021/ja072027p
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.25 , pp. 7750-7751
    • Lim, H.S.1    Archer, C.T.2    Kodadek, T.3
  • 30
    • 35848935013 scopus 로고    scopus 로고
    • Periodate-Triggered Cross-Linking Reveals Sug2/Rpt4 as the Molecular Target of a Peptoid Inhibitor of the 19S Proteasome Regulatory Particle
    • Lim, H. S.; Cai, D.; Archer, C. T.; Kodadek, T. Periodate-Triggered Cross-Linking Reveals Sug2/Rpt4 as the Molecular Target of a Peptoid Inhibitor of the 19S Proteasome Regulatory Particle J. Am. Chem. Soc. 2007, 129 ( 43 ) 12936-12937 10.1021/ja075469+
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.43 , pp. 12936-12937
    • Lim, H.S.1    Cai, D.2    Archer, C.T.3    Kodadek, T.4
  • 31
    • 84930221978 scopus 로고    scopus 로고
    • A Reversible and Highly Selective Inhibitor of the Proteasomal Ubiquitin Receptor Rpn13 Is Toxic to Multiple Myeloma Cells
    • Trader, D. J.; Simanski, S.; Kodadek, T. A Reversible and Highly Selective Inhibitor of the Proteasomal Ubiquitin Receptor Rpn13 Is Toxic to Multiple Myeloma Cells J. Am. Chem. Soc. 2015, 137 ( 19 ) 6312-6319 10.1021/jacs.5b02069
    • (2015) J. Am. Chem. Soc. , vol.137 , Issue.19 , pp. 6312-6319
    • Trader, D.J.1    Simanski, S.2    Kodadek, T.3
  • 33
    • 84897022669 scopus 로고    scopus 로고
    • A Novel Small Molecule Inhibitor of Deubiquitylating Enzyme USP14 and UCHL5 Induces Apoptosis in Multiple Myeloma and Overcomes Bortezomib Resistance
    • Tian, Z.; D’Arcy, P.; Wang, X.; Ray, A.; Tai, Y. T.; Hu, Y. G.; Carrasco, R. D.; Richardson, P.; Linder, S.; Chauhan, D.; Anderson, K. C. A Novel Small Molecule Inhibitor of Deubiquitylating Enzyme USP14 and UCHL5 Induces Apoptosis in Multiple Myeloma and Overcomes Bortezomib Resistance Blood 2014, 123 ( 5 ) 706-716 10.1182/blood-2013-05-500033
    • (2014) Blood , vol.123 , Issue.5 , pp. 706-716
    • Tian, Z.1    D’Arcy, P.2    Wang, X.3    Ray, A.4    Tai, Y.T.5    Hu, Y.G.6    Carrasco, R.D.7    Richardson, P.8    Linder, S.9    Chauhan, D.10    Anderson, K.C.11
  • 34
    • 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 10.1021/jm101266s
    • (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
  • 35
    • 84865042837 scopus 로고    scopus 로고
    • 3-Hydroxy-1-alkyl-2-methylpyridine-4(1H)-thiones: Inhibition of the Pseudomonas aeruginosa Virulence Factor LasB
    • Garner, A. L.; Struss, A. K.; Fullagar, J. L.; Agrawal, A.; Moreno, A. Y.; Cohen, S. M.; Janda, K. D. 3-Hydroxy-1-alkyl-2-methylpyridine-4(1H)-thiones: Inhibition of the Pseudomonas aeruginosa Virulence Factor LasB ACS Med. Chem. Lett. 2012, 3 ( 8 ) 668-672 10.1021/ml300128f
    • (2012) ACS Med. Chem. Lett. , vol.3 , Issue.8 , pp. 668-672
    • Garner, A.L.1    Struss, A.K.2    Fullagar, J.L.3    Agrawal, A.4    Moreno, A.Y.5    Cohen, S.M.6    Janda, K.D.7
  • 36
    • 84875444608 scopus 로고    scopus 로고
