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Volumn 484, Issue C, 2010, Pages 53-73

Modulation of the constitutive activity of the ghrelin receptor by use of pharmacological tools and mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARTIC ACID; CALCIUM ION; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; DIACYLGLYCEROL; GHRELIN RECEPTOR; GHRELIN RECEPTOR 1A; GHRELIN RECEPTOR 1B; GHRELIN RECEPTOR AGONIST; GHRELIN RECEPTOR ANTAGONIST; GLUTAMIC ACID; GUANINE NUCLEOTIDE BINDING PROTEIN; HORMONE RECEPTOR BLOCKING AGENT; HORMONE RECEPTOR STIMULATING AGENT; INOSITOL 1,4,5 TRISPHOSPHATE; INOSITOL MONOPHOSPHATASE; INOSITOL PHOSPHATE; LITHIUM ION; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MONOAMINE; MUTANT PROTEIN; NEUROTENSIN RECEPTOR; PHOSPHATASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE C; SUBSTANCE P [1 DEXTRO ARGININE 5 DEXTRO PHENYLALANINE 7,9 DEXTRO TRYPTOPHAN 11 LEUCINE]; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 78049237699     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-381298-8.00003-4     Document Type: Chapter
Times cited : (19)

References (66)
  • 2
    • 69549108193 scopus 로고    scopus 로고
    • Multiple switches in G protein-coupled receptor activation
    • Ahuja S., Smith S.O. Multiple switches in G protein-coupled receptor activation. Trends Pharmacol. Sci. 2009, 30:494-502.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 494-502
    • Ahuja, S.1    Smith, S.O.2
  • 6
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros J.A., Shi L., Javitch J.A. Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol. Pharmacol. 2001, 60:1-19.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 8
    • 0021322884 scopus 로고
    • On the in vitro and in vivo activity of a new synthetic hexapeptide that acts on the pituitary to specifically release growth hormone
    • Bowers C.Y., Momany F.A., Reynolds G.A., Hong A. On the in vitro and in vivo activity of a new synthetic hexapeptide that acts on the pituitary to specifically release growth hormone. Endocrinology 1984, 114:1537-1545.
    • (1984) Endocrinology , vol.114 , pp. 1537-1545
    • Bowers, C.Y.1    Momany, F.A.2    Reynolds, G.A.3    Hong, A.4
  • 9
    • 27744451411 scopus 로고    scopus 로고
    • Historical review: Negative efficacy and the constitutive activity of G-protein-coupled receptors
    • Costa T., Cotecchia S. Historical review: Negative efficacy and the constitutive activity of G-protein-coupled receptors. Trends Pharmacol. Sci. 2005, 26:618-624.
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 618-624
    • Costa, T.1    Cotecchia, S.2
  • 12
    • 63849294621 scopus 로고    scopus 로고
    • Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations
    • Dror R.O., Arlow D.H., Borhani D.W., Jensen M.O., Piana S., Shaw D.E. Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations. Proc. Natl. Acad. Sci. USA 2009, 106:4689-4694.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4689-4694
    • Dror, R.O.1    Arlow, D.H.2    Borhani, D.W.3    Jensen, M.O.4    Piana, S.5    Shaw, D.E.6
  • 13
  • 14
    • 33745224117 scopus 로고    scopus 로고
    • Metal ion site engineering indicates a global toggle switch model for seven-transmembrane receptor activation
    • Elling C.E., Frimurer T.M., Gerlach L.O., Jorgensen R., Holst B., Schwartz T.W. Metal ion site engineering indicates a global toggle switch model for seven-transmembrane receptor activation. J. Biol. Chem. 2006, 281:17337-17346.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17337-17346
    • Elling, C.E.1    Frimurer, T.M.2    Gerlach, L.O.3    Jorgensen, R.4    Holst, B.5    Schwartz, T.W.6
  • 15
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr. Rev. 2000, 21:90-113.
