메뉴 건너뛰기




Volumn 10, Issue 2, 2013, Pages

The concept of allosteric modulation: An overview

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; 4 AMINOBUTYRIC ACID A RECEPTOR; 6 PHOSPHOFRUCTOKINASE; BENZODIAZEPINE DERIVATIVE; CADMIUM; CHLORPROMAZINE; GLYCINE RECEPTOR; HEMOGLOBIN; LIDOCAINE; LIGAND GATED ION CHANNEL; NEUROTRANSMITTER RECEPTOR; NICOTINIC AGENT; NICOTINIC RECEPTOR; PICROTOXIN; TETRABUTYLAMMONIUM; TETRYLAMMONIUM; TRANSITION ELEMENT; ZINC;

EID: 84879882962     PISSN: None     EISSN: 17406749     Source Type: Journal    
DOI: 10.1016/j.ddtec.2012.07.007     Document Type: Review
Times cited : (65)

References (65)
  • 1
    • 0242603739 scopus 로고
    • Experiments with the chemostat on the rates of amino acid synthesis in bacteria
    • Princeton University Press pp. 21-32
    • A. Novick, and L. Szilard Experiments with the chemostat on the rates of amino acid synthesis in bacteria Dynamics of Growth Processes 1954 Princeton University Press pp. 21-32
    • (1954) Dynamics of Growth Processes
    • Novick, A.1    Szilard, L.2
  • 2
    • 0000832972 scopus 로고
    • Evidence for a negative-feedback mechanism in the biosynthesis of isoleucine
    • H.E. Umbarger Evidence for a negative-feedback mechanism in the biosynthesis of isoleucine Science 123 1956 848
    • (1956) Science , vol.123 , pp. 848
    • Umbarger, H.E.1
  • 3
    • 0001738507 scopus 로고
    • Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism
    • R.A. Yates, and A.B. Pardee Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism J. Biol. Chem. 221 1956 757 770
    • (1956) J. Biol. Chem. , vol.221 , pp. 757-770
    • Yates, R.A.1    Pardee, A.B.2
  • 4
    • 73049119821 scopus 로고
    • The feedback control mechanism of biosynthetic l-threonine deaminase by l-isoleucine
    • J-P. Changeux The feedback control mechanism of biosynthetic l-threonine deaminase by l-isoleucine Cold Spring Harb. Symp. Quant. Biol. 26 1961 313 318
    • (1961) Cold Spring Harb. Symp. Quant. Biol. , vol.26 , pp. 313-318
    • Changeux, J.-P.1
  • 5
    • 73049167504 scopus 로고
    • Teleonomic mechanisms in cellular metabolism, growth, and differentiation
    • J. Monod, and F. Jacob Teleonomic mechanisms in cellular metabolism, growth, and differentiation Cold Spring Harb. Symp. Quant. Biol. 26 1961 389 401
    • (1961) Cold Spring Harb. Symp. Quant. Biol. , vol.26 , pp. 389-401
    • Monod, J.1    Jacob, F.2
  • 6
    • 0042882982 scopus 로고
    • Enzyme flexibility and enzyme action
    • D.E. Koshland Jr. Enzyme flexibility and enzyme action J. Cell. Comp. Physiol. 54 1959 245 258
    • (1959) J. Cell. Comp. Physiol. , vol.54 , pp. 245-258
    • Koshland, Jr.D.E.1
  • 7
    • 73649152457 scopus 로고
    • Allosteric proteins and cellular control systems
    • J. Monod Allosteric proteins and cellular control systems J. Mol. Biol. 6 1963 306 329
    • (1963) J. Mol. Biol. , vol.6 , pp. 306-329
    • Monod, J.1
  • 8
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • J. Monod On the nature of allosteric transitions: a plausible model J. Mol. Biol. 12 1965 88 118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1
  • 9
    • 84861219631 scopus 로고    scopus 로고
    • Allostery and the Monod-Wyman-Changeux model after 50 years
    • J-P. Changeux Allostery and the Monod-Wyman-Changeux model after 50 years Ann. Rev. Biophys. 41 2012 103 133
    • (2012) Ann. Rev. Biophys. , vol.41 , pp. 103-133
    • Changeux, J.-P.1
  • 10
    • 69949159308 scopus 로고    scopus 로고
    • Nicotinic receptors: Allosteric transitions and therapeutic targets in the nervous system
    • A. Taly Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system Nat. Rev. Drug Discov. 8 2009 733 750
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 733-750
    • Taly, A.1
  • 11
