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Volumn 3, Issue 3, 2004, Pages 104-111

The targetable G protein proteome: Where is the next generation of drug targets?

Author keywords

7TM receptors; Cell biology; Drug Discovery; G proteins; Genetics; peptidomimetic; Pharmacology; protein complexes; proteomics; signalling specificity

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; LIPOSOME; PROTEIN DERIVATIVE; PROTEOME; SMAD PROTEIN;

EID: 12344307930     PISSN: 17418372     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1741-8372(04)02429-6     Document Type: Review
Times cited : (5)

References (93)
  • 1
    • 0034724508 scopus 로고    scopus 로고
    • Genomic characterization of the human heterotrimeric G protein alpha, beta, and gamma subunit genes
    • Hurowitz E.H., et al. Genomic characterization of the human heterotrimeric G protein alpha, beta, and gamma subunit genes. DNA Res. 7:2000;111-120
    • (2000) DNA Res. , vol.7 , pp. 111-120
    • Hurowitz, E.H.1
  • 2
    • 0037345375 scopus 로고    scopus 로고
    • Distribution analysis of nonsynonymous polymorphisms within the G-protein-coupled receptor gene family
    • Lee A., et al. Distribution analysis of nonsynonymous polymorphisms within the G-protein-coupled receptor gene family. Genomics. 81:2003;245-248
    • (2003) Genomics , vol.81 , pp. 245-248
    • Lee, A.1
  • 3
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson R., et al. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 63:2003;1256-1272
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1256-1272
    • Fredriksson, R.1
  • 4
    • 0029971060 scopus 로고    scopus 로고
    • Diversity and selectivity of receptor-G protein interaction
    • Gudermann T., et al. Diversity and selectivity of receptor-G protein interaction. Annu. Rev. Pharmacol. Toxicol. 36:1996;429-459
    • (1996) Annu. Rev. Pharmacol. Toxicol. , vol.36 , pp. 429-459
    • Gudermann, T.1
  • 5
    • 0031050888 scopus 로고    scopus 로고
    • Functional and structural complexity of signal transduction via G-protein-coupled receptors
    • Gudermann T., et al. Functional and structural complexity of signal transduction via G-protein-coupled receptors. Annu. Rev. Neurosci. 20:1997;399-427
    • (1997) Annu. Rev. Neurosci. , vol.20 , pp. 399-427
    • Gudermann, T.1
  • 6
    • 0032959367 scopus 로고    scopus 로고
    • Stable association of G proteins with beta 2AR is independent of the state of receptor activation
    • Lachance M., et al. Stable association of G proteins with beta 2AR is independent of the state of receptor activation. Cell. Signal. 11:1999;523-533
    • (1999) Cell. Signal. , vol.11 , pp. 523-533
    • Lachance, M.1
  • 7
    • 0030881617 scopus 로고    scopus 로고
    • Ribozyme-mediated suppression of the G protein gamma7 subunit suggests a role in hormone regulation of adenylylcyclase activity
    • Wang Q., et al. Ribozyme-mediated suppression of the G protein gamma7 subunit suggests a role in hormone regulation of adenylylcyclase activity. J. Biol. Chem. 272:1997;26040-26048
    • (1997) J. Biol. Chem. , vol.272 , pp. 26040-26048
    • Wang, Q.1
  • 8
    • 0033546420 scopus 로고    scopus 로고
    • Ribozyme approach identifies a functional association between the G protein beta1gamma7 subunits in the beta-adrenergic receptor signaling pathway
    • Wang Q., et al. Ribozyme approach identifies a functional association between the G protein beta1gamma7 subunits in the beta-adrenergic receptor signaling pathway. J. Biol. Chem. 274:1999;17365-17371
    • (1999) J. Biol. Chem. , vol.274 , pp. 17365-17371
    • Wang, Q.1
  • 9
    • 0035914348 scopus 로고    scopus 로고
    • Differential dependence of the D1 and D5 dopamine receptors on the G protein gamma 7 subunit for activation of adenylylcyclase
    • Wang Q., et al. Differential dependence of the D1 and D5 dopamine receptors on the G protein gamma 7 subunit for activation of adenylylcyclase. J. Biol. Chem. 276:2001;39386-39393