    • (2000) Endocr. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 16
    • 0028856707 scopus 로고
    • Fluorescent labeling of purified beta 2 adrenergic receptor. Evidence for ligand-specific conformational changes
    • Gether U., Lin S., Kobilka B.K. Fluorescent labeling of purified beta 2 adrenergic receptor. Evidence for ligand-specific conformational changes. J. Biol. Chem. 1995, 270:28268-28275.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28268-28275
    • Gether, U.1    Lin, S.2    Kobilka, B.K.3
  • 17
    • 0031018485 scopus 로고    scopus 로고
    • Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility
    • Gether U., Ballesteros J.A., Seifert R., Sanders-Bush E., Weinstein H., Kobilka B.K. Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility. J. Biol. Chem. 1997, 272:2587-2590.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2587-2590
    • Gether, U.1    Ballesteros, J.A.2    Seifert, R.3    Sanders-Bush, E.4    Weinstein, H.5    Kobilka, B.K.6
  • 19
    • 50249156843 scopus 로고    scopus 로고
    • Selective structure-based virtual screening for full and partial agonists of the beta2 adrenergic receptor
    • Graaf de C., Rognan D. Selective structure-based virtual screening for full and partial agonists of the beta2 adrenergic receptor. J. Med. Chem. 2008, 51:4978-4985.
    • (2008) J. Med. Chem. , vol.51 , pp. 4978-4985
    • Graaf de, C.1    Rognan, D.2
  • 20
    • 33846435771 scopus 로고    scopus 로고
    • Acylated and unacylated ghrelin promote proliferation and inhibit apoptosis of pancreatic beta-cells and human islets: Involvement of 3',5'-cyclic adenosine monophosphate/protein kinase A, extracellular signal-regulated kinase 1/2, and phosphatidyl inositol 3-Kinase/Akt signaling
    • Granata R., Settanni F., Biancone L., Trovato L., Nano R., Bertuzzi F., Destefanis S., Annunziata M., Martinetti M., Catapano F., Ghe C., Isgaard J., et al. Acylated and unacylated ghrelin promote proliferation and inhibit apoptosis of pancreatic beta-cells and human islets: Involvement of 3',5'-cyclic adenosine monophosphate/protein kinase A, extracellular signal-regulated kinase 1/2, and phosphatidyl inositol 3-Kinase/Akt signaling. Endocrinology 2007, 148:512-529.
    • (2007) Endocrinology , vol.148 , pp. 512-529
    • Granata, R.1    Settanni, F.2    Biancone, L.3    Trovato, L.4    Nano, R.5    Bertuzzi, F.6    Destefanis, S.7    Annunziata, M.8    Martinetti, M.9    Catapano, F.10    Ghe, C.11    Isgaard, J.12
  • 22
    • 0036894327 scopus 로고    scopus 로고
    • The rat arcuate nucleus integrates peripheral signals provided by leptin, insulin, and a ghrelin mimetic
    • Hewson A.K., Tung L.Y., Connell D.W., Tookman L., Dickson S.L. The rat arcuate nucleus integrates peripheral signals provided by leptin, insulin, and a ghrelin mimetic. Diabetes 2002, 51:3412-3419.
    • (2002) Diabetes , vol.51 , pp. 3412-3419
    • Hewson, A.K.1    Tung, L.Y.2    Connell, D.W.3    Tookman, L.4    Dickson, S.L.5
  • 23
    • 1342264249 scopus 로고    scopus 로고
    • Constitutive ghrelin receptor activity as a signaling set-point in appetite regulation
    • Holst B., Schwartz T.W. Constitutive ghrelin receptor activity as a signaling set-point in appetite regulation. Trends Pharmacol. Sci. 2004, 25:113-117.
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 113-117
    • Holst, B.1    Schwartz, T.W.2
  • 24
    • 33644658516 scopus 로고    scopus 로고
    • Ghrelin receptor mutations-Too little height and too much hunger
    • Holst B., Schwartz T.W. Ghrelin receptor mutations-Too little height and too much hunger. J. Clin. Invest. 2006, 116:637-641.
    • (2006) J. Clin. Invest. , vol.116 , pp. 637-641
    • Holst, B.1    Schwartz, T.W.2
  • 25
    • 0242330291 scopus 로고    scopus 로고
    • High constitutive signaling of the ghrelin receptor-Identification of a potent inverse agonist
    • Holst B., Cygankiewicz A., Jensen T.H., Ankersen M., Schwartz T.W. High constitutive signaling of the ghrelin receptor-Identification of a potent inverse agonist. Mol. Endocrinol. 2003, 17:2201-2210.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 2201-2210
    • Holst, B.1    Cygankiewicz, A.2    Jensen, T.H.3    Ankersen, M.4    Schwartz, T.W.5
  • 26
    • 11144225093 scopus 로고    scopus 로고
    • Common structural basis for constitutive activity of the ghrelin receptor family
    • Holst B., Holliday N.D., Bach A., Elling C.E., Cox H.M., Schwartz T.W. Common structural basis for constitutive activity of the ghrelin receptor family. J. Biol. Chem. 2004, 279:53806-53817.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53806-53817
    • Holst, B.1    Holliday, N.D.2    Bach, A.3    Elling, C.E.4    Cox, H.M.5    Schwartz, T.W.6
  • 27
    • 33747603675 scopus 로고    scopus 로고
    • Ghrelin receptor inverse agonists: Identification of an active peptide core and its interaction epitopes on the receptor
    • Holst B., Lang M., Brandt E., Bach A., Howard A., Frimurer T.M., Beck-Sickinger A., Schwartz T.W. Ghrelin receptor inverse agonists: Identification of an active peptide core and its interaction epitopes on the receptor. Mol. Pharmacol. 2006, 70:936-946.
