메뉴 건너뛰기




Volumn 9, Issue 3, 2009, Pages 329-339

Oligomerization of the heptahelical G protein coupling receptors: A case for association using transmembrane helices

Author keywords

Receptor heterodimer; Receptor homodimer; Receptor oligomer; Rhodopsin like receptor; Signal transduction

Indexed keywords

CELL ENZYME; G PROTEIN COUPLED RECEPTOR; HETERODIMER; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; HOMODIMER; MEMBRANE PROTEIN; MONOMER; OLIGOMER; PROTEINASE; PROTEIN SUBUNIT;

EID: 65349135865     PISSN: 13895575     EISSN: None     Source Type: Journal    
DOI: 10.2174/1389557510909030329     Document Type: Article
Times cited : (8)

References (147)
  • 1
    • 0027193530 scopus 로고
    • Sequence homology between bacteriorhodopsin and G-protein coupled receptors: Exon shuffling or evolution by duplication?
    • Taylor, E.W.; Agarwal, A. Sequence homology between bacteriorhodopsin and G-protein coupled receptors: exon shuffling or evolution by duplication? FEBS Lett., 1993, 325, 161-6.
    • (1993) FEBS Lett , vol.325 , pp. 161-166
    • Taylor, E.W.1    Agarwal, A.2
  • 2
    • 33645020555 scopus 로고    scopus 로고
    • Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved
    • Lin, X.; Tan, S.M.; Law, S.K.; Torres, J. Two types of transmembrane homomeric interactions in the integrin receptor family are evolutionarily conserved. Proteins, 2006, 63, 16-23.
    • (2006) Proteins , vol.63 , pp. 16-23
    • Lin, X.1    Tan, S.M.2    Law, S.K.3    Torres, J.4
  • 3
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • Senes, A.; Gerstein, M.; Engelman, D.M. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions. J. Mol. Biol., 2000, 296, 921-36.
    • (2000) J. Mol. Biol , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 4
    • 21344467203 scopus 로고    scopus 로고
    • The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics
    • Filizola, M.; Weinstein, H. The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics. FEBS J., 2005, 272, 2926-38.
    • (2005) FEBS J , vol.272 , pp. 2926-2938
    • Filizola, M.1    Weinstein, H.2
  • 5
    • 33645796458 scopus 로고    scopus 로고
    • Ago-allosteric modulation and other types of allostery in dimeric 7TM receptors
    • Schwartz, T.W.; Holst, B. Ago-allosteric modulation and other types of allostery in dimeric 7TM receptors. J. Recept. Signal Transduct., 2006, 26, 107-28.
    • (2006) J. Recept. Signal Transduct , vol.26 , pp. 107-128
    • Schwartz, T.W.1    Holst, B.2
  • 6
    • 34548151596 scopus 로고    scopus 로고
    • Molecular mechanisms involved in vasoactive intestinal peptide receptor activation and regulation: Current knowledge, similarities to and differences from the A family of G-protein-coupled receptors
    • Langer, I.; Robberecht, P. Molecular mechanisms involved in vasoactive intestinal peptide receptor activation and regulation: current knowledge, similarities to and differences from the A family of G-protein-coupled receptors. Biochem. Soc. Trans., 2007, 35, 724-8.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 724-728
    • Langer, I.1    Robberecht, P.2
  • 7
    • 36448968578 scopus 로고    scopus 로고
    • Allosteric modulation of heterodimeric G-protein-coupled receptors
    • Milligan, G.; Smith, N.J. Allosteric modulation of heterodimeric G-protein-coupled receptors. Trends Pharmacol. Sci., 2007, 28, 615-20.
    • (2007) Trends Pharmacol. Sci , vol.28 , pp. 615-620
    • Milligan, G.1    Smith, N.J.2
  • 9
    • 30444435782 scopus 로고    scopus 로고
    • Heterotrimeric G-proteins: A short history
    • Milligan, G.; Kostenis, E. Heterotrimeric G-proteins: a short history. Br. J. Pharmacol., 2006, 147(Suppl 1), S46-55.
    • (2006) Br. J. Pharmacol , vol.147 , Issue.SUPPL. 1
    • Milligan, G.1    Kostenis, E.2
  • 11
    • 50549102892 scopus 로고    scopus 로고
    • Importance of a N-terminal aspartate in the internalization of the neuropeptide Y Y2 receptor
    • Parker, S.L.; Parker, M.S.; Wong, Y.Y.; Sah, R.; Balasubramaniam, A.; Sallee, F. Importance of a N-terminal aspartate in the internalization of the neuropeptide Y Y2 receptor. Eur. J. Pharmacol., 2008, 594, 26-31.
    • (2008) Eur. J. Pharmacol , vol.594 , pp. 26-31
    • Parker, S.L.1    Parker, M.S.2    Wong, Y.Y.3    Sah, R.4    Balasubramaniam, A.5    Sallee, F.6
  • 12
    • 0021329612 scopus 로고
    • Rat pineal alpha 1-adrenoceptors: Identification and characterization using [125]Iiodo-2-[beta-(4-hydroxyphenyl)-ethylaminomethyltetralone
    • Sugden, D.; Klein, D.C. Rat pineal alpha 1-adrenoceptors: identification and characterization using [125]Iiodo-2-[beta-(4-hydroxyphenyl)-ethylaminomethyltetralone. Endocrinology, 1984, 114, 435-40.
    • (1984) Endocrinology , vol.114 , pp. 435-440
    • Sugden, D.1    Klein, D.C.2
  • 13
    • 0024808143 scopus 로고
    • Y2-type receptors for peptide YY on renal proximal tubular cells in the rabbit
    • Sheikh, S.P.; Sheikh, M.I.; Schwartz, T.W. Y2-type receptors for peptide YY on renal proximal tubular cells in the rabbit. Am. J. Physiol., 1989, 257, F978-84.
    • (1989) Am. J. Physiol , vol.257
    • Sheikh, S.P.1    Sheikh, M.I.2    Schwartz, T.W.3
  • 14
    • 17844400914 scopus 로고    scopus 로고
    • The repertoire of G-protein-coupled receptors in fully sequenced genomes
    • Fredriksson, R.; Schioth, H.B. The repertoire of G-protein-coupled receptors in fully sequenced genomes. Mol. Pharmacol., 2005, 67, 1414-25.
    • (2005) Mol. Pharmacol , vol.67 , pp. 1414-1425
    • Fredriksson, R.1    Schioth, H.B.2
  • 15
    • 33846589324 scopus 로고    scopus 로고
    • Consequences of over-expression of rat Scavenger Receptor, SR-BI, in an adrenal cell model
    • Reaven, E.; Nomoto, A.; Cortez, Y.; Azhar, S. Consequences of over-expression of rat Scavenger Receptor, SR-BI, in an adrenal cell model. Nutr. Metab. (London), 2006, 3, 43.
    • (2006) Nutr. Metab. (London) , vol.3 , pp. 43
    • Reaven, E.1    Nomoto, A.2    Cortez, Y.3    Azhar, S.4
  • 16
    • 33645902491 scopus 로고    scopus 로고
    • Alpha2A- and alpha2C-adrenergic receptors form homo- and heterodimers: The heterodimeric state impairs agonist-promoted GRK phosphorylation and beta-arrestin recruitment
    • Small, K.M.; Schwarb, M.R.; Glinka, C.; Theiss, C.T.; Brown, K.M.; Seman, C.A.; Liggett, S.B. Alpha2A- and alpha2C-adrenergic receptors form homo- and heterodimers: the heterodimeric state impairs agonist-promoted GRK phosphorylation and beta-arrestin recruitment. Biochemistry, 2006, 45, 4760-7.
    • (2006) Biochemistry , vol.45 , pp. 4760-4767
    • Small, K.M.1    Schwarb, M.R.2    Glinka, C.3    Theiss, C.T.4    Brown, K.M.5    Seman, C.A.6    Liggett, S.B.7
  • 17
    • 0034724192 scopus 로고    scopus 로고
    • Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers, S.; Salahpour, A.; Joly, E.; Hilairet, S.; Chelsky, D.; Dennis, M.; Bouvier, M. Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci., USA, 2000, 97, 3684-9.