    • Antagonism of a Zinc Metalloprotease Using a Unique Metal-Chelating Scaffold: Tropolones as Inhibitors of P. aeruginosa Elastase
    • Fullagar, J. L.; Garner, A. L.; Struss, A. K.; Day, J. A.; Martin, D. P.; Yu, J.; Cai, X. Q.; Janda, K. D.; Cohen, S. M. Antagonism of a Zinc Metalloprotease Using a Unique Metal-Chelating Scaffold: Tropolones as Inhibitors of P. aeruginosa Elastase Chem. Commun. 2013, 49 ( 31 ) 3197-3199 10.1039/c3cc41191e
    • (2013) Chem. Commun. , vol.49 , Issue.31 , pp. 3197-3199
    • Fullagar, J.L.1    Garner, A.L.2    Struss, A.K.3    Day, J.A.4    Martin, D.P.5    Yu, J.6    Cai, X.Q.7    Janda, K.D.8    Cohen, S.M.9
  • 37
    • 85013850280 scopus 로고    scopus 로고
    • uHTS Identification of Inhibitors of Rpn11 in a Fluorescent Polarization Assay
    • National Center for Biotechnology Information: Bethesda, MD,; (accessed September 16, 2016).
    • uHTS Identification of Inhibitors of Rpn11 in a Fluorescent Polarization Assay. PubChem BioAssay Database; AID = 588493; National Center for Biotechnology Information: Bethesda, MD, 2012; https://pubchem.ncbi.nlm.nih.gov/bioassay/588493 (accessed September 16, 2016).
    • (2012) PubChem BioAssay Database; AID = 588493
  • 38
    • 85013809962 scopus 로고    scopus 로고
    • uHTS Identification of Small Molecule Inhibitors of Csn-Mediated Deneddylation of Cullin-Ring Ligases, vis a Fluorescence Polarization Assay
    • National Center for Biotechnology Information: Bethesda, MD,; (accessed September 16, 2016).
    • uHTS Identification of Small Molecule Inhibitors of Csn-Mediated Deneddylation of Cullin-Ring Ligases, vis a Fluorescence Polarization Assay. PubChem BioAssay Database; AID = 651999; National Center for Biotechnology Information: Bethesda, MD, 2013; https://pubchem.ncbi.nlm.nih.gov/bioassay/651999 (accessed September 16, 2016).
    • (2013) PubChem BioAssay Database; AID = 651999
  • 39
    • 1942453243 scopus 로고    scopus 로고
    • Ligand Efficiency: A Useful Metric for Lead Selection
    • Hopkins, A. L.; Groom, C. R.; Alex, A. Ligand Efficiency: A Useful Metric for Lead Selection Drug Discovery Today 2004, 9 ( 10 ) 430-431 10.1016/S1359-6446(04)03069-7
    • (2004) Drug Discovery Today , vol.9 , Issue.10 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 40
    • 0028280999 scopus 로고
    • Effect of 8-Hydroxy-Quinoline, 8-Mercapto-Quinoline and 5-Chloro-7-Iodo-8-Hydroxy-Quinoline on the Uptake and Distribution of Nickel in Mice
    • Borgneczak, K.; Tjalve, H. Effect of 8-Hydroxy-Quinoline, 8-Mercapto-Quinoline and 5-Chloro-7-Iodo-8-Hydroxy-Quinoline on the Uptake and Distribution of Nickel in Mice Pharmacol. Toxicol. 1994, 74 ( 3 ) 185-192 10.1111/j.1600-0773.1994.tb01097.x
    • (1994) Pharmacol. Toxicol. , vol.74 , Issue.3 , pp. 185-192
    • Borgneczak, K.1    Tjalve, H.2
  • 42
    • 3242780853 scopus 로고    scopus 로고
    • The Copper(I)/Copper(II) Transition in Complexes With 8-Alkylthioquinoline Based Multidentate Ligands
