메뉴 건너뛰기




Volumn 23, Issue 4-5, 2004, Pages 301-317

Functional consequences of 7TM receptor dimerization

Author keywords

7TM receptor; Dimerization; G protein; GPCR; Oligomerization

Indexed keywords

7TM RECEPTOR; ADENOSINE A2 RECEPTOR; ANTIBODY; DOPAMINE 2 RECEPTOR; LEUKOTRIENE B4 AGONIST; LEUKOTRIENE RECEPTOR STIMULATING AGENT; LIGAND; METABOTROPIC RECEPTOR 5; OPIATE AGONIST; OXYTOCIN; RECEPTOR; RECEPTOR ANTIBODY; SIGMA OPIATE RECEPTOR; UNCLASSIFIED DRUG;

EID: 9644263918     PISSN: 09280987     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejps.2004.08.004     Document Type: Review
Times cited : (33)

References (159)
  • 1
    • 0035955732 scopus 로고    scopus 로고
    • The angiotensin II AT2 receptor is an AT1 receptor antagonist
    • S. AbdAlla, H. Lother, A.M. Abdel-tawab, and U. Quitterer The angiotensin II AT2 receptor is an AT1 receptor antagonist J. Biol. Chem. 276 2001 39721 39726
    • (2001) J. Biol. Chem. , vol.276 , pp. 39721-39726
    • Abdalla, S.1    Lother, H.2    Abdel-Tawab, A.M.3    Quitterer, U.4
  • 2
    • 0034785580 scopus 로고    scopus 로고
    • Increased AT(1) receptor heterodimers in preeclampsia mediate enhanced angiotensin II responsiveness
    • S. AbdAlla, H. Lother, A. el Massiery, and U. Quitterer Increased AT(1) receptor heterodimers in preeclampsia mediate enhanced angiotensin II responsiveness Nat. Med. 7 2001 1003 1009
    • (2001) Nat. Med. , vol.7 , pp. 1003-1009
    • Abdalla, S.1    Lother, H.2    El Massiery, A.3    Quitterer, U.4
  • 3
    • 0034618268 scopus 로고    scopus 로고
    • AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration
    • S. AbdAlla, H. Lother, and U. Quitterer AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration Nature 407 2000 94 98
    • (2000) Nature , vol.407 , pp. 94-98
    • Abdalla, S.1    Lother, H.2    Quitterer, U.3
  • 4
    • 0033543572 scopus 로고    scopus 로고
    • Involvement of the amino terminus of the B(2) receptor in agonist-induced receptor dimerization
    • S. AbdAlla, E. Zaki, H. Lother, and U. Quitterer Involvement of the amino terminus of the B(2) receptor in agonist-induced receptor dimerization J. Biol. Chem. 274 1999 26079 26084
    • (1999) J. Biol. Chem. , vol.274 , pp. 26079-26084
    • Abdalla, S.1    Zaki, E.2    Lother, H.3    Quitterer, U.4
  • 5
    • 0033538567 scopus 로고    scopus 로고
    • Ig-hepta, a novel member of the G protein-coupled hepta-helical receptor (GPCR) family that has immunoglobulin-like repeats in a long N-terminal extracellular domain and defines a new subfamily of GPCRs
    • J. Abe, H. Suzuki, M. Notoya, T. Yamamoto, and S. Hirose Ig-hepta, a novel member of the G protein-coupled hepta-helical receptor (GPCR) family that has immunoglobulin-like repeats in a long N-terminal extracellular domain and defines a new subfamily of GPCRs J. Biol. Chem. 274 1999 19957 19964
    • (1999) J. Biol. Chem. , vol.274 , pp. 19957-19964
    • Abe, J.1    Suzuki, H.2    Notoya, M.3    Yamamoto, T.4    Hirose, S.5
  • 6
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G-protein-coupled receptor ontogeny and function
    • S. Angers, A. Salahpour, and M. Bouvier Dimerization: an emerging concept for G-protein-coupled receptor ontogeny and function Annu. Rev. Pharmacol. Toxicol. 42 2002 409 435
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 7
    • 0034724192 scopus 로고    scopus 로고
    • Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • S. Angers, A. Salahpour, E. Joly, S. Hilairet, D. Chelsky, M. Dennis, and M. Bouvier Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET) Proc. Natl. Acad. Sci. USA 97 2000 3684 3689
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3684-3689
    • Angers, S.1    Salahpour, A.2    Joly, E.3    Hilairet, S.4    Chelsky, D.5    Dennis, M.6    Bouvier, M.7
  • 8
    • 0035933747 scopus 로고    scopus 로고
    • Dopamine D2 receptor dimer formation: Evidence from ligand binding
    • D. Armstrong, and P.G. Strange Dopamine D2 receptor dimer formation: evidence from ligand binding J. Biol. Chem. 276 2001 22621 22629
    • (2001) J. Biol. Chem. , vol.276 , pp. 22621-22629
    • Armstrong, D.1    Strange, P.G.2
  • 9
    • 0020666568 scopus 로고
    • Oligomeric structure of muscarinic receptors is shown by photoaffinity labeling: Subunit assembly may explain high- and low-affinity agonist states
    • S. Avissar, G. Amitai, and M. Sokolovsky Oligomeric structure of muscarinic receptors is shown by photoaffinity labeling: subunit assembly may explain high- and low-affinity agonist states Proc. Natl. Acad. Sci. USA 80 1983 156 159
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 156-159
    • Avissar, S.1    Amitai, G.2    Sokolovsky, M.3
  • 10
    • 0037077208 scopus 로고    scopus 로고
    • Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer
    • M.A. Ayoub, C. Couturier, E. Lucas-Meunier, S. Angers, P. Fossier, M. Bouvier, and R. Jockers Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer J. Biol. Chem. 277 2002 21522 21528
    • (2002) J. Biol. Chem. , vol.277 , pp. 21522-21528
    • Ayoub, M.A.1    Couturier, C.2    Lucas-Meunier, E.3    Angers, S.4    Fossier, P.5    Bouvier, M.6    Jockers, R.7
  • 11
    • 0037474238 scopus 로고    scopus 로고
    • Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor
    • G.J. Babcock, M. Farzan, and J. Sodroski Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor J. Biol. Chem. 278 2003 3378 3385
    • (2003) J. Biol. Chem. , vol.278 , pp. 3378-3385
    • Babcock, G.J.1    Farzan, M.2    Sodroski, J.3
  • 12
    • 0242572132 scopus 로고    scopus 로고
    • Dimerization of G-protein-coupled receptors: Roles in signal transduction
    • M. Bai Dimerization of G-protein-coupled receptors: roles in signal transduction Cell. Signal. 16 2004 175 186
    • (2004) Cell. Signal. , vol.16 , pp. 175-186
    • Bai, M.1
  • 13
    • 0032483541 scopus 로고    scopus 로고
    • Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells
    • M. Bai, S. Trivedi, and E.M. Brown Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells J. Biol. Chem. 273 1998 23605 23610
    • (1998) J. Biol. Chem. , vol.273 , pp. 23605-23610
    • Bai, M.1    Trivedi, S.2    Brown, E.M.3
  • 14
    • 0038392702 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein
    • J.L. Baneres, and J. Parello Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein J. Mol. Biol. 329 2003 815 829
    • (2003) J. Mol. Biol. , vol.329 , pp. 815-829
    • Baneres, J.L.1    Parello, J.2
  • 16
    • 0141841603 scopus 로고    scopus 로고
    • Dual inhibition of {beta}-Adrenergic and Angiotensin II receptors by a single antagonist: A functional role for receptor-receptor interaction in vivo
    • L. Barki-Harrington, L.M. Luttrell, and H.A. Rockman Dual inhibition of {beta}-Adrenergic and Angiotensin II receptors by a single antagonist: a functional role for receptor-receptor interaction in vivo Circulation 108 2003 1611 1618
    • (2003) Circulation , vol.108 , pp. 1611-1618
    • Barki-Harrington, L.1    Luttrell, L.M.2    Rockman, H.A.3
  • 17
    • 0030712312 scopus 로고    scopus 로고
    • Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32
    • M. Benkirane, D.Y. Jin, R.F. Chun, R.A. Koup, and K.T. Jeang Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32 J. Biol. Chem. 272 1997 30603 30606
    • (1997) J. Biol. Chem. , vol.272 , pp. 30603-30606
    • Benkirane, M.1    Jin, D.Y.2    Chun, R.F.3    Koup, R.A.4    Jeang, K.T.5
  • 20
    • 0036174898 scopus 로고    scopus 로고
    • G-protein-coupled receptor interacting proteins: Emerging roles in localization and signal transduction
    • A.E. Brady, and L.E. Limbird G-protein-coupled receptor interacting proteins: emerging roles in localization and signal transduction Cell. Signal. 14 2002 297 309
    • (2002) Cell. Signal. , vol.14 , pp. 297-309
    • Brady, A.E.1    Limbird, L.E.2
  • 21
    • 0346059583 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization: Implications for G protein activation and cell signaling
    • G.E. Breitwieser G-protein-coupled receptor oligomerization: implications for G protein activation and cell signaling Circ. Res. 94 2004 17 27
    • (2004) Circ. Res. , vol.94 , pp. 17-27
    • Breitwieser, G.E.1
  • 24
    • 0030198872 scopus 로고    scopus 로고
    • Synthesis and characterization of bivalent peptide ligands targeted to G-protein-coupled receptors
    • M.D. Carrithers, and M.R. Lerner Synthesis and characterization of bivalent peptide ligands targeted to G-protein-coupled receptors Chem. Biol. 3 1996 537 542
    • (1996) Chem. Biol. , vol.3 , pp. 537-542
    • Carrithers, M.D.1    Lerner, M.R.2
  • 25
    • 0023283062 scopus 로고
    • Physicochemical characterization of photoaffinity-labeled angiotensin II receptors
    • M.C. Carson, C.M. Harper, A.J. Baukal, G. Aguilera, and K.J. Catt Physicochemical characterization of photoaffinity-labeled angiotensin II receptors Mol. Endocrinol. 1 1987 147 153
    • (1987) Mol. Endocrinol. , vol.1 , pp. 147-153
    • Carson, M.C.1    Harper, C.M.2    Baukal, A.J.3    Aguilera, G.4    Catt, K.J.5
  • 26
    • 0029802727 scopus 로고    scopus 로고
    • Evidence for negative cooperativity among human thyrotropin receptors overexpressed in mammalian cells
    • G.D. Chazenbalk, A. Kakinuma, J.C. Jaume, S.M. McLachlan, and B. Rapoport Evidence for negative cooperativity among human thyrotropin receptors overexpressed in mammalian cells Endocrinol. 137 1996 4586 4591
    • (1996) Endocrinol. , vol.137 , pp. 4586-4591
    • Chazenbalk, G.D.1    Kakinuma, A.2    Jaume, J.C.3    McLachlan, S.M.4    Rapoport, B.5
  • 27
    • 0035930602 scopus 로고    scopus 로고
    • Agonist-dependent dissociation of oligomeric complexes of G-protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer
    • Z.J. Cheng, and L.J. Miller Agonist-dependent dissociation of oligomeric complexes of G-protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer J. Biol. Chem. 276 2001 48040 48047
    • (2001) J. Biol. Chem. , vol.276 , pp. 48040-48047
    • Cheng, Z.J.1    Miller, L.J.2
  • 28
    • 1942501726 scopus 로고    scopus 로고
    • Subunits of a yeast G-protein-coupled receptor are activated independently by agonist but function in concert to activate G protein heterotrimers
    • S.L. Chinault, M.C. Overton, and K.J. Blumer Subunits of a yeast G-protein-coupled receptor are activated independently by agonist but function in concert to activate G protein heterotrimers J. Biol. Chem. 2004
    • (2004) J. Biol. Chem.
