메뉴 건너뛰기




Volumn 18, Issue 9, 2012, Pages 1311-1316

The different ways through which specificity works in orthosteric and allosteric drugs

Author keywords

Affinity; Allosteric drug design; Allosteric drug development; Allosteric drug specificity; Allostery; Cellular network; Concentration; Dynamic landscape; Pathways

Indexed keywords

ADENOSINE TRIPHOSPHATE; CINACALCET; GLYCINE RECEPTOR; IFENPRODIL; IMATINIB; MARAVIROC; PROTEIN P53; RNA POLYMERASE II;

EID: 84857759143     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161212799436377     Document Type: Article
Times cited : (97)

References (58)
  • 1
    • 77956310878 scopus 로고    scopus 로고
    • Emerging principles in protease-based drug discovery
    • Drag M, Salvesen GS. Emerging principles in protease-based drug discovery. Nature Reviews Drug Discovery 2010; 9: 690-701.
    • (2010) Nature Reviews Drug Discovery , vol.9 , pp. 690-701
    • Drag, M.1    Salvesen, G.S.2
  • 2
    • 79953213637 scopus 로고    scopus 로고
    • Molecular Switches on mGluR Allosteric Ligands That Modulate Modes of Pharmacology
    • Wood MR, Hopkins CR, Brogan JT, Conn PJ, Lindsley CW. Molecular Switches on mGluR Allosteric Ligands That Modulate Modes of Pharmacology. Biochemistry 2011; 50: 2403-10.
    • (2011) Biochemistry , vol.50 , pp. 2403-2410
    • Wood, M.R.1    Hopkins, C.R.2    Brogan, J.T.3    Conn, P.J.4    Lindsley, C.W.5
  • 5
    • 77949407879 scopus 로고    scopus 로고
    • Ligand Detection in the Allosteric World
    • Kenakin TP. Ligand Detection in the Allosteric World. Journal of Biomolecular Screening 2010; 15: 119-30.
    • (2010) Journal of Biomolecular Screening , vol.15 , pp. 119-130
    • Kenakin, T.P.1
  • 8
    • 77958485620 scopus 로고    scopus 로고
    • Discovery of a Novel Chemical Class of mGlu(5) Allosteric Ligands with Distinct Modes of Pharmacology
    • Hammond AS, Rodriguez AL, Townsend SD, et al. Discovery of a Novel Chemical Class of mGlu(5) Allosteric Ligands with Distinct Modes of Pharmacology. Acs Chemical Neuroscience 2010; 1: 702-16.
    • (2010) Acs Chemical Neuroscience , vol.1 , pp. 702-716
    • Hammond, A.S.1    Rodriguez, A.L.2    Townsend, S.D.3
  • 9
    • 77952354490 scopus 로고    scopus 로고
    • Seven Transmembrane Receptors as Shapeshifting Proteins: The Impact of Allosteric Modulation and Functional Selectivity on New Drug Discovery
    • Kenakin T, Miller LJ. Seven Transmembrane Receptors as Shapeshifting Proteins: The Impact of Allosteric Modulation and Functional Selectivity on New Drug Discovery. Pharmacological Reviews 2010; 62: 265-304.
    • (2010) Pharmacological Reviews , vol.62 , pp. 265-304
    • Kenakin, T.1    Miller, L.J.2
  • 10
    • 69649097791 scopus 로고    scopus 로고
    • '7TM Receptor Allostery: Putting Numbers to Shapeshifting Proteins
    • Kenakin TP. '7TM Receptor Allostery: Putting Numbers to Shapeshifting Proteins. Trends in Pharmacological Sciences 2009; 30: 460-9.
    • (2009) Trends In Pharmacological Sciences , vol.30 , pp. 460-469
    • Kenakin, T.P.1
  • 11
    • 58149193205 scopus 로고    scopus 로고
    • Allosteric modulators of GPCRs: A novel approach for the treatment of CNS disorders
    • Conn PJ, Christopoulos A, Lindsley CW. Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders. Nature Reviews Drug Discovery 2009; 8: 41-54.
    • (2009) Nature Reviews Drug Discovery , vol.8 , pp. 41-54
    • Conn, P.J.1    Christopoulos, A.2    Lindsley, C.W.3
  • 12
  • 15
