메뉴 건너뛰기




Volumn 20, Issue 6, 2015, Pages 788-800

A fragment-based ligand screen against part of a large protein machine: The ND1 domains of the AAA+ ATPase p97/VCP

Author keywords

AAA+ ATPase p97; fragment based drug design; valosin containing protein (VCP)

Indexed keywords

ADENOSINE TRIPHOSPHATASE; LIGAND; PROTEIN P97; VALOSIN CONTAINING PROTEIN; CDC48 PROTEIN; CELL CYCLE PROTEIN; NUCLEAR PROTEIN; P97 ATPASE; PROTEIN BINDING;

EID: 84931310475     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057115570550     Document Type: Article
Times cited : (11)

References (30)
  • 1
    • 84856474838 scopus 로고    scopus 로고
    • Emerging Functions of the VCP/p97 AAA-ATPase in the Ubiquitin System
    • Meyer H., Bug M., Bremer S.. Emerging Functions of the VCP/p97 AAA-ATPase in the Ubiquitin System. Nat. Cell Biol. 2012 ; 14: 117-123
    • (2012) Nat. Cell Biol , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 3
    • 84920861391 scopus 로고    scopus 로고
    • Proteotoxic Crisis, the Ubiquitin-Proteasome System, and Cancer
    • Deshaies R. J.. Proteotoxic Crisis, the Ubiquitin-Proteasome System, and Cancer. BMC Biol. 2014 ; 12: 94
    • (2014) BMC Biol , vol.12 , pp. 94
    • Deshaies, R.J.1
  • 4
    • 0037423187 scopus 로고    scopus 로고
    • ATPase Activity of p97-Valosin-Containing Protein (VCP): D2 Mediates the Major Enzyme Activity, and D1 Contributes to the Heat-Induced Activity
    • Song C., Wang Q., Li C. C. H., et al. ATPase Activity of p97-Valosin-Containing Protein (VCP): D2 Mediates the Major Enzyme Activity, and D1 Contributes to the Heat-Induced Activity. J. Biol. Chem. 2003 ; 278: 3648-3655
    • (2003) J. Biol. Chem , vol.278 , pp. 3648-3655
    • Song, C.1    Wang, Q.2    Li, C.C.H.3
  • 5
    • 46649111025 scopus 로고    scopus 로고
    • Analysis of Nucleotide Binding to P97 Reveals the Properties of a Tandem AAA Hexameric ATPase
    • Briggs L. C., Baldwin G. S., Miyata N., et al. Analysis of Nucleotide Binding to P97 Reveals the Properties of a Tandem AAA Hexameric ATPase. J. Biol. Chem. 2008 ; 283: 13745-13752
    • (2008) J. Biol. Chem , vol.283 , pp. 13745-13752
    • Briggs, L.C.1    Baldwin, G.S.2    Miyata, N.3
  • 6
    • 84904269269 scopus 로고    scopus 로고
    • Specific Inhibition of p97/VCP ATPase and Kinetic Analysis Demonstrate Interaction between D1 and D2 ATPase Domains
    • Chou T. F., Bulfer S. L., Weihl C. C., et al. Specific Inhibition of p97/VCP ATPase and Kinetic Analysis Demonstrate Interaction between D1 and D2 ATPase Domains. J. Mol. Biol. 2014 ; 28: 2886-2899
    • (2014) J. Mol. Biol , vol.28 , pp. 2886-2899
    • Chou, T.F.1    Bulfer, S.L.2    Weihl, C.C.3
  • 7
    • 84883196231 scopus 로고    scopus 로고
    • Covalent and Allosteric Inhibitors of the ATPase VCP/p97 Induce Cancer Cell Death
    • Magnaghi P., D'Alessio R., Valsasina B., et al. Covalent and Allosteric Inhibitors of the ATPase VCP/p97 Induce Cancer Cell Death. Nat. Chem. Biol. 2013 ; 9: 548-556
    • (2013) Nat. Chem. Biol , vol.9 , pp. 548-556
    • Magnaghi, P.1    D'Alessio, R.2    Valsasina, B.3