    • (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
  • 19
    • 3342934656 scopus 로고    scopus 로고
    • High-affinity interactions between human alpha1A-adrenoceptor C-terminal splice variants produce homo- and heterodimers but do not generate the alpha1Ladrenoceptor
    • Ramsay, D.; Carr, I.C.; Pediani, J.; Lopez-Gimenez, J.F.; Thurlow, R.; Fidock, M.; Milligan, G. High-affinity interactions between human alpha1A-adrenoceptor C-terminal splice variants produce homo- and heterodimers but do not generate the alpha1Ladrenoceptor. Mol. Pharmacol., 2004, 66, 228-39.
    • (2004) Mol. Pharmacol , vol.66 , pp. 228-239
    • Ramsay, D.1    Carr, I.C.2    Pediani, J.3    Lopez-Gimenez, J.F.4    Thurlow, R.5    Fidock, M.6    Milligan, G.7
  • 20
    • 33746217413 scopus 로고    scopus 로고
    • Oligomerization of recombinant and endogenously expressed human histamine H(4) receptors
    • van Rijn, R.M.; Chazot, P.L.; Shenton, F.C.; Sansuk, K.; Bakker, R.A.; Leurs, R. Oligomerization of recombinant and endogenously expressed human histamine H(4) receptors. Mol. Pharmacol., 2006, 70, 604-15.
    • (2006) Mol. Pharmacol , vol.70 , pp. 604-615
    • van Rijn, R.M.1    Chazot, P.L.2    Shenton, F.C.3    Sansuk, K.4    Bakker, R.A.5    Leurs, R.6
  • 21
    • 0035170508 scopus 로고    scopus 로고
    • Collecting and harvesting biological data: The GPCRDB and NucleaRDB information systems
    • Horn, F.; Vriend, G.; Cohen, F.E. Collecting and harvesting biological data: the GPCRDB and NucleaRDB information systems. Nucleic Acids Res., 2001, 29, 346-9.
    • (2001) Nucleic Acids Res , vol.29 , pp. 346-349
    • Horn, F.1    Vriend, G.2    Cohen, F.E.3
  • 22
    • 0037016757 scopus 로고    scopus 로고
    • Very large G protein-coupled receptor-1, the largest known cell surface protein, is highly expressed in the developing central nervous system
    • McMillan, D.R.; Kayes-Wandover, K.M.; Richardson, J.A.; White, P.C. Very large G protein-coupled receptor-1, the largest known cell surface protein, is highly expressed in the developing central nervous system. J. Biol. Chem., 2002, 277, 785-92.
    • (2002) J. Biol. Chem , vol.277 , pp. 785-792
    • McMillan, D.R.1    Kayes-Wandover, K.M.2    Richardson, J.A.3    White, P.C.4
  • 25
    • 0036759170 scopus 로고    scopus 로고
    • No ligand binding in the GB2 subunit of the GABA(B) receptor is required for activation and allosteric interaction between the subunits
    • Kniazeff, J.; Galvez, T.; Labesse, G.; Pin, J.P. No ligand binding in the GB2 subunit of the GABA(B) receptor is required for activation and allosteric interaction between the subunits. J. Neurosci., 2002, 22, 7352-61.
    • (2002) J. Neurosci , vol.22 , pp. 7352-7361
    • Kniazeff, J.1    Galvez, T.2    Labesse, G.3    Pin, J.P.4
  • 27
    • 34548476934 scopus 로고    scopus 로고
    • Critical role for the second extracellular loop in the binding of both orthosteric and allosteric G proteincoupled receptor ligands
    • Avlani, V.A.; Gregory, K.J.; Morton, C.J.; Parker, M.W.; Sexton, P.M.; Christopoulos, A. Critical role for the second extracellular loop in the binding of both orthosteric and allosteric G proteincoupled receptor ligands. J. Biol. Chem., 2007, 282, 25677-86.
    • (2007) J. Biol. Chem , vol.282 , pp. 25677-25686
    • Avlani, V.A.1    Gregory, K.J.2    Morton, C.J.3    Parker, M.W.4    Sexton, P.M.5    Christopoulos, A.6
  • 29
    • 47849133116 scopus 로고    scopus 로고
    • Evidence for a mu-delta opioid receptor complex in CHO cells co-expressing mu and delta opioid peptide receptors
    • Rutherford, J.M.; Wang, J.; Xu, H.; Dersch, C.M.; Partilla, J.S.; Rice, K.C.; Rothman, R.B. Evidence for a mu-delta opioid receptor complex in CHO cells co-expressing mu and delta opioid peptide receptors. Peptides, 2008, 29, 1424-31.
    • (2008) Peptides , vol.29 , pp. 1424-1431
    • Rutherford, J.M.1    Wang, J.2    Xu, H.3    Dersch, C.M.4    Partilla, J.S.5    Rice, K.C.6    Rothman, R.B.7
  • 30
    • 34547434085 scopus 로고    scopus 로고
    • Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit
    • Ernst, O.P.; Gramse, V.; Kolbe, M.; Hofmann, K.P.; Heck, M. Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit. Proc. Natl. Acad. Sci., USA, 2007, 104, 10859-64.
    • (2007) Proc. Natl. Acad. Sci., USA , vol.104 , pp. 10859-10864
    • Ernst, O.P.1    Gramse, V.2    Kolbe, M.3    Hofmann, K.P.4    Heck, M.5
  • 33
    • 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
    • Baneres, J.L.; Parello, J. 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., 2003, 329, 815-29.
    • (2003) J. Mol. Biol , vol.329 , pp. 815-829
    • Baneres, J.L.1    Parello, J.2
  • 34
    • 28444493656 scopus 로고    scopus 로고
    • Crosstalk in G protein-coupled receptors: Changes at the transmembrane homodimer interface determine activation
    • Guo, W.; Shi, L.; Filizola, M.; Weinstein, H.; Javitch, J.A. Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation. Proc. Natl. Acad. Sci., USA, 2005, 102, 17495-500.
    • (2005) Proc. Natl. Acad. Sci., USA , vol.102 , pp. 17495-17500
    • Guo, W.1    Shi, L.2    Filizola, M.3    Weinstein, H.4    Javitch, J.A.5
  • 35
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • Palczewski, K. G protein-coupled receptor rhodopsin. Annu. Rev. Biochem., 2006, 75, 743-67.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 36
    • 3543036363 scopus 로고    scopus 로고
    • Closed state of both binding domains of homodimeric mGlu receptors is required for full activity
    • Kniazeff, J.; Bessis, A.S.; Maurel, D.; Ansanay, H.; Prezeau, L.; Pin, J.P. Closed state of both binding domains of homodimeric mGlu receptors is required for full activity. Nat. Struct. Mol. Biol., 2004, 11, 706-13.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 706-713
    • Kniazeff, J.1    Bessis, A.S.2    Maurel, D.3    Ansanay, H.4    Prezeau, L.5    Pin, J.P.6
  • 37
    • 33845720603 scopus 로고    scopus 로고
    • Asymmetric conformational changes in a GPCR dimer controlled by G-proteins
    • Damian, M.; Martin, A.; Mesnier, D.; Pin, J.P.; Baneres, J.L. Asymmetric conformational changes in a GPCR dimer controlled by G-proteins. EMBO J., 2006, 25, 5693-702.
    • (2006) EMBO J , vol.25 , pp. 5693-5702
    • Damian, M.1    Martin, A.2    Mesnier, D.3    Pin, J.P.4    Baneres, J.L.5
  • 38
    • 0021000027 scopus 로고
    • amplifier proteins in vision
    • and the cyclic GMP phosphodiesterase
    • Stryer, L. Transducin and the cyclic GMP phosphodiesterase: amplifier proteins in vision. Cold Spring Harbor Symp. Quant. Biol., 1983, 48, 841-52.