    • Chinault, S.L.1    Overton, M.C.2    Blumer, K.J.3
  • 30
    • 0028914025 scopus 로고
    • Defective intracellular transport is the molecular basis of rhodopsin-dependent dominant retinal degeneration
    • N.J. Colley, J.A. Cassill, E.K. Baker, and C.S. Zuker Defective intracellular transport is the molecular basis of rhodopsin-dependent dominant retinal degeneration Proc. Natl. Acad. Sci. USA 92 1995 3070 3074
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3070-3074
    • Colley, N.J.1    Cassill, J.A.2    Baker, E.K.3    Zuker, C.S.4
  • 31
    • 0020328255 scopus 로고
    • Conversion of a gonadotropin-releasing hormone antagonist to an agonist
    • P.M. Conn, D.C. Rogers, J.M. Stewart, J. Niedel, and T. Sheffield Conversion of a gonadotropin-releasing hormone antagonist to an agonist Nature 296 1982 653 655
    • (1982) Nature , vol.296 , pp. 653-655
    • Conn, P.M.1    Rogers, D.C.2    Stewart, J.M.3    Niedel, J.4    Sheffield, T.5
  • 32
    • 0036385647 scopus 로고    scopus 로고
    • Measurement of changes in fluorescence resonance energy transfer between gonadotropin-releasing hormone receptors in response to agonists
    • A. Cornea, and P.M. Conn Measurement of changes in fluorescence resonance energy transfer between gonadotropin-releasing hormone receptors in response to agonists Methods 27 2002 333 339
    • (2002) Methods , vol.27 , pp. 333-339
    • Cornea, A.1    Conn, P.M.2
  • 33
    • 0035910464 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone receptor microaggregation Rate monitored by fluorescence resonance energy transfer
    • A. Cornea, J.A. Janovick, G. Maya-Nunez, and P.M. Conn Gonadotropin-releasing hormone receptor microaggregation Rate monitored by fluorescence resonance energy transfer J. Biol. Chem. 276 2001 2153 2158
    • (2001) J. Biol. Chem. , vol.276 , pp. 2153-2158
    • Cornea, A.1    Janovick, J.A.2    Maya-Nunez, G.3    Conn, P.M.4
  • 34
    • 0030760634 scopus 로고    scopus 로고
    • Dimerization of the delta opioid receptor: Implication for a role in receptor internalization
    • S. Cvejic, and L.A. Devi Dimerization of the delta opioid receptor: implication for a role in receptor internalization J. Biol. Chem. 272 1997 26959 26964
    • (1997) J. Biol. Chem. , vol.272 , pp. 26959-26964
    • Cvejic, S.1    Devi, L.A.2
  • 35
    • 0035811492 scopus 로고    scopus 로고
    • Insights into Wnt binding and signalling from the structures of two frizzled cysteine-rich domains
    • C.E. Dann, J.C. Hsieh, A. Rattner, D. Sharma, J. Nathans, and D.J. Leahy Insights into Wnt binding and signalling from the structures of two frizzled cysteine-rich domains Nature 412 2001 86 90
    • (2001) Nature , vol.412 , pp. 86-90
    • Dann, C.E.1    Hsieh, J.C.2    Rattner, A.3    Sharma, D.4    Nathans, J.5    Leahy, D.J.6
  • 36
    • 0036479250 scopus 로고    scopus 로고
    • A single subunit (GB2) is required for G-protein activation by the heterodimeric GABA(B) receptor
    • B. Duthey, S. Caudron, J. Perroy, B. Bettler, L. Fagni, J.P. Pin, and L. Prezeau A single subunit (GB2) is required for G-protein activation by the heterodimeric GABA(B) receptor J. Biol. Chem. 277 2002 3236 3241
    • (2002) J. Biol. Chem. , vol.277 , pp. 3236-3241
    • Duthey, B.1    Caudron, S.2    Perroy, J.3    Bettler, B.4    Fagni, L.5    Pin, J.P.6    Prezeau, L.7
  • 37
  • 40
    • 0036878162 scopus 로고    scopus 로고
    • Prediction of heterodimerization interfaces of G-protein-coupled receptors with a new subtractive correlated mutation method
    • M. Filizola, O. Olmea, and H. Weinstein Prediction of heterodimerization interfaces of G-protein-coupled receptors with a new subtractive correlated mutation method Protein Eng. 15 2002 881 885
    • (2002) Protein Eng. , vol.15 , pp. 881-885
    • Filizola, M.1    Olmea, O.2    Weinstein, H.3
  • 41
    • 0036997276 scopus 로고    scopus 로고
    • Structural models for dimerization of G-protein-coupled receptors: The opioid receptor homodimers
    • M. Filizola, and H. Weinstein Structural models for dimerization of G-protein-coupled receptors: the opioid receptor homodimers Biopolymers 66 2002 317 325
    • (2002) Biopolymers , vol.66 , pp. 317-325
    • Filizola, M.1    Weinstein, H.2
  • 42
    • 0041315583 scopus 로고    scopus 로고
    • C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G-protein-coupled receptor expressed in yeast
    • D.H. Floyd, A. Geva, S.P. Bruinsma, M.C. Overton, K.J. Blumer, and T.J. Baranski C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G-protein-coupled receptor expressed in yeast J. Biol. Chem. 278 2003 35354 35361
    • (2003) J. Biol. Chem. , vol.278 , pp. 35354-35361
    • Floyd, D.H.1    Geva, A.2    Bruinsma, S.P.3    Overton, M.C.4    Blumer, K.J.5    Baranski, T.J.6
  • 46
    • 0035341213 scopus 로고    scopus 로고
    • Allosteric interactions between GB1 and GB2 subunits are required for optimal GABA(B) receptor function
    • T. Galvez, B. Duthey, J. Kniazeff, J. Blahos, G. Rovelli, B. Bettler, L. Prezeau, and J.P. Pin Allosteric interactions between GB1 and GB2 subunits are required for optimal GABA(B) receptor function EMBO J. 20 2001 2152 2159
    • (2001) EMBO J. , vol.20 , pp. 2152-2159
    • Galvez, T.1    Duthey, B.2    Kniazeff, J.3    Blahos, J.4    Rovelli, G.5    Bettler, B.6    Prezeau, L.7    Pin, J.P.8
  • 47
    • 0034714335 scopus 로고    scopus 로고
    • Oligomerization of mu- and delta-opioid receptors. Generation of novel functional properties
    • S.R. George, T. Fan, Z. Xie, R. Tse, V. Tam, G. Varghese, and B.F. O'Dowd Oligomerization of mu- and delta-opioid receptors. Generation of novel functional properties J. Biol. Chem. 275 2000 26128 26135
    • (2000) J. Biol. Chem. , vol.275 , pp. 26128-26135
    • George, S.R.1    Fan, T.2    Xie, Z.3    Tse, R.4    Tam, V.5    Varghese, G.6    O'Dowd, B.F.7
  • 48
    • 0032515074 scopus 로고    scopus 로고
    • A transmembrane domain-derived peptide inhibits D1 dopamine receptor function without affecting receptor oligomerization
    • S.R. George, S.P. Lee, G. Varghese, P.R. Zeman, P. Seeman, G.Y. Ng, and B.F. O'Dowd A transmembrane domain-derived peptide inhibits D1 dopamine receptor function without affecting receptor oligomerization J. Biol. Chem. 273 1998 30244 30248
    • (1998) J. Biol. Chem. , vol.273 , pp. 30244-30248
    • George, S.R.1    Lee, S.P.2    Varghese, G.3    Zeman, P.R.4    Seeman, P.5    Ng, G.Y.6    O'Dowd, B.F.7
  • 49
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • S.R. George, B.F. O'Dowd, and S.P. Lee G-protein-coupled receptor oligomerization and its potential for drug discovery Nat. Rev. Drug Discov. 1 2002 808 820
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 808-820
    • George, S.R.1    O'Dowd, B.F.2    Lee, S.P.3
  • 50
    • 0034634690 scopus 로고    scopus 로고
    • Genetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function
    • A. Geva, T.B. Lassere, O. Lichtarge, S.K. Pollitt, and T.J. Baranski Genetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function J. Biol. Chem. 275 2000 35393 35401
    • (2000) J. Biol. Chem. , vol.275 , pp. 35393-35401
    • Geva, A.1    Lassere, T.B.2    Lichtarge, O.3    Pollitt, S.K.4    Baranski, T.J.5
  • 53
    • 0034937698 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Implications in modulating receptor function
    • I. Gomes, B.A. Jordan, A. Gupta, C. Rios, N. Trapaidze, and L.A. Devi G-protein-coupled receptor dimerization: implications in modulating receptor function J. Mol. Med. 79 2001 226 242
    • (2001) J. Mol. Med. , vol.79 , pp. 226-242
    • Gomes, I.1    Jordan, B.A.2    Gupta, A.3    Rios, C.4    Trapaidze, N.5    Devi, L.A.6
  • 57
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer
    • W. Guo, L. Shi, and J.A. Javitch The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer J. Biol. Chem. 278 2003 4385 4388
    • (2003) J. Biol. Chem. , vol.278 , pp. 4385-4388
    • Guo, W.1    Shi, L.2    Javitch, J.A.3
  • 59
    • 84862476691 scopus 로고    scopus 로고
    • Oligomerization of wild type and non-functional mutant Angiotensin II type I (AT1) receptors inhibits Gaq protein signaling but not ERK activation
    • in press.