    • 77953091045 scopus 로고    scopus 로고
    • Structure of the Human mTOR Complex I and Its Implications for Rapamycin Inhibition
    • Yip CK, Murata K, Walz T, Sabatini DM, Kang SA. Structure of the Human mTOR Complex I and Its Implications for Rapamycin Inhibition. Molecular Cell 2010; 38: 768-74.
    • (2010) Molecular Cell , vol.38 , pp. 768-774
    • Yip, C.K.1    Murata, K.2    Walz, T.3    Sabatini, D.M.4    Kang, S.A.5
  • 16
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai CJ, Kumar S, Ma BY, Nussinov R. Folding funnels, binding funnels, and protein function. Protein Science 1999; 8: 1181-90.
    • (1999) Protein Science , vol.8 , pp. 1181-1190
    • Tsai, C.J.1    Kumar, S.2    Ma, B.Y.3    Nussinov, R.4
  • 19
    • 0033970020 scopus 로고    scopus 로고
    • Folding and binding cascades: Dynamic landscapes and population shifts
    • Kumar S, Ma BY, Tsai CJ, Sinha N, Nussinov R. Folding and binding cascades: Dynamic landscapes and population shifts. Protein Science 2000; 9: 10-9.
    • (2000) Protein Science , vol.9 , pp. 10-19
    • Kumar, S.1    Ma, B.Y.2    Tsai, C.J.3    Sinha, N.4    Nussinov, R.5
  • 20
    • 60649109828 scopus 로고    scopus 로고
    • Protein allostery, signal transmission and dynamics: A classification scheme of allosteric mechanisms
    • Tsai CJ, Del Sol A, Nussinov R. Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms. Molecular Biosystems 2009; 5: 207-16.
    • (2009) Molecular Biosystems , vol.5 , pp. 207-216
    • Tsai, C.J.1    Del Sol, A.2    Nussinov, R.3
  • 21
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr DD, Nussinov R, Wright PE. The role of dynamic conformational ensembles in biomolecular recognition. Nature Chemical Biology 2009; 5: 789-96.
    • (2009) Nature Chemical Biology , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 22
    • 0032993447 scopus 로고    scopus 로고
    • Polymer principles and protein folding
    • Dill KA. Polymer principles and protein folding. Protein Science 1999; 8: 1166-80.
    • (1999) Protein Science , vol.8 , pp. 1166-1180
    • Dill, K.A.1
  • 23
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar SG, Wolynes PG. The energy landscapes and motions of proteins. Science 1991; 254: 1598-603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 24
    • 68149157248 scopus 로고    scopus 로고
    • The Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways
    • Del Sol A, Tsai CJ, Ma BY, Nussinov R. The Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways. Structure 2009; 17: 1042-50.
    • (2009) Structure , vol.17 , pp. 1042-1050
    • Del Sol, A.1    Tsai, C.J.2    Ma, B.Y.3    Nussinov, R.4
  • 25
    • 77954749964 scopus 로고    scopus 로고
    • Pathophysiological Mechanisms of Dominant and Recessive GLRA1 Mutations in Hyperekplexia
    • Chung SK, Vanbellinghen JF, et al. Pathophysiological Mechanisms of Dominant and Recessive GLRA1 Mutations in Hyperekplexia. Journal of Neuroscience 2010; 30: 9612-20.
    • (2010) Journal of Neuroscience , vol.30 , pp. 9612-9620
    • Chung, S.K.1    Vanbellinghen, J.F.2
  • 26
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • Hibbs RE, Gouaux E. Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature 2011; 474: 54-U80.
    • (2011) Nature , vol.474
    • Hibbs, R.E.1    Gouaux, E.2
  • 27
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf RJC, Dutzler R. Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 2009; 457: 115-22.
