메뉴 건너뛰기




Volumn 58, Issue 4, 2015, Pages 1581-1595

Inhibiting the deubiquitinating enzymes (DUBs)

Author keywords

[No Author keywords available]

Indexed keywords

DEUBIQUITINATING ENZYME INHIBITOR; SMALL MOLECULE TRANSPORT AGENT; UNCLASSIFIED DRUG; DEUBIQUITINASE; ENZYME INHIBITOR;

EID: 84924082223     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm501061a     Document Type: Review
Times cited : (75)

References (105)
  • 1
    • 84898802930 scopus 로고    scopus 로고
    • Toward Understanding Ubiquitin-Modifying Enzymes: From Pharmacological Targeting to Proteomics
    • Lill, J. R.; Wertz, I. E. Toward Understanding Ubiquitin-Modifying Enzymes: From Pharmacological Targeting to Proteomics Trends Pharmacol. Sci. 2014, 35, 187-207
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 187-207
    • Lill, J.R.1    Wertz, I.E.2
  • 2
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and Cellular Roles of Ubiquitin-Specific Deubiquitinating Enzymes
    • Reyes-Turcu, F. E.; Ventii, K. H.; Wilkinson, K. D. Regulation and Cellular Roles of Ubiquitin-Specific Deubiquitinating Enzymes Annu. Rev. Biochem. 2009, 78, 363-397
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 3
    • 84864448811 scopus 로고    scopus 로고
    • Proteasome Deubiquitinases as Novel Targets for Cancer Therapy
    • D'Arcy, P.; Linder, S. Proteasome Deubiquitinases as Novel Targets for Cancer Therapy Int. J. Biochem. Cell Biol. 2012, 44, 1729-1738
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1729-1738
    • D'Arcy, P.1    Linder, S.2
  • 4
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin Chains: Polymeric Protein Signals
    • Pickart, C. M.; Fushman, D. Polyubiquitin Chains: Polymeric Protein Signals Curr. Opin. Chem. Biol. 2004, 8, 610-616
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 6
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and Ubiquitin-like Proteins as Multifunctional Signals
    • Welchman, R. L.; Gordon, C.; Mayer, R. J. Ubiquitin and Ubiquitin-like Proteins as Multifunctional Signals Nat. Rev. Mol. Cell Biol. 2005, 6, 599-609
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 9
    • 84880966633 scopus 로고    scopus 로고
    • Deubiquitinating Enzymes as Therapeutic Targets in Cancer
    • Lim, K.-H.; Baek, K.-H. Deubiquitinating Enzymes as Therapeutic Targets in Cancer Curr. Pharm. Des. 2013, 19, 4039-4052
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 4039-4052
    • Lim, K.-H.1    Baek, K.-H.2
  • 10
    • 3943054838 scopus 로고    scopus 로고
    • De-Ubiquitination and Ubiquitin Ligase Domains of A20 Downregulate NF-[Kappa]B Signalling
    • Wertz, I. E.; O'Rourke, K. M.; Zhou, H.; Eby, M.; Aravind, L. De-Ubiquitination and Ubiquitin Ligase Domains of A20 Downregulate NF-[Kappa]B Signalling Nature 2004, 430, 694-699
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1    O'Rourke, K.M.2    Zhou, H.3    Eby, M.4    Aravind, L.5
  • 11
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the Chains: Structure and Function of the Deubiquitinases
    • Komander, D.; Clague, M. J.; Urbé, S. Breaking the Chains: Structure and Function of the Deubiquitinases Nat. Rev. Mol. Cell Biol. 2009, 10, 550-563
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 12
    • 77953694906 scopus 로고    scopus 로고
    • The Potential Role of Ubiquitin C-Terminal Hydrolase in Oncogenesis
    • Fang, Y.; Da, Fu; Shen, X.-Z. The Potential Role of Ubiquitin C-Terminal Hydrolase in Oncogenesis Biochim. Biophys. Acta 2010, 1806, 1-6