    • Hansen JL, J.T., Haunsø, S., Sheikh, S.P., 2004. Oligomerization of wild type and non-functional mutant Angiotensin II type I (AT1) receptors inhibits Gaq protein signaling but not ERK activation. JBC in press.
    • (2004) JBC
    • Hansen, J.L.J.T.1    Haunsø, S.2    Sheikh, S.P.3
  • 60
    • 0037184966 scopus 로고    scopus 로고
    • Homo- and hetero-oligomerization of thyrotropin-releasing hormone (TRH) receptor subtypes. Differential regulation of beta-arrestins 1 and 2
    • A.C. Hanyaloglu, R.M. Seeber, T.A. Kohout, R.J. Lefkowitz, and K.A. Eidne Homo- and hetero-oligomerization of thyrotropin-releasing hormone (TRH) receptor subtypes. Differential regulation of beta-arrestins 1 and 2 J. Biol. Chem. 277 2002 50422 50430
    • (2002) J. Biol. Chem. , vol.277 , pp. 50422-50430
    • Hanyaloglu, A.C.1    Seeber, R.M.2    Kohout, T.A.3    Lefkowitz, R.J.4    Eidne, K.A.5
  • 61
    • 0020040541 scopus 로고
    • Increased biological activity of dimers of oxymorphone and enkephalin: Possible role of receptor cross-linking
    • E. Hazum, K.J. Chang, H.J. Leighton, O.W. Lever Jr., and P. Cuatrecasas Increased biological activity of dimers of oxymorphone and enkephalin: possible role of receptor cross-linking Biochem. Biophys. Res. Commun. 104 1982 347 353
    • (1982) Biochem. Biophys. Res. Commun. , vol.104 , pp. 347-353
    • Hazum, E.1    Chang, K.J.2    Leighton, H.J.3    Lever Jr., O.W.4    Cuatrecasas, P.5
  • 62
    • 0022338628 scopus 로고
    • Gonadotropin releasing hormone activation is mediated by dimerization of occupied receptors
    • E. Hazum, and D. Keinan Gonadotropin releasing hormone activation is mediated by dimerization of occupied receptors Biochem. Biophys. Res. Commun. 133 1985 449 456
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 449-456
    • Hazum, E.1    Keinan, D.2
  • 63
    • 0037169345 scopus 로고    scopus 로고
    • Regulation of opioid receptor trafficking and morphine tolerance by receptor oligomerization
    • L. He, J. Fong, M. von Zastrow, and J.L. Whistler Regulation of opioid receptor trafficking and morphine tolerance by receptor oligomerization Cell 108 2002 271 282
    • (2002) Cell , vol.108 , pp. 271-282
    • He, L.1    Fong, J.2    Von Zastrow, M.3    Whistler, J.L.4
  • 64
    • 0032519493 scopus 로고    scopus 로고
    • Functional rescue of a constitutively desensitized beta2AR through receptor dimerization
    • T.E. Hebert, T.P. Loisel, L. Adam, N. Ethier, S.S. Onge, and M. Bouvier Functional rescue of a constitutively desensitized beta2AR through receptor dimerization Biochem. J. 330 Pt 1 1998 287 293
    • (1998) Biochem. J. , vol.330 , Issue.1 , pp. 287-293
    • Hebert, T.E.1    Loisel, T.P.2    Adam, L.3    Ethier, N.4    Onge, S.S.5    Bouvier, M.6
  • 65
    • 0029666267 scopus 로고    scopus 로고
    • A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
    • T.E. Hebert, S. Moffett, J.P. Morello, T.P. Loisel, D.G. Bichet, C. Barret, and M. Bouvier 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
    • Hebert, T.E.1    Moffett, S.2    Morello, J.P.3    Loisel, T.P.4    Bichet, D.G.5    Barret, C.6    Bouvier, M.7
  • 66
    • 0021165094 scopus 로고
    • The hepatic glucagon receptor. Solubilization, characterization, and development of an affinity adsorption assay for the soluble receptor
    • J.T. Herberg, J. Codina, K.A. Rich, F.J. Rojas, and R. Iyengar The hepatic glucagon receptor. Solubilization, characterization, and development of an affinity adsorption assay for the soluble receptor J. Biol. Chem. 259 1984 9285 9294
    • (1984) J. Biol. Chem. , vol.259 , pp. 9285-9294
    • Herberg, J.T.1    Codina, J.2    Rich, K.A.3    Rojas, F.J.4    Iyengar, R.5
  • 69
    • 0035002343 scopus 로고    scopus 로고
    • Binding of agonist but not antagonist leads to fluorescence resonance energy transfer between intrinsically fluorescent gonadotropin-releasing hormone receptors
    • R.D. Horvat, D.A. Roess, S.E. Nelson, B.G. Barisas, and C.M. Clay Binding of agonist but not antagonist leads to fluorescence resonance energy transfer between intrinsically fluorescent gonadotropin-releasing hormone receptors Mol. Endocrinol. 15 2001 695 703
    • (2001) Mol. Endocrinol. , vol.15 , pp. 695-703
    • Horvat, R.D.1    Roess, D.A.2    Nelson, S.E.3    Barisas, B.G.4    Clay, C.M.5
  • 70
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • S.M. Hurtley, and A. Helenius Protein oligomerization in the endoplasmic reticulum Annu. Rev. Cell. Biol. 5 1989 277 307
    • (1989) Annu. Rev. Cell. Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 71
    • 0037144581 scopus 로고    scopus 로고
    • Constitutive agonist-independent CCR5 oligomerization and antibody- mediated clustering occurring at physiological levels of receptors
    • H. Issafras, S. Angers, S. Bulenger, C. Blanpain, M. Parmentier, C. Labbe-Jullie, M. Bouvier, and S. Marullo Constitutive agonist-independent CCR5 oligomerization and antibody- mediated clustering occurring at physiological levels of receptors J. Biol. Chem. 277 2002 34666 34673
    • (2002) J. Biol. Chem. , vol.277 , pp. 34666-34673
    • Issafras, H.1    Angers, S.2    Bulenger, S.3    Blanpain, C.4    Parmentier, M.5    Labbe-Jullie, C.6    Bouvier, M.7    Marullo, S.8
  • 72
    • 0036415131 scopus 로고    scopus 로고
    • Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET)
    • A.A. Jensen, J.L. Hansen, S.P. Sheikh, and H. Brauner-Osborne Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET) Eur. J. Biochem. 269 2002 5076 5087
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5076-5087
    • Jensen, A.A.1    Hansen, J.L.2    Sheikh, S.P.3    Brauner-Osborne, H.4
  • 74
    • 0033578005 scopus 로고    scopus 로고
    • G-protein-coupled receptor heterodimerization modulates receptor function
    • B.A. Jordan, and L.A. Devi G-protein-coupled receptor heterodimerization modulates receptor function Nature 399 1999 697 700
    • (1999) Nature , vol.399 , pp. 697-700