  • 8
    • 84873838455 scopus 로고    scopus 로고
    • Structure-Activity Relationship Study Reveals ML240 and ML241 as Potent and Selective Inhibitors of p97 ATPase
    • Chou T. F., Li K., Frankowski K. J., et al. Structure-Activity Relationship Study Reveals ML240 and ML241 as Potent and Selective Inhibitors of p97 ATPase. Chem. Med. Chem. 2013 ; 8: 297-312
    • (2013) Chem. Med. Chem , vol.8 , pp. 297-312
    • Chou, T.F.1    Li, K.2    Frankowski, K.J.3
  • 9
    • 79953171555 scopus 로고    scopus 로고
    • Reversible Inhibitor of p97, DBeQ, Impairs Both Ubiquitin-Dependent and Autophagic Protein Clearance Pathways
    • Chou T. F., Brown S. J., Minond D., et al. Reversible Inhibitor of p97, DBeQ, Impairs Both Ubiquitin-Dependent and Autophagic Protein Clearance Pathways. PNAS. 2011 ; 108: 4834-4839
    • (2011) PNAS , vol.108 , pp. 4834-4839
    • Chou, T.F.1    Brown, S.J.2    Minond, D.3
  • 10
    • 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: 16546-16554
    • (2011) J. Biol. Chem , vol.286 , pp. 16546-16554
    • Chou, T.F.1    Deshaies, R.J.2
  • 11
    • 84863272299 scopus 로고    scopus 로고
    • The Role of the N-Domain in the ATPase Activity of the Mammalian AAA ATPase p97/VCP
    • Niwa H., Ewens C. A., Tsang C., et al. The Role of the N-Domain in the ATPase Activity of the Mammalian AAA ATPase p97/VCP. J. Biol. Chem. 2012 ; 287: 8561-8570
    • (2012) J. Biol. Chem , vol.287 , pp. 8561-8570
    • Niwa, H.1    Ewens, C.A.2    Tsang, C.3
  • 12
    • 84870704332 scopus 로고    scopus 로고
    • ATP Binding to p97/VCP D1 Domain Regulates Selective Recruitment of Adaptors to Its Proximal N-Domain
    • Chia W. S., Chia D. X., Rao F., et al. ATP Binding to p97/VCP D1 Domain Regulates Selective Recruitment of Adaptors to Its Proximal N-Domain. PLoS ONE. 2012 ; 7: e50490
    • (2012) PLoS ONE , vol.7 , pp. 50490
    • Chia, W.S.1    Chia, D.X.2    Rao, F.3
  • 13
    • 84863230166 scopus 로고    scopus 로고
    • Interprotomer Motion-Transmission Mechanism for the Hexameric AAA ATPase p97
    • Li G., Huang C., Zhao G., et al. Interprotomer Motion-Transmission Mechanism for the Hexameric AAA ATPase p97. PNAS. 2012 ; 109: 3737-3741
    • (2012) PNAS , vol.109 , pp. 3737-3741
    • Li, G.1    Huang, C.2    Zhao, G.3
  • 14
    • 84862574175 scopus 로고    scopus 로고
    • Dynamic Flexibility of the ATPase p97 is Important for Its Interprotomer Motion Transmission
    • Huang C., Li G., Lennarz W. J.. Dynamic Flexibility of the ATPase p97 Is Important for Its Interprotomer Motion Transmission. PNAS. 2012 ; 109: 9792-9797
    • (2012) PNAS , vol.109 , pp. 9792-9797
    • Huang, C.1    Li, G.2    Lennarz, W.J.3
  • 15
    • 84872815788 scopus 로고    scopus 로고
    • Alkylsulfanyl-1,2,4-Triazoles, a New Class of Allosteric Valosine Containing Protein Inhibitors. Synthesis and Structure-Activity Relationships
    • Polucci P., Magnaghi P., Angiolini M., et al. Alkylsulfanyl-1,2,4-Triazoles, a New Class of Allosteric Valosine Containing Protein Inhibitors. Synthesis and Structure-Activity Relationships. J. Med. Chem. 2013 ; 56: 437-450