    • (2009) Nature , vol.457 , pp. 115-122
    • Hilf, R.J.C.1    Dutzler, R.2
  • 28
    • 37249027595 scopus 로고    scopus 로고
    • Conformational variability of the glycine receptor M2 domain in response to activation by different agonists
    • Pless SA, Dibas MI, Lester HA, Lynch JW. Conformational variability of the glycine receptor M2 domain in response to activation by different agonists. Journal of Biological Chemistry 2007; 282: 36057-67.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 36057-36067
    • Pless, S.A.1    Dibas, M.I.2    Lester, H.A.3    Lynch, J.W.4
  • 29
    • 38049148291 scopus 로고    scopus 로고
    • Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel
    • Sadovsky E, Yifrach O. Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel. Proceedings of the National Academy of Sciences of the United States of America 2007; 104: 19813-8.
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , pp. 19813-19818
    • Sadovsky, E.1    Yifrach, O.2
  • 30
    • 77957245574 scopus 로고    scopus 로고
    • Probing the Transition State of the Allosteric Pathway of the Shaker Kv Channel Pore by Linear Free-Energy Relations
    • Azaria R, Irit O, Ben-Abu Y, Yifrach O. Probing the Transition State of the Allosteric Pathway of the Shaker Kv Channel Pore by Linear Free-Energy Relations. Journal of Molecular Biology 2010; 403: 167-73.
    • (2010) Journal of Molecular Biology , vol.403 , pp. 167-173
    • Azaria, R.1    Irit, O.2    Ben-Abu, Y.3    Yifrach, O.4
  • 32
    • 76149132685 scopus 로고    scopus 로고
    • Generic binding sites, generic DNA-binding domains: Where does specific promoter recognition come from?
    • Georges AB, Benayoun BA, Caburet S, Veitia RA. Generic binding sites, generic DNA-binding domains: where does specific promoter recognition come from? FASEB Journal 2010; 24: 346-56.
    • (2010) FASEB Journal , vol.24 , pp. 346-356
    • Georges, A.B.1    Benayoun, B.A.2    Caburet, S.3    Veitia, R.A.4
  • 35
    • 0037039776 scopus 로고    scopus 로고
    • Structure, function, and activator-induced conformations of the CRSP coactivator
    • Taatjes DJ, Naar AM, Andel F, Nogales E, Tjian R. Structure, function, and activator-induced conformations of the CRSP coactivator. Science 2002; 295: 1058-62.
    • (2002) Science , vol.295 , pp. 1058-1062
    • Taatjes, D.J.1    Naar, A.M.2    Andel, F.3    Nogales, E.4    Tjian, R.5
  • 36
    • 1842839787 scopus 로고    scopus 로고
    • RNA polymerase II structure, and organization of the preinitiation complex
    • Asturias FJ. RNA polymerase II structure, and organization of the preinitiation complex. Current Opinion in Structural Biology 2004; 14: 121-9.
    • (2004) Current Opinion In Structural Biology , vol.14 , pp. 121-129
    • Asturias, F.J.1
  • 37
    • 0036671095 scopus 로고    scopus 로고
    • Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction
    • Davis JA, Takagi Y, Kornberg RD, Asturias FJ. Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction. Molecular Cell 2002; 10: 409-15.
    • (2002) Molecular Cell , vol.10 , pp. 409-415
    • Davis, J.A.1    Takagi, Y.2    Kornberg, R.D.3    Asturias, F.J.4
  • 38
    • 0033821977 scopus 로고    scopus 로고
    • A transactivation-deficient mouse model provides insights into Trp53 regulation and function
    • Jimenez GS, Nister M, Stommel JM, et al. A transactivation-deficient mouse model provides insights into Trp53 regulation and function. Nature Genetics 2000; 26: 37-43.