    • (2010) Biochim. Biophys. Acta , vol.1806 , pp. 1-6
    • Fang, Y.1    Da, F.2    Shen, X.-Z.3
  • 13
    • 38849110179 scopus 로고    scopus 로고
    • Targeting Ubiquitin Specific Proteases for Drug Discovery
    • Daviet, L.; Colland, F. Targeting Ubiquitin Specific Proteases for Drug Discovery Biochimie 2008, 90, 270-283
    • (2008) Biochimie , vol.90 , pp. 270-283
    • Daviet, L.1    Colland, F.2
  • 14
    • 84890190983 scopus 로고    scopus 로고
    • Regulation of Proteolysis by Human Deubiquitinating Enzymes
    • Eletr, Z. M.; Wilkinson, K. D. Regulation of Proteolysis by Human Deubiquitinating Enzymes Biochim. Biophys. Acta 2014, 1843, 114-128
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 114-128
    • Eletr, Z.M.1    Wilkinson, K.D.2
  • 15
    • 84915770915 scopus 로고    scopus 로고
    • Deubiquitinating Enzyme Regulation of the P53 Pathway: A Lesson from OTUB1
    • Sun, X.-X.; Dai, M.-S. Deubiquitinating Enzyme Regulation of the P53 Pathway: A Lesson From OTUB1 World J. Biol. Chem. 2014, 5, 75-84
    • (2014) World J. Biol. Chem. , vol.5 , pp. 75-84
    • Sun, X.-X.1    Dai, M.-S.2
  • 17
    • 33646193928 scopus 로고    scopus 로고
    • Cytokine-Regulated Protein Degradation by the Ubiquitination System
    • Baek, K.-H. Cytokine-Regulated Protein Degradation by the Ubiquitination System Curr. Protein Pept. Sci. 2006, 7, 171-177
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 171-177
    • Baek, K.-H.1
  • 18
    • 67649634849 scopus 로고    scopus 로고
    • Defining the Human Deubiquitinating Enzyme Interaction Landscape
    • Sowa, M. E.; Bennett, E. J.; Gygi, S. P.; Harper, J. W. Defining the Human Deubiquitinating Enzyme Interaction Landscape Cell 2009, 138, 389-403
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 19
    • 0033565867 scopus 로고    scopus 로고
    • Structural Basis for the Specificity of Ubiquitin C-Terminal Hydrolases
    • Johnston, S. C.; Riddle, S. M.; Cohen, R. E.; Hill, C. P. Structural Basis for the Specificity of Ubiquitin C-Terminal Hydrolases EMBO J. 1999, 18, 3877-3887
    • (1999) EMBO J. , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 20
    • 84892365810 scopus 로고    scopus 로고
    • Development of Inhibitors in the Ubiquitination Cascade
    • Zhang, W.; Sidhu, S. S. Development of Inhibitors in the Ubiquitination Cascade FEBS Lett. 2014, 588, 356-367
    • (2014) FEBS Lett. , vol.588 , pp. 356-367
    • Zhang, W.1    Sidhu, S.S.2
  • 23
    • 0037184947 scopus 로고    scopus 로고
    • Crystal Structure of a UBP-Family Deubiquitinating Enzyme in Isolation and in Complex with Ubiquitin Aldehyde
    • Hu, M.; Li, P.; Li, M.; Li, W.; Yao, T.; Wu, J.-W.; Gu, W.; Cohen, R. E.; Shi, Y. Crystal Structure of a UBP-Family Deubiquitinating Enzyme in Isolation and in Complex with Ubiquitin Aldehyde Cell 2002, 111, 1041-1054
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.-W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 24
    • 33846021632 scopus 로고    scopus 로고
    • Amino-Terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-Specific Protease 8 (USP8)
    • Avvakumov, G. V.; Walker, J. R.; Xue, S.; Finerty, P. J.; Mackenzie, F.; Newman, E. M.; Dhe-Paganon, S. Amino-Terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-Specific Protease 8 (USP8) J. Biol. Chem. 2006, 281, 38061-38070
    • (2006) J. Biol. Chem. , vol.281 , pp. 38061-38070