    • Su, C. Y.; Liao, S.; Wanner, M.; Fiedler, J.; Zhang, C.; Kang, B. S.; Kaim, W. The Copper(I)/Copper(II) Transition in Complexes With 8-Alkylthioquinoline Based Multidentate Ligands Dalton Trans. 2003, 2, 189-202 10.1039/b208120m
    • (2003) Dalton Trans. , vol.2 , pp. 189-202
    • Su, C.Y.1    Liao, S.2    Wanner, M.3    Fiedler, J.4    Zhang, C.5    Kang, B.S.6    Kaim, W.7
  • 43
    • 0037037494 scopus 로고    scopus 로고
    • Elucidating Drug-Metalloprotein Interactions with Tris(pyrazolyl)borate Model Complexes
    • Puerta, D. T.; Cohen, S. M. Elucidating Drug-Metalloprotein Interactions with Tris(pyrazolyl)borate Model Complexes Inorg. Chem. 2002, 41 ( 20 ) 5075-5082 10.1021/ic0204272
    • (2002) Inorg. Chem. , vol.41 , Issue.20 , pp. 5075-5082
    • Puerta, D.T.1    Cohen, S.M.2
  • 44
    • 0034718069 scopus 로고    scopus 로고
    • Lead Poisoning and the inactivation of 5-Aminolevulinate Dehydratase as Modeled by the Tris(2-mercapto-1-phenylimidazolyl)hydroborato Lead Complex, {[Tm-Ph]Pb}[ClO4]
    • Bridgewater, B. M.; Parkin, G. Lead Poisoning and the inactivation of 5-Aminolevulinate Dehydratase as Modeled by the Tris(2-mercapto-1-phenylimidazolyl)hydroborato Lead Complex, {[Tm-Ph]Pb}[ClO4] J. Am. Chem. Soc. 2000, 122 ( 29 ) 7140-7141 10.1021/ja001530y
    • (2000) J. Am. Chem. Soc. , vol.122 , Issue.29 , pp. 7140-7141
    • Bridgewater, B.M.1    Parkin, G.2
  • 45
    • 0035952110 scopus 로고    scopus 로고
    • Methylation of (2-Methylethanethiol-bis-3,5-dimethylpyrazolyl)methane Zinc Complexes and Coordination of the Resulting Thioether: Relevance to Zinc-Containing Alkyl Transfer Enzymes
    • Hammes, B. S.; Carrano, C. J. Methylation of (2-Methylethanethiol-bis-3,5-dimethylpyrazolyl)methane Zinc Complexes and Coordination of the Resulting Thioether: Relevance to Zinc-Containing Alkyl Transfer Enzymes Inorg. Chem. 2001, 40 ( 5 ) 919-927 10.1021/ic001178p
    • (2001) Inorg. Chem. , vol.40 , Issue.5 , pp. 919-927
    • Hammes, B.S.1    Carrano, C.J.2
  • 46
    • 0010636960 scopus 로고
    • Recent Advances in Poly(Pyrazolyl)Borate (Scorpionate) Chemistry
    • Trofimenko, S. Recent Advances in Poly(Pyrazolyl)Borate (Scorpionate) Chemistry Chem. Rev. 1993, 93 ( 3 ) 943-980 10.1021/cr00019a006
    • (1993) Chem. Rev. , vol.93 , Issue.3 , pp. 943-980
    • Trofimenko, S.1
  • 47
    • 0035973693 scopus 로고    scopus 로고
    • Sulfur-Rich Zinc Chemistry: New Tris(thioimidazolyl)hydroborate Ligands and Their Zinc Complex Chemistry Related to the Structure and Function of Alcohol Dehydrogenase
    • Tesmer, M.; Shu, M. H.; Vahrenkamp, H. Sulfur-Rich Zinc Chemistry: New Tris(thioimidazolyl)hydroborate Ligands and Their Zinc Complex Chemistry Related to the Structure and Function of Alcohol Dehydrogenase Inorg. Chem. 2001, 40 ( 16 ) 4022-4029 10.1021/ic0101275
    • (2001) Inorg. Chem. , vol.40 , Issue.16 , pp. 4022-4029
    • Tesmer, M.1    Shu, M.H.2    Vahrenkamp, H.3