    • (1983) Cold Spring Harbor Symp. Quant. Biol , vol.48 , pp. 841-852
    • Stryer, L.T.1
  • 39
    • 34347370129 scopus 로고    scopus 로고
    • Dynamic models of G-protein coupled receptor dimers: Indications of asymmetry in the rhodopsin dimer from molecular dynamics simulations in a POPC bilayer
    • Filizola, M.; Wang, S.X.; Weinstein, H. Dynamic models of G-protein coupled receptor dimers: indications of asymmetry in the rhodopsin dimer from molecular dynamics simulations in a POPC bilayer. J. Comput. Aided Mol. Des., 2006, 20, 405-16.
    • (2006) J. Comput. Aided Mol. Des , vol.20 , pp. 405-416
    • Filizola, M.1    Wang, S.X.2    Weinstein, H.3
  • 40
    • 33750508943 scopus 로고    scopus 로고
    • Computational prediction of homodimerization of the A3 adenosine receptor
    • Kim, S.K.; Jacobson, K.A. Computational prediction of homodimerization of the A3 adenosine receptor. J. Mol. Graph. Model., 2006, 25, 549-61.
    • (2006) J. Mol. Graph. Model , vol.25 , pp. 549-561
    • Kim, S.K.1    Jacobson, K.A.2
  • 41
    • 48749126827 scopus 로고    scopus 로고
    • Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor
    • Mancia, F.; Assur, Z.; Herman, A.G.; Siegel, R.; Hendrickson, W.A. Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor. EMBO Rep., 2008, 9, 363-9.
    • (2008) EMBO Rep , vol.9 , pp. 363-369
    • Mancia, F.1    Assur, Z.2    Herman, A.G.3    Siegel, R.4    Hendrickson, W.A.5
  • 45
    • 33845926059 scopus 로고    scopus 로고
    • Seven transmembrane receptor core signaling complexes are assembled prior to plasma membrane trafficking
    • Dupre, D.J.; Robitaille, M.; Ethier, N.; Villeneuve, L.R.; Mamarbachi, A.M.; Hebert, T.E. Seven transmembrane receptor core signaling complexes are assembled prior to plasma membrane trafficking. J. Biol. Chem., 2006, 281, 34561-73.
    • (2006) J. Biol. Chem , vol.281 , pp. 34561-34573
    • Dupre, D.J.1    Robitaille, M.2    Ethier, N.3    Villeneuve, L.R.4    Mamarbachi, A.M.5    Hebert, T.E.6
  • 46
    • 29444446964 scopus 로고    scopus 로고
    • Heterotrimeric G proteins precouple with G protein-coupled receptors in living cells
    • Nobles, M.; Benians, A.; Tinker, A. Heterotrimeric G proteins precouple with G protein-coupled receptors in living cells. Proc. Natl. Acad. Sci., USA, 2005, 102, 18706-11.
    • (2005) Proc. Natl. Acad. Sci., USA , vol.102 , pp. 18706-18711
    • Nobles, M.1    Benians, A.2    Tinker, A.3
  • 47
    • 33846781730 scopus 로고    scopus 로고
    • Parallel inactivation of Y2 receptor and G-proteins in CHO cells by pertussis toxin
    • Parker, S.L.; Parker, M.S.; Sah, R.; Sallee, F.R.; Balasubramaniam, A. Parallel inactivation of Y2 receptor and G-proteins in CHO cells by pertussis toxin. Regul. Pept., 2007, 139, 128-35.
    • (2007) Regul. Pept , vol.139 , pp. 128-135
    • Parker, S.L.1    Parker, M.S.2    Sah, R.3    Sallee, F.R.4    Balasubramaniam, A.5
  • 48
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang, Y.; Fotiadis, D.; Filipek, S.; Saperstein, D.A.; Palczewski, K.; Engel, A. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem., 2003, 278, 21655-62.
    • (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
  • 50
    • 0032973978 scopus 로고    scopus 로고
    • Characterization of the dimerization of metabotropic glutamate receptors using an N-terminal truncation of mGluR1alpha
    • Robbins, M.J.; Ciruela, F.; Rhodes, A.; McIlhinney, R.A. Characterization of the dimerization of metabotropic glutamate receptors using an N-terminal truncation of mGluR1alpha. J. Neurochem., 1999, 72, 2539-47.
    • (1999) J. Neurochem , vol.72 , pp. 2539-2547
    • Robbins, M.J.1    Ciruela, F.2    Rhodes, A.3    McIlhinney, R.A.4
  • 51
    • 0036415131 scopus 로고    scopus 로고
    • Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET)
    • Jensen, A.A.; Hansen, J.L.; Sheikh, S.P.; Brauner-Osborne, H. Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET). Eur. J. Biochem., 2002, 269, 5076-87.
    • (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
  • 52
    • 0033597249 scopus 로고    scopus 로고
    • Dimerization of the calcium-sensing receptor occurs within the extracellular domain and is eliminated by Cys -> Ser mutations at Cys101 and Cys236
    • Pace, A.J.; Gama, L.; Breitwieser, G.E. Dimerization of the calcium-sensing receptor occurs within the extracellular domain and is eliminated by Cys -> Ser mutations at Cys101 and Cys236. J. Biol. Chem., 1999, 274, 11629-34.
    • (1999) J. Biol. Chem , vol.274 , pp. 11629-11634
    • Pace, A.J.1    Gama, L.2    Breitwieser, G.E.3
  • 53
    • 33745603726 scopus 로고    scopus 로고
    • Calcium-sensing receptor dimerizes in the endoplasmic reticulum: Biochemical and biophysical characterization of CASR mutants retained intracellularly
    • Pidasheva, S.; Grant, M.; Canaff, L.; Ercan, O.; Kumar, U.; Hendy, G.N. Calcium-sensing receptor dimerizes in the endoplasmic reticulum: biochemical and biophysical characterization of CASR mutants retained intracellularly. Hum. Mol. Genet., 2006, 15, 2200-9.
    • (2006) Hum. Mol. Genet , vol.15 , pp. 2200-2209
    • Pidasheva, S.1    Grant, M.2    Canaff, L.3    Ercan, O.4    Kumar, U.5    Hendy, G.N.6
  • 55
    • 2942700100 scopus 로고    scopus 로고
    • Dimerization of the transmembrane domain of Integrin alphaIIb subunit in cell membranes
    • Li, R.; Gorelik, R.; Nanda, V.; Law, P.B.; Lear, J.D.; DeGrado, W.F.; Bennett, J.S. Dimerization of the transmembrane domain of Integrin alphaIIb subunit in cell membranes. J. Biol. Chem., 2004, 279, 26666-73.
    • (2004) J. Biol. Chem , vol.279 , pp. 26666-26673
    • Li, R.1    Gorelik, R.2    Nanda, V.3    Law, P.B.4    Lear, J.D.5    DeGrado, W.F.6    Bennett, J.S.7
  • 57
    • 0037436390 scopus 로고    scopus 로고
    • Higher-order interhelical spatial interactions in membrane proteins
    • Adamian, L.; Jackups, R., Jr.; Binkowski, T.A.; Liang, J. Higher-order interhelical spatial interactions in membrane proteins. J. Mol. Biol., 2003, 327, 251-72.
    • (2003) J. Mol. Biol , vol.327 , pp. 251-272
    • Adamian, L.1    Jackups Jr., R.2    Binkowski, T.A.3    Liang, J.4
  • 58
    • 33947362780 scopus 로고    scopus 로고
    • The alpha1b-adrenoceptor exists as a higher-order oligomer: Effective oligomerization is required for receptor maturation, surface delivery, and function
    • Lopez-Gimenez, J.F.; Canals, M.; Pediani, J.D.; Milligan, G. The alpha1b-adrenoceptor exists as a higher-order oligomer: effective oligomerization is required for receptor maturation, surface delivery, and function. Mol. Pharmacol., 2007, 71, 1015-29.
