메뉴 건너뛰기




Volumn 321, Issue 2, 2010, Pages 112-122

Dominant negative effects of human follicle-stimulating hormone receptor expression-deficient mutants on wild-type receptor cell surface expression. Rescue of oligomerization-dependent defective receptor expression by using cognate decoys

Author keywords

Decoy; Dimerization; Dominant negative receptor; Endoplasmic reticulum; Follicle stimulating hormone receptor; Intracellular trafficking

Indexed keywords

COMPLEMENTARY DNA; CYCLIC AMP; FOLLITROPIN RECEPTOR; LUTEINIZING HORMONE RECEPTOR; THYROTROPIN RECEPTOR; CELL SURFACE RECEPTOR;

EID: 77951258353     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2010.02.027     Document Type: Article
Times cited : (41)

References (79)
  • 1
    • 2442529839 scopus 로고    scopus 로고
    • Hetero-oligomerization between GABAA and GABAB receptors regulates GABAB receptor trafficking
    • Balasubramanian S., Teissere J.A., Raju D.V., Hall R.A. Hetero-oligomerization between GABAA and GABAB receptors regulates GABAB receptor trafficking. J. Biol. Chem. 2004, 279:18840-18850.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18840-18850
    • Balasubramanian, S.1    Teissere, J.A.2    Raju, D.V.3    Hall, R.A.4
  • 3
    • 0030712312 scopus 로고    scopus 로고
    • Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32
    • Benkirane M., Jin D.Y., Chun R.F., Koup R.A., Jeang K.T. Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32. J. Biol. Chem. 1997, 272:30603-30606.
    • (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
  • 4
    • 33751247054 scopus 로고    scopus 로고
    • Ligand-selective determinants in gonadotropin receptors
    • Bogerd J. Ligand-selective determinants in gonadotropin receptors. Mol. Cell. Endocrinol. 2007, 260-262:144-152.
    • (2007) Mol. Cell. Endocrinol. , pp. 144-152
    • Bogerd, J.1
  • 5
    • 3142617997 scopus 로고    scopus 로고
    • Hetero-oligomerization between beta2- and beta3-adrenergic receptors generates a beta-adrenergic signaling unit with distinct functional properties
    • Breit A., Lagace M., Bouvier M. Hetero-oligomerization between beta2- and beta3-adrenergic receptors generates a beta-adrenergic signaling unit with distinct functional properties. J. Biol. Chem. 2004, 279:28756-28765.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28756-28765
    • Breit, A.1    Lagace, M.2    Bouvier, M.3
  • 6
    • 3042800569 scopus 로고    scopus 로고
    • Human loss-of-function gonadotropin-releasing hormone receptor mutants retain wild-type receptors in the endoplasmic reticulum: molecular basis of the dominant-negative effect
    • Brothers S.P., Cornea A., Janovick J.A., Conn P.M. Human loss-of-function gonadotropin-releasing hormone receptor mutants retain wild-type receptors in the endoplasmic reticulum: molecular basis of the dominant-negative effect. Mol. Endocrinol. 2004, 18:1787-1797.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1787-1797
    • Brothers, S.P.1    Cornea, A.2    Janovick, J.A.3    Conn, P.M.4
  • 7
    • 14644387575 scopus 로고    scopus 로고
    • Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation
    • Bulenger S., Marullo S., Bouvier M. Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends Pharmacol. Sci. 2005, 26:131-137.
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 131-137
    • Bulenger, S.1    Marullo, S.2    Bouvier, M.3
  • 9
    • 0029809348 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases by gonadotropins and cyclic adenosine 5′-monophosphates in porcine granulosa cells
    • Cameron M.R., Foster J.S., Bukovsky A., Wimalasena J. Activation of mitogen-activated protein kinases by gonadotropins and cyclic adenosine 5′-monophosphates in porcine granulosa cells. Biol. Reprod. 1996, 55:111-119.