    • (2006) Mol. Pharmacol. , vol.70 , pp. 936-946
    • Holst, B.1    Lang, M.2    Brandt, E.3    Bach, A.4    Howard, A.5    Frimurer, T.M.6    Beck-Sickinger, A.7    Schwartz, T.W.8
  • 28
    • 34447530948 scopus 로고    scopus 로고
    • Identification of an efficacy switch region in the ghrelin receptor responsible for interchange between agonism and inverse agonism
    • Holst B., Mokrosinski J., Lang M., Brandt E., Nygaard R., Frimurer T.M., Beck-Sickinger A.G., Schwartz T.W. Identification of an efficacy switch region in the ghrelin receptor responsible for interchange between agonism and inverse agonism. J. Biol. Chem. 2007, 282:15799-15811.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15799-15811
    • Holst, B.1    Mokrosinski, J.2    Lang, M.3    Brandt, E.4    Nygaard, R.5    Frimurer, T.M.6    Beck-Sickinger, A.G.7    Schwartz, T.W.8
  • 31
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell W.L., Altenbach C., Hubbell C.M., Khorana H.G. Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv. Protein Chem. 2003, 63:243-290.
    • (2003) Adv. Protein Chem. , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 32
    • 0030611331 scopus 로고    scopus 로고
    • Constitutive activation of the beta2 adrenergic receptor alters the orientation of its sixth membrane-spanning segment
    • Javitch J.A., Fu D., Liapakis G., Chen J. Constitutive activation of the beta2 adrenergic receptor alters the orientation of its sixth membrane-spanning segment. J. Biol. Chem. 1997, 272:18546-18549.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18546-18549
    • Javitch, J.A.1    Fu, D.2    Liapakis, G.3    Chen, J.4
  • 34
    • 67650239912 scopus 로고    scopus 로고
    • Analysis of full and partial agonists binding to beta2-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes
    • Katritch V., Reynolds K.A., Cherezov V., Hanson M.A., Roth C.B., Yeager M., Abagyan R. Analysis of full and partial agonists binding to beta2-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes. J. Mol. Recognit. 2009, 22:307-318.
    • (2009) J. Mol. Recognit. , vol.22 , pp. 307-318
    • Katritch, V.1    Reynolds, K.A.2    Cherezov, V.3    Hanson, M.A.4    Roth, C.B.5    Yeager, M.6    Abagyan, R.7
  • 36
    • 15544385058 scopus 로고    scopus 로고
    • Ghrelin: Structure and function
    • Kojima M., Kangawa K. Ghrelin: Structure and function. Physiol. Rev. 2005, 85:495-522.
    • (2005) Physiol. Rev. , vol.85 , pp. 495-522
    • Kojima, M.1    Kangawa, K.2
  • 37
    • 0033540056 scopus 로고    scopus 로고
    • Ghrelin is a growth-hormone-releasing acylated peptide from stomach
    • Kojima M., Hosoda H., Date Y., Nakazato M., Matsuo H., Kangawa K. Ghrelin is a growth-hormone-releasing acylated peptide from stomach. Nature 1999, 402:656-660.
    • (1999) Nature , vol.402 , pp. 656-660
    • Kojima, M.1    Hosoda, H.2    Date, Y.3    Nakazato, M.4    Matsuo, H.5    Kangawa, K.6
  • 38
    • 0035320623 scopus 로고    scopus 로고
    • Ghrelin: Discovery of the natural endogenous ligand for the growth hormone secretagogue receptor
    • Kojima M., Hosoda H., Matsuo H., Kangawa K. Ghrelin: Discovery of the natural endogenous ligand for the growth hormone secretagogue receptor. Trends Endocrinol. Metab. 2001, 12:118-122.