    • (2001) J. Biol. Chem. , vol.276 , pp. 39386-39393
    • Wang, Q.1
  • 10
    • 0037458639 scopus 로고    scopus 로고
    • Loss of G protein gamma 7 alters behavior and reduces striatal alpha(olf) level and cAMP production
    • Schwindinger W.F., et al. Loss of G protein gamma 7 alters behavior and reduces striatal alpha(olf) level and cAMP production. J. Biol. Chem. 278:2003;6575-6579
    • (2003) J. Biol. Chem. , vol.278 , pp. 6575-6579
    • Schwindinger, W.F.1
  • 11
    • 0033626331 scopus 로고    scopus 로고
    • G-beta-gamma subunit combinations differentially modulate receptor and effector coupling in vivo
    • Robillard L., et al. G-beta-gamma subunit combinations differentially modulate receptor and effector coupling in vivo. Cell. Signal. 12:2000;673-682
    • (2000) Cell. Signal. , vol.12 , pp. 673-682
    • Robillard, L.1
  • 12
    • 0025880464 scopus 로고
    • Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents
    • Kleuss C., et al. Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents. Nature. 353:1991;43-48
    • (1991) Nature , vol.353 , pp. 43-48
    • Kleuss, C.1
  • 13
    • 0026752495 scopus 로고
    • Different beta-subunits determine G-protein interaction with transmembrane receptors
    • Kleuss C., et al. Different beta-subunits determine G-protein interaction with transmembrane receptors. Nature. 358:1992;424-426
    • (1992) Nature , vol.358 , pp. 424-426
    • Kleuss, C.1
  • 14
    • 0027530916 scopus 로고
    • Selectivity in signal transduction determined by gamma subunits of heterotrimeric G proteins
    • Kleuss C., et al. Selectivity in signal transduction determined by gamma subunits of heterotrimeric G proteins. Science. 259:1993;832-834
    • (1993) Science , vol.259 , pp. 832-834
    • Kleuss, C.1
  • 15
    • 0028982350 scopus 로고
    • Subunit composition of G(o) proteins functionally coupling galanin receptors to voltage-gated calcium channels
    • Kalkbrenner F., et al. Subunit composition of G(o) proteins functionally coupling galanin receptors to voltage-gated calcium channels. EMBO J. 14:1995;4728-4737
    • (1995) EMBO J. , vol.14 , pp. 4728-4737
    • Kalkbrenner, F.1
  • 16
    • 1542441193 scopus 로고    scopus 로고
    • Ribozymes as tools for suppression of G protein gamma subunits
    • Robishaw J.D., et al. Ribozymes as tools for suppression of G protein gamma subunits. Methods Mol. Biol. 237:2004;169-180
    • (2004) Methods Mol. Biol. , vol.237 , pp. 169-180
    • Robishaw, J.D.1
  • 17
    • 0036191893 scopus 로고    scopus 로고
    • G protein specificity: Traffic direction required
    • Albert P.R., Robillard L. G protein specificity: traffic direction required. Cell. Signal. 14:2002;407-418
    • (2002) Cell. Signal. , vol.14 , pp. 407-418
    • Albert, P.R.1    Robillard, L.2
  • 18
    • 0038646059 scopus 로고    scopus 로고
    • Structural and functional aspects of G protein-coupled receptor oligomerization
    • Hébert T.E., Bouvier M. Structural and functional aspects of G protein-coupled receptor oligomerization. Biochem. Cell Biol. 76:1998;1-11
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 1-11
    • Hébert, T.E.1    Bouvier, M.2
  • 19
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled transmitter receptors
    • Bouvier M. Oligomerization of G-protein-coupled transmitter receptors. Nat. Rev. Neurosci. 2:2001;274-286
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 274-286
    • Bouvier, M.1
  • 20
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Modulation of receptor function
    • Rios C.D., et al. G-protein-coupled receptor dimerization: modulation of receptor function. Pharmacol. Ther. 92:2001;71-87
    • (2001) Pharmacol. Ther. , vol.92 , pp. 71-87
    • Rios, C.D.1
  • 21
    • 0035816616 scopus 로고    scopus 로고
    • A beta2 adrenergic receptor signaling complex assembled with the Ca2+ channel Cav1.2