    • (1996) Biol. Reprod. , vol.55 , pp. 111-119
    • Cameron, M.R.1    Foster, J.S.2    Bukovsky, A.3    Wimalasena, J.4
  • 10
    • 0025924420 scopus 로고
    • Specific activation of Gs by synthetic peptides corresponding to an intracellular loop of the beta-adrenergic receptor
    • Cheung A.H., Huang R.R., Graziano M.P., Strader C.D. Specific activation of Gs by synthetic peptides corresponding to an intracellular loop of the beta-adrenergic receptor. FEBS Lett. 1991, 279:277-280.
    • (1991) FEBS Lett. , vol.279 , pp. 277-280
    • Cheung, A.H.1    Huang, R.R.2    Graziano, M.P.3    Strader, C.D.4
  • 11
    • 44649101927 scopus 로고    scopus 로고
    • G protein-coupled receptor dimers: functional consequences, disease states and drug targets
    • Dalrymple M.B., Pfleger K.D., Eidne K.A. G protein-coupled receptor dimers: functional consequences, disease states and drug targets. Pharmacol. Ther. 2008, 118:359-371.
    • (2008) Pharmacol. Ther. , vol.118 , pp. 359-371
    • Dalrymple, M.B.1    Pfleger, K.D.2    Eidne, K.A.3
  • 14
    • 3142714503 scopus 로고    scopus 로고
    • A conserved motif for the transport of G protein-coupled receptors from the endoplasmic reticulum to the cell surface
    • Duvernay M.T., Zhou F., Wu G. A conserved motif for the transport of G protein-coupled receptors from the endoplasmic reticulum to the cell surface. J. Biol. Chem. 2004, 279:30741-30750.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30741-30750
    • Duvernay, M.T.1    Zhou, F.2    Wu, G.3
  • 15
    • 33644684672 scopus 로고    scopus 로고
    • A role for the distal carboxyl tails in generating the novel pharmacology and G protein activation profile of mu and delta opioid receptor hetero-oligomers
    • Fan T., Varghese G., Nguyen T., Tse R., O'Dowd B.F., George S.R. A role for the distal carboxyl tails in generating the novel pharmacology and G protein activation profile of mu and delta opioid receptor hetero-oligomers. J. Biol. Chem. 2005, 280:38478-38488.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38478-38488
    • Fan, T.1    Varghese, G.2    Nguyen, T.3    Tse, R.4    O'Dowd, B.F.5    George, S.R.6
  • 16
    • 33746339971 scopus 로고    scopus 로고
    • Oligomerization of the yeast alpha-factor receptor: implications for dominant negative effects of mutant receptors
    • Gehret A.U., Bajaj A., Naider F., Dumont M.E. Oligomerization of the yeast alpha-factor receptor: implications for dominant negative effects of mutant receptors. J. Biol. Chem. 2006, 281:20698-20714.
    • (2006) J. Biol. Chem. , vol.281 , pp. 20698-20714
    • Gehret, A.U.1    Bajaj, A.2    Naider, F.3    Dumont, M.E.4
  • 17
    • 0034463096 scopus 로고    scopus 로고
    • Follicle-Stimulating hormone (FSH) stimulates phosphorylation and activation of protein kinase B (PKB/Akt) and serum and glucocorticoid-lnduced kinase (Sgk): evidence for A kinase-independent signaling by FSH in granulosa cells
    • Gonzalez-Robayna I.J., Falender A.E., Ochsner S., Firestone G.L., Richards J.S. Follicle-Stimulating hormone (FSH) stimulates phosphorylation and activation of protein kinase B (PKB/Akt) and serum and glucocorticoid-lnduced kinase (Sgk): evidence for A kinase-independent signaling by FSH in granulosa cells. Mol. Endocrinol. 2000, 14:1283-1300.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1283-1300
    • Gonzalez-Robayna, I.J.1    Falender, A.E.2    Ochsner, S.3    Firestone, G.L.4    Richards, J.S.5
  • 18
    • 0031446639 scopus 로고    scopus 로고
    • Inhibition of gonadotropin-releasing hormone receptor signaling by expression of a splice variant of the human receptor
    • Grosse R., Schoneberg T., Schultz G., Gudermann T. Inhibition of gonadotropin-releasing hormone receptor signaling by expression of a splice variant of the human receptor. Mol. Endocrinol. 1997, 11:1305-1318.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1305-1318