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3    Finerty, P.J.4    Mackenzie, F.5    Newman, E.M.6    Dhe-Paganon, S.7
  • 25
    • 27744516748 scopus 로고    scopus 로고
    • Structure and Mechanisms of the Proteasome-Associated Deubiquitinating Enzyme USP14
    • Hu, M.; Li, P.; Song, L.; Jeffrey, P. D.; Chenova, T. A.; Wilkinson, K. D.; Cohen, R. E.; Shi, Y. Structure and Mechanisms of the Proteasome-Associated Deubiquitinating Enzyme USP14 EMBO J. 2005, 24, 3747-3756
    • (2005) EMBO J. , vol.24 , pp. 3747-3756
    • Hu, M.1    Li, P.2    Song, L.3    Jeffrey, P.D.4    Chenova, T.A.5    Wilkinson, K.D.6    Cohen, R.E.7    Shi, Y.8
  • 29
    • 84901670584 scopus 로고    scopus 로고
    • Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating Activity of SARS-CoV Papain-like Protease
    • Ratia, K.; Kilianski, A.; Baez-Santos, Y. M.; Baker, S. C.; Mesecar, A. Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating Activity of SARS-CoV Papain-like Protease PLoS Pathog. 2014, 10, e1004113
    • (2014) PLoS Pathog. , vol.10 , pp. 1004113
    • Ratia, K.1    Kilianski, A.2    Baez-Santos, Y.M.3    Baker, S.C.4    Mesecar, A.5
  • 30
    • 44449109533 scopus 로고    scopus 로고
    • Mechanism and Consequences for Paralog-Specific Sumoylation of Ubiquitin-Specific Protease 25
    • Meulmeester, E.; Kunze, M.; Hsiao, H. H.; Urlaub, H.; Melchior, F. Mechanism and Consequences for Paralog-Specific Sumoylation of Ubiquitin-Specific Protease 25 Mol. Cell 2008, 30, 610-619
    • (2008) Mol. Cell , vol.30 , pp. 610-619
    • Meulmeester, E.1    Kunze, M.2    Hsiao, H.H.3    Urlaub, H.4    Melchior, F.5
  • 31
    • 50949126350 scopus 로고    scopus 로고
    • Protein Partners of Deubiquitinating Enzymes
    • Ventii, K. H.; Wilkinson, K. D. Protein Partners of Deubiquitinating Enzymes Biochem. J. 2008, 414, 161-175
    • (2008) Biochem. J. , vol.414 , pp. 161-175
    • Ventii, K.H.1    Wilkinson, K.D.2
  • 32
    • 64149129169 scopus 로고    scopus 로고
    • UAF1 is a Subunit of Multiple Deubiquitinating Enzyme Complexes
    • Cohn, M. A.; Kee, Y.; Haas, W.; Gygi, S. P.; D'Andrea, A. D. UAF1 Is a Subunit of Multiple Deubiquitinating Enzyme Complexes J. Biol. Chem. 2009, 284, 5343-5351
    • (2009) J. Biol. Chem. , vol.284 , pp. 5343-5351
    • Cohn, M.A.1    Kee, Y.2    Haas, W.3    Gygi, S.P.4    D'Andrea, A.D.5
  • 33
    • 33244490784 scopus 로고    scopus 로고
    • Structural Basis of Competitive Recognition of P53 and MDM2 by HAUSP/USP7: Implications for the Regulation of the P53-MDM2 Pathway
    • Hu, M.; Gu, L.; Li, M.; Jeffrey, P. D.; Gu, W.; Shi, Y. Structural Basis of Competitive Recognition of P53 and MDM2 by HAUSP/USP7: Implications for the Regulation of the P53-MDM2 Pathway PLoS Biol. 2006, 4, e27
    • (2006) PLoS Biol. , vol.4 , pp. 27
    • Hu, M.1    Gu, L.2    Li, M.3    Jeffrey, P.D.4    Gu, W.5    Shi, Y.6
  • 34
    • 80053594090 scopus 로고    scopus 로고
    • Mechanism of USP7/HAUSP Activationby Its C-Terminal Ubiquitin-like Domainand Allosteric Regulation by GMP-Synthetase
    • Faesen, A. C.; Dirac, A. M. G.; Shanmugham, A.; Ovaa, H.; Perrakis, A.; Sixma, T. K. Mechanism of USP7/HAUSP Activationby Its C-Terminal Ubiquitin-like Domainand Allosteric Regulation by GMP-Synthetase Mol. Cell 2011, 44, 147-159
    • (2011) Mol. Cell , vol.44 , pp. 147-159
    • Faesen, A.C.1    Dirac, A.M.G.2    Shanmugham, A.3    Ovaa, H.4    Perrakis, A.5    Sixma, T.K.6
  • 35