    • (2001) Trends Endocrinol. Metab. , vol.12 , pp. 118-122
    • Kojima, M.1    Hosoda, H.2    Matsuo, H.3    Kangawa, K.4
  • 40
    • 33947301456 scopus 로고    scopus 로고
    • The truncated ghrelin receptor polypeptide (GHS-R1b) acts as a dominant-negative mutant of the ghrelin receptor
    • Leung P.K., Chow K.B., Lau P.N., Chu K.M., Chan C.B., Cheng C.H., Wise H. The truncated ghrelin receptor polypeptide (GHS-R1b) acts as a dominant-negative mutant of the ghrelin receptor. Cell. Signal. 2007, 19:1011-1022.
    • (2007) Cell. Signal. , vol.19 , pp. 1011-1022
    • Leung, P.K.1    Chow, K.B.2    Lau, P.N.3    Chu, K.M.4    Chan, C.B.5    Cheng, C.H.6    Wise, H.7
  • 42
    • 0027981633 scopus 로고
    • Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression
    • Matthews R.P., Guthrie C.R., Wailes L.M., Zhao X., Means A.R., McKnight G.S. Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression. Mol. Cell. Biol. 1994, 14:6107-6116.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6107-6116
    • Matthews, R.P.1    Guthrie, C.R.2    Wailes, L.M.3    Zhao, X.4    Means, A.R.5    McKnight, G.S.6
  • 43
    • 0037452868 scopus 로고    scopus 로고
    • Sequence analyses of G-protein-coupled receptors: Similarities to rhodopsin
    • Mirzadegan T., Benko G., Filipek S., Palczewski K. Sequence analyses of G-protein-coupled receptors: Similarities to rhodopsin. Biochemistry 2003, 42:2759-2767.
    • (2003) Biochemistry , vol.42 , pp. 2759-2767
    • Mirzadegan, T.1    Benko, G.2    Filipek, S.3    Palczewski, K.4
  • 44
    • 0035044615 scopus 로고    scopus 로고
    • Effect of alendronate and MK-677 (a growth hormone secretagogue), individually and in combination, on markers of bone turnover and bone mineral density in postmenopausal osteoporotic women
    • Murphy M.G., Weiss S., McClung M., Schnitzer T., Cerchio K., Connor J., Krupa D., Gertz B.J. Effect of alendronate and MK-677 (a growth hormone secretagogue), individually and in combination, on markers of bone turnover and bone mineral density in postmenopausal osteoporotic women. J. Clin. Endocrinol. Metab. 2001, 86:1116-1125.
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 1116-1125
    • Murphy, M.G.1    Weiss, S.2    McClung, M.3    Schnitzer, T.4    Cerchio, K.5    Connor, J.6    Krupa, D.7    Gertz, B.J.8
  • 45
    • 4644249772 scopus 로고    scopus 로고
    • Regulation of growth hormone secretagogue receptor gene expression in the arcuate nuclei of the rat by leptin and ghrelin
    • Nogueiras R., Tovar S., Mitchell S.E., Rayner D.V., Archer Z.A., Dieguez C., Williams L.M. Regulation of growth hormone secretagogue receptor gene expression in the arcuate nuclei of the rat by leptin and ghrelin. Diabetes 2004, 53:2552-2558.
    • (2004) Diabetes , vol.53 , pp. 2552-2558
    • Nogueiras, R.1    Tovar, S.2    Mitchell, S.E.3    Rayner, D.V.4    Archer, Z.A.5    Dieguez, C.6    Williams, L.M.7
  • 51
    • 0033061256 scopus 로고    scopus 로고
    • Mutation of a highly conserved aspartic acid in the beta2 adrenergic receptor: Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6
    • Rasmussen S.G., Jensen A.D., Liapakis G., Ghanouni P., Javitch J.A., Gether U. Mutation of a highly conserved aspartic acid in the beta2 adrenergic receptor: Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6. Mol. Pharmacol. 1999, 56:175-184.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 175-184
    • Rasmussen, S.G.1    Jensen, A.D.2    Liapakis, G.3    Ghanouni, P.4    Javitch, J.A.5    Gether, U.6
  • 52
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model
    • Samama P., Cotecchia S., Costa T., Lefkowitz R.J. A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 1993, 268:4625-4636.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 55
    • 0036033424 scopus 로고    scopus 로고
    • Constitutive activity of G-protein-coupled receptors: Cause of disease and common property of wild-type receptors
    • Seifert R., Wenzel-Seifert K. Constitutive activity of G-protein-coupled receptors: Cause of disease and common property of wild-type receptors. Naunyn Schmiedebergs Arch. Pharmacol. 2002, 366:381-416.