    • (2007) Mol. Pharmacol , vol.71 , pp. 1015-1029
    • Lopez-Gimenez, J.F.1    Canals, M.2    Pediani, J.D.3    Milligan, G.4
  • 59
    • 33644781659 scopus 로고    scopus 로고
    • Opsin is present as dimers in COS1 cells: Identification of amino acids at the dimeric interface
    • Kota, P.; Reeves, P.J.; Rajbhandary, U.L.; Khorana, H.G. Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface. Proc. Natl. Acad. Sci., USA, 2006, 103, 3054-9.
    • (2006) Proc. Natl. Acad. Sci., USA , vol.103 , pp. 3054-3059
    • Kota, P.1    Reeves, P.J.2    Rajbhandary, U.L.3    Khorana, H.G.4
  • 60
    • 33845398829 scopus 로고    scopus 로고
    • Transmembrane segment peptides can disrupt cholecystokinin receptor oligomerization without affecting receptor function
    • Harikumar, K.G.; Dong, M.; Cheng, Z.; Pinon, D.I.; Lybrand, T.P.; Miller, L.J. Transmembrane segment peptides can disrupt cholecystokinin receptor oligomerization without affecting receptor function. Biochemistry, 2006, 45, 14706-16.
    • (2006) Biochemistry , vol.45 , pp. 14706-14716
    • Harikumar, K.G.1    Dong, M.2    Cheng, Z.3    Pinon, D.I.4    Lybrand, T.P.5    Miller, L.J.6
  • 62
    • 0345016983 scopus 로고    scopus 로고
    • Distribution of mGluR1alpha and mGluR5 immunolabeling in primate prefrontal cortex
    • Muly, E.C.; Maddox, M.; Smith, Y. Distribution of mGluR1alpha and mGluR5 immunolabeling in primate prefrontal cortex. J. Comp. Neurol., 2003, 467, 521-35.
    • (2003) J. Comp. Neurol , vol.467 , pp. 521-535
    • Muly, E.C.1    Maddox, M.2    Smith, Y.3
  • 63
    • 4043125390 scopus 로고    scopus 로고
    • Homodimerization of the beta2-adrenergic receptor as a prerequisite for cell surface targeting
    • Salahpour, A.; Angers, S.; Mercier, J.F.; Lagace, M.; Marullo, S.; Bouvier, M. Homodimerization of the beta2-adrenergic receptor as a prerequisite for cell surface targeting. J. Biol. Chem., 2004, 279, 33390-7.
    • (2004) J. Biol. Chem , vol.279 , pp. 33390-33397
    • Salahpour, A.1    Angers, S.2    Mercier, J.F.3    Lagace, M.4    Marullo, S.5    Bouvier, M.6
  • 64
    • 33748751347 scopus 로고    scopus 로고
    • Serotonin 5-HT2C receptor homodimer biogenesis in the endoplasmic reticulum: Real-time visualization with confocal fluorescence resonance energy transfer
    • Herrick-Davis, K.; Weaver, B.A.; Grinde, E.; Mazurkiewicz, J.E. Serotonin 5-HT2C receptor homodimer biogenesis in the endoplasmic reticulum: real-time visualization with confocal fluorescence resonance energy transfer. J. Biol. Chem., 2006, 281, 27109-16.
    • (2006) J. Biol. Chem , vol.281 , pp. 27109-27116
    • Herrick-Davis, K.1    Weaver, B.A.2    Grinde, E.3    Mazurkiewicz, J.E.4
  • 65
    • 37549001048 scopus 로고    scopus 로고
    • Pertussis toxin induces parallel loss of neuropeptide Y Y(1) receptor dimers and G(i) alpha subunit function in CHO cells
    • Parker, S.L.; Parker, M.S.; Sah, R.; Balasubramaniam, A.; Sallee, F.R. Pertussis toxin induces parallel loss of neuropeptide Y Y(1) receptor dimers and G(i) alpha subunit function in CHO cells. Eur. J. Pharmacol., 2008, 579, 13-25.
    • (2008) Eur. J. Pharmacol , vol.579 , pp. 13-25
    • Parker, S.L.1    Parker, M.S.2    Sah, R.3    Balasubramaniam, A.4    Sallee, F.R.5
  • 66
    • 0035910278 scopus 로고    scopus 로고
    • Hydrogen bonds with pi-acceptors in proteins: Frequencies and role in stabilizing local 3D structures
    • Steiner, T.; Koellner, G. Hydrogen bonds with pi-acceptors in proteins: frequencies and role in stabilizing local 3D structures. J. Mol. Biol., 2001, 305, 535-57.
    • (2001) J. Mol. Biol , vol.305 , pp. 535-557
    • Steiner, T.1    Koellner, G.2
  • 67
    • 33747330131 scopus 로고    scopus 로고
    • A transmembrane leucine zipper is required for activation of the dimeric receptor tyrosine kinase DDR1
    • Noordeen, N.A.; Carafoli, F.; Hohenester, E.; Horton, M.A.; Leitinger, B. A transmembrane leucine zipper is required for activation of the dimeric receptor tyrosine kinase DDR1. J. Biol. Chem., 2006, 281, 22744-51.
    • (2006) J. Biol. Chem , vol.281 , pp. 22744-22751
    • Noordeen, N.A.1    Carafoli, F.2    Hohenester, E.3    Horton, M.A.4    Leitinger, B.5
  • 69
    • 20444366920 scopus 로고    scopus 로고
    • Interdependence between transcription and mRNP processing and export, and its impact on genetic stability
    • Luna, R.; Jimeno, S.; Marin, M.; Huertas, P.; Garcia-Rubio, M.; Aguilera, A. Interdependence between transcription and mRNP processing and export, and its impact on genetic stability. Mol. Cell, 2005, 18, 711-22.
    • (2005) Mol. Cell , vol.18 , pp. 711-722
    • Luna, R.1    Jimeno, S.2    Marin, M.3    Huertas, P.4    Garcia-Rubio, M.5    Aguilera, A.6
  • 70
    • 6944234943 scopus 로고    scopus 로고
    • Multiple interactions between transmembrane helices generate the oligomeric alpha1b-adrenoceptor
    • Carrillo, J.J.; Lopez-Gimenez, J.F.; Milligan, G. Multiple interactions between transmembrane helices generate the oligomeric alpha1b-adrenoceptor. Mol. Pharmacol., 2004, 66, 1123-37.
    • (2004) Mol. Pharmacol , vol.66 , pp. 1123-1137
    • Carrillo, J.J.1    Lopez-Gimenez, J.F.2    Milligan, G.3
  • 71
    • 33744807250 scopus 로고    scopus 로고
    • Characterization of a membrane protein folding motif, the Ser zipper, using designed peptides
    • North, B.; Cristian, L.; Fu Stowell, X.; Lear, J.D.; Saven, J.G.; Degrado, W.F. Characterization of a membrane protein folding motif, the Ser zipper, using designed peptides. J. Mol. Biol., 2006, 359, 930-9.
    • (2006) J. Mol. Biol , vol.359 , pp. 930-939
    • North, B.1    Cristian, L.2    Fu Stowell, X.3    Lear, J.D.4    Saven, J.G.5    Degrado, W.F.6
  • 72
    • 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
    • Cheng, Z.J.; Miller, L.J. Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer. J. Biol. Chem., 2001, 276, 48040-7.
    • (2001) J. Biol. Chem , vol.276 , pp. 48040-48047
    • Cheng, Z.J.1    Miller, L.J.2
  • 73
    • 4344571483 scopus 로고    scopus 로고
    • Agonist-dependent dissociation of human somatostatin receptor 2 dimers: A role in receptor trafficking
    • Grant, M.; Collier, B.; Kumar, U. Agonist-dependent dissociation of human somatostatin receptor 2 dimers: a role in receptor trafficking. J. Biol. Chem., 2004, 279, 36179-83.