    • 0031011721 scopus 로고    scopus 로고
    • Crystal Structure of a Deubiquitinating Enzyme (Human UCH-L3) at 1.8 Å Resolution
    • Johnston, S. C.; Larsen, C. N.; Cook, W. J.; Wilkinson, K. D.; Hill, C. P. Crystal Structure of a Deubiquitinating Enzyme (Human UCH-L3) at 1.8 Å Resolution EMBO J. 1997, 16, 3787-3796
    • (1997) EMBO J. , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 37
    • 84055178186 scopus 로고    scopus 로고
    • Length of the Active-Site Crossover Loop Defines the Substrate Specificity of Ubiquitin C-Terminal Hydrolases for Ubiquitin Chains
    • Zhou, Z. R.; Zhang, Y. H.; Liu, S.; Song, A. X.; Hu, H. Y. Length of the Active-Site Crossover Loop Defines the Substrate Specificity of Ubiquitin C-Terminal Hydrolases for Ubiquitin Chains Biochem. J. 2012, 441, 143-149
    • (2012) Biochem. J. , vol.441 , pp. 143-149
    • Zhou, Z.R.1    Zhang, Y.H.2    Liu, S.3    Song, A.X.4    Hu, H.Y.5
  • 39
    • 63649131003 scopus 로고    scopus 로고
    • Substrate Filtering by the Active Site Crossover Loop in UCHL3 Revealed by Sortagging and Gain-of-Function Mutations
    • Popp, M. W.; Artavanis-Tsakonas, K.; Ploegh, H. L. Substrate Filtering by the Active Site Crossover Loop in UCHL3 Revealed by Sortagging and Gain-of-Function Mutations J. Biol. Chem. 2009, 284, 3593-3602
    • (2009) J. Biol. Chem. , vol.284 , pp. 3593-3602
    • Popp, M.W.1    Artavanis-Tsakonas, K.2    Ploegh, H.L.3
  • 40
    • 0032502276 scopus 로고    scopus 로고
    • Substrate Specificity of Deubiquitinating Enzymes: Ubiquitin C-Terminal Hydrolases
    • Larsen, C. N. C.; Krantz, B. A. B.; Wilkinson, K. D. K. Substrate Specificity of Deubiquitinating Enzymes: Ubiquitin C-Terminal Hydrolases Biochemistry 1998, 37, 3358-3368
    • (1998) Biochemistry , vol.37 , pp. 3358-3368
    • Larsen, C.N.C.1    Krantz, B.A.B.2    Wilkinson, K.D.K.3
  • 41
    • 82755187438 scopus 로고    scopus 로고
    • Crystal Structure of the Catalytic Domain of UCHL5, a Proteasome-Associated Human Deubiquitinating Enzyme, Reveals an Unproductive Form of the Enzyme
    • Maiti, T. K.; Permaul, M.; Boudreaux, D. A.; Mahanic, C.; Mauney, S.; Das, C. Crystal Structure of the Catalytic Domain of UCHL5, a Proteasome-Associated Human Deubiquitinating Enzyme, Reveals an Unproductive Form of the Enzyme FEBS J. 2011, 278, 4917-4926
    • (2011) FEBS J. , vol.278 , pp. 4917-4926
    • Maiti, T.K.1    Permaul, M.2    Boudreaux, D.A.3    Mahanic, C.4    Mauney, S.5    Das, C.6
  • 42
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and Mechanistic Studies on the Hydrolysis of Ubiquitin C-Terminal 7-Amido-4-Methylcoumarin by Deubiquitinating Enzymes
    • Dang, L. C.; Melandri, F. D.; Stein, R. L. Kinetic and Mechanistic Studies on the Hydrolysis of Ubiquitin C-Terminal 7-Amido-4-Methylcoumarin by Deubiquitinating Enzymes Biochemistry 1998, 37, 1868-1879
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 44
    • 35548991428 scopus 로고    scopus 로고
    • A Sensitive Fluorescence Intensity Assay for Deubiquitinating Proteases Using Ubiquitin-Rhodamine110-Glycine as Substrate
    • Hassiepen, U.; Eidhoff, U.; Meder, G.; Bulber, J.-F.; Hein, A.; Bodendorf, U.; Lorthiois, E.; Martoglio, B. A Sensitive Fluorescence Intensity Assay for Deubiquitinating Proteases Using Ubiquitin-Rhodamine110-Glycine as Substrate Anal. Biochem. 2007, 371, 201-207
    • (2007) Anal. Biochem. , vol.371 , pp. 201-207