    • Davare M.A., et al. A beta2 adrenergic receptor signaling complex assembled with the Ca2+ channel Cav1.2. Science. 293:2001;98-101
    • (2001) Science , vol.293 , pp. 98-101
    • Davare, M.A.1
  • 22
    • 0037195909 scopus 로고    scopus 로고
    • G protein-coupled receptors form stable complexes with inwardly rectifying potassium channels and adenylyl cyclase
    • Lavine N., et al. G protein-coupled receptors form stable complexes with inwardly rectifying potassium channels and adenylyl cyclase. J. Biol. Chem. 277:2002;46010-46019
    • (2002) J. Biol. Chem. , vol.277 , pp. 46010-46019
    • Lavine, N.1
  • 23
    • 17144473106 scopus 로고    scopus 로고
    • Chemokine receptor homo- or heterodimerization activates distinct signaling pathways
    • Mellado M., et al. Chemokine receptor homo- or heterodimerization activates distinct signaling pathways. EMBO J. 20:2001;2497-2507
    • (2001) EMBO J. , vol.20 , pp. 2497-2507
    • Mellado, M.1
  • 24
    • 0032498963 scopus 로고    scopus 로고
    • The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange
    • Hall R.A., et al. The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange. Nature. 392:1998;626-630
    • (1998) Nature , vol.392 , pp. 626-630
    • Hall, R.A.1
  • 25
    • 0034623942 scopus 로고    scopus 로고
    • Beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors
    • Hu L.A., et al. Beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors. J. Biol. Chem. 275:2000;38659-38666
    • (2000) J. Biol. Chem. , vol.275 , pp. 38659-38666
    • Hu, L.A.1
  • 26
    • 0035798618 scopus 로고    scopus 로고
    • Beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD- 95
    • Xu J., et al. Beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD- 95. J. Biol. Chem. 276:2001;41310-41317
    • (2001) J. Biol. Chem. , vol.276 , pp. 41310-41317
    • Xu, J.1
  • 27
    • 0036827005 scopus 로고    scopus 로고
    • Direct binding of the beta 1 adrenergic receptor to the cyclic AMP-dependent guanine nucleotide exchange factor CNrasGEF leads to Ras activation
    • Pak Y., et al. Direct binding of the beta 1 adrenergic receptor to the cyclic AMP-dependent guanine nucleotide exchange factor CNrasGEF leads to Ras activation. Mol. Cell. Biol. 22:2002;7942-7952
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7942-7952
    • Pak, Y.1
  • 28
    • 0034705227 scopus 로고    scopus 로고
    • Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties
    • Levchenko A., et al. Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties. Proc. Natl. Acad. Sci. U. S. A. 97:2000;5818-5823
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5818-5823
    • Levchenko, A.1
  • 29
    • 0034976707 scopus 로고    scopus 로고
    • Altered beta-adrenergic receptor gene regulation and signaling in chronic heart failure
    • Port J.D., Bristow M.R. Altered beta-adrenergic receptor gene regulation and signaling in chronic heart failure. J. Mol. Cell. Cardiol. 33:2001;887-905
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 887-905
    • Port, J.D.1    Bristow, M.R.2
  • 30
    • 17144439929 scopus 로고    scopus 로고
    • Beta-adrenergic signaling in the heart: Dual coupling of the beta2-adrenergic receptor to G(s) and G(i) proteins
    • Xiao R.P. Beta-adrenergic signaling in the heart: dual coupling of the beta2-adrenergic receptor to G(s) and G(i) proteins. Sci. STKE. 1:2001;RE15
    • (2001) Sci. STKE , vol.1 , pp. 15
    • Xiao, R.P.1
  • 31
    • 0035487327 scopus 로고    scopus 로고
    • Classical and new roles of beta-arrestins in the regulation of G-protein-coupled receptors
    • Pierce K.L., Lefkowitz R.J. Classical and new roles of beta-arrestins in the regulation of G-protein-coupled receptors. Nat. Rev. Neurosci. 2:2001;727-733
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 727-733
    • Pierce, K.L.1    Lefkowitz, R.J.2
  • 32
    • 0141608640 scopus 로고    scopus 로고
    • Beta-blocker therapy and severe heart failure: Myth or reality?