    • Grosse, R.1    Schoneberg, T.2    Schultz, G.3    Gudermann, T.4
  • 19
    • 65549163519 scopus 로고    scopus 로고
    • Bioluminescence resonance energy transfer studies reveal constitutive dimerization of the human lutropin receptor and a lack of correlation between receptor activation and the propensity for dimerization
    • Guan R., Feng X., Wu X., Zhang M., Zhang X., Hebert T.E., Segaloff D.L. Bioluminescence resonance energy transfer studies reveal constitutive dimerization of the human lutropin receptor and a lack of correlation between receptor activation and the propensity for dimerization. J. Biol. Chem. 2009, 284:7483-7494.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7483-7494
    • Guan, R.1    Feng, X.2    Wu, X.3    Zhang, M.4    Zhang, X.5    Hebert, T.E.6    Segaloff, D.L.7
  • 20
    • 70450233609 scopus 로고    scopus 로고
    • Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors
    • Guan R., Wu X., Feng X., Zhang M., Hébert T.E., Segaloff D.L. Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors. Cell. Signal. 2010, 22:247-256.
    • (2010) Cell. Signal. , vol.22 , pp. 247-256
    • Guan, R.1    Wu, X.2    Feng, X.3    Zhang, M.4    Hébert, T.E.5    Segaloff, D.L.6
  • 21
    • 0029666267 scopus 로고    scopus 로고
    • A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
    • Hebert T.E., Moffett S., Morello J.P., Loisel T.P., Bichet D.G., Barret C., Bouvier M. A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation. J. Biol. Chem. 1996, 271:16384-16392.
    • (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
  • 22
    • 0023161268 scopus 로고
    • Use of lithium ion in measurement of stimulated pituitary inositol phospholipid turnover
    • Huckle W.R., Conn P.M. Use of lithium ion in measurement of stimulated pituitary inositol phospholipid turnover. Methods Enzymol. 1987, 141:149-155.
    • (1987) Methods Enzymol. , vol.141 , pp. 149-155
    • Huckle, W.R.1    Conn, P.M.2
  • 24
    • 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
    • Karpa K.D., Lin R., Kabbani N., Levenson R. The dopamine D3 receptor interacts with itself and the truncated D3 splice variant d3nf: D3-D3nf interaction causes mislocalization of D3 receptors. Mol. Pharmacol. 2000, 58:677-683.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 677-683
    • Karpa, K.D.1    Lin, R.2    Kabbani, N.3    Levenson, R.4
  • 28
    • 0038637206 scopus 로고    scopus 로고
    • Dominant-negative action of disease-causing gonadotropin-releasing hormone receptor (GnRHR) mutants: a trait that potentially coevolved with decreased plasma membrane expression of GnRHR in humans
    • Leaños-Miranda A., Ulloa-Aguirre A., Ji T.H., Janovick J.A., Conn P.M. Dominant-negative action of disease-causing gonadotropin-releasing hormone receptor (GnRHR) mutants: a trait that potentially coevolved with decreased plasma membrane expression of GnRHR in humans. J. Clin. Endocrinol. Metab. 2003, 88:3360-3367.
    • (2003) J. Clin. Endocrinol. Metab. , vol.88 , pp. 3360-3367
    • Leaños-Miranda, A.1    Ulloa-Aguirre, A.2    Ji, T.H.3    Janovick, J.A.4    Conn, P.M.5
  • 29
    • 18844451476 scopus 로고    scopus 로고
    • In vitro coexpression and pharmacological rescue of mutant gonadotropin-releasing hormone receptors causing hypogonadotropic hypogonadism in humans expressing compound heterozygous alleles
    • Leaños-Miranda A., Ulloa-Aguirre A., Janovick J.A., Conn P.M. In vitro coexpression and pharmacological rescue of mutant gonadotropin-releasing hormone receptors causing hypogonadotropic hypogonadism in humans expressing compound heterozygous alleles. J. Clin. Endocrinol. Metab. 2005, 90:3001-3008.