    • (2013) J. Med. Chem , vol.56 , pp. 437-450
    • Polucci, P.1    Magnaghi, P.2    Angiolini, M.3
  • 16
    • 77956308900 scopus 로고    scopus 로고
    • Binding-Site Assessment by Virtual Fragment Screening
    • Huang N., Jacobson M. P.. Binding-Site Assessment by Virtual Fragment Screening. PLoS ONE. 2012 ; 5: e10109
    • (2012) PLoS ONE , vol.5 , pp. 10109
    • Huang, N.1    Jacobson, M.P.2
  • 17
    • 79952372796 scopus 로고    scopus 로고
    • Medicinal Chemistry Inspired Fragment-Based Drug Discovery
    • Lanter J., Zhang X., Sui Z.. Medicinal Chemistry Inspired Fragment-Based Drug Discovery. Methods Enzymol. 2011 ; 493: 421-445
    • (2011) Methods Enzymol , vol.493 , pp. 421-445
    • Lanter, J.1    Zhang, X.2    Sui, Z.3
  • 18
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy
    • Mayer M., Mayer B.. Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy. Angewandte. Chemie-Int. Ed. 1999 ; 38: 1784-1788
    • (1999) Angewandte. Chemie-Int. Ed , vol.38 , pp. 1784-1788
    • Mayer, M.1    Mayer, B.2
  • 19
    • 51249121331 scopus 로고    scopus 로고
    • Perspectives on NMR in Drug Discovery: A Technique Comes of Age
    • Pellecchia M., Bertini I., Cowburn D., et al. Perspectives on NMR in Drug Discovery: A Technique Comes of Age. Nat. Rev. Drug. Discov. 2008 ; 7: 738-745
    • (2008) Nat. Rev. Drug. Discov , vol.7 , pp. 738-745
    • Pellecchia, M.1    Bertini, I.2    Cowburn, D.3
  • 20
    • 79952383501 scopus 로고    scopus 로고
    • From Experimental Design to Validated Hits a Comprehensive Walk-Through of Fragment Lead Identification Using Surface Plasmon Resonance
    • Giannetti A. M.. From Experimental Design to Validated Hits a Comprehensive Walk-Through of Fragment Lead Identification Using Surface Plasmon Resonance. Methods Enzymol. 2011 ; 493: 169-218
    • (2011) Methods Enzymol , vol.493 , pp. 169-218
    • Giannetti, A.M.1
  • 21
    • 0029912748 scopus 로고    scopus 로고
    • Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids
    • Jorgensen W. L., Maxwell D. S., Tirado-Rives J.. Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids. J. Am. Chem. Soc. 1996 ; 118: 11225-11236
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 22
    • 33750124980 scopus 로고    scopus 로고
    • Extra Precision Glide: Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein-Ligand Complexes
    • Friesner R. A., Murphy R. B., Repasky M. P., et al. Extra Precision Glide: Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein-Ligand Complexes. J. Med. Chem. 2006 ; 49: 6177-6196
    • (2006) J. Med. Chem , vol.49 , pp. 6177-6196
    • Friesner, R.A.1    Murphy, R.B.2    Repasky, M.P.3
  • 23
    • 39149130730 scopus 로고    scopus 로고
    • Surface Plasmon Resonance Based Assay for the Detection and Characterization of Promiscuous Inhibitors
    • Giannetti A. M., Koch B. D., Browner M. F.. Surface Plasmon Resonance Based Assay for the Detection and Characterization of Promiscuous Inhibitors. J. Med. Chem. 2008 ; 51: 574-580
    • (2008) J. Med. Chem , vol.51 , pp. 574-580