    • Ventura H.O., Kalapura T. Beta-blocker therapy and severe heart failure: myth or reality? Congest. Heart Fail. 9:2003;197-202
    • (2003) Congest. Heart Fail. , vol.9 , pp. 197-202
    • Ventura, H.O.1    Kalapura, T.2
  • 33
    • 0037170607 scopus 로고    scopus 로고
    • Benefits of beta-blocker therapy for heart failure: Weighing the evidence
    • Goldstein S. Benefits of beta-blocker therapy for heart failure: weighing the evidence. Arch. Intern. Med. 162:2002;641-648
    • (2002) Arch. Intern. Med. , vol.162 , pp. 641-648
    • Goldstein, S.1
  • 34
    • 0033607558 scopus 로고    scopus 로고
    • Recent advances in cardiac beta(2)-adrenergic signal transduction
    • Xiao R.P., et al. Recent advances in cardiac beta(2)-adrenergic signal transduction. Circ. Res. 85:1999;1092-1100
    • (1999) Circ. Res. , vol.85 , pp. 1092-1100
    • Xiao, R.P.1
  • 35
    • 0033607665 scopus 로고    scopus 로고
    • The molecular basis for distinct beta-adrenergic receptor subtype actions in cardiomyocytes
    • Steinberg S.F. The molecular basis for distinct beta-adrenergic receptor subtype actions in cardiomyocytes. Circ. Res. 85:1999;1101-1111
    • (1999) Circ. Res. , vol.85 , pp. 1101-1111
    • Steinberg, S.F.1
  • 36
    • 0037144542 scopus 로고    scopus 로고
    • Beta 1/beta 2-adrenergic receptor heterodimerization regulates beta 2-adrenergic receptor internalization and ERK signaling efficacy
    • Lavoie C., et al. Beta 1/beta 2-adrenergic receptor heterodimerization regulates beta 2-adrenergic receptor internalization and ERK signaling efficacy. J. Biol. Chem. 277:2002;35402-35410
    • (2002) J. Biol. Chem. , vol.277 , pp. 35402-35410
    • Lavoie, C.1
  • 37
    • 0037307486 scopus 로고    scopus 로고
    • Pharmacological characterization of putative beta1-beta2-adrenergic receptor heterodimers
    • Lavoie C., Hébert T.E. Pharmacological characterization of putative beta1-beta2-adrenergic receptor heterodimers. Can. J. Physiol. Pharmacol. 81:2003;186-195
    • (2003) Can. J. Physiol. Pharmacol. , vol.81 , pp. 186-195
    • Lavoie, C.1    Hébert, T.E.2
  • 38
    • 0034255905 scopus 로고    scopus 로고
    • Growth factor receptor signaling: Location, location, location
    • Leof E.B. Growth factor receptor signaling: location, location, location. Trends Cell Biol. 10:2000;343-348
    • (2000) Trends Cell Biol. , vol.10 , pp. 343-348
    • Leof, E.B.1
  • 39
    • 0035977051 scopus 로고    scopus 로고
    • Binding of the beta 2 adrenergic receptor to N-ethylmaleimide-sensitive factor regulates receptor recycling
    • Cong M., et al. Binding of the beta 2 adrenergic receptor to N-ethylmaleimide-sensitive factor regulates receptor recycling. J. Biol. Chem. 276:2001;45145-45152
    • (2001) J. Biol. Chem. , vol.276 , pp. 45145-45152
    • Cong, M.1
  • 40
    • 0035252096 scopus 로고    scopus 로고
    • Role of endocytosis in mediating downregulation of G-protein-coupled receptors
    • Tsao P., et al. Role of endocytosis in mediating downregulation of G-protein-coupled receptors. Trends Pharmacol. Sci. 22:2001;91-96
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 91-96
    • Tsao, P.1
  • 41
    • 0035055204 scopus 로고    scopus 로고
    • Diversity and specificity in the regulated endocytic membrane trafficking of G-protein-coupled receptors
    • Tsao P.I., von Zastrow M. Diversity and specificity in the regulated endocytic membrane trafficking of G-protein-coupled receptors. Pharmacol. Ther. 89:2001;139-147
    • (2001) Pharmacol. Ther. , vol.89 , pp. 139-147
    • Tsao, P.I.1    Von Zastrow, M.2
  • 42
    • 0041706091 scopus 로고    scopus 로고
    • Functional endothelin receptors are present on nuclei in cardiac ventricular myocytes
    • Boivin B., et al. Functional endothelin receptors are present on nuclei in cardiac ventricular myocytes. J. Biol. Chem. 278:2003;29153-29163
    • (2003) J. Biol. Chem. , vol.278 , pp. 29153-29163
    • Boivin, B.1
  • 43
    • 0037304634 scopus 로고    scopus 로고
    • Nuclear prostaglandin signaling system: Biogenesis and actions via heptahelical receptors