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • M.F. Perutz Mechanisms of cooperativity and allosteric regulation in proteins Q. Rev. Biophys. 22 1989 139 237
    • (1989) Q. Rev. Biophys. , vol.22 , pp. 139-237
    • Perutz, M.F.1
  • 12
    • 0014531939 scopus 로고
    • The oxygenation of hemoglobin in the presence of 2,3-iphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration
    • R.E. Benesh The oxygenation of hemoglobin in the presence of 2,3-iphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration Biochemistry 8 1969 2567 2571
    • (1969) Biochemistry , vol.8 , pp. 2567-2571
    • Benesh, R.E.1
  • 13
    • 60549097684 scopus 로고    scopus 로고
    • Enhanced exercise capacity in mice with severe heart failure treated with an allosteric effector of hemoglobin, myo-inositol trispyrophosphate
    • A. Biolo Enhanced exercise capacity in mice with severe heart failure treated with an allosteric effector of hemoglobin, myo-inositol trispyrophosphate Proc. Natl. Acad. Sci. U. S. A. 1106 2009 1926 1929
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.1106 , pp. 1926-1929
    • Biolo, A.1
  • 14
    • 79960663414 scopus 로고    scopus 로고
    • Polyphosphates and pyrophosphates of pentopyranoses and pentofuranoses as allosteric effectors of human hemoglobin: Synthesis, molecular recognition, and oxygen release
    • K.C. Fylaktakidou Polyphosphates and pyrophosphates of pentopyranoses and pentofuranoses as allosteric effectors of human hemoglobin: synthesis, molecular recognition, and oxygen release Chem. Med. Chem. 6 2011 1495 1508
    • (2011) Chem. Med. Chem. , vol.6 , pp. 1495-1508
    • Fylaktakidou, K.C.1
  • 15
    • 0014877189 scopus 로고
    • Use of a snake venom toxin to characterize the cholinergic receptor protein
    • J.P. Changeux Use of a snake venom toxin to characterize the cholinergic receptor protein Proc. Natl. Acad. Sci. U. S. A. 67 1970 1241 1247
    • (1970) Proc. Natl. Acad. Sci. U. S. A. , vol.67 , pp. 1241-1247
    • Changeux, J.P.1
  • 17
    • 77949534717 scopus 로고    scopus 로고
    • Allosteric receptors: From electric organ to cognition
    • J.P. Changeux Allosteric receptors: from electric organ to cognition Annu. Rev. Pharmacol. Toxicol. 50 2010 1 38
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 1-38
    • Changeux, J.P.1
  • 18
    • 33846106078 scopus 로고    scopus 로고
    • A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family
    • N. Bocquet A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family Nature 445 2007 116 119
    • (2007) Nature , vol.445 , pp. 116-119
    • Bocquet, N.1
  • 19
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • N. Bocquet X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation Nature 457 2009 111 114
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1
  • 20
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • R. Hilf, and R. Dutzler X-ray structure of a prokaryotic pentameric ligand-gated ion channel Nature 452 2008 375 379
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.1    Dutzler, R.2
  • 21
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • R. Hilf, and R. Dutzler Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel Nature 457 2009 115 118
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.1    Dutzler, R.2
  • 22
    • 79959775185 scopus 로고    scopus 로고
    • Ligand activation of the prokaryotic pentameric ligand-gated ion channel ELIC
    • I. Zimmermann, and R. Dutzler Ligand activation of the prokaryotic pentameric ligand-gated ion channel ELIC PLoS Biol. 9 2011 e1001101
    • (2011) PLoS Biol. , vol.9 , pp. 1001101
    • Zimmermann, I.1    Dutzler, R.2
  • 23
    • 84859173541 scopus 로고    scopus 로고
    • Structure of the pentameric ligand-gated ion channel ELIC cocrystallized with its competitive antagonist acetylcholine
    • MARCH 10.1038/ncomms1703