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , pp. 3001-3008
    • Leaños-Miranda, A.1    Ulloa-Aguirre, A.2    Janovick, J.A.3    Conn, P.M.4
  • 30
    • 0033924207 scopus 로고    scopus 로고
    • Inhibition of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell
    • Lee S.P., O'Dowd B.F., Ng G.Y., Varghese G., Akil H., Mansour A., Nguyen T., George S.R. Inhibition of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell. Mol. Pharmacol. 2000, 58:120-128.
    • (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
  • 31
    • 0141431029 scopus 로고    scopus 로고
    • D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4
    • Lee S.P., O'Dowd B.F., Rajaram R.D., Nguyen T., George S.R. D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4. Biochemistry 2003, 42:11023-11031.
    • (2003) Biochemistry , vol.42 , pp. 11023-11031
    • Lee, S.P.1    O'Dowd, B.F.2    Rajaram, R.D.3    Nguyen, T.4    George, S.R.5
  • 32
    • 0034607465 scopus 로고    scopus 로고
    • P38JAB1 binds to the intracellular precursor of the lutropin/choriogonadotropin receptor and promotes its degradation
    • Li S., Liu X., Ascoli M. p38JAB1 binds to the intracellular precursor of the lutropin/choriogonadotropin receptor and promotes its degradation. J. Biol. Chem. 2000, 275:13386-13393.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13386-13393
    • Li, S.1    Liu, X.2    Ascoli, M.3
  • 33
    • 0028064305 scopus 로고
    • Identification of amino acids in the C-terminal region of human follicle-stimulating hormone (FSH) beta-subunit involved in binding to human FSH receptor
    • Lindau-Shepard B., Roth K.E., Dias J.A. Identification of amino acids in the C-terminal region of human follicle-stimulating hormone (FSH) beta-subunit involved in binding to human FSH receptor. Endocrinology 1994, 135:1235-1240.
    • (1994) Endocrinology , vol.135 , pp. 1235-1240
    • Lindau-Shepard, B.1    Roth, K.E.2    Dias, J.A.3
  • 34
    • 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, 71:1015-1029.
    • (2007) Mol. Pharmacol. , vol.71 , pp. 1015-1029
    • Lopez-Gimenez, J.F.1    Canals, M.2    Pediani, J.D.3    Milligan, G.4
  • 35
    • 0031786371 scopus 로고    scopus 로고
    • Follicle stimulating hormone (FSH) activates the p38 mitogen-activated protein kinase pathway, inducing small heat shock protein phosphorylation and cell rounding in immature rat ovarian granulosa cells
    • Maizels E.T., Cottom J., Jones J.C., Hunzicker-Dunn M. Follicle stimulating hormone (FSH) activates the p38 mitogen-activated protein kinase pathway, inducing small heat shock protein phosphorylation and cell rounding in immature rat ovarian granulosa cells. Endocrinology 1998, 139:3353-3356.
    • (1998) Endocrinology , vol.139 , pp. 3353-3356
    • Maizels, E.T.1    Cottom, J.2    Jones, J.C.3    Hunzicker-Dunn, M.4
  • 36
    • 0034351870 scopus 로고    scopus 로고
    • Combined modification of intracellular and extracellular loci on human gonadotropin-releasing hormone receptor provides a mechanism for enhanced expression
    • Maya-Nunez G., Janovick J.A., Conn P.M. Combined modification of intracellular and extracellular loci on human gonadotropin-releasing hormone receptor provides a mechanism for enhanced expression. Endocrine 2000, 13:401-407.
    • (2000) Endocrine , vol.13 , pp. 401-407
    • Maya-Nunez, G.1    Janovick, J.A.2    Conn, P.M.3
  • 37
    • 33645502893 scopus 로고    scopus 로고
    • A dominant-negative human growth hormone-releasing hormone (GHRH) receptor splice variant inhibits GHRH binding
    • McElvaine A.T., Mayo K.E. A dominant-negative human growth hormone-releasing hormone (GHRH) receptor splice variant inhibits GHRH binding. Endocrinology 2006, 147:1884-1894.