    • Gobeil F. Jr, et al. Nuclear prostaglandin signaling system: biogenesis and actions via heptahelical receptors. Can. J. Physiol. Pharmacol. 81:2003;196-204
    • (2003) Can. J. Physiol. Pharmacol. , vol.81 , pp. 196-204
    • Gobeil Jr., F.1
  • 44
    • 0036897218 scopus 로고    scopus 로고
    • Intracellular targeting of protein kinases and phosphatases
    • Alto N., et al. Intracellular targeting of protein kinases and phosphatases. Diabetes. 51:(Suppl 3):2002;S385-S388
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 3
    • Alto, N.1
  • 45
    • 0036196195 scopus 로고    scopus 로고
    • Intracellular transport mechanisms of signal transducers
    • Dorn G.W. 2nd, Mochly-Rosen D. Intracellular transport mechanisms of signal transducers. Annu. Rev. Physiol. 64:2002;407-429
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 407-429
    • Dorn II, G.W.1    Mochly-Rosen, D.2
  • 46
    • 0038001261 scopus 로고    scopus 로고
    • A-kinase anchoring proteins and neuronal signaling mechanisms
    • Carnegie G.K., Scott J.D. A-kinase anchoring proteins and neuronal signaling mechanisms. Genes Dev. 17:2003;1557-1568
    • (2003) Genes Dev. , vol.17 , pp. 1557-1568
    • Carnegie, G.K.1    Scott, J.D.2
  • 47
    • 0035195491 scopus 로고    scopus 로고
    • The Ste5p scaffold
    • Elion E.A. The Ste5p scaffold. J. Cell Sci. 114:2001;3967-3978
    • (2001) J. Cell Sci. , vol.114 , pp. 3967-3978
    • Elion, E.A.1
  • 48
    • 0037039328 scopus 로고    scopus 로고
    • Signaling complexes: Junctions on the intracellular information super highway
    • Smith F.D., Scott J.D. Signaling complexes: junctions on the intracellular information super highway. Curr. Biol. 12:2002;R32-R40
    • (2002) Curr. Biol. , vol.12
    • Smith, F.D.1    Scott, J.D.2
  • 49
    • 0034690931 scopus 로고    scopus 로고
    • Use of mass spectrometry to study signaling pathways
    • Pandey A., et al. Use of mass spectrometry to study signaling pathways. Sci. STKE. 1:2000;PL1
    • (2000) Sci. STKE , vol.1 , pp. 1
    • Pandey, A.1
  • 50
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • Mann M., et al. Analysis of proteins and proteomes by mass spectrometry. Annu. Rev. Biochem. 70:2001;437-473
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 437-473
    • Mann, M.1
  • 51
    • 32344441627 scopus 로고    scopus 로고
    • Proteomic approaches to the analysis of early events in colony-stimulating factor-1 signal transduction
    • Yeung Y.G., Stanley E.R. Proteomic approaches to the analysis of early events in colony-stimulating factor-1 signal transduction. Mol. Cell. Proteomics. 2:2003;1143-1155
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1143-1155
    • Yeung, Y.G.1    Stanley, E.R.2
  • 52
    • 12144289400 scopus 로고    scopus 로고
    • A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway
    • Bouwmeester T., et al. A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. Nat. Cell Biol. 6:2004;97-105
    • (2004) Nat. Cell Biol. , vol.6 , pp. 97-105
    • Bouwmeester, T.1
  • 53
    • 1842556785 scopus 로고    scopus 로고
    • Identification of novel protein-protein interactions using a versatile mammalian tandem affinity purification expression system
    • Knuesel M., et al. Identification of novel protein-protein interactions using a versatile mammalian tandem affinity purification expression system. Mol. Cell. Proteomics. 2:2003;1225-1233
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1225-1233
    • Knuesel, M.1
  • 54
    • 0037862083 scopus 로고    scopus 로고
    • The 'magic tail' of G protein-coupled receptors: An anchorage for functional protein networks
    • Bockaert J., et al. The 'magic tail' of G protein-coupled receptors: an anchorage for functional protein networks. FEBS Lett. 546:2003;65-72
    • (2003) FEBS Lett. , vol.546 , pp. 65-72
    • Bockaert, J.1
  • 55
    • 0036448992 scopus 로고    scopus 로고
    • A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors
    • Becamel C., et al. A proteomic approach based on peptide affinity chromatography, 2-dimensional electrophoresis and mass spectrometry to identify multiprotein complexes interacting with membrane-bound receptors. Biol. Proced. Online. 4:2002;94-104