    • J. Pan Structure of the pentameric ligand-gated ion channel ELIC cocrystallized with its competitive antagonist acetylcholine Nat. Commun. 3 March 2012 714 10.1038/ncomms1703
    • (2012) Nat. Commun. , vol.3 , pp. 714
    • Pan, J.1
  • 24
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • R. Hibbs, and E. Gouaux Principles of activation and permeation in an anion-selective Cys-loop receptor Nature 474 2011 54 60
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.1    Gouaux, E.2
  • 25
    • 22244438519 scopus 로고    scopus 로고
    • Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism
    • A. Taly Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism Biophys. J. 88 2005 3954 3965
    • (2005) Biophys. J. , vol.88 , pp. 3954-3965
    • Taly, A.1
  • 26
    • 84861963413 scopus 로고    scopus 로고
    • Structure and pharmacology of pentameric receptor-channels: From bacteria to brain
    • P.J. Corringer Structure and pharmacology of pentameric receptor-channels: from bacteria to brain Structure 20 2012 941 956
    • (2012) Structure , vol.20 , pp. 941-956
    • Corringer, P.J.1
  • 27
    • 0026716690 scopus 로고
    • Potentiation of nicotinic receptor response by external calcium in rat central neurons
    • C. Mulle Potentiation of nicotinic receptor response by external calcium in rat central neurons Neuron 8 1992 937 945
    • (1992) Neuron , vol.8 , pp. 937-945
    • Mulle, C.1
  • 28
    • 0026586188 scopus 로고
    • Calcium modulation and high calcium permeability of neuronal nicotinic acetylcholine receptors
    • S. Vernino Calcium modulation and high calcium permeability of neuronal nicotinic acetylcholine receptors Neuron 8 1992 127 134
    • (1992) Neuron , vol.8 , pp. 127-134
    • Vernino, S.1
  • 29
    • 0036891522 scopus 로고    scopus 로고
    • The diversity of subunit composition in nAChRs: Evolutionary origins, physiologic and pharmacologic consequences
    • N. Le Novère The diversity of subunit composition in nAChRs: evolutionary origins, physiologic and pharmacologic consequences J. Neurobiol. 53 2002 447 456
    • (2002) J. Neurobiol. , vol.53 , pp. 447-456
    • Le Novère, N.1
  • 30
    • 30044440798 scopus 로고    scopus 로고
    • Determinants of zinc potentiation on the alpha4 subunit of neuronal nicotinic receptors
    • B. Hsiao Determinants of zinc potentiation on the alpha4 subunit of neuronal nicotinic receptors Mol. Pharmacol. 69 2006 27 36
    • (2006) Mol. Pharmacol. , vol.69 , pp. 27-36
    • Hsiao, B.1
  • 31
    • 0028031541 scopus 로고
    • Neurotransmitter-gated ion channels as unconventional allosteric proteins
    • J.L. Galzi, and J.P. Changeux Neurotransmitter-gated ion channels as unconventional allosteric proteins Curr. Opin. Struct. Biol. 4 1994 554 565
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 554-565
    • Galzi, J.L.1    Changeux, J.P.2
  • 32
    • 0028988637 scopus 로고
    • Functional domains of GABAA receptors
    • G.B. Smith, and R.W. Olsen Functional domains of GABAA receptors Trends Pharmacol. Sci. 16 1995 162 168
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 162-168
    • Smith, G.B.1    Olsen, R.W.2
  • 33
    • 0030693304 scopus 로고    scopus 로고
    • The benzodiazepine binding site of GABAA receptors
    • E. Sigel, and A. Buhr The benzodiazepine binding site of GABAA receptors Trends Pharmacol. Sci. 18 1997 425 429
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 425-429
    • Sigel, E.1    Buhr, A.2
  • 34
    • 20344392658 scopus 로고    scopus 로고
    • The benzodiazepine binding site of GABA(A) receptors as a target for the development of novel anxiolytics
    • J.R. Atack The benzodiazepine binding site of GABA(A) receptors as a target for the development of novel anxiolytics Expert Opin. Investig. Drugs 14 2005 601 618
    • (2005) Expert Opin. Investig. Drugs , vol.14 , pp. 601-618
    • Atack, J.R.1
  • 35
    • 0022634647 scopus 로고