    • Hassiepen, U.1    Eidhoff, U.2    Meder, G.3    Bulber, J.-F.4    Hein, A.5    Bodendorf, U.6    Lorthiois, E.7    Martoglio, B.8
  • 48
    • 84855873408 scopus 로고    scopus 로고
    • A General Chemical Ligation Approach towards Isopeptide-Linked Ubiquitin and Ubiquitin-like Assay Reagents
    • Geurink, P. P.; El Oualid, F.; Jonker, A.; Hameed, D. S.; Ovaa, H. A General Chemical Ligation Approach towards Isopeptide-Linked Ubiquitin and Ubiquitin-like Assay Reagents ChemBioChem 2011, 13, 293-297
    • (2011) ChemBioChem , vol.13 , pp. 293-297
    • Geurink, P.P.1    El Oualid, F.2    Jonker, A.3    Hameed, D.S.4    Ovaa, H.5
  • 49
    • 84856846038 scopus 로고    scopus 로고
    • Targeting Deubiquitinases Enabled by Chemical Synthesis of Proteins
    • Ohayon, S.; Spasser, L.; Aharoni, A.; Brik, A. Targeting Deubiquitinases Enabled by Chemical Synthesis of Proteins J. Am. Chem. Soc. 2012, 134, 3281-3289
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3281-3289
    • Ohayon, S.1    Spasser, L.2    Aharoni, A.3    Brik, A.4
  • 52
    • 84890859198 scopus 로고    scopus 로고
    • Deubiquitinating Enzyme Specificity for Ubiquitin Chain Topology Profiled by Di-Ubiquitin Activity Probes
    • McGouran, J. F.; Gaertner, S. R.; Altun, M.; Kramer, H. B.; Kessler, B. M. Deubiquitinating Enzyme Specificity for Ubiquitin Chain Topology Profiled by Di-Ubiquitin Activity Probes Chem. Biol. 2013, 20, 1447-1455
    • (2013) Chem. Biol. , vol.20 , pp. 1447-1455
    • McGouran, J.F.1    Gaertner, S.R.2    Altun, M.3    Kramer, H.B.4    Kessler, B.M.5
  • 54
    • 84889020913 scopus 로고    scopus 로고
    • Activity-Based Diubiquitin Probes for Elucidating the Linkage Specificity of Deubiquitinating Enzymes
    • Li, G.; Liang, Q.; Gong, P.; Tencer, A. H.; Zhuang, Z. Activity-Based Diubiquitin Probes for Elucidating the Linkage Specificity of Deubiquitinating Enzymes Chem. Commun. 2014, 50, 216-218
    • (2014) Chem. Commun. , vol.50 , pp. 216-218
    • Li, G.1    Liang, Q.2    Gong, P.3    Tencer, A.H.4    Zhuang, Z.5
  • 55
    • 13444275087 scopus 로고    scopus 로고
    • Chemistry-Based Functional Proteomics: Mechanism-Based Activity-Profiling Tools for Ubiquitin and Ubiquitin-like Specific Proteases
    • Hemelaar, J.; Galardy, P. J.; Borodovsky, A.; Kessler, B. M.; Ploegh, H. L.; Ovaa, H. Chemistry-Based Functional Proteomics: Mechanism-Based Activity-Profiling Tools for Ubiquitin and Ubiquitin-like Specific Proteases J. Proteome Res. 2004, 3, 268-276
    • (2004) J. Proteome Res. , vol.3 , pp. 268-276
    • Hemelaar, J.1    Galardy, P.J.2    Borodovsky, A.3    Kessler, B.M.4    Ploegh, H.L.5    Ovaa, H.6
  • 57
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of P53 by HAUSP is an Important Pathway for P53 Stabilization
    • Li, M.; Chen, D.; Shiloh, A.; Luo, J.; Nikolaev, A. Y.; Qin, J.; Gu, W. Deubiquitination of P53 by HAUSP Is an Important Pathway for P53 Stabilization Nature 2002, 416, 648-653
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 59
    • 1842421376 scopus 로고    scopus 로고
    • A Dynamic Role of HAUSP in the P53-Mdm2 Pathway
    • Li, M.; Brooks, C. L.; Kon, N.; Gu, W. A Dynamic Role of HAUSP in the P53-Mdm2 Pathway Mol. Cell 2004, 13, 879-886
    • (2004) Mol. Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 60
    • 31544457877 scopus 로고    scopus 로고
    • P53 Ubiquitination: Mdm2 and beyond
    • Brooks, C. L.; Gu, W. P53 Ubiquitination: Mdm2 and Beyond Mol. Cell 2006, 21, 307-315