    • Jordan, B.A.1    Devi, L.A.2
  • 75
    • 0035793079 scopus 로고    scopus 로고
    • Oligomerization of opioid receptors with beta 2-adrenergic receptors: A role in trafficking and mitogen-activated protein kinase activation
    • B.A. Jordan, N. Trapaidze, I. Gomes, R. Nivarthi, and L.A. Devi Oligomerization of opioid receptors with beta 2-adrenergic receptors: a role in trafficking and mitogen-activated protein kinase activation Proc. Natl. Acad. Sci. USA 98 2001 343 348
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 343-348
    • Jordan, B.A.1    Trapaidze, N.2    Gomes, I.3    Nivarthi, R.4    Devi, L.A.5
  • 76
    • 0033798153 scopus 로고    scopus 로고
    • The dopamine D3 receptor interacts with itself and the truncated D3 splice variant d3nf: D3-D3nf interaction causes mislocalization of D3 receptors
    • K.D. Karpa, R. Lin, N. Kabbani, and R. Levenson The dopamine D3 receptor interacts with itself and the truncated D3 splice variant d3nf: D3-D3nf interaction causes mislocalization of D3 receptors Mol. Pharmacol. 58 2000 677 683
    • (2000) Mol. Pharmacol. , vol.58 , pp. 677-683
    • Karpa, K.D.1    Lin, R.2    Kabbani, N.3    Levenson, R.4
  • 78
    • 1342332090 scopus 로고    scopus 로고
    • Mutant frizzled 4 associated with vitreoretinopathy traps wild-type frizzled in the endoplasmic reticulum by oligomerization
    • A. Kaykas, J. Yang-Snyder, M. Heroux, K.V. Shah, M. Bouvier, and R.T. Moon Mutant frizzled 4 associated with vitreoretinopathy traps wild-type frizzled in the endoplasmic reticulum by oligomerization Nat. Cell. Biol. 6 2004 52 58
    • (2004) Nat. Cell. Biol. , vol.6 , pp. 52-58
    • Kaykas, A.1    Yang-Snyder, J.2    Heroux, M.3    Shah, K.V.4    Bouvier, M.5    Moon, R.T.6
  • 79
    • 0041315589 scopus 로고    scopus 로고
    • C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G-protein-coupled receptor
    • J.M. Klco, T.B. Lassere, and T.J. Baranski C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G-protein-coupled receptor J. Biol. Chem. 278 2003 35345 35353
    • (2003) J. Biol. Chem. , vol.278 , pp. 35345-35353
    • Klco, J.M.1    Lassere, T.B.2    Baranski, T.J.3
  • 80
    • 0035918215 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer
    • K.M. Kroeger, A.C. Hanyaloglu, R.M. Seeber, L.E. Miles, and K.A. Eidne Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer J. Biol. Chem. 276 2001 12736 12743
    • (2001) J. Biol. Chem. , vol.276 , pp. 12736-12743
    • Kroeger, K.M.1    Hanyaloglu, A.C.2    Seeber, R.M.3    Miles, L.E.4    Eidne, K.A.5
  • 84
    • 0035976910 scopus 로고    scopus 로고
    • Oligomerization of the human thyrotropin receptor: Fluorescent protein-tagged hTSHR reveals post-translational complexes
    • R. Latif, P. Graves, and T.F. Davies Oligomerization of the human thyrotropin receptor: fluorescent protein-tagged hTSHR reveals post-translational complexes J. Biol. Chem. 276 2001 45217 45224
    • (2001) J. Biol. Chem. , vol.276 , pp. 45217-45224
    • Latif, R.1    Graves, P.2    Davies, T.F.3
  • 85
    • 0037160035 scopus 로고    scopus 로고
    • Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor
    • R. Latif, P. Graves, and T.F. Davies Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor J. Biol. Chem. 277 2002 45059 45067
    • (2002) J. Biol. Chem. , vol.277 , pp. 45059-45067
    • Latif, R.1    Graves, P.2    Davies, T.F.3
  • 86
    • 0037307486 scopus 로고    scopus 로고
    • Pharmacological characterization of putative beta1-beta2-adrenergic receptor heterodimers
    • C. Lavoie, and T.E. Hebert 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    Hebert, T.E.2
  • 90
    • 0033924207 scopus 로고    scopus 로고
    • Inhibition of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell
    • S.P. Lee, B.F. O'Dowd, G.Y. Ng, G. Varghese, H. Akil, A. Mansour, T. Nguyen, and S.R. George Inhibition of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell Mol. Pharmacol. 58 2000 120 128
    • (2000) Mol. Pharmacol. , vol.58 , pp. 120-128
    • Lee, S.P.1    O'Dowd, B.F.2    Ng, G.Y.3    Varghese, G.4    Akil, H.5    Mansour, A.6    Nguyen, T.7    George, S.R.8
  • 91
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G-protein-coupled receptors rhodopsin and opsin in native membranes
    • Y. Liang, D. Fotiadis, S. Filipek, D.A. Saperstein, K. Palczewski, and A. Engel Organization of the G-protein-coupled receptors rhodopsin and opsin in native membranes J. Biol. Chem. 278 2003 21655 21662
    • (2003) J. Biol. Chem. , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 92
    • 0017190266 scopus 로고
    • Negative cooperativity among beta-adrenergic receptors in frog erythrocyte membranes
    • L.E. Limbird, and R.J. Lefkowitz Negative cooperativity among beta-adrenergic receptors in frog erythrocyte membranes J. Biol. Chem. 251 1976 5007 5014
    • (1976) J. Biol. Chem. , vol.251 , pp. 5007-5014
    • Limbird, L.E.1    Lefkowitz, R.J.2
  • 94
    • 1942469528 scopus 로고    scopus 로고
    • Molecular determinants involved in the allosteric control of agonist affinity in the GABAB receptor by the GABAB2 subunit
    • J. Liu, D. Maurel, S. Etzol, I. Brabet, H. Ansanay, J.P. Pin, and P. Rondard Molecular determinants involved in the allosteric control of agonist affinity in the GABAB receptor by the GABAB2 subunit J. Biol. Chem. 279 2004 15824 15830
    • (2004) J. Biol. Chem. , vol.279 , pp. 15824-15830
    • Liu, J.1    Maurel, D.2    Etzol, S.3    Brabet, I.4    Ansanay, H.5    Pin, J.P.6    Rondard, P.7
  • 96
    • 0033667466 scopus 로고    scopus 로고
    • A trafficking checkpoint controls GABA(B) receptor heterodimerization
    • M. Margeta-Mitrovic, Y.N. Jan, and L.Y. Jan A trafficking checkpoint controls GABA(B) receptor heterodimerization Neuron 27 2000 97 106
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 97
    • 0035958023 scopus 로고    scopus 로고
    • Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy
    • M. McVey, D. Ramsay, E. Kellett, S. Rees, S. Wilson, A.J. Pope, and G. Milligan Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy J. Biol. Chem. 276 2001 14092 14099
    • (2001) J. Biol. Chem. , vol.276 , pp. 14092-14099
    • McVey, M.1    Ramsay, D.2    Kellett, E.3    Rees, S.4    Wilson, S.5    Pope, A.J.6    Milligan, G.7
  • 99
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • J.F. Mercier, A. Salahpour, S. Angers, A. Breit, and M. Bouvier Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer J. Biol. Chem. 277 2002 44925 44931
    • (2002) J. Biol. Chem. , vol.277 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 100
    • 0033916687 scopus 로고    scopus 로고
    • From agonist to antagonist: Fab fragments of an agonist-like monoclonal anti-beta (2)-adrenoceptor antibody behave as antagonists
    • A. Mijares, D. Lebesgue, G. Wallukat, and J. Hoebeke From agonist to antagonist: fab fragments of an agonist-like monoclonal anti-beta (2)-adrenoceptor antibody behave as antagonists Mol. Pharmacol. 58 2000 373 379
    • (2000) Mol. Pharmacol. , vol.58 , pp. 373-379
    • Mijares, A.1    Lebesgue, D.2    Wallukat, G.3    Hoebeke, J.4
  • 101
    • 0030028756 scopus 로고    scopus 로고
    • Polar residues in the transmembrane domains of the type 1 angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by co-expression of two deficient mutants
    • C. Monnot, C. Bihoreau, S. Conchon, K.M. Curnow, P. Corvol, and E. Clauser Polar residues in the transmembrane domains of the type 1 angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by co-expression of two deficient mutants J. Biol. Chem. 271 1996 1507 1513
    • (1996) J. Biol. Chem. , vol.271 , pp. 1507-1513
    • Monnot, C.1    Bihoreau, C.2    Conchon, S.3    Curnow, K.M.4    Corvol, P.5    Clauser, E.6
  • 106
    • 0030613635 scopus 로고    scopus 로고
    • Expression of dopamine D3 receptor dimers and tetramers in brain and in transfected cells
    • E.A. Nimchinsky, P.R. Hof, W.G. Janssen, J.H. Morrison, and C. Schmauss Expression of dopamine D3 receptor dimers and tetramers in brain and in transfected cells J. Biol. Chem. 272 1997 29229 29237
    • (1997) J. Biol. Chem. , vol.272 , pp. 29229-29237
    • Nimchinsky, E.A.1    Hof, P.R.2    Janssen, W.G.3    Morrison, J.H.4    Schmauss, C.5
  • 107
    • 1542379979 scopus 로고    scopus 로고
    • The paired activation of the two components of the muscarinic M3 receptor dimer is required for induction of ERK1/2 phosphorylation
    • F. Novi, M. Scarselli, G.U. Corsini, and R. Maggio The paired activation of the two components of the muscarinic M3 receptor dimer is required for induction of ERK1/2 phosphorylation J. Biol. Chem. 2003
    • (2003) J. Biol. Chem.
    • Novi, F.1    Scarselli, M.2    Corsini, G.U.3    Maggio, R.4
  • 108
    • 0034704906 scopus 로고    scopus 로고
    • G-protein-coupled receptors function as oligomers in vivo
    • M.C. Overton, and K.J. Blumer G-protein-coupled receptors function as oligomers in vivo Curr. Biol. 10 2000 341 344
    • (2000) Curr. Biol. , vol.10 , pp. 341-344
    • Overton, M.C.1    Blumer, K.J.2
  • 109
    • 0036829815 scopus 로고    scopus 로고
    • The extracellular N-terminal domain and transmembrane domains 1 and 2 mediate oligomerization of a yeast G-protein-coupled receptor
    • M.C. Overton, and K.J. Blumer The extracellular N-terminal domain and transmembrane domains 1 and 2 mediate oligomerization of a yeast G-protein-coupled receptor J. Biol. Chem. 277 2002 41463 41472
    • (2002) J. Biol. Chem. , vol.277 , pp. 41463-41472
    • Overton, M.C.1    Blumer, K.J.2
  • 110
    • 1542467519 scopus 로고    scopus 로고
    • Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G-protein-coupled receptor
    • M.C. Overton, S.L. Chinault, and K.J. Blumer Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G-protein-coupled receptor J. Biol. Chem. 278 2003 49369 49377
    • (2003) J. Biol. Chem. , vol.278 , pp. 49369-49377
    • Overton, M.C.1    Chinault, S.L.2    Blumer, K.J.3
  • 112
    • 0019935990 scopus 로고
    • Covalent cross-linking of angiotensin II to its binding sites in rat adrenal membranes
    • S. Paglin, and J.D. Jamieson Covalent cross-linking of angiotensin II to its binding sites in rat adrenal membranes Proc. Natl. Acad. Sci. USA 79 1982 3739 3743
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3739-3743
    • Paglin, S.1    Jamieson, J.D.2
  • 113
    • 0036387204 scopus 로고    scopus 로고
    • Dimerization of morphine and orphanin FQ/nociceptin receptors: Generation of a novel opioid receptor subtype
    • Y.X. Pan, E. Bolan, and G.W. Pasternak Dimerization of morphine and orphanin FQ/nociceptin receptors: generation of a novel opioid receptor subtype Biochem. Biophys. Res. Commun. 297 2002 659 663
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 659-663
    • Pan, Y.X.1    Bolan, E.2    Pasternak, G.W.3
  • 114
    • 0035370058 scopus 로고    scopus 로고
    • Nature of the oligomers formed by muscarinic m2 acetylcholine receptors in Sf9 cells
    • P. Park, C.S. Sum, D.R. Hampson, H.H. Van Tol, and J.W. Wells Nature of the oligomers formed by muscarinic m2 acetylcholine receptors in Sf9 cells Eur. J. Pharmacol. 421 2001 11 22
    • (2001) Eur. J. Pharmacol. , vol.421 , pp. 11-22
    • Park, P.1    Sum, C.S.2    Hampson, D.R.3    Van Tol, H.H.4    Wells, J.W.5
  • 115
    • 0037197663 scopus 로고    scopus 로고
    • Cooperativity and oligomeric status of cardiac muscarinic cholinergic receptors
    • P.S. Park, C.S. Sum, A.B. Pawagi, and J.W. Wells Cooperativity and oligomeric status of cardiac muscarinic cholinergic receptors Biochemistry 41 2002 5588 5604
    • (2002) Biochemistry , vol.41 , pp. 5588-5604
    • Park, P.S.1    Sum, C.S.2    Pawagi, A.B.3    Wells, J.W.4
  • 117
    • 0036385623 scopus 로고    scopus 로고
    • Photobleaching fluorescence resonance energy transfer reveals ligand-induced oligomer formation of human somatostatin receptor subtypes