    • Hemoglobin as a receptor of drugs and peptides. X-ray studies of the stereochemistry of binding
    • M.F. Perutz Hemoglobin as a receptor of drugs and peptides. X-ray studies of the stereochemistry of binding J. Am. Chem. Soc. 108 1986 1064 1078
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 1064-1078
    • Perutz, M.F.1
  • 36
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • S.B. Hansen Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations EMBO J. 24 2005 3635 3646
    • (2005) EMBO J. , vol.24 , pp. 3635-3646
    • Hansen, S.B.1
  • 37
    • 0019795816 scopus 로고
    • Ultraviolet light-induced labeling by noncompetitive blockers of the acetylcholine receptor from Torpedo marmorata
    • R. Oswald, and J.P. Changeux Ultraviolet light-induced labeling by noncompetitive blockers of the acetylcholine receptor from Torpedo marmorata Proc. Natl. Acad. Sci. U. S. A. 78 1981 3925 3929
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 3925-3929
    • Oswald, R.1    Changeux, J.P.2
  • 38
    • 0345363642 scopus 로고
    • Time-resolved photolabeling by the noncompetitive blocker chlorpromazine of the acetylcholine receptor in its transiently open and closed ion channel conformations
    • T. Heidmann, and J.P. Changeux Time-resolved photolabeling by the noncompetitive blocker chlorpromazine of the acetylcholine receptor in its transiently open and closed ion channel conformations Proc. Natl. Acad. Sci. U. S. A. 81 1984 1897 1901
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 1897-1901
    • Heidmann, T.1    Changeux, J.P.2
  • 39
    • 78549271990 scopus 로고    scopus 로고
    • Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel
    • R. Hilf Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel Nat. Struct. Mol. Biol. 17 2010 1330 1336
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1330-1336
    • Hilf, R.1
  • 40
    • 0031887759 scopus 로고    scopus 로고
    • Ivermectin: A positive allosteric effector of the alpha7 neuronal nicotinic acetylcholine receptor
    • R.M. Krause Ivermectin: a positive allosteric effector of the alpha7 neuronal nicotinic acetylcholine receptor Mol. Pharmacol. 53 1998 283 294
    • (1998) Mol. Pharmacol. , vol.53 , pp. 283-294
    • Krause, R.M.1
  • 41
    • 20944441082 scopus 로고    scopus 로고
    • A novel positive allosteric modulator of the alpha7 neuronal nicotinic acetylcholine receptor: In vitro and in vivo characterization
    • R.S. Hurst A novel positive allosteric modulator of the alpha7 neuronal nicotinic acetylcholine receptor: in vitro and in vivo characterization J. Neurosci. 25 2005 4396 4405
    • (2005) J. Neurosci. , vol.25 , pp. 4396-4405
    • Hurst, R.S.1
  • 42
    • 80052026910 scopus 로고    scopus 로고
    • Positive allosteric modulators as an approach to nicotinic acetylcholine receptor-targeted therapeutics: Advantages and limitations
    • D.K. Williams Positive allosteric modulators as an approach to nicotinic acetylcholine receptor-targeted therapeutics: advantages and limitations Biochem. Pharmacol. 82 2011 915 930
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 915-930
    • Williams, D.K.1
  • 43
    • 84863073472 scopus 로고    scopus 로고
    • 3H]TDBzl-etomidate, a photoreactive etomidate analogue
    • 3H]TDBzl- etomidate, a photoreactive etomidate analogue Biochemistry 51 2012 836 847
    • (2012) Biochemistry , vol.51 , pp. 836-847
    • Chiara, D.C.1
  • 44
    • 78751673139 scopus 로고    scopus 로고
    • X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel
    • H. Nury X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel Nature 469 2011 428 431
    • (2011) Nature , vol.469 , pp. 428-431
    • Nury, H.1
  • 45
    • 79959652664 scopus 로고    scopus 로고
    • Microsecond simulations indicate that ethanol binds between subunits and could stabilize an open-state model of a glycine receptor