    • (2002) Biol. Proced. Online , vol.4 , pp. 94-104
    • Becamel, C.1
  • 56
  • 57
    • 0036857488 scopus 로고    scopus 로고
    • Application of zwitterionic detergents to the solubilization of integral membrane proteins for two-dimensional gel electrophoresis and mass spectrometry
    • Henningsen R., et al. Application of zwitterionic detergents to the solubilization of integral membrane proteins for two-dimensional gel electrophoresis and mass spectrometry. Proteomics. 2:2002;1479-1488
    • (2002) Proteomics , vol.2 , pp. 1479-1488
    • Henningsen, R.1
  • 58
    • 0347134596 scopus 로고    scopus 로고
    • Affinity enrichment of plasma membrane for proteomics analysis
    • Zhang W., et al. Affinity enrichment of plasma membrane for proteomics analysis. Electrophoresis. 24:2003;2855-2863
    • (2003) Electrophoresis , vol.24 , pp. 2855-2863
    • Zhang, W.1
  • 59
    • 0042563232 scopus 로고    scopus 로고
    • Capillary high-performance liquid chromatography/mass spectrometric analysis of proteins from affinity-purified plasma membrane
    • Zhao Y., et al. Capillary high-performance liquid chromatography/mass spectrometric analysis of proteins from affinity-purified plasma membrane. Anal. Chem. 75:2003;3751-3757
    • (2003) Anal. Chem. , vol.75 , pp. 3751-3757
    • Zhao, Y.1
  • 60
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • Terrillon S., Bouvier M. Roles of G-protein-coupled receptor dimerization. EMBO Rep. 5:2004;30-34
    • (2004) EMBO Rep. , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 61
    • 0037435022 scopus 로고    scopus 로고
    • Protein analysis on a proteomic scale
    • Phizicky E., et al. Protein analysis on a proteomic scale. Nature. 422:2003;208-215
    • (2003) Nature , vol.422 , pp. 208-215
    • Phizicky, E.1
  • 62
    • 0036849482 scopus 로고    scopus 로고
    • Analysis of membrane protein interactions using yeast-based technologies
    • Stagljar I., Fields S. Analysis of membrane protein interactions using yeast-based technologies. Trends Biochem. Sci. 27:2002;559-563
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 559-563
    • Stagljar, I.1    Fields, S.2
  • 63
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin A.C., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature. 415:2002;141-147
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1
  • 64
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y., et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature. 415:2002;180-183
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1
  • 65
    • 2442626585 scopus 로고    scopus 로고
    • The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins
    • Feb published online ahead of print; doi: 10.1074/jbc.M312106200
    • Bécamel, C. et al. The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins. J. Biol. Chem. Feb 2004, published online ahead of print; doi: 10.1074/jbc.M312106200
    • (2004) J. Biol. Chem.
    • Bécamel, C.1
  • 66
    • 0030835610 scopus 로고    scopus 로고
    • A multivalent PDZ-domain protein assembles signaling complexes in a G- protein-coupled cascade
    • Tsunoda S., et al. A multivalent PDZ-domain protein assembles signaling complexes in a G- protein-coupled cascade. Nature. 388:1997;243-249
    • (1997) Nature , vol.388 , pp. 243-249
    • Tsunoda, S.1
  • 67
    • 0030815874 scopus 로고    scopus 로고
    • New light on TRP and TRPL
    • Montell C. New light on TRP and TRPL. Mol. Pharmacol. 52:1997;755-763
    • (1997) Mol. Pharmacol. , vol.52 , pp. 755-763
    • Montell, C.1
  • 68
    • 0033946468 scopus 로고    scopus 로고
    • Proteomic analysis of NMDA receptor-adhesion protein signaling complexes
    • Husi H., et al. Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. Nat. Neurosci. 3:2000;661-669
    • (2000) Nat. Neurosci. , vol.3 , pp. 661-669
    • Husi, H.1
  • 69
    • 0035341239 scopus 로고    scopus 로고
    • Proteomics of the nervous system