    • R.C. Patel, D.C. Lange, and Y.C. Patel Photobleaching fluorescence resonance energy transfer reveals ligand-induced oligomer formation of human somatostatin receptor subtypes Methods 27 2002 340 348
    • (2002) Methods , vol.27 , pp. 340-348
    • Patel, R.C.1    Lange, D.C.2    Patel, Y.C.3
  • 118
    • 0041845294 scopus 로고    scopus 로고
    • Agonist-independent desensitization and internalization of the human platelet-activating factor receptor by coumermycin-gyrase B-induced dimerization
    • A. Perron, Z.G. Chen, D. Gingras, D.J. Dupre, J. Stankova, and M. Rola-Pleszczynski Agonist-independent desensitization and internalization of the human platelet-activating factor receptor by coumermycin-gyrase B-induced dimerization J. Biol. Chem. 278 2003 27956 27965
    • (2003) J. Biol. Chem. , vol.278 , pp. 27956-27965
    • Perron, A.1    Chen, Z.G.2    Gingras, D.3    Dupre, D.J.4    Stankova, J.5    Rola-Pleszczynski, M.6
  • 120
    • 0035830863 scopus 로고    scopus 로고
    • Newly synthesized human delta opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome
    • U.E. Petaja-Repo, M. Hogue, A. Laperriere, S. Bhalla, P. Walker, and M. Bouvier Newly synthesized human delta opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome J. Biol. Chem. 276 2001 4416 4423
    • (2001) J. Biol. Chem. , vol.276 , pp. 4416-4423
    • Petaja-Repo, U.E.1    Hogue, M.2    Laperriere, A.3    Bhalla, S.4    Walker, P.5    Bouvier, M.6
  • 121
    • 0034607918 scopus 로고    scopus 로고
    • Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor
    • U.E. Petaja-Repo, M. Hogue, A. Laperriere, P. Walker, and M. Bouvier Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor J. Biol. Chem. 275 2000 13727 13736
    • (2000) J. Biol. Chem. , vol.275 , pp. 13727-13736
    • Petaja-Repo, U.E.1    Hogue, M.2    Laperriere, A.3    Walker, P.4    Bouvier, M.5
  • 122
    • 0022536212 scopus 로고
    • Physical properties of the purified cardiac muscarinic acetylcholine receptor
    • G.L. Peterson, L.C. Rosenbaum, D.J. Broderick, and M.I. Schimerlik Physical properties of the purified cardiac muscarinic acetylcholine receptor Biochemistry 25 1986 3189 3202
    • (1986) Biochemistry , vol.25 , pp. 3189-3202
    • Peterson, G.L.1    Rosenbaum, L.C.2    Broderick, D.J.3    Schimerlik, M.I.4
  • 123
    • 0035958027 scopus 로고    scopus 로고
    • Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A)
    • M. Pfeiffer, T. Koch, H. Schroder, M. Klutzny, S. Kirscht, H.J. Kreienkamp, V. Hollt, and S. Schulz Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A) J. Biol. Chem. 276 2001 14027 14036
    • (2001) J. Biol. Chem. , vol.276 , pp. 14027-14036
    • Pfeiffer, M.1    Koch, T.2    Schroder, H.3    Klutzny, M.4    Kirscht, S.5    Kreienkamp, H.J.6    Hollt, V.7    Schulz, S.8
  • 124
    • 0037205489 scopus 로고    scopus 로고
    • Heterodimerization of somatostatin and opioid receptors cross-modulates phosphorylation, internalization, and desensitization
    • M. Pfeiffer, T. Koch, H. Schroder, M. Laugsch, V. Hollt, and S. Schulz Heterodimerization of somatostatin and opioid receptors cross-modulates phosphorylation, internalization, and desensitization J. Biol. Chem. 277 2002 19762 19772
    • (2002) J. Biol. Chem. , vol.277 , pp. 19762-19772
    • Pfeiffer, M.1    Koch, T.2    Schroder, H.3    Laugsch, M.4    Hollt, V.5    Schulz, S.6
  • 125
    • 0037101774 scopus 로고    scopus 로고
    • Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): Hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences
    • D. Ramsay, E. Kellett, M. McVey, S. Rees, and G. Milligan Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than between less closely related sequences Biochem. J. 365 2002 429 440
    • (2002) Biochem. J. , vol.365 , pp. 429-440
    • Ramsay, D.1    Kellett, E.2    McVey, M.3    Rees, S.4    Milligan, G.5
  • 126
    • 0033600911 scopus 로고    scopus 로고
    • Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization Implications for function of monomeric Ca(2+) receptor
    • K. Ray, B.C. Hauschild, P.J. Steinbach, P.K. Goldsmith, O. Hauache, and A.M. Spiegel Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization Implications for function of monomeric Ca(2+) receptor J. Biol. Chem. 274 1999 27642 27650
    • (1999) J. Biol. Chem. , vol.274 , pp. 27642-27650
    • Ray, K.1    Hauschild, B.C.2    Steinbach, P.J.3    Goldsmith, P.K.4    Hauache, O.5    Spiegel, A.M.6
  • 128
    • 0034616021 scopus 로고    scopus 로고
    • Receptors for dopamine and somatostatin: Formation of hetero-oligomers with enhanced functional activity
    • M. Rocheville, D.C. Lange, U. Kumar, S.C. Patel, R.C. Patel, and Y.C. Patel Receptors for dopamine and somatostatin: formation of hetero-oligomers with enhanced functional activity Science 288 2000 154 157
    • (2000) Science , vol.288 , pp. 154-157
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Patel, S.C.4    Patel, R.C.5    Patel, Y.C.6
  • 129
    • 0034677745 scopus 로고    scopus 로고
    • Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers
    • M. Rocheville, D.C. Lange, U. Kumar, R. Sasi, R.C. Patel, and Y.C. Patel Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers J. Biol. Chem. 275 2000 7862 7869
    • (2000) J. Biol. Chem. , vol.275 , pp. 7862-7869
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Sasi, R.4    Patel, R.C.5    Patel, Y.C.6
  • 132
    • 0021265101 scopus 로고
    • High affinity angiotensin II receptors in myocardial sarcolemmal membranes. Characterization of receptors and covalent linkage of 125I-angiotensin II to a membrane component of 116,000 daltons
    • T.B. Rogers High affinity angiotensin II receptors in myocardial sarcolemmal membranes. Characterization of receptors and covalent linkage of 125I-angiotensin II to a membrane component of 116,000 daltons. J. Biol. Chem. 259 1984 8106 8114
    • (1984) J. Biol. Chem. , vol.259 , pp. 8106-8114
    • Rogers, T.B.1
  • 133
    • 0029903640 scopus 로고    scopus 로고
    • Metabotropic glutamate receptor 5 is a disulfide-linked dimer