    • (2006) Endocrinology , vol.147 , pp. 1884-1894
    • McElvaine, A.T.1    Mayo, K.E.2
  • 38
    • 33947369500 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerisation: molecular basis and relevance to function
    • Milligan G. G protein-coupled receptor dimerisation: molecular basis and relevance to function. Biochim. Biophys. Acta 2007, 1768:825-835.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 825-835
    • Milligan, G.1
  • 39
    • 40349085622 scopus 로고    scopus 로고
    • A day in the life of a G protein-coupled receptor: the contribution to function of G protein-coupled receptor dimerization
    • Milligan G. A day in the life of a G protein-coupled receptor: the contribution to function of G protein-coupled receptor dimerization. Br. J. Pharmacol. 2008, 153(Suppl. 1):S216-S229.
    • (2008) Br. J. Pharmacol. , vol.153 , Issue.1 SUPPL.
    • Milligan, G.1
  • 40
    • 33751218036 scopus 로고    scopus 로고
    • The effect of splice variant of the human luteinizing hormone (LH) receptor on the expression of gonadotropin receptor
    • Minegishi T., Nakamura K., Yamashita S., Omori Y. The effect of splice variant of the human luteinizing hormone (LH) receptor on the expression of gonadotropin receptor. Mol. Cell. Endocrinol. 2007, 260-262:117-125.
    • (2007) Mol. Cell. Endocrinol. , pp. 117-125
    • Minegishi, T.1    Nakamura, K.2    Yamashita, S.3    Omori, Y.4
  • 41
    • 0033580998 scopus 로고    scopus 로고
    • Identification of the G protein-activating domain of the natriuretic peptide clearance receptor (NPR-C)
    • Murthy K.S., Makhlouf G.M. Identification of the G protein-activating domain of the natriuretic peptide clearance receptor (NPR-C). J. Biol. Chem. 1999, 274:17587-17592.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17587-17592
    • Murthy, K.S.1    Makhlouf, G.M.2
  • 42
    • 2542496712 scopus 로고    scopus 로고
    • A splice variant of the human luteinizing hormone (LH) receptor modulates the expression of wild-type human LH receptor
    • Nakamura K., Yamashita S., Omori Y., Minegishi T. A splice variant of the human luteinizing hormone (LH) receptor modulates the expression of wild-type human LH receptor. Mol. Endocrinol. 2004, 18:1461-1470.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1461-1470
    • Nakamura, K.1    Yamashita, S.2    Omori, Y.3    Minegishi, T.4
  • 43
    • 0037471203 scopus 로고    scopus 로고
    • Point mutations in follitropin receptor result in ER retention
    • Nechamen C.A., Dias J.A. Point mutations in follitropin receptor result in ER retention. Mol. Cell. Endocrinol. 2003, 201:123-131.
    • (2003) Mol. Cell. Endocrinol. , vol.201 , pp. 123-131
    • Nechamen, C.A.1    Dias, J.A.2
  • 44
    • 33751239461 scopus 로고    scopus 로고
    • APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling complex
    • Nechamen C.A., Thomas R.M., Dias J.A. APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling complex. Mol. Cell. Endocrinol. 2007, 260-262:93-99.
    • (2007) Mol. Cell. Endocrinol. , pp. 93-99
    • Nechamen, C.A.1    Thomas, R.M.2    Dias, J.A.3
  • 46
    • 0026630552 scopus 로고
    • Detection of G protein-activator regions in M4 subtype muscarinic, cholinergic, and alpha 2-adrenergic receptors based upon characteristics in primary structure
    • Okamoto T., Nishimoto I. Detection of G protein-activator regions in M4 subtype muscarinic, cholinergic, and alpha 2-adrenergic receptors based upon characteristics in primary structure. J. Biol. Chem. 1992, 267:8342-8346.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8342-8346
    • Okamoto, T.1    Nishimoto, I.2
  • 47
    • 0029913957 scopus 로고    scopus 로고
    • Suppression of prostaglandin E receptor signaling by the variant form of EP1 subtype
    • Okuda-Ashitaka E., Sakamoto K., Ezashi T., Miwa K., Ito S., Hayaishi O. Suppression of prostaglandin E receptor signaling by the variant form of EP1 subtype. J. Biol. Chem. 1996, 271:31255-31261.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31255-31261
    • Okuda-Ashitaka, E.1    Sakamoto, K.2    Ezashi, T.3    Miwa, K.4    Ito, S.5    Hayaishi, O.6
  • 48
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park J.H., Scheerer P., Hofmann K.P., Choe H.W., Ernst O.P. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 2008, 454:183-187.