    • Husi H., Grant S.G. Proteomics of the nervous system. Trends Neurosci. 24:2001;259-266
    • (2001) Trends Neurosci. , vol.24 , pp. 259-266
    • Husi, H.1    Grant, S.G.2
  • 70
    • 0010697803 scopus 로고    scopus 로고
    • Proteomics of multiprotein complexes: Answering fundamental questions in neuroscience
    • Grant S.G., Husi H. Proteomics of multiprotein complexes: answering fundamental questions in neuroscience. Trends Biotechnol. 19:2001;S49-S54
    • (2001) Trends Biotechnol. , vol.19
    • Grant, S.G.1    Husi, H.2
  • 71
    • 0035895890 scopus 로고    scopus 로고
    • Proteomics characterization of abundant Golgi membrane proteins
    • Bell A.W., et al. Proteomics characterization of abundant Golgi membrane proteins. J. Biol. Chem. 276:2001;5152-5165
    • (2001) J. Biol. Chem. , vol.276 , pp. 5152-5165
    • Bell, A.W.1
  • 72
    • 0036224270 scopus 로고    scopus 로고
    • Organellar proteomics: The prizes and pitfalls of opening the nuclear envelope
    • Schirmer E.C., Gerace L. Organellar proteomics: the prizes and pitfalls of opening the nuclear envelope. Genome Biol. 3:2002;1008
    • (2002) Genome Biol. , vol.3 , pp. 1008
    • Schirmer, E.C.1    Gerace, L.2
  • 73
    • 0032246648 scopus 로고    scopus 로고
    • Dual activation and inhibition of adenylyl cyclase by cannabinoid receptor agonists: Evidence for agonist-specific trafficking of intracellular responses
    • Bonhaus D.W., et al. Dual activation and inhibition of adenylyl cyclase by cannabinoid receptor agonists: evidence for agonist-specific trafficking of intracellular responses. J. Pharmacol. Exp. Ther. 287:1998;884-888
    • (1998) J. Pharmacol. Exp. Ther. , vol.287 , pp. 884-888
    • Bonhaus, D.W.1
  • 74
    • 0032907370 scopus 로고    scopus 로고
    • Novel actions of inverse agonists on 5-HT2C receptor systems
    • Berg K.A., et al. Novel actions of inverse agonists on 5-HT2C receptor systems. Mol. Pharmacol. 55:1999;863-872
    • (1999) Mol. Pharmacol. , vol.55 , pp. 863-872
    • Berg, K.A.1
  • 75
    • 0036463901 scopus 로고    scopus 로고
    • Efficacy at G-protein-coupled receptors
    • Kenakin T. Efficacy at G-protein-coupled receptors. Nat. Rev. Drug Discov. 1:2002;103-110
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 103-110
    • Kenakin, T.1
  • 76
    • 0036177114 scopus 로고    scopus 로고
    • Drug efficacy at G protein-coupled receptors
    • Kenakin T. Drug efficacy at G protein-coupled receptors. Annu. Rev. Pharmacol. Toxicol. 42:2002;349-379
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 349-379
    • Kenakin, T.1
  • 77
    • 0028350901 scopus 로고
    • Inverse agonist activity of beta-adrenergic antagonists
    • Chidiac P., et al. Inverse agonist activity of beta-adrenergic antagonists. Mol. Pharmacol. 45:1994;490-499
    • (1994) Mol. Pharmacol. , vol.45 , pp. 490-499
    • Chidiac, P.1
  • 78
    • 0029787046 scopus 로고    scopus 로고
    • Agonist-induced modulation of inverse agonist efficacy at the beta 2-adrenergic receptor
    • Chidiac P., et al. Agonist-induced modulation of inverse agonist efficacy at the beta 2-adrenergic receptor. Mol. Pharmacol. 50:1996;662-669
    • (1996) Mol. Pharmacol. , vol.50 , pp. 662-669
    • Chidiac, P.1
  • 79
    • 0141593597 scopus 로고    scopus 로고
    • Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors
    • Azzi M., et al. Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors. Proc. Natl. Acad. Sci. U. S. A. 100:2003;11406-11411
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 11406-11411
    • Azzi, M.1
  • 80
    • 0037388679 scopus 로고    scopus 로고
    • Protein-protein interactions as a target for drugs in proteomics
    • Archakov A.I., et al. Protein-protein interactions as a target for drugs in proteomics. Proteomics. 3:2003;380-391
    • (2003) Proteomics , vol.3 , pp. 380-391
    • Archakov, A.I.1
  • 81
    • 1542390499 scopus 로고    scopus 로고
    • Identification of protein-protein interaction sites from docking energy landscapes
    • Fernandez-Recio J., et al. Identification of protein-protein interaction sites from docking energy landscapes. J. Mol. Biol. 335:2004;843-865