    • (2006) Mol. Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 64
    • 77950678464 scopus 로고    scopus 로고
    • Synthesis and Biological Evaluation of 9-Oxo-9 H -Indeno[1,2- b ]pyrazine-2,3-dicarbonitrile Analogues as Potential Inhibitors of Deubiquitinating Enzymes
    • Colombo, M.; Vallese, S.; Peretto, I.; Jacq, X.; Rain, J. C.; Colland, F.; Guedat, P. Synthesis and Biological Evaluation of 9-Oxo-9 H -Indeno[1,2- b ]pyrazine-2,3-dicarbonitrile Analogues as Potential Inhibitors of Deubiquitinating Enzymes ChemMedChem 2010, 5, 552-558
    • (2010) ChemMedChem , vol.5 , pp. 552-558
    • Colombo, M.1    Vallese, S.2    Peretto, I.3    Jacq, X.4    Rain, J.C.5    Colland, F.6    Guedat, P.7
  • 66
    • 0034736034 scopus 로고    scopus 로고
    • New Tacrine-Huperzine A Hybrids (Huprines): Highly Potent Tight-Binding Acetylcholinesterase Inhibitors of Interest for the Treatment of Alzheimer's Disease
    • Camps, P.; El Achab, R.; Morral, J.; Munoz-Torrero, D.; Badia, A.; Banos, J. E.; Vivas, N. M.; Barril, X.; Orozco, M.; Luque, F. J. New Tacrine-Huperzine A Hybrids (Huprines): Highly Potent Tight-Binding Acetylcholinesterase Inhibitors of Interest for the Treatment of Alzheimer's Disease J. Med. Chem. 2000, 43, 4657-4666
    • (2000) J. Med. Chem. , vol.43 , pp. 4657-4666
    • Camps, P.1    El Achab, R.2    Morral, J.3    Munoz-Torrero, D.4    Badia, A.5    Banos, J.E.6    Vivas, N.M.7    Barril, X.8    Orozco, M.9    Luque, F.J.10
  • 67
    • 84866992804 scopus 로고    scopus 로고
    • Detection of Ubiquitin-Proteasome Enzymatic Activities in Cells: Application of Activity-Based Probes to Inhibitor Development
    • Kramer, H. B.; Nicholson, B.; Kessler, B. M.; Altun, M. Detection of Ubiquitin-Proteasome Enzymatic Activities in Cells: Application of Activity-Based Probes to Inhibitor Development Biochim. Biophys. Acta 2012, 1823, 2029-2037
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 2029-2037
    • Kramer, H.B.1    Nicholson, B.2    Kessler, B.M.3    Altun, M.4
  • 70
    • 48249124967 scopus 로고    scopus 로고
    • Regulation of Mitochondrial Morphology by USP30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane
    • Nakamura, N.; Hirose, S. Regulation of Mitochondrial Morphology by USP30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane Mol. Biol. Cell 2008, 19, 1903-1911
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1903-1911
    • Nakamura, N.1    Hirose, S.2
  • 72
    • 84884843703 scopus 로고    scopus 로고
    • Diterpenoid Derivate Compound Targets Selenocysteine of Thioredoxin Reductases and Induces Bax/Bak-Independent Apoptosis
    • Liu, J.; Mu, C.; Yue, W.; Li, J.; Ma, B.; Zhao, L.; Liu, L. A.; Hao, X.; Zhu, Y. Diterpenoid Derivate Compound Targets Selenocysteine of Thioredoxin Reductases and Induces Bax/Bak-Independent Apoptosis Free Radical Biol. Med. 2013, 63, 485-494
    • (2013) Free Radical Biol. Med. , vol.63 , pp. 485-494
    • Liu, J.1    Mu, C.2    Yue, W.3    Li, J.4    Ma, B.5    Zhao, L.6    Liu, L.A.7    Hao, X.8    Zhu, Y.9
  • 73
    • 79955613593 scopus 로고    scopus 로고
    • A Diterpenoid Derivative 15-Oxospiramilactone Inhibits Wnt/B-Catenin Signaling and Colon Cancer Cell Tumorigenesis
    • Wang, W.; Liu, H.; Wang, S.; Hao, X.; Li, L. A Diterpenoid Derivative 15-Oxospiramilactone Inhibits Wnt/B-Catenin Signaling and Colon Cancer Cell Tumorigenesis Cell Res. 2011, 21, 730-740
    • (2011) Cell Res. , vol.21 , pp. 730-740