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 49
    • 0035885203 scopus 로고    scopus 로고
    • Differential signalling of both wild-type and Thr(343)Arg dopamine D(2short) receptor by partial agonists in a G-protein-dependent manner
    • Pauwels P.J., Tardif S., Colpaert F.C. Differential signalling of both wild-type and Thr(343)Arg dopamine D(2short) receptor by partial agonists in a G-protein-dependent manner. Biochem. Pharmacol. 2001, 62:723-732.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 723-732
    • Pauwels, P.J.1    Tardif, S.2    Colpaert, F.C.3
  • 50
    • 18844450990 scopus 로고    scopus 로고
    • Inhibition of human type 1 gonadotropin-releasing hormone receptor (GnRHR) function by expression of a human type II GnRHR gene fragment
    • Pawson A.J., Maudsley S., Morgan K., Davidson L., Naor Z., Millar R.P. Inhibition of human type 1 gonadotropin-releasing hormone receptor (GnRHR) function by expression of a human type II GnRHR gene fragment. Endocrinology 2005, 146:2639-2649.
    • (2005) Endocrinology , vol.146 , pp. 2639-2649
    • Pawson, A.J.1    Maudsley, S.2    Morgan, K.3    Davidson, L.4    Naor, Z.5    Millar, R.P.6
  • 53
    • 0030600396 scopus 로고    scopus 로고
    • Follitropin signal transduction: alternative splicing of the FSH receptor gene produces a dominant negative form of receptor which inhibits hormone action
    • Sairam M.R., Jiang L.G., Yarney T.A., Khan H. Follitropin signal transduction: alternative splicing of the FSH receptor gene produces a dominant negative form of receptor which inhibits hormone action. Biochem. Biophys. Res. Commun. 1996, 226:717-722.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 717-722
    • Sairam, M.R.1    Jiang, L.G.2    Yarney, T.A.3    Khan, H.4
  • 54
    • 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, 279:33390-33397.
    • (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
  • 58
    • 0031457992 scopus 로고    scopus 로고
    • The follicle-stimulating hormone receptor: biochemistry, molecular biology, physiology, and pathophysiology
    • Simoni M., Gromoll J., Nieschlag E. The follicle-stimulating hormone receptor: biochemistry, molecular biology, physiology, and pathophysiology. Endocr. Rev. 1997, 18:739-773.
    • (1997) Endocr. Rev. , vol.18 , pp. 739-773
    • Simoni, M.1    Gromoll, J.2    Nieschlag, E.3
  • 59
    • 41149127699 scopus 로고    scopus 로고
    • Dimerization and oligomerization of G-protein-coupled receptors: debated structures with established and emerging functions
    • Szidonya L., Cserzó M., Hunyady L. Dimerization and oligomerization of G-protein-coupled receptors: debated structures with established and emerging functions. J. Endocrinol. 2008, 196:435-453.
    • (2008) J. Endocrinol. , vol.196 , pp. 435-453
    • Szidonya, L.1    Cserzó, M.2    Hunyady, L.3
  • 60
    • 1242272013 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent self-association of the cell surface human lutropin receptor
    • Tao Y.X., Johnson N.B., Segaloff D.L. Constitutive and agonist-dependent self-association of the cell surface human lutropin receptor. J. Biol. Chem. 2004, 279:5904-5914.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5904-5914
    • Tao, Y.X.1    Johnson, N.B.2    Segaloff, D.L.3
  • 61
    • 34249792937 scopus 로고    scopus 로고
    • Follice-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. Follice-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing. Endocrinology 2007, 148:1987-1995.