    • (2004) J. Mol. Biol. , vol.335 , pp. 843-865
    • Fernandez-Recio, J.1
  • 82
    • 0032737399 scopus 로고    scopus 로고
    • Non-binding site modulation of G protein-coupled receptor signaling
    • Jones P.G., et al. Non-binding site modulation of G protein-coupled receptor signaling. Expert Opin. Ther. Pat. 9:1999;1641-1654
    • (1999) Expert Opin. Ther. Pat. , vol.9 , pp. 1641-1654
    • Jones, P.G.1
  • 83
    • 0035719142 scopus 로고    scopus 로고
    • Design and use of C-terminal minigene vectors for studying role of heterotrimeric G proteins
    • Gilchrist A., et al. Design and use of C-terminal minigene vectors for studying role of heterotrimeric G proteins. Methods Enzymol. 344:2002;58-69
    • (2002) Methods Enzymol. , vol.344 , pp. 58-69
    • Gilchrist, A.1
  • 84
    • 0029666267 scopus 로고    scopus 로고
    • A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
    • Hébert T.E., et al. A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation. J. Biol. Chem. 271:1996;16384-16392
    • (1996) J. Biol. Chem. , vol.271 , pp. 16384-16392
    • Hébert, T.E.1
  • 85
    • 0037827724 scopus 로고    scopus 로고
    • Stimulation of cellular signaling and G protein subunit dissociation by G protein betagamma subunit-binding peptides
    • Goubaeva F., et al. Stimulation of cellular signaling and G protein subunit dissociation by G protein betagamma subunit-binding peptides. J. Biol. Chem. 278:2003;19634-19641
    • (2003) J. Biol. Chem. , vol.278 , pp. 19634-19641
    • Goubaeva, F.1
  • 86
    • 0034796216 scopus 로고    scopus 로고
    • Isozyme-specific inhibitors and activators of protein kinase C
    • Schechtman D., Mochly-Rosen D. Isozyme-specific inhibitors and activators of protein kinase C. Methods Enzymol. 345:2002;470-489
    • (2002) Methods Enzymol. , vol.345 , pp. 470-489
    • Schechtman, D.1    Mochly-Rosen, D.2
  • 87
    • 0038025879 scopus 로고    scopus 로고
    • Identification and characterization of peptide probes directed against PKCalpha conformations
    • Ashraf S.S., et al. Identification and characterization of peptide probes directed against PKCalpha conformations. J. Pept. Res. 61:2003;263-273
    • (2003) J. Pept. Res. , vol.61 , pp. 263-273
    • Ashraf, S.S.1
  • 88
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang Z., et al. SH2 domains recognize specific phosphopeptide sequences. Cell. 72:1993;767-778
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1
  • 89
    • 0037116524 scopus 로고    scopus 로고
    • Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding
    • Davidson J.P., et al. Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding. J. Am. Chem. Soc. 124:2002;205-215
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 205-215
    • Davidson, J.P.1
  • 90
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev L.T., et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science. 303:2004;844-848
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1
  • 91
    • 0033609895 scopus 로고    scopus 로고
    • A new potent HIV-1 reverse transcriptase inhibitor. A synthetic peptide derived from the interface subunit domains
    • Morris M.C., et al. A new potent HIV-1 reverse transcriptase inhibitor. A synthetic peptide derived from the interface subunit domains. J. Biol. Chem. 274:1999;24941-24946
    • (1999) J. Biol. Chem. , vol.274 , pp. 24941-24946
    • Morris, M.C.1
  • 92
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • Wurtele M., et al. Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J. 22:2003;987-994
    • (2003) EMBO J. , vol.22 , pp. 987-994
    • Wurtele, M.1
  • 93
    • 0038445997 scopus 로고    scopus 로고
    • Protein complexes involved in heptahelical receptor-mediated signal transduction
    • Rebois R.V., Hébert T.E. Protein complexes involved in heptahelical receptor-mediated signal transduction. Receptors Channels. 9:2003;169-194
    • (2003) Receptors Channels , vol.9 , pp. 169-194
    • Rebois, R.V.1    Hébert, T.E.2


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