    • (2004) J. Biol. Chem , vol.279 , pp. 36179-36183
    • Grant, M.1    Collier, B.2    Kumar, U.3
  • 74
    • 35648961306 scopus 로고    scopus 로고
    • Oligomerization of neuropeptide Y (NPY) Y2 receptors in CHO cells depends on functional pertussis toxin-sensitive G-proteins
    • Parker, S.L.; Parker, M.S.; Sallee, F.R.; Balasubramaniam, A. Oligomerization of neuropeptide Y (NPY) Y2 receptors in CHO cells depends on functional pertussis toxin-sensitive G-proteins. Regul. Pept., 2007, 144, 72-81.
    • (2007) Regul. Pept , vol.144 , pp. 72-81
    • Parker, S.L.1    Parker, M.S.2    Sallee, F.R.3    Balasubramaniam, A.4
  • 75
    • 0033990061 scopus 로고    scopus 로고
    • Flexible sequence similarity searching with the FASTA3 program package
    • Pearson, W.R. Flexible sequence similarity searching with the FASTA3 program package. Methods Mol. Biol., 2000, 132, 185-219.
    • (2000) Methods Mol. Biol , vol.132 , pp. 185-219
    • Pearson, W.R.1
  • 76
    • 0035979146 scopus 로고    scopus 로고
    • The Calpha - - H...O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • Senes, A.; Ubarretxena-Belandia, I.; Engelman, D.M. The Calpha - - H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions. Proc. Natl. Acad. Sci., USA, 2001, 98, 9056-61.
    • (2001) Proc. Natl. Acad. Sci., USA , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 77
    • 0034595858 scopus 로고    scopus 로고
    • Growth hormone (GH)-independent dimerization of GH receptor by a leucine zipper results in constitutive activation
    • Behncken, S.N.; Billestrup, N.; Brown, R.; Amstrup, J.; Conway-Campbell, B.; Waters, M.J. Growth hormone (GH)-independent dimerization of GH receptor by a leucine zipper results in constitutive activation. J. Biol. Chem., 2000, 275, 17000-7.
    • (2000) J. Biol. Chem , vol.275 , pp. 17000-17007
    • Behncken, S.N.1    Billestrup, N.2    Brown, R.3    Amstrup, J.4    Conway-Campbell, B.5    Waters, M.J.6
  • 78
    • 0021755525 scopus 로고
    • Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins
    • Gray, T.M.; Matthews, B.W. Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins. J. Mol. Biol., 1984, 175, 75-81.
    • (1984) J. Mol. Biol , vol.175 , pp. 75-81
    • Gray, T.M.1    Matthews, B.W.2
  • 79
    • 23844539432 scopus 로고    scopus 로고
    • Internalization of gonadotropin-releasing hormone receptors (GnRHRs): Does arrestin binding to the C-terminal tail target GnRHRs for dynamin-dependent internalization?
    • Hislop, J.N.; Caunt, C.J.; Sedgley, K.R.; Kelly, E.; Mundell, S.; Green, L.D.; McArdle, C.A. Internalization of gonadotropin-releasing hormone receptors (GnRHRs): does arrestin binding to the C-terminal tail target GnRHRs for dynamin-dependent internalization? J Mol. Endocrinol., 2005, 35, 177-89.
    • (2005) J Mol. Endocrinol , vol.35 , pp. 177-189
    • Hislop, J.N.1    Caunt, C.J.2    Sedgley, K.R.3    Kelly, E.4    Mundell, S.5    Green, L.D.6    McArdle, C.A.7
  • 80
    • 34748812548 scopus 로고    scopus 로고
    • The Frizzled family of unconventional G-protein-coupled receptors
    • Schulte, G.; Bryja, V. The Frizzled family of unconventional G-protein-coupled receptors. Trends Pharmacol. Sci., 2007, 28, 518-25.
    • (2007) Trends Pharmacol. Sci , vol.28 , pp. 518-525
    • Schulte, G.1    Bryja, V.2
  • 81
    • 27844587815 scopus 로고    scopus 로고
    • Delineating a Ca2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor
    • Silve, C.; Petrel, C.; Leroy, C.; Bruel, H.; Mallet, E.; Rognan, D.; Ruat, M. Delineating a Ca2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor. J. Biol. Chem., 2005, 280, 37917-23.
    • (2005) J. Biol. Chem , vol.280 , pp. 37917-37923
    • Silve, C.1    Petrel, C.2    Leroy, C.3    Bruel, H.4    Mallet, E.5    Rognan, D.6    Ruat, M.7
  • 82
    • 33544461370 scopus 로고    scopus 로고
    • The Venus flytrap of periplasmic binding proteins: An ancient protein module present in multiple drug receptors
    • Felder, C.B.; Graul, R.C.; Lee, A.Y.; Merkle, H.P.; Sadee, W. The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. AAPS PharmSci., 1999, 1, 1-14.
    • (1999) AAPS PharmSci , vol.1 , pp. 1-14
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.P.4    Sadee, W.5
  • 83
    • 0035940464 scopus 로고    scopus 로고
    • Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: Proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4
    • Cai, K.; Klein-Seetharaman, J.; Altenbach, C.; Hubbell, W.L.; Khorana, H.G. Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4. Biochemistry, 2001, 40, 12479-85.
    • (2001) Biochemistry , vol.40 , pp. 12479-12485
    • Cai, K.1    Klein-Seetharaman, J.2    Altenbach, C.3    Hubbell, W.L.4    Khorana, H.G.5
  • 84
    • 34548186725 scopus 로고    scopus 로고
    • Structural basis of natural ligand binding and activation of the Class II G-protein-coupled secretin receptor
    • Miller, L.J.; Dong, M.; Harikumar, K.G.; Gao, F. Structural basis of natural ligand binding and activation of the Class II G-protein-coupled secretin receptor. Biochem. Soc. Trans., 2007, 35, 709-12.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 709-712
    • Miller, L.J.1    Dong, M.2    Harikumar, K.G.3    Gao, F.4
  • 86
    • 0029977976 scopus 로고    scopus 로고
    • Requirement of cysteine residues in exons 1-6 of the extracellular domain of the luteinizing hormone receptor for gonadotropin binding
    • Zhang, R.; Buczko, E.; Dufau, M.L. Requirement of cysteine residues in exons 1-6 of the extracellular domain of the luteinizing hormone receptor for gonadotropin binding. J. Biol. Chem., 1996, 271, 5755-60.
    • (1996) J. Biol. Chem , vol.271 , pp. 5755-5760
    • Zhang, R.1    Buczko, E.2    Dufau, M.L.3
  • 87
    • 0034716854 scopus 로고    scopus 로고
    • Human Ca2+ receptor cysteine-rich domain. Analysis of function of mutant and chimeric receptors
    • Hu, J.; Hauache, O.; Spiegel, A.M. Human Ca2+ receptor cysteine-rich domain. Analysis of function of mutant and chimeric receptors. J. Biol. Chem., 2000, 275, 16382-9.
    • (2000) J. Biol. Chem , vol.275 , pp. 16382-16389
    • Hu, J.1    Hauache, O.2    Spiegel, A.M.3
  • 88
    • 45649083683 scopus 로고    scopus 로고
    • Evolution and functional diversity of jellyfish opsins
    • Suga, H.; Schmid, V.; Gehring, W.J. Evolution and functional diversity of jellyfish opsins. Curr. Biol., 2008, 18, 51-55.
    • (2008) Curr. Biol , vol.18 , pp. 51-55
    • Suga, H.1    Schmid, V.2    Gehring, W.J.3
  • 89
    • 0033118238 scopus 로고    scopus 로고
    • A molecular mechanism for the cleavage of a disulfide bond as the primary function of agonist binding to G-protein-coupled receptors based on theoretical calculations supported by experiments
    • Brandt, W.; Golbraikh, A.; Tager, M.; Lendeckel, U. A molecular mechanism for the cleavage of a disulfide bond as the primary function of agonist binding to G-protein-coupled receptors based on theoretical calculations supported by experiments. Eur. J. Biochem., 1999, 261, 89-97.