    • Wang, W.1    Liu, H.2    Wang, S.3    Hao, X.4    Li, L.5
  • 75
  • 76
    • 77957260099 scopus 로고    scopus 로고
    • The Lys63-Specific Deubiquitinating Enzyme BRCC36 is Regulated by Two Scaffold Proteins Localizing in Different Subcellular Compartments
    • Feng, L.; Wang, J.; Chen, J. The Lys63-Specific Deubiquitinating Enzyme BRCC36 Is Regulated by Two Scaffold Proteins Localizing in Different Subcellular Compartments J. Biol. Chem. 2010, 285, 30982-30988
    • (2010) J. Biol. Chem. , vol.285 , pp. 30982-30988
    • Feng, L.1    Wang, J.2    Chen, J.3
  • 77
    • 62549140202 scopus 로고    scopus 로고
    • The Rap80-BRCC36 De-Ubiquitinating Enzyme Complex Antagonizes RNF8-Ubc13-Dependent Ubiquitination Events at DNA Double Strand Breaks
    • Shao, G.; Lilli, D. R.; Patterson-Fortin, J.; Coleman, K. A.; Morrissey, D. E.; Greenberg, R. A. The Rap80-BRCC36 De-Ubiquitinating Enzyme Complex Antagonizes RNF8-Ubc13-Dependent Ubiquitination Events at DNA Double Strand Breaks Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 3166-3171
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 3166-3171
    • Shao, G.1    Lilli, D.R.2    Patterson-Fortin, J.3    Coleman, K.A.4    Morrissey, D.E.5    Greenberg, R.A.6
  • 80
    • 59649114341 scopus 로고    scopus 로고
    • Inactivation of Murine USP1 Results in Genomic Instability and a Fanconi Anemia Phenotype
    • Kim, J. M.; Parmar, K.; Huang, M.; Weinstock, D. M.; Ruit, C. A.; Kutok, J. L.; D'Andrea, A. D. Inactivation of Murine USP1 Results in Genomic Instability and a Fanconi Anemia Phenotype Dev. Cell 2009, 16, 314-320
    • (2009) Dev. Cell , vol.16 , pp. 314-320
    • Kim, J.M.1    Parmar, K.2    Huang, M.3    Weinstock, D.M.4    Ruit, C.A.5    Kutok, J.L.6    D'Andrea, A.D.7
  • 83
    • 82255194029 scopus 로고    scopus 로고
    • Selective and Cell-Active Inhibitors of the USP1/ UAF1 Deubiquitinase Complex Reverse Cisplatin Resistance in Non-Small Cell Lung Cancer Cells
    • Chen, J.; Dexheimer, T. S.; Ai, Y.; Liang, Q.; Villamil, M. A.; Inglese, J.; Maloney, D. J.; Jadhav, A.; Simeonov, A.; Zhuang, Z. Selective and Cell-Active Inhibitors of the USP1/ UAF1 Deubiquitinase Complex Reverse Cisplatin Resistance in Non-Small Cell Lung Cancer Cells Chem. Biol. 2011, 18, 1390-1400
    • (2011) Chem. Biol. , vol.18 , pp. 1390-1400
    • Chen, J.1    Dexheimer, T.S.2    Ai, Y.3    Liang, Q.4    Villamil, M.A.5    Inglese, J.6    Maloney, D.J.7    Jadhav, A.8    Simeonov, A.9    Zhuang, Z.10
  • 87
    • 84907886762 scopus 로고    scopus 로고
    • Synthesis and Structure-Activity Relationship Studies of N -Benzyl-2-phenylpyrimidin-4-amine Derivatives as Potent USP1/UAF1 Deubiquitinase Inhibitors with Anticancer Activity against Nonsmall Cell Lung Cancer
    • Dexheimer, T. S.; Rosenthal, A. S.; Luci, D. K.; Liang, Q.; Villamil, M. A.; Chen, J.; Sun, H.; Kerns, E. H.; Simeonov, A.; Jadhav, A.; Zhuang, Z.; Maloney, D. J. Synthesis and Structure-Activity Relationship Studies of N -Benzyl-2-phenylpyrimidin-4-amine Derivatives as Potent USP1/UAF1 Deubiquitinase Inhibitors with Anticancer Activity against Nonsmall Cell Lung Cancer J. Med. Chem. 2014, 57, 8099-8110
    • (2014) J. Med. Chem. , vol.57 , pp. 8099-8110
    • Dexheimer, T.S.1    Rosenthal, A.S.2    Luci, D.K.3    Liang, Q.4    Villamil, M.A.5    Chen, J.6    Sun, H.7    Kerns, E.H.8    Simeonov, A.9    Jadhav, A.10    Zhuang, Z.11    Maloney, D.J.12
  • 88
    • 2942618660 scopus 로고    scopus 로고