    • (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
  • 62
    • 0037187331 scopus 로고    scopus 로고
    • Structural determinants in the second intracellular loop of the human follicle-stimulating hormone receptor are involved in G(s) protein activation
    • Timossi C., Maldonado D., Vizcaino A., Lindau-Shepard B., Conn P.M., Ulloa-Aguirre A. Structural determinants in the second intracellular loop of the human follicle-stimulating hormone receptor are involved in G(s) protein activation. Mol. Cell. Endocrinol. 2002, 189:157-168.
    • (2002) Mol. Cell. Endocrinol. , vol.189 , pp. 157-168
    • Timossi, C.1    Maldonado, D.2    Vizcaino, A.3    Lindau-Shepard, B.4    Conn, P.M.5    Ulloa-Aguirre, A.6
  • 63
    • 3342955466 scopus 로고    scopus 로고
    • Functional significance of the BBXXB motif reversed present in the cytoplasmic domains of the human follicle-stimulating hormone receptor
    • Timossi C., Ortiz-Elizondo C., Pineda D.B., Dias J.A., Conn P.M., Ulloa-Aguirre A. Functional significance of the BBXXB motif reversed present in the cytoplasmic domains of the human follicle-stimulating hormone receptor. Mol. Cell. Endocrinol. 2004, 223:17-26.
    • (2004) Mol. Cell. Endocrinol. , vol.223 , pp. 17-26
    • Timossi, C.1    Ortiz-Elizondo, C.2    Pineda, D.B.3    Dias, J.A.4    Conn, P.M.5    Ulloa-Aguirre, A.6
  • 64
    • 15744405558 scopus 로고    scopus 로고
    • Heterodimerization with beta2-adrenergic receptors promotes surface expression and functional activity of alpha1D-adrenergic receptors
    • Uberti M.A., Hague C., Oller H., Minneman K.P., Hall R.A. Heterodimerization with beta2-adrenergic receptors promotes surface expression and functional activity of alpha1D-adrenergic receptors. J. Pharmacol. Exp. Ther. 2005, 313:16-23.
    • (2005) J. Pharmacol. Exp. Ther. , vol.313 , pp. 16-23
    • Uberti, M.A.1    Hague, C.2    Oller, H.3    Minneman, K.P.4    Hall, R.A.5
  • 66
    • 0031695446 scopus 로고    scopus 로고
    • Structure-function relationship of follicle-stimulating hormone and its receptor
    • Ulloa-Aguirre A., Timossi C. Structure-function relationship of follicle-stimulating hormone and its receptor. Hum. Reprod. Update 1998, 4:260-283.
    • (1998) Hum. Reprod. Update , vol.4 , pp. 260-283
    • Ulloa-Aguirre, A.1    Timossi, C.2
  • 67
    • 7244253015 scopus 로고    scopus 로고
    • Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease
    • Ulloa-Aguirre A., Janovick J.A., Brothers S.P., Conn P.M. Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease. Traffic 2004, 5:821-837.
    • (2004) Traffic , vol.5 , pp. 821-837
    • Ulloa-Aguirre, A.1    Janovick, J.A.2    Brothers, S.P.3    Conn, P.M.4
  • 70
    • 43249110396 scopus 로고    scopus 로고
    • Functional and structural roles of conserved cysteine residues in the carboxyl-terminal domain of the follicle-stimulating hormone receptor in human embryonic kidney 293 cells
    • Uribe A., Zarinan T., Perez-Solis M.A., Gutierrez-Sagal R., Jardon-Valadez E., Pineiro A., Dias J.A., Ulloa-Aguirre A. Functional and structural roles of conserved cysteine residues in the carboxyl-terminal domain of the follicle-stimulating hormone receptor in human embryonic kidney 293 cells. Biol. Reprod. 2008, 78:869-882.