    • S. Murail Microsecond simulations indicate that ethanol binds between subunits and could stabilize an open-state model of a glycine receptor Biophys. J. 100 2011 1642 1650
    • (2011) Biophys. J. , vol.100 , pp. 1642-1650
    • Murail, S.1
  • 46
    • 79961074761 scopus 로고    scopus 로고
    • Structural basis for alcohol modulation of a pentameric ligand-gated ion channel
    • R. Howard Structural basis for alcohol modulation of a pentameric ligand-gated ion channel Proc. Natl. Acad. Sci. U. S. A. 108 2011 12149 12154
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 12149-12154
    • Howard, R.1
  • 47
    • 80053244433 scopus 로고    scopus 로고
    • Single-channel and structural foundations of neuronal α7 acetylcholine receptor potentiation
    • C.J. daCosta Single-channel and structural foundations of neuronal α7 acetylcholine receptor potentiation J. Neurosci. 31 2011 13870 13879
    • (2011) J. Neurosci. , vol.31 , pp. 13870-13879
    • Dacosta, C.J.1
  • 48
    • 84859949261 scopus 로고    scopus 로고
    • A series of α7 nicotinic acetylcholine receptor allosteric modulators with close chemical similarity but diverse pharmacological properties
    • J.K. Gill A series of α7 nicotinic acetylcholine receptor allosteric modulators with close chemical similarity but diverse pharmacological properties Mol. Pharmacol. 81 2012 710 718
    • (2012) Mol. Pharmacol. , vol.81 , pp. 710-718
    • Gill, J.K.1
  • 49
    • 79951721809 scopus 로고    scopus 로고
    • GABA(A) receptors as molecular targets of general anesthetics: Identification of binding sites provides clues to allosteric modulation
    • R.W. Olsen, and G.D. Li GABA(A) receptors as molecular targets of general anesthetics: identification of binding sites provides clues to allosteric modulation Can. J. Anaesth. 58 2011 206 215
    • (2011) Can. J. Anaesth. , vol.58 , pp. 206-215
    • Olsen, R.W.1    Li, G.D.2
  • 50
    • 79951722762 scopus 로고    scopus 로고
    • Anesthetic sites and allosteric mechanisms of action on Cys-loop ligand-gated ion channels
    • S.A. Forman, and K.W. Miller Anesthetic sites and allosteric mechanisms of action on Cys-loop ligand-gated ion channels Can. J. Anaesth. 58 2011 191 205
    • (2011) Can. J. Anaesth. , vol.58 , pp. 191-205
    • Forman, S.A.1    Miller, K.W.2
  • 51
    • 0017368198 scopus 로고
    • In vitro phosphorylation of the acetylcholine receptor
    • V.I. Teichberg In vitro phosphorylation of the acetylcholine receptor Nature 267 1977 540 542
    • (1977) Nature , vol.267 , pp. 540-542
    • Teichberg, V.I.1
  • 52
    • 0022501502 scopus 로고
    • Phosphorylation of the nicotinic acetylcholine receptor regulates its rate of desensitization
    • R.L. Huganir Phosphorylation of the nicotinic acetylcholine receptor regulates its rate of desensitization Nature 321 1986 774 776
    • (1986) Nature , vol.321 , pp. 774-776
    • Huganir, R.L.1
  • 53
    • 79957825777 scopus 로고    scopus 로고
    • Adenosine A2A receptor induces protein kinase A-dependent functional modulation of human (alpha)3(beta)4 nicotinic receptor
    • S. Di Angelantonio Adenosine A2A receptor induces protein kinase A-dependent functional modulation of human (alpha)3(beta)4 nicotinic receptor J. Physiol. 589 Pt 11 2011 2755 2766
    • (2011) J. Physiol. , vol.589 , Issue.PART 11 , pp. 2755-2766
    • Di Angelantonio, S.1
  • 54
    • 43849113999 scopus 로고    scopus 로고
    • Rapsyn carboxyl terminal domains mediate muscle specific kinase-induced phosphorylation of the muscle acetylcholine receptor
    • Y. Lee Rapsyn carboxyl terminal domains mediate muscle specific kinase-induced phosphorylation of the muscle acetylcholine receptor Neuroscience 153 2008 997 1007
    • (2008) Neuroscience , vol.153 , pp. 997-1007
    • Lee, Y.1
  • 55
    • 0017708049 scopus 로고
    • Large-scale purification of the acetylcholine-receptor protein in its membrane-bound and detergent-extracted forms from Torpedo marmorata electric organ