    • (2002) Naunyn Schmiedebergs Arch. Pharmacol. , vol.366 , pp. 381-416
    • Seifert, R.1    Wenzel-Seifert, K.2
  • 56
    • 0037174606 scopus 로고    scopus 로고
    • Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch
    • Shi L., Liapakis G., Xu R., Guarnieri F., Ballesteros J.A., Javitch J.A. Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. J. Biol. Chem. 2002, 277:40989-40996.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40989-40996
    • Shi, L.1    Liapakis, G.2    Xu, R.3    Guarnieri, F.4    Ballesteros, J.A.5    Javitch, J.A.6
  • 57
    • 0035490104 scopus 로고    scopus 로고
    • Hexosamine-induced fibronectin protein synthesis in mesangial cells is associated with increases in cAMP responsive element binding (CREB) phosphorylation and nuclear CREB: The involvement of protein kinases A and C
    • Singh L.P., Andy J., Anyamale V., Greene K., Alexander M., Crook E.D. Hexosamine-induced fibronectin protein synthesis in mesangial cells is associated with increases in cAMP responsive element binding (CREB) phosphorylation and nuclear CREB: The involvement of protein kinases A and C. Diabetes 2001, 50:2355-2362.
    • (2001) Diabetes , vol.50 , pp. 2355-2362
    • Singh, L.P.1    Andy, J.2    Anyamale, V.3    Greene, K.4    Alexander, M.5    Crook, E.D.6
  • 59
    • 0345791508 scopus 로고    scopus 로고
    • Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states
    • Swaminath G., Xiang Y., Lee T.W., Steenhuis J., Parnot C., Kobilka B.K. Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states. J. Biol. Chem. 2004, 279:686-691.
    • (2004) J. Biol. Chem. , vol.279 , pp. 686-691
    • Swaminath, G.1    Xiang, Y.2    Lee, T.W.3    Steenhuis, J.4    Parnot, C.5    Kobilka, B.K.6
  • 60
    • 20444499405 scopus 로고    scopus 로고
    • Probing the beta2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists
    • Swaminath G., Deupi X., Lee T.W., Zhu W., Thian F.S., Kobilka T.S., Kobilka B. Probing the beta2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists. J. Biol. Chem. 2005, 280:22165-22171.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22165-22171
    • Swaminath, G.1    Deupi, X.2    Lee, T.W.3    Zhu, W.4    Thian, F.S.5    Kobilka, T.S.6    Kobilka, B.7
  • 62
    • 0034687376 scopus 로고    scopus 로고
    • Ghrelin induces adiposity in rodents
    • Tschop M., Smiley D.L., Heiman M.L. Ghrelin induces adiposity in rodents. Nature 2000, 407:908-913.
    • (2000) Nature , vol.407 , pp. 908-913
    • Tschop, M.1    Smiley, D.L.2    Heiman, M.L.3
  • 63
    • 66749144240 scopus 로고    scopus 로고
    • Observation of "ionic lock" formation in molecular dynamics simulations of wild-type beta 1 and beta 2 adrenergic receptors
    • Vanni S., Neri M., Tavernelli I., Rothlisberger U. Observation of "ionic lock" formation in molecular dynamics simulations of wild-type beta 1 and beta 2 adrenergic receptors. Biochemistry 2009, 48:4789-4797.
    • (2009) Biochemistry , vol.48 , pp. 4789-4797
    • Vanni, S.1    Neri, M.2    Tavernelli, I.3    Rothlisberger, U.4
  • 64
    • 38849090670 scopus 로고    scopus 로고
    • Identification of the acyltransferase that octanoylates ghrelin, an appetite-stimulating peptide hormone
    • Yang J., Brown M.S., Liang G., Grishin N.V., Goldstein J.L. Identification of the acyltransferase that octanoylates ghrelin, an appetite-stimulating peptide hormone. Cell 2008, 132:387-396.
    • (2008) Cell , vol.132 , pp. 387-396
    • Yang, J.1    Brown, M.S.2    Liang, G.3    Grishin, N.V.4    Goldstein, J.L.5
  • 66
    • 50449085374 scopus 로고    scopus 로고
    • Effect of des-acyl ghrelin on adiposity and glucose metabolism
    • Zhang W., Chai B., Li J.Y., Wang H., Mulholland M.W. Effect of des-acyl ghrelin on adiposity and glucose metabolism. Endocrinology 2008, 149:4710-4716.
    • (2008) Endocrinology , vol.149 , pp. 4710-4716
    • Zhang, W.1    Chai, B.2    Li, J.Y.3    Wang, H.4    Mulholland, M.W.5


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