    • (2008) Biol. Reprod. , vol.78 , pp. 869-882
    • Uribe, A.1    Zarinan, T.2    Perez-Solis, M.A.3    Gutierrez-Sagal, R.4    Jardon-Valadez, E.5    Pineiro, A.6    Dias, J.A.7    Ulloa-Aguirre, A.8
  • 71
    • 1542316313 scopus 로고    scopus 로고
    • A molecular dissection of the glycoprotein hormone receptors
    • Vassart G., Pardo L., Costagliola S. A molecular dissection of the glycoprotein hormone receptors. Trends Biochem. Sci. 2004, 29:119-126.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 119-126
    • Vassart, G.1    Pardo, L.2    Costagliola, S.3
  • 72
    • 0026795060 scopus 로고
    • Biochemical analyses of proteolytic nicking of the human glycoprotein hormone alpha-subunit and its effect on conformational epitopes
    • Weiner R.S., Dias J.A. Biochemical analyses of proteolytic nicking of the human glycoprotein hormone alpha-subunit and its effect on conformational epitopes. Endocrinology 1992, 131:1026-1036.
    • (1992) Endocrinology , vol.131 , pp. 1026-1036
    • Weiner, R.S.1    Dias, J.A.2
  • 74
    • 23344447877 scopus 로고    scopus 로고
    • The CXCR1 and CXCR2 receptors form constitutive homo- and heterodimers selectively and with equal apparent affinities
    • Wilson S., Wilkinson G., Milligan G. The CXCR1 and CXCR2 receptors form constitutive homo- and heterodimers selectively and with equal apparent affinities. J. Biol. Chem. 2005, 280:28663-28674.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28663-28674
    • Wilson, S.1    Wilkinson, G.2    Milligan, G.3
  • 75
    • 0028986787 scopus 로고
    • Different alpha 1-adrenergic receptor sequences required for activating different G alpha subunits of Gq class of G proteins
    • Wu D., Jiang H., Simon M.I. Different alpha 1-adrenergic receptor sequences required for activating different G alpha subunits of Gq class of G proteins. J. Biol. Chem. 1995, 270:9828-9832.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9828-9832
    • Wu, D.1    Jiang, H.2    Simon, M.I.3
  • 76
    • 0030202118 scopus 로고    scopus 로고
    • Studies on the relative in-vitro biological potency of the naturally-occurring isoforms of intrapituitary follicle stimulating hormone
    • Zambrano E., Barrios-de-Tomasi J., Cardenas M., Ulloa-Aguirre A. Studies on the relative in-vitro biological potency of the naturally-occurring isoforms of intrapituitary follicle stimulating hormone. Mol. Hum. Reprod. 1996, 2:563-571.
    • (1996) Mol. Hum. Reprod. , vol.2 , pp. 563-571
    • Zambrano, E.1    Barrios-de-Tomasi, J.2    Cardenas, M.3    Ulloa-Aguirre, A.4
  • 77
    • 69049102935 scopus 로고    scopus 로고
    • Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors
    • Zhang M., Feng X., Guan R., Hébert T.E., Segaloff D.L. Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors. Cell. Signal. 2009, 21:1663-1671.
    • (2009) Cell. Signal. , vol.21 , pp. 1663-1671
    • Zhang, M.1    Feng, X.2    Guan, R.3    Hébert, T.E.4    Segaloff, D.L.5
  • 78
    • 0347003505 scopus 로고    scopus 로고
    • The CCT promoter directs high-level transgene expression in distal lung epithelial cell lines
    • Zhou J., You Y., Zabner J., Ryan A.J., Mallampalli R.K. The CCT promoter directs high-level transgene expression in distal lung epithelial cell lines. Am. J. Respir. Cell Mol. Biol. 2004, 30:61-68.
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.30 , pp. 61-68
    • Zhou, J.1    You, Y.2    Zabner, J.3    Ryan, A.J.4    Mallampalli, R.K.5
  • 79
    • 0032506160 scopus 로고    scopus 로고
    • Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function
    • Zhu X., Wess J. Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function. Biochemistry 1998, 37:15773-15784.
    • (1998) Biochemistry , vol.37 , pp. 15773-15784
    • Zhu, X.1    Wess, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.