    • C. Romano, W.L. Yang, and K.L. O'Malley Metabotropic glutamate receptor 5 is a disulfide-linked dimer J. Biol. Chem. 271 1996 28612 28616
    • (1996) J. Biol. Chem. , vol.271 , pp. 28612-28616
    • Romano, C.1    Yang, W.L.2    O'Malley, K.L.3
  • 134
    • 0025339135 scopus 로고
    • Hydrodynamic properties of the angiotensin II receptor from bovine adrenal zona glomerulosa
    • J.J. Rondeau, N. McNicoll, E. Escher, S. Meloche, H. Ong, and A. De Lean Hydrodynamic properties of the angiotensin II receptor from bovine adrenal zona glomerulosa Biochem. J. 268 1990 443 448
    • (1990) Biochem. J. , vol.268 , pp. 443-448
    • Rondeau, J.J.1    McNicoll, N.2    Escher, E.3    Meloche, S.4    Ong, H.5    De Lean, A.6
  • 137
    • 0142038894 scopus 로고    scopus 로고
    • Functional rescue of the inactive splice variant of the dopamine D3 receptor D3nf
    • M. Scarselli, F. Novi, G.U. Corsini, and R. Maggio Functional rescue of the inactive splice variant of the dopamine D3 receptor D3nf. Brain Res. 987 2003 244 247
    • (2003) Brain Res. , vol.987 , pp. 244-247
    • Scarselli, M.1    Novi, F.2    Corsini, G.U.3    Maggio, R.4
  • 138
    • 0034723169 scopus 로고    scopus 로고
    • Structural implication for receptor oligomerization from functional reconstitution studies of mutant V2 vasopressin receptors
    • A. Schulz, R. Grosse, G. Schultz, T. Gudermann, and T. Schoneberg Structural implication for receptor oligomerization from functional reconstitution studies of mutant V2 vasopressin receptors J. Biol. Chem. 275 2000 2381 2389
    • (2000) J. Biol. Chem. , vol.275 , pp. 2381-2389
    • Schulz, A.1    Grosse, R.2    Schultz, G.3    Gudermann, T.4    Schoneberg, T.5
  • 139
    • 0028913136 scopus 로고
    • Fluorescence resonance energy transfer
    • P.R. Selvin Fluorescence resonance energy transfer Methods Enzymol. 246 1995 300 334
    • (1995) Methods Enzymol. , vol.246 , pp. 300-334
    • Selvin, P.R.1
  • 140
    • 0025900323 scopus 로고
    • Solubilization and partial characterization of angiotensin II receptors from rat brain
    • I.R. Siemens, G.N. Swanson, S.J. Fluharty, and J.W. Harding Solubilization and partial characterization of angiotensin II receptors from rat brain J. Neurochem. 57 1991 690 700
    • (1991) J. Neurochem. , vol.57 , pp. 690-700
    • Siemens, I.R.1    Swanson, G.N.2    Fluharty, S.J.3    Harding, J.W.4
  • 141
    • 1242274647 scopus 로고    scopus 로고
    • Heterodimerization of V1a and V2 vasopressin receptors determines the interaction with beta-arrestin and their trafficking patterns
    • S. Terrillon, C. Barberis, and M. Bouvier Heterodimerization of V1a and V2 vasopressin receptors determines the interaction with beta-arrestin and their trafficking patterns Proc. Natl. Acad. Sci. USA 101 2004 1548 1553
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1548-1553
    • Terrillon, S.1    Barberis, C.2    Bouvier, M.3
  • 142
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • S. Terrillon, and M. Bouvier 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
  • 147
    • 0037162063 scopus 로고    scopus 로고
    • Homodimerization and heterodimerization of S1P/EDG sphingosine-1- phosphate receptors
    • J.R. Van Brocklyn, B. Behbahani, and N.H. Lee Homodimerization and heterodimerization of S1P/EDG sphingosine-1-phosphate receptors Biochim. Biophys. Acta 1582 2002 89 93
    • (2002) Biochim. Biophys. Acta , vol.1582 , pp. 89-93
    • Van Brocklyn, J.R.1    Behbahani, B.2    Lee, N.H.3
  • 152
    • 0029083945 scopus 로고
    • Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors
    • K.A. Wreggett, and J.W. Wells Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors J. Biol. Chem. 270 1995 22488 22499
    • (1995) J. Biol. Chem. , vol.270 , pp. 22488-22499
    • Wreggett, K.A.1    Wells, J.W.2
  • 153
    • 0032587196 scopus 로고    scopus 로고
    • Serotonin 5-HT1B and 5-HT1D receptors form homodimers when expressed alone and heterodimers when co-expressed
    • Z. Xie, S.P. Lee, B.F. O'Dowd, and S.R. George Serotonin 5-HT1B and
    • (1999) FEBS Lett. , vol.456 , pp. 63-67
    • Xie, Z.1    Lee, S.P.2    O'Dowd, B.F.3    George, S.R.4
  • 154
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Y. Xu, D.W. Piston, and C.H. Johnson A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins Proc. Natl. Acad. Sci. USA 96 1999 151 156
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 155
    • 0035912846 scopus 로고    scopus 로고
    • Heteromeric association creates a P2Y-like adenosine receptor
    • K. Yoshioka, O. Saitoh, and H. Nakata Heteromeric association creates a P2Y-like adenosine receptor Proc. Natl. Acad. Sci. USA 98 2001 7617 7622
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7617-7622
    • Yoshioka, K.1    Saitoh, O.2    Nakata, H.3
  • 156
    • 0037125187 scopus 로고    scopus 로고
    • Agonist-promoted heteromeric oligomerization between adenosine A(1) and P2Y(1) receptors in living cells
    • K. Yoshioka, O. Saitoh, and H. Nakata Agonist-promoted heteromeric oligomerization between adenosine A(1) and P2Y(1) receptors in living cells FEBS Lett. 523 2002 147 151
    • (2002) FEBS Lett. , vol.523 , pp. 147-151
    • Yoshioka, K.1    Saitoh, O.2    Nakata, H.3
  • 158
    • 0033516576 scopus 로고    scopus 로고
    • Identification and molecular characterization of m3 muscarinic receptor dimers
    • F.Y. Zeng, and J. Wess Identification and molecular characterization of m3 muscarinic receptor dimers J. Biol. Chem. 274 1999 19487 19497
    • (1999) J. Biol. Chem. , vol.274 , pp. 19487-19497
    • Zeng, F.Y.1    Wess, J.2
  • 159
    • 0032506160 scopus 로고    scopus 로고
    • Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function
    • X. Zhu, and J. Wess Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function Biochemistry 37 1998 15773 15784
    • (1998) Biochemistry , vol.37 , pp. 15773-15784
    • Zhu, X.1    Wess, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.