    • (2000) Nature Genetics , vol.26 , pp. 37-43
    • Jimenez, G.S.1    Nister, M.2    Stommel, J.M.3
  • 39
    • 0028303752 scopus 로고
    • Several hydrophobic amino-acids in the P53 amino-terminal domain are required for transcriptional activation, binding to MDM-2 and the adenovirus-5 E1B 55-KD protein
    • Lin JY, Chen JD, Elenbaas B, Levine AJ. Several hydrophobic amino-acids in the P53 amino-terminal domain are required for transcriptional activation, binding to MDM-2 and the adenovirus-5 E1B 55-KD protein. Genes & Development 1994; 8: 1235-46.
    • (1994) Genes & Development , vol.8 , pp. 1235-1246
    • Lin, J.Y.1    Chen, J.D.2    Elenbaas, B.3    Levine, A.J.4
  • 40
    • 34547817154 scopus 로고    scopus 로고
    • A new paradigm for protein kinase inhibition: Blocking phosphorylation without directly targeting ATP binding
    • Bogoyevitch MA, Fairlie DP. A new paradigm for protein kinase inhibition: blocking phosphorylation without directly targeting ATP binding. Drug Discovery Today 2007; 12: 622-33.
    • (2007) Drug Discovery Today , vol.12 , pp. 622-633
    • Bogoyevitch, M.A.1    Fairlie, D.P.2
  • 43
    • 44949181722 scopus 로고    scopus 로고
    • Allosteric modulation of kinases and GPCRs: Design principles and structural diversity
    • Lewis JA, Lebois EP, Lindsley CW. Allosteric modulation of kinases and GPCRs: design principles and structural diversity. Current Opinion in Chemical Biology 2008; 12: 269-80.
    • (2008) Current Opinion In Chemical Biology , vol.12 , pp. 269-280
    • Lewis, J.A.1    Lebois, E.P.2    Lindsley, C.W.3
  • 45
    • 74049158987 scopus 로고    scopus 로고
    • Design of phosphodiesterase 4D (PDE4D) allosteric modulators for enhancing cognition with improved safety
    • Burgin AB, Magnusson OT, Singh J, et al. Design of phosphodiesterase 4D (PDE4D) allosteric modulators for enhancing cognition with improved safety. Nature Biotechnology 2010; 28: 63-U93.
    • (2010) Nature Biotechnology , vol.28
    • Burgin, A.B.1    Magnusson, O.T.2    Singh, J.3
  • 46
    • 79960417429 scopus 로고    scopus 로고
    • Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors
    • Karakas E, Simorowski N, Furukawa H. Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors. Nature 2011; 475: 249-U170.
    • (2011) Nature , vol.475
    • Karakas, E.1    Simorowski, N.2    Furukawa, H.3
  • 47
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic Allostery: Linkers Are Not Merely Flexible
    • Ma B, Tsai C-J, Haliloglu T, Nussinov R. Dynamic Allostery: Linkers Are Not Merely Flexible. Structure 2011; 19: 907-17.
    • (2011) Structure , vol.19 , pp. 907-917
    • Ma, B.1    Tsai, C.-J.2    Haliloglu, T.3    Nussinov, R.4
  • 48
    • 33847612920 scopus 로고    scopus 로고
    • Thiazolone-acylsulfonamides as novel HCV NS5B polymerase allosteric inhibitors: Convergence of structure-based drug design and X-ray crystallographic study
    • Yan S, Appleby T, Larson G, et al. Thiazolone-acylsulfonamides as novel HCV NS5B polymerase allosteric inhibitors: Convergence of structure-based drug design and X-ray crystallographic study. Bioorganic & Medicinal Chemistry Letters 2007; 17: 1991-5.
    • (2007) Bioorganic & Medicinal Chemistry Letters , vol.17 , pp. 1991-1995
    • Yan, S.1    Appleby, T.2    Larson, G.3
  • 49
    • 67650473173 scopus 로고    scopus 로고
    • The Positive Allosteric Modulator Morantel Binds at Noncanonical Subunit Interfaces of Neuronal Nicotinic Acetylcholine Receptors