    • (1999) Eur. J. Biochem , vol.261 , pp. 89-97
    • Brandt, W.1    Golbraikh, A.2    Tager, M.3    Lendeckel, U.4
  • 90
    • 36248992965 scopus 로고    scopus 로고
    • Opsin stability and folding: The role of Cys185 and abnormal disulfide bond formation in the intradiscal domain
    • McKibbin, C.; Toye, A.M.; Reeves, P.J.; Khorana, H.G.; Edwards, P.C.; Villa, C.; Booth, P.J. Opsin stability and folding: the role of Cys185 and abnormal disulfide bond formation in the intradiscal domain. J. Mol. Biol., 2007, 374, 1309-18.
    • (2007) J. Mol. Biol , vol.374 , pp. 1309-1318
    • McKibbin, C.1    Toye, A.M.2    Reeves, P.J.3    Khorana, H.G.4    Edwards, P.C.5    Villa, C.6    Booth, P.J.7
  • 91
    • 0033516576 scopus 로고    scopus 로고
    • Identification and molecular characterization of m3 muscarinic receptor dimers
    • Zeng, F.Y.; Wess, J. Identification and molecular characterization of m3 muscarinic receptor dimers. J. Biol. Chem., 1999, 274, 19487-97.
    • (1999) J. Biol. Chem , vol.274 , pp. 19487-19497
    • Zeng, F.Y.1    Wess, J.2
  • 92
    • 0025121206 scopus 로고
    • Muscarinic acetylcholine receptors. Peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation
    • Kurtenbach, E.; Curtis, C.A.; Pedder, E.K.; Aitken, A.; Harris, A.C.; Hulme, E.C. Muscarinic acetylcholine receptors. Peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation. J. Biol. Chem., 1990, 265, 13702-8.
    • (1990) J. Biol. Chem , vol.265 , pp. 13702-13708
    • Kurtenbach, E.1    Curtis, C.A.2    Pedder, E.K.3    Aitken, A.4    Harris, A.C.5    Hulme, E.C.6
  • 93
    • 0030663873 scopus 로고    scopus 로고
    • Irreversible activation of the gonadotropin-releasing hormone receptor by photoaffinity cross-linking: Localization of attachment site to Cys residue in N-terminal segment
    • Davidson, J.S.; Assefa, D.; Pawson, A.; Davies, P.; Hapgood, J.; Becker, I.; Flanagan, C.; Roeske, R.; Millar, R. Irreversible activation of the gonadotropin-releasing hormone receptor by photoaffinity cross-linking: localization of attachment site to Cys residue in N-terminal segment. Biochemistry, 1997, 36, 12881-9.
    • (1997) Biochemistry , vol.36 , pp. 12881-12889
    • Davidson, J.S.1    Assefa, D.2    Pawson, A.3    Davies, P.4    Hapgood, J.5    Becker, I.6    Flanagan, C.7    Roeske, R.8    Millar, R.9
  • 94
    • 33645223519 scopus 로고    scopus 로고
    • Role of the PAR1 receptor 8th helix in signaling: The 7-8-1 receptor activation mechanism
    • Swift, S.; Leger, A.J.; Talavera, J.; Zhang, L.; Bohm, A.; Kuliopulos, A. Role of the PAR1 receptor 8th helix in signaling: the 7-8-1 receptor activation mechanism. J. Biol. Chem., 2006, 281, 4109-16.
    • (2006) J. Biol. Chem , vol.281 , pp. 4109-4116
    • Swift, S.1    Leger, A.J.2    Talavera, J.3    Zhang, L.4    Bohm, A.5    Kuliopulos, A.6
  • 96
    • 0036584774 scopus 로고    scopus 로고
    • Differential palmitoylation directs the AMPA receptor-binding protein ABP to spines or to intracellular clusters
    • DeSouza, S.; Fu, J.; States, B.A.; Ziff, E.B. Differential palmitoylation directs the AMPA receptor-binding protein ABP to spines or to intracellular clusters. J. Neurosci., 2002, 22, 3493-503.
    • (2002) J. Neurosci , vol.22 , pp. 3493-3503
    • DeSouza, S.1    Fu, J.2    States, B.A.3    Ziff, E.B.4
  • 97
    • 46249107751 scopus 로고    scopus 로고
    • Opioid and chemokine receptor heterodimers: Arranged marriages or dangerous liaisons?
    • Hebert, T.E. Opioid and chemokine receptor heterodimers: arranged marriages or dangerous liaisons? Biochem. J., 2008, 412, 245-56.
    • (2008) Biochem. J , vol.412 , pp. 245-256
    • Hebert, T.E.1
  • 99
    • 0032569017 scopus 로고    scopus 로고
    • Brefeldin A (BFA) inhibits basolateral membrane (BLM) delivery and dimerization of transcobalamin II receptor in human intestinal epithelial Caco-2 cells. BFA effects on BLM cholesterol content
    • Bose, S.; Chapin, S.J.; Seetharam, S.; Feix, J.; Mostov, K.E.; Seetharam, B. Brefeldin A (BFA) inhibits basolateral membrane (BLM) delivery and dimerization of transcobalamin II receptor in human intestinal epithelial Caco-2 cells. BFA effects on BLM cholesterol content. J. Biol. Chem., 1998, 273, 16163-9.
    • (1998) J. Biol. Chem , vol.273 , pp. 16163-16169
    • Bose, S.1    Chapin, S.J.2    Seetharam, S.3    Feix, J.4    Mostov, K.E.5    Seetharam, B.6
  • 100
    • 0024356196 scopus 로고
    • The cation-dependent mannose 6-phosphate receptor. Structural requirements for mannose 6-phosphate binding and oligomerization
    • Dahms, N.M.; Kornfeld, S. The cation-dependent mannose 6-phosphate receptor. Structural requirements for mannose 6-phosphate binding and oligomerization. J. Biol. Chem., 1989, 264, 11458-67.
    • (1989) J. Biol. Chem , vol.264 , pp. 11458-11467
    • Dahms, N.M.1    Kornfeld, S.2
  • 101
    • 0035871210 scopus 로고    scopus 로고
    • Molecular pathogenesis of a disease: Structural consequences of aspartylglucosaminuria mutations
    • Saarela, J.; Laine, M.; Oinonen, C.; Schantz, C.; Jalanko, A.; Rouvinen, J.; Peltonen, L. Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations. Hum. Mol. Genet., 2001, 10, 983-95.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 983-995
    • Saarela, J.1    Laine, M.2    Oinonen, C.3    Schantz, C.4    Jalanko, A.5    Rouvinen, J.6    Peltonen, L.7
  • 102
    • 1442299241 scopus 로고    scopus 로고
    • The molecular defect leading to Fabry disease: Structure of human alpha-galactosidase
    • Garman, S.C.; Garboczi, D.N. The molecular defect leading to Fabry disease: structure of human alpha-galactosidase. J. Mol. Biol., 2004, 337, 319-35.
    • (2004) J. Mol. Biol , vol.337 , pp. 319-335
    • Garman, S.C.1    Garboczi, D.N.2
  • 103
    • 33645888144 scopus 로고    scopus 로고
    • Coding GNAS mutations leading to hormone resistance impair in vitro agonist- and cholera toxin-induced adenosine cyclic 3′,5′-monophosphate formation mediated by human XLalphas
    • Linglart, A.; Mahon, M.J.; Kerachian, M.A.; Berlach, D.M.; Hendy, G.N.; Juppner, H.; Bastepe, M. Coding GNAS mutations leading to hormone resistance impair in vitro agonist- and cholera toxin-induced adenosine cyclic 3′,5′-monophosphate formation mediated by human XLalphas. Endocrinology, 2006, 147, 2253-62.
    • (2006) Endocrinology , vol.147 , pp. 2253-2262
    • Linglart, A.1    Mahon, M.J.2    Kerachian, M.A.3    Berlach, D.M.4    Hendy, G.N.5    Juppner, H.6    Bastepe, M.7
  • 106
    • 0347992917 scopus 로고    scopus 로고
    • Heterodimerization of type A and B cholecystokinin receptors enhance signaling and promote cell growth
    • Cheng, Z.J.; Harikumar, K.G.; Holicky, E.L.; Miller, L.J. Heterodimerization of type A and B cholecystokinin receptors enhance signaling and promote cell growth. J. Biol. Chem., 2003, 278, 52972-9.