    • The Role of the Ubiquitin-Proteasomal Pathway in Parkinson's Disease and Other Neurodegenerative Disorders
    • Chung, K. K.; Dawson, V. L.; Dawson, T. M. The Role of the Ubiquitin-Proteasomal Pathway in Parkinson's Disease and Other Neurodegenerative Disorders Trends Neurosci. 2001, 24, S7-S14
    • (2001) Trends Neurosci. , vol.24 , pp. 7-S14
    • Chung, K.K.1    Dawson, V.L.2    Dawson, T.M.3
  • 89
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 Gene Encodes Two Opposing Enzymatic Activities That Affect Alpha-Synuclein Degradation and Parkinson's Disease Susceptibility
    • Liu, Y.; Fallon, L.; Lashuel, H. A.; Liu, Z.; Lansbury, P. T. The UCH-L1 Gene Encodes Two Opposing Enzymatic Activities That Affect Alpha-Synuclein Degradation and Parkinson's Disease Susceptibility Cell 2002, 111, 209-218
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1    Fallon, L.2    Lashuel, H.A.3    Liu, Z.4    Lansbury, P.T.5
  • 91
    • 34250160956 scopus 로고    scopus 로고
    • Structure-Activity Relationship, Kinetic Mechanism, and Selectivity for a New Class of Ubiquitin C-Terminal Hydrolase-L1 (UCH-L1) Inhibitors
    • Mermerian, A. H.; Case, A.; Stein, R. L.; Cuny, G. D. Structure-Activity Relationship, Kinetic Mechanism, and Selectivity for a New Class of Ubiquitin C-Terminal Hydrolase-L1 (UCH-L1) Inhibitors Bioorg. Med. Chem. Lett. 2007, 17, 3729-3732
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 3729-3732
    • Mermerian, A.H.1    Case, A.2    Stein, R.L.3    Cuny, G.D.4
  • 94
    • 84908530414 scopus 로고    scopus 로고
    • Chemistry: Chemical Con Artists Foil Drug Discovery
    • Baell, J.; Walters, M. A. Chemistry: Chemical Con Artists Foil Drug Discovery Nature 2014, 513, 481-483
    • (2014) Nature , vol.513 , pp. 481-483
    • Baell, J.1    Walters, M.A.2
  • 95
    • 77950571108 scopus 로고    scopus 로고
    • New Substructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclusion in Bioassays
    • Baell, J. B.; Holloway, G. A. New Substructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclusion in Bioassays J. Med. Chem. 2010, 53, 2719-2740
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 96
    • 77958044565 scopus 로고    scopus 로고
    • Observations on Screening-Based Research and Some Concerning Trends in the Literature
    • Baell, J. B. Observations on Screening-Based Research and Some Concerning Trends in the Literature Future Med. Chem. 2010, 2, 1529-1546
    • (2010) Future Med. Chem. , vol.2 , pp. 1529-1546
    • Baell, J.B.1
  • 97
    • 78549247880 scopus 로고    scopus 로고
    • Deubiquitinase Inhibition by Small-Molecule WP1130 Triggers Aggresome Formation and Tumor Cell Apoptosis
    • Kapuria, V.; Peterson, L. F.; Fang, D.; Bornmann, W. G.; Talpaz, M.; Donato, N. J. Deubiquitinase Inhibition by Small-Molecule WP1130 Triggers Aggresome Formation and Tumor Cell Apoptosis Cancer Res. 2010, 70, 9265-9276
    • (2010) Cancer Res. , vol.70 , pp. 9265-9276
    • Kapuria, V.1    Peterson, L.F.2    Fang, D.3    Bornmann, W.G.4    Talpaz, M.5    Donato, N.J.6
  • 101
    • 77649204688 scopus 로고    scopus 로고
    • Selectively Nonselective Kinase Inhibition: Striking the Right Balance
    • Morphy, R. Selectively Nonselective Kinase Inhibition: Striking the Right Balance J. Med. Chem. 2010, 53, 1413-1437
    • (2010) J. Med. Chem. , vol.53 , pp. 1413-1437
    • Morphy, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.