  • 48
    • 0032795252 scopus 로고    scopus 로고
    • Transitions, Transition Sstates, Transition State Analogues: Zinc Pyrazolylborate Chemistry Related to Zinc Enzymes
    • Vahrenkamp, H. Transitions, Transition Sstates, Transition State Analogues: Zinc Pyrazolylborate Chemistry Related to Zinc Enzymes Acc. Chem. Res. 1999, 32 ( 7 ) 589-596 10.1021/ar9703185
    • (1999) Acc. Chem. Res. , vol.32 , Issue.7 , pp. 589-596
    • Vahrenkamp, H.1
  • 49
    • 50449108516 scopus 로고    scopus 로고
    • Structural Insights Into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation
    • Duda, D. M.; Borg, L. A.; Scott, D. C.; Hunt, H. W.; Hammel, M.; Schulman, B. A. Structural Insights Into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation Cell 2008, 134 ( 6 ) 995-1006 10.1016/j.cell.2008.07.022
    • (2008) Cell , vol.134 , Issue.6 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 50
    • 79953215473 scopus 로고    scopus 로고
    • Quantitative Cell-based Protein Degradation Assays to Identify and Classify Drugs That Target the Ubiquitin-Proteasome System
    • Chou, T. F.; Deshaies, R. J. Quantitative Cell-based Protein Degradation Assays to Identify and Classify Drugs That Target the Ubiquitin-Proteasome System J. Biol. Chem. 2011, 286 ( 19 ) 16546-16554 10.1074/jbc.M110.215319
    • (2011) J. Biol. Chem. , vol.286 , Issue.19 , pp. 16546-16554
    • Chou, T.F.1    Deshaies, R.J.2
  • 51
    • 80054717381 scopus 로고    scopus 로고
    • Structural and Thermodynamic Comparison of the Catalytic Domain of AMSH and AMSH-LP: Nearly Identical Fold but Different Stability
    • Davies, C. W.; Paul, L. N.; Kim, M. I.; Das, C. Structural and Thermodynamic Comparison of the Catalytic Domain of AMSH and AMSH-LP: Nearly Identical Fold but Different Stability J. Mol. Biol. 2011, 413 ( 2 ) 416-429 10.1016/j.jmb.2011.08.029
    • (2011) J. Mol. Biol. , vol.413 , Issue.2 , pp. 416-429
    • Davies, C.W.1    Paul, L.N.2    Kim, M.I.3    Das, C.4
  • 52
    • 32444434063 scopus 로고    scopus 로고
    • Heterocyclic Zinc-Binding Groups for Use in Next-Generation Matrix Metalloproteinase Inhibitors: Potency, Toxicity, and Reactivity
    • Puerta, D. T.; Griffin, M. O.; Lewis, J. A.; Romero-Perez, D.; Garcia, R.; Villarreal, F. J.; Cohen, S. M. Heterocyclic Zinc-Binding Groups for Use in Next-Generation Matrix Metalloproteinase Inhibitors: Potency, Toxicity, and Reactivity JBIC, J. Biol. Inorg. Chem. 2006, 11 ( 2 ) 131-138 10.1007/s00775-005-0053-x
    • (2006) JBIC, J. Biol. Inorg. Chem. , vol.11 , Issue.2 , pp. 131-138
    • Puerta, D.T.1    Griffin, M.O.2    Lewis, J.A.3    Romero-Perez, D.4    Garcia, R.5    Villarreal, F.J.6    Cohen, S.M.7
  • 54
    • 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 10.1021/ic400295f
    • (2013) Inorg. Chem. , vol.52 , Issue.21 , pp. 12207-12215
    • Martin, D.P.1    Hann, Z.S.2    Cohen, S.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.