    • (2003) J. Biol. Chem , vol.278 , pp. 52972-52979
    • Cheng, Z.J.1    Harikumar, K.G.2    Holicky, E.L.3    Miller, L.J.4
  • 107
    • 31344468061 scopus 로고    scopus 로고
    • FGFR3 dimer stabilization due to a single amino acid pathogenic mutation
    • Li, E.; You, M.; Hristova, K. FGFR3 dimer stabilization due to a single amino acid pathogenic mutation. J. Mol. Biol., 2006, 356, 600-12.
    • (2006) J. Mol. Biol , vol.356 , pp. 600-612
    • Li, E.1    You, M.2    Hristova, K.3
  • 109
    • 0030013607 scopus 로고    scopus 로고
    • Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins
    • Belshaw, P.J.; Ho, S.N.; Crabtree, G.R.; Schreiber, S.L. Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins. Proc. Natl. Acad. Sci., USA, 1996, 93, 4604-7.
    • (1996) Proc. Natl. Acad. Sci., USA , vol.93 , pp. 4604-4607
    • Belshaw, P.J.1    Ho, S.N.2    Crabtree, G.R.3    Schreiber, S.L.4
  • 110
    • 28844437680 scopus 로고    scopus 로고
    • Inhibition of serotonin 5-hydroxytryptamine2c receptor function through heterodimerization: Receptor dimers bind two molecules of ligand and one G-protein
    • Herrick-Davis, K.; Grinde, E.; Harrigan, T.J.; Mazurkiewicz, J.E. Inhibition of serotonin 5-hydroxytryptamine2c receptor function through heterodimerization: receptor dimers bind two molecules of ligand and one G-protein. J. Biol. Chem., 2005, 280, 40144-51.
    • (2005) J. Biol. Chem , vol.280 , pp. 40144-40151
    • Herrick-Davis, K.1    Grinde, E.2    Harrigan, T.J.3    Mazurkiewicz, J.E.4
  • 113
    • 0141890300 scopus 로고    scopus 로고
    • Oligomerization of the alpha 1a- and alpha 1b-adrenergic receptor subtypes. Potential implications in receptor internalization
    • Stanasila, L.; Perez, J.B.; Vogel, H.; Cotecchia, S. Oligomerization of the alpha 1a- and alpha 1b-adrenergic receptor subtypes. Potential implications in receptor internalization. J. Biol. Chem., 2003, 278, 40239-51.
    • (2003) J. Biol. Chem , vol.278 , pp. 40239-40251
    • Stanasila, L.1    Perez, J.B.2    Vogel, H.3    Cotecchia, S.4
  • 114
    • 0142149074 scopus 로고    scopus 로고
    • Dimers of class A G protein-coupled receptors function via agonist-mediated trans-activation of associated G proteins
    • Carrillo, J.J.; Pediani, J.; Milligan, G. Dimers of class A G protein-coupled receptors function via agonist-mediated trans-activation of associated G proteins. J. Biol. Chem., 2003, 278, 42578-87.
    • (2003) J. Biol. Chem , vol.278 , pp. 42578-42587
    • Carrillo, J.J.1    Pediani, J.2    Milligan, G.3
  • 115
    • 25844464220 scopus 로고    scopus 로고
    • The specificity and molecular basis of alpha1-adrenoceptor and CXCR chemokine receptor dimerization
    • Milligan, G.; Wilson, S.; Lopez-Gimenez, J.F. The specificity and molecular basis of alpha1-adrenoceptor and CXCR chemokine receptor dimerization. J. Mol. Neurosci., 2005, 26, 161-8.
    • (2005) J. Mol. Neurosci , vol.26 , pp. 161-168
    • Milligan, G.1    Wilson, S.2    Lopez-Gimenez, J.F.3
  • 117
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • Mercier, J.F.; Salahpour, A.; Angers, S.; Breit, A.; Bouvier, M. Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J. Biol. Chem., 2002, 277, 44925-31.
    • (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
  • 119
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer
    • Guo, W.; Shi, L.; Javitch, J.A. The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer. J. Biol. Chem., 2003, 278, 4385-8.
    • (2003) J. Biol. Chem , vol.278 , pp. 4385-4388
    • Guo, W.1    Shi, L.2    Javitch, J.A.3
  • 120
    • 0032515074 scopus 로고    scopus 로고
    • A transmembrane domain-derived peptide inhibits D1 dopamine receptor function without affecting receptor oligomerization
    • George, S.R.; Lee, S.P.; Varghese, G.; Zeman, P.R.; Seeman, P.; Ng, G.Y.; O'Dowd, B.F. A transmembrane domain-derived peptide inhibits D1 dopamine receptor function without affecting receptor oligomerization. J. Biol. Chem., 1998, 273, 30244-8.
    • (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
  • 121
    • 33745257629 scopus 로고    scopus 로고
    • Agonist-induced cell surface trafficking of an intracellularly sequestered D1 dopamine receptor homo-oligomer
    • Kong, M.M.; Fan, T.; Varghese, G.; O'Dowd B, F.; George, S.R. Agonist-induced cell surface trafficking of an intracellularly sequestered D1 dopamine receptor homo-oligomer. Mol. Pharmacol., 2006, 70, 78-89.
    • (2006) Mol. Pharmacol , vol.70 , pp. 78-89
    • Kong, M.M.1    Fan, T.2    Varghese, G.3    O'Dowd, B.F.4    George, S.R.5
  • 125
    • 30444457212 scopus 로고    scopus 로고
    • Homo- or heterodimerization of muscarinic receptor subtypes is not mediated by direct protein-protein interaction through intracellular and extracellular regions
    • Kang, Y.K.; Yoon, T.; Lee, K.; Kim, H.J. Homo- or heterodimerization of muscarinic receptor subtypes is not mediated by direct protein-protein interaction through intracellular and extracellular regions. Arch. Pharm. Res., 2003, 26, 846-54.
    • (2003) Arch. Pharm. Res , vol.26 , pp. 846-854
    • Kang, Y.K.1    Yoon, T.2    Lee, K.3    Kim, H.J.4
  • 126
    • 33646500642 scopus 로고    scopus 로고
    • Quantitative analysis of muscarinic acetylcholine receptor homo- and heterodimerization in live cells: Regulation of receptor down-regulation by heterodimerization
    • Goin, J.C.; Nathanson, N.M. Quantitative analysis of muscarinic acetylcholine receptor homo- and heterodimerization in live cells: regulation of receptor down-regulation by heterodimerization. J. Biol. Chem., 2006, 281, 5416-25.
    • (2006) J. Biol. Chem , vol.281 , pp. 5416-5425
    • Goin, J.C.1    Nathanson, N.M.2
  • 127
    • 2942522705 scopus 로고    scopus 로고
    • Role of extracellular cysteine residues in dimerization/oligomerization of the human prostacyclin receptor
    • Giguere, V.; Gallant, M.A.; de Brum-Fernandes, A.J.; Parent, J.L. Role of extracellular cysteine residues in dimerization/oligomerization of the human prostacyclin receptor. Eur. J. Pharmacol., 2004, 494, 11-22.
    • (2004) Eur. J. Pharmacol , vol.494 , pp. 11-22
    • Giguere, V.1    Gallant, M.A.2    de Brum-Fernandes, A.J.3    Parent, J.L.4
  • 128
    • 0041315589 scopus 로고    scopus 로고
    • C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor
    • Klco, J.M.; Lassere, T.B.; Baranski, T.J. C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor. J. Biol. Chem., 2003, 278, 35345-53.
    • (2003) J. Biol. Chem , vol.278 , pp. 35345-35353
    • Klco, J.M.1    Lassere, T.B.2    Baranski, T.J.3
  • 131
    • 0037474238 scopus 로고    scopus 로고
    • Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor
    • Babcock, G.J.; Farzan, M.; Sodroski, J. Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor. J. Biol. Chem., 2003, 278, 3378-85.