    • Giannetti, A.M.1    Koch, B.D.2    Browner, M.F.3
  • 24
    • 0041930989 scopus 로고    scopus 로고
    • Cross-Correlated Relaxation Enhanced 1H-13C NMR Spectroscopy of Methyl Groups in Very High Molecular Weight Proteins and Protein Complexes
    • Tugarinov V., Hwang P. M., Ollerenshaw J. E., et al. Cross-Correlated Relaxation Enhanced 1H-13C NMR Spectroscopy of Methyl Groups in Very High Molecular Weight Proteins and Protein Complexes. J. Am. Chem. Soc. 2003 ; 125: 10420-10428
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3
  • 25
    • 65249117514 scopus 로고    scopus 로고
    • Identifying and Characterizing Binding Sites and Assessing Druggability
    • Halgren T. A.. Identifying and Characterizing Binding Sites and Assessing Druggability. J. Chem. Inf. Model. 2009 ; 49: 377-389
    • (2009) J. Chem. Inf. Model , vol.49 , pp. 377-389
    • Halgren, T.A.1
  • 26
    • 84872508886 scopus 로고    scopus 로고
    • Parallel Screening of Low Molecular Weight Fragment Libraries: Do Differences in Methodology Affect Hit Identification?
    • Wielens J., Headey S. J., Rhodes D. I., et al. Parallel Screening of Low Molecular Weight Fragment Libraries: Do Differences in Methodology Affect Hit Identification?. J. Biomol. Screen. 2013 ; 18: 147-159
    • (2013) J. Biomol. Screen , vol.18 , pp. 147-159
    • Wielens, J.1    Headey, S.J.2    Rhodes, D.I.3
  • 27
    • 0033794450 scopus 로고    scopus 로고
    • New Developments in Isotope Labeling Strategies for Protein Solution NMR Spectroscopy
    • Goto N. K., Kay L. E.. New Developments in Isotope Labeling Strategies for Protein Solution NMR Spectroscopy. Curr. Opin. Struct. Biol. 2000 ; 10: 585-592
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 28
    • 37849041010 scopus 로고    scopus 로고
    • A New Labeling Method for Methyl Transverse Relaxation-Optimized Spectroscopy NMR Spectra of Alanine Residues
    • Isaacson R. L., Simpson P. J., Liu M., et al. A New Labeling Method for Methyl Transverse Relaxation-Optimized Spectroscopy NMR Spectra of Alanine Residues. J. Am. Chem. Soc. 2007 ; 129: 15428-15429
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 15428-15429
    • Isaacson, R.L.1    Simpson, P.J.2    Liu, M.3
  • 29
    • 84901044474 scopus 로고    scopus 로고
    • Inter-ring Rotations of AAA+ ATPase p97 Revealed by Electron Cryomicroscopy
    • Yeung H. O., Foerster A., Bebeacua C., et al. Inter-ring Rotations of AAA+ ATPase p97 Revealed by Electron Cryomicroscopy. Open Biol. 2014 ; 4: 130142-130142
    • (2014) Open Biol , vol.4 , pp. 130142-130142
    • Yeung, H.O.1    Foerster, A.2    Bebeacua, C.3
  • 30
    • 73349111643 scopus 로고    scopus 로고
    • Quantifying Correlations between Allosteric Sites in Thermodynamic Ensembles
    • McClendon C. L., Friedland G., Mobley D. L., et al. Quantifying Correlations between Allosteric Sites in Thermodynamic Ensembles. J. Chem. Theory Comput. 2009 ; 5: 2486-2502
    • (2009) J. Chem. Theory Comput , vol.5 , pp. 2486-2502
    • McClendon, C.L.1    Friedland, G.2    Mobley, D.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.