    • A. Sobel Large-scale purification of the acetylcholine-receptor protein in its membrane-bound and detergent-extracted forms from Torpedo marmorata electric organ Eur. J. Biochem. 80 1977 215 224
    • (1977) Eur. J. Biochem. , vol.80 , pp. 215-224
    • Sobel, A.1
  • 56
    • 0023643406 scopus 로고
    • The 43-kilodalton protein of Torpedo nicotinic postsynaptic membranes: Purification and determination of primary structure
    • C. Carr The 43-kilodalton protein of Torpedo nicotinic postsynaptic membranes: purification and determination of primary structure Biochemistry 26 1987 7090 7102
    • (1987) Biochemistry , vol.26 , pp. 7090-7102
    • Carr, C.1
  • 57
    • 60149093772 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase A and protein kinase C phosphorylate alpha4beta2 nicotinic receptor subunits at distinct stages of receptor formation and maturation
    • V.V. Pollock Cyclic AMP-dependent protein kinase A and protein kinase C phosphorylate alpha4beta2 nicotinic receptor subunits at distinct stages of receptor formation and maturation Neuroscience 158 2009 1311 1325
    • (2009) Neuroscience , vol.158 , pp. 1311-1325
    • Pollock, V.V.1
  • 58
    • 77957865465 scopus 로고    scopus 로고
    • Nicotine-induced up regulation of α4β2 neuronal nicotinic receptors is mediated by the protein kinase C-dependent phosphorylation of α4 subunits
    • L. Wecker Nicotine-induced up regulation of α4β2 neuronal nicotinic receptors is mediated by the protein kinase C-dependent phosphorylation of α4 subunits Neuroscience 171 2010 12 22
    • (2010) Neuroscience , vol.171 , pp. 12-22
    • Wecker, L.1
  • 59
    • 20444375156 scopus 로고    scopus 로고
    • Nicotine upregulates its own receptors through enhanced intracellular maturation
    • J. Sallette Nicotine upregulates its own receptors through enhanced intracellular maturation Neuron 46 2005 595 607
    • (2005) Neuron , vol.46 , pp. 595-607
    • Sallette, J.1
  • 60
    • 38049107601 scopus 로고    scopus 로고
    • Intracellular complexes of the beta2 subunit of the nicotinic acetylcholine receptor in brain identified by proteomics
    • N. Kabbani Intracellular complexes of the beta2 subunit of the nicotinic acetylcholine receptor in brain identified by proteomics Proc. Natl. Acad. Sci. U. S. A. 104 2007 20570 20575
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 20570-20575
    • Kabbani, N.1
  • 61
    • 84863434758 scopus 로고    scopus 로고
    • Synaptopathies: Diseases of the synaptome
    • S.G. Grant Synaptopathies: diseases of the synaptome Curr. Opin. Neurobiol. 22 2012 522 529
    • (2012) Curr. Opin. Neurobiol. , vol.22 , pp. 522-529
    • Grant, S.G.1
  • 62
    • 84863950667 scopus 로고    scopus 로고
    • Allosteric modulation of endogenous metabolites as an avenue for drug discovery
    • D. Wootten Allosteric modulation of endogenous metabolites as an avenue for drug discovery Mol. Pharmacol. 82 2012 281 290
    • (2012) Mol. Pharmacol. , vol.82 , pp. 281-290
    • Wootten, D.1
  • 63
    • 84857375139 scopus 로고    scopus 로고
    • Allosteric modulation of seven transmembrane spanning receptors: Theory, practice, and opportunities for central nervous system drug discovery
    • B.J. Melancon Allosteric modulation of seven transmembrane spanning receptors: theory, practice, and opportunities for central nervous system drug discovery J. Med. Chem. 55 2012 1445 1464
    • (2012) J. Med. Chem. , vol.55 , pp. 1445-1464
    • Melancon, B.J.1
  • 64
    • 84863115467 scopus 로고    scopus 로고
    • Structure and dynamics of the M3 muscarinic acetylcholine receptor
    • A.C. Kruse Structure and dynamics of the M3 muscarinic acetylcholine receptor Nature 482 2012 552 556
    • (2012) Nature , vol.482 , pp. 552-556
    • Kruse, A.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.