    • (2003) J. Biol. Chem , vol.278 , pp. 3378-3385
    • Babcock, G.J.1    Farzan, M.2    Sodroski, J.3
  • 132
    • 0037131325 scopus 로고    scopus 로고
    • Rescue of HIV-1 receptor function through cooperation between different forms of the CCR5 chemokine receptor
    • Chelli, M.; Alizon, M. Rescue of HIV-1 receptor function through cooperation between different forms of the CCR5 chemokine receptor. J. Biol. Chem., 2002, 277, 39388-96.
    • (2002) J. Biol. Chem , vol.277 , pp. 39388-39396
    • Chelli, M.1    Alizon, M.2
  • 133
    • 0346056873 scopus 로고    scopus 로고
    • Heterodimerization and cross-desensitization between the muopioid receptor and the chemokine CCR5 receptor
    • Chen, C.; Li, J.; Bot, G.; Szabo, I.; Rogers, T.J.; Liu-Chen, L.Y. Heterodimerization and cross-desensitization between the muopioid receptor and the chemokine CCR5 receptor. Eur. J. Pharmacol., 2004, 483, 175-86.
    • (2004) Eur. J. Pharmacol , vol.483 , pp. 175-186
    • Chen, C.1    Li, J.2    Bot, G.3    Szabo, I.4    Rogers, T.J.5    Liu-Chen, L.Y.6
  • 135
    • 23644460494 scopus 로고    scopus 로고
    • Oligomerization of the fifth transmembrane domain from the adenosine A2A receptor
    • Thevenin, D.; Lazarova, T.; Roberts, M.F.; Robinson, C.R. Oligomerization of the fifth transmembrane domain from the adenosine A2A receptor. Protein Sci., 2005, 14, 2177-86.
    • (2005) Protein Sci , vol.14 , pp. 2177-2186
    • Thevenin, D.1    Lazarova, T.2    Roberts, M.F.3    Robinson, C.R.4
  • 136
    • 35048820405 scopus 로고    scopus 로고
    • Fluorescence studies of homooligomerization of adenosine A(2A) and serotonin 5-HT(1A) receptors reveal the specificity of receptor interactions in the plasma membrane
    • Lukasiewicz, S.; Blasiak, E.; Faron-Gorecka, A.; Polit, A.; Tworzydlo, M.; Gorecki, A.; Wasylewski, Z.; Dziedzicka-Wasylewska, M. Fluorescence studies of homooligomerization of adenosine A(2A) and serotonin 5-HT(1A) receptors reveal the specificity of receptor interactions in the plasma membrane. Pharmacol. Rep., 2007, 59, 379-92.
    • (2007) Pharmacol. Rep , vol.59 , pp. 379-392
    • Lukasiewicz, S.1    Blasiak, E.2    Faron-Gorecka, A.3    Polit, A.4    Tworzydlo, M.5    Gorecki, A.6    Wasylewski, Z.7    Dziedzicka-Wasylewska, M.8
  • 137
    • 34547124343 scopus 로고    scopus 로고
    • Signaling through a G Protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model
    • Philip, F.; Sengupta, P.; Scarlata, S. Signaling through a G Protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model. J. Biol. Chem., 2007, 282, 19203-16.
    • (2007) J. Biol. Chem , vol.282 , pp. 19203-19216
    • Philip, F.1    Sengupta, P.2    Scarlata, S.3
  • 139
    • 34249792937 scopus 로고    scopus 로고
    • Follicle-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing
    • Thomas, R.M.; Nechamen, C.A.; Mazurkiewicz, J.E.; Muda, M.; Palmer, S.; Dias, J.A. Follicle-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing. Endocrinology, 2007, 148, 1987-95.
    • (2007) Endocrinology , vol.148 , pp. 1987-1995
    • Thomas, R.M.1    Nechamen, C.A.2    Mazurkiewicz, J.E.3    Muda, M.4    Palmer, S.5    Dias, J.A.6
  • 140
    • 0037160035 scopus 로고    scopus 로고
    • Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor
    • Latif, R.; Graves, P.; Davies, T.F. Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor. J. Biol. Chem., 2002, 277, 45059-67.
    • (2002) J. Biol. Chem , vol.277 , pp. 45059-45067
    • Latif, R.1    Graves, P.2    Davies, T.F.3
  • 141
    • 40849096162 scopus 로고    scopus 로고
    • Cloning, expression, and functional characterization of relaxin receptor (leucine-rich repeat-containing G protein-coupled receptor 7) splice variants from human fetal membranes
    • Kern, A.; Hubbard, D.; Amano, A.; Bryant-Greenwood, G.D. Cloning, expression, and functional characterization of relaxin receptor (leucine-rich repeat-containing G protein-coupled receptor 7) splice variants from human fetal membranes. Endocrinology, 2008, 149, 1277-94.
    • (2008) Endocrinology , vol.149 , pp. 1277-1294
    • Kern, A.1    Hubbard, D.2    Amano, A.3    Bryant-Greenwood, G.D.4
  • 142
    • 2442438851 scopus 로고    scopus 로고
    • Homo- and hetero-dimeric complex formations of the human oxytocin receptor
    • Devost, D.; Zingg, H.H. Homo- and hetero-dimeric complex formations of the human oxytocin receptor. J. Neuroendocrinol., 2004, 16, 372-7.
    • (2004) J. Neuroendocrinol , vol.16 , pp. 372-377
    • Devost, D.1    Zingg, H.H.2
  • 143
    • 0034677745 scopus 로고    scopus 로고
    • Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers
    • Rocheville, M.; Lange, D.C.; Kumar, U.; Sasi, R.; Patel, R.C.; Patel, Y.C. Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers. J. Biol. Chem., 2000, 275, 7862-9.
    • (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
  • 144
    • 0035958027 scopus 로고    scopus 로고
    • Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A)
    • Pfeiffer, M.; Koch, T.; Schroder, H.; Klutzny, M.; Kirscht, S.; Kreienkamp, H.J.; Hollt, V.; Schulz, S. Homo- and heterodimerization of somatostatin receptor subtypes. Inactivation of sst(3) receptor function by heterodimerization with sst(2A). J. Biol. Chem., 2001, 276, 14027-36.
    • (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
  • 145
    • 0038237527 scopus 로고    scopus 로고
    • Homodimerization of neuropeptide y receptors investigated by fluorescence resonance energy transfer in living cells
    • Dinger, M.C.; Bader, J.E.; Kobor, A.D.; Kretzschmar, A.K.; Beck-Sickinger, A.G. Homodimerization of neuropeptide y receptors investigated by fluorescence resonance energy transfer in living cells. J. Biol. Chem., 2003, 278, 10562-71.
    • (2003) J. Biol. Chem , vol.278 , pp. 10562-10571
    • Dinger, M.C.1    Bader, J.E.2    Kobor, A.D.3    Kretzschmar, A.K.4    Beck-Sickinger, A.G.5
  • 146
    • 0037105663 scopus 로고    scopus 로고
    • Silencing of secretin receptor function by dimerization with a misspliced variant secretin receptor in ductal pancreatic adenocarcinoma
    • Ding, W.Q.; Cheng, Z.J.; McElhiney, J.; Kuntz, S.M.; Miller, L.J. Silencing of secretin receptor function by dimerization with a misspliced variant secretin receptor in ductal pancreatic adenocarcinoma. Cancer Res., 2002, 62, 5223-9.
    • (2002) Cancer Res , vol.62 , pp. 5223-5229
    • Ding, W.Q.1    Cheng, Z.J.2    McElhiney, J.3    Kuntz, S.M.4    Miller, L.J.5
  • 147
    • 33745854483 scopus 로고    scopus 로고
    • Secretin receptor oligomers form intracellularly during maturation through receptor core domains
    • Lisenbee, C.S.; Miller, L.J. Secretin receptor oligomers form intracellularly during maturation through receptor core domains. Biochemistry, 2006, 45, 8216-26.
    • (2006) Biochemistry , vol.45 , pp. 8216-8226
    • Lisenbee, C.S.1    Miller, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.