    • Seo S, Henry JT, Lewis AH, Wang N, Levandoski MM. The Positive Allosteric Modulator Morantel Binds at Noncanonical Subunit Interfaces of Neuronal Nicotinic Acetylcholine Receptors. J Neuroscience 2009; 29: 8734-42.
    • (2009) J Neuroscience , vol.29 , pp. 8734-8742
    • Seo, S.1    Henry, J.T.2    Lewis, A.H.3    Wang, N.4    Levandoski, M.M.5
  • 50
    • 47949088448 scopus 로고    scopus 로고
    • Morantel allosterically enhances channel gating of neuronal nicotinic acetylcholine alpha 3 beta 2 receptors
    • Wu TY, Smith CM, Sine SM, Levandoski MM. Morantel allosterically enhances channel gating of neuronal nicotinic acetylcholine alpha 3 beta 2 receptors. Molecular Pharmacology 2008; 74: 466-75.
    • (2008) Molecular Pharmacology , vol.74 , pp. 466-475
    • Wu, T.Y.1    Smith, C.M.2    Sine, S.M.3    Levandoski, M.M.4
  • 51
    • 18344395134 scopus 로고    scopus 로고
    • Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
    • Pargellis C, Tong L, Churchill L, et al. Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Nature Structural Biology 2002; 9: 268-72.
    • (2002) Nature Structural Biology , vol.9 , pp. 268-272
    • Pargellis, C.1    Tong, L.2    Churchill, L.3
  • 52
    • 33645360875 scopus 로고    scopus 로고
    • Keynote review: Allosterism in membrane receptors
    • Gao ZG, Jacobson KA. Keynote review: Allosterism in membrane receptors. Drug Discovery Today 2006; 11: 191-202.
    • (2006) Drug Discovery Today , vol.11 , pp. 191-202
    • Gao, Z.G.1    Jacobson, K.A.2
  • 53
    • 38949190032 scopus 로고    scopus 로고
    • Allosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design
    • Liu J, Nussinov R. Allosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design. Proceedings of the National Academy of Sciences of the United States of America 2008; 105: 901-6.
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , pp. 901-906
    • Liu, J.1    Nussinov, R.2
  • 54
    • 33845524054 scopus 로고    scopus 로고
    • Assay principle for modulators of protein-protein interactions and its application to non-ATP-competitiveligands targeting protein kinase A
    • Saldanha SA, Kaler G, Cottam HB, Abagyan R, Taylor SS. Assay principle for modulators of protein-protein interactions and its application to non-ATP-competitiveligands targeting protein kinase A. Analytical Chemistry 2006; 78: 8265-72.
    • (2006) Analytical Chemistry , vol.78 , pp. 8265-8272
    • Saldanha, S.A.1    Kaler, G.2    Cottam, H.B.3    Abagyan, R.4    Taylor, S.S.5
  • 55
    • 79251503920 scopus 로고    scopus 로고
    • Small Molecule Probes of Cellular Pathways and Networks
    • Castoreno AB, Eggert US. Small Molecule Probes of Cellular Pathways and Networks. Acs Chemical Biology 2011; 6: 86-94.
    • (2011) Acs Chemical Biology , vol.6 , pp. 86-94
    • Castoreno, A.B.1    Eggert, U.S.2
  • 58
    • 84858171456 scopus 로고    scopus 로고
    • Allosteric modulators can restore function in an amino acid neurotransmitter receptor by slightly altering intra-molecular communication pathways
    • doi: 10.1111/j.1476-5381.2011.01793.x. PMID: 22122331
    • [R. Allosteric modulators can restore function in an amino acid neurotransmitter receptor by slightly altering intra-molecular communication pathways. Br J Pharmacol 2012; doi: 10.1111/j.1476-5381.2011.01793.x. PMID: 22122331.
    • (2012) Br J Pharmacol


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.