메뉴 건너뛰기




Volumn 53, Issue 1, 2012, Pages 137-148

Differential sensitivity of types 1 and 2 cholecystokinin receptors to membrane cholesterol

Author keywords

Biological activity; Chimeric receptors; G protein coupled receptors; Perfringolysin; Receptor binding

Indexed keywords

CHOLECYSTOKININ RECEPTOR; CHOLESTEROL; G PROTEIN COUPLED RECEPTOR; MEMBRANE LIPID; MEMBRANE PROTEIN; PROTEIN CCK1R; PROTEIN CCK2R; TYPE 1 CHOLECYSTOKININ RECEPTOR; TYPE 2 CHOLECYSTOKININ RECEPTOR; UNCLASSIFIED DRUG;

EID: 84455191720     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M020065     Document Type: Article
Times cited : (44)

References (62)
  • 1
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • DOI 10.1074/jbc.R000005200
    • Brown, D. A., and E. London. 2000. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275: 17221-17224. (Pubitemid 30430750)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.23 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 2
    • 0035575575 scopus 로고    scopus 로고
    • Shrinking patches and slippery rafts: Scales of domains in the plasma membrane
    • DOI 10.1016/S0962-8924(01)02139-0, PII S0962892401021390
    • Edidin, M. 2001. Shrinking patches and slippery rafts: scales of domains in the plasma membrane. Trends Cell Biol. 11: 492-496. (Pubitemid 33079142)
    • (2001) Trends in Cell Biology , vol.11 , Issue.12 , pp. 492-496
    • Edidin, M.1
  • 3
    • 0041494100 scopus 로고    scopus 로고
    • Lipid rafts: Bringing order to chaos
    • DOI 10.1194/jlr.R200021-JLR200
    • Pike, L. J. 2003. Lipid rafts: bringing order to chaos. J. Lipid Res. 44: 655-667. (Pubitemid 37279667)
    • (2003) Journal of Lipid Research , vol.44 , Issue.4 , pp. 655-667
    • Pike, L.J.1
  • 4
    • 77952302051 scopus 로고    scopus 로고
    • Cholesterol effects on nicotinic acetylcholine receptor: Cellular aspects
    • Barrantes, F. J. 2010. Cholesterol effects on nicotinic acetylcholine receptor: cellular aspects. Subcell. Biochem. 51: 467-487.
    • (2010) Subcell. Biochem. , vol.51 , pp. 467-487
    • Barrantes, F.J.1
  • 5
    • 0034024809 scopus 로고    scopus 로고
    • Human oxytocin receptors in cholesterol-rich vs. cholesterol-poor microdomains of the plasma membrane
    • DOI 10.1046/j.1432-1327.2000.01280.x
    • Gimpl, G., and F. Fahrenholz. 2000. Human oxytocin receptors in cholesterol-rich vs. cholesterol-poor microdomains of the plasma membrane. Eur. J. Biochem. 267: 2483-2497. (Pubitemid 30304242)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.9 , pp. 2483-2497
    • Gimpl, G.1    Fahrenholz, F.2
  • 6
    • 67651174545 scopus 로고    scopus 로고
    • The function of G-protein coupled receptors and membrane cholesterol: Specific or general interaction?
    • Paila, Y. D., and A. Chattopadhyay. 2009. The function of G-protein coupled receptors and membrane cholesterol: specific or general interaction? Glycoconj. J. 26: 711-720.
    • (2009) Glycoconj. J. , vol.26 , pp. 711-720
    • Paila, Y.D.1    Chattopadhyay, A.2
  • 7
    • 12544257434 scopus 로고    scopus 로고
    • Differential effects of modification of membrane cholesterol and sphingolipids on the conformation, function, and trafficking of the G protein-coupled cholecystokinin receptor
    • Harikumar, K. G., V. Puri, R. D. Singh, K. Hanada, R. E. Pagano, and L. J. Miller. 2005. Differential effects of modification of membrane cholesterol and sphingolipids on the conformation, function, and trafficking of the G protein-coupled cholecystokinin receptor. J. Biol. Chem. 280: 2176-2185.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2176-2185
    • Harikumar, K.G.1    Puri, V.2    Singh, R.D.3    Hanada, K.4    Pagano, R.E.5    Miller, L.J.6
  • 8
    • 0030774729 scopus 로고    scopus 로고
    • Cholesterol as modulator of receptor function
    • DOI 10.1021/bi963138w
    • Gimpl, G., K. Burger, and F. Fahrenholz. 1997. Cholesterol as modulator of receptor function. Biochemistry. 36: 10959-10974. (Pubitemid 27396253)
    • (1997) Biochemistry , vol.36 , Issue.36 , pp. 10959-10974
    • Gimpl, G.1    Burger, K.2    Fahrenholz, F.3
  • 9
    • 0037072273 scopus 로고    scopus 로고
    • Cholesterol levels modulate EGF receptor-mediated signaling by altering receptor function and trafficking
    • DOI 10.1021/bi025943i
    • Pike, L. J., and L. Casey. 2002. Cholesterol levels modulate EGF receptor-mediated signaling by altering receptor function and trafficking. Biochemistry. 41: 10315-10322. (Pubitemid 34856457)
    • (2002) Biochemistry , vol.41 , Issue.32 , pp. 10315-10322
    • Pike, L.J.1    Casey, L.2
  • 10
    • 2442509293 scopus 로고    scopus 로고
    • 1A receptors from bovine hippocampus
    • DOI 10.1016/j.bbamem.2004.03.010, PII S0005273604000896
    • Pucadyil, T. J., and A. Chattopadhyay. 2004. Cholesterol modulates ligand binding and G-protein coupling to serotonin(1A) receptors from bovine hippocampus. Biochim. Biophys. Acta. 1663: 188-200. (Pubitemid 38625593)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1663 , Issue.1-2 , pp. 188-200
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 11
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • Li, H., and V. Papadopoulos. 1998. Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology. 139: 4991-4997. (Pubitemid 28533447)
    • (1998) Endocrinology , vol.139 , Issue.12 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 13
    • 79751537491 scopus 로고    scopus 로고
    • Lipid-binding surfaces of membrane proteins: Evidence from evolutionary and structural analysis
    • Adamian, L., H. Naveed, and J. Liang. 2011. Lipid-binding surfaces of membrane proteins: evidence from evolutionary and structural analysis. Biochim. Biophys. Acta. 1808: 1092-1102.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1092-1102
    • Adamian, L.1    Naveed, H.2    Liang, J.3
  • 15
    • 33644841711 scopus 로고    scopus 로고
    • Cholecystokinin and gastrin receptors
    • DOI 10.1152/physrev.00014.2005
    • Dufresne, M., C. Seva, and D. Fourmy. 2006. Cholecystokinin and gastrin receptors. Physiol. Rev. 86: 805-847. (Pubitemid 44033383)
    • (2006) Physiological Reviews , vol.86 , Issue.3 , pp. 805-847
    • Dufresne, M.1    Seva, C.2    Fourmy, D.3
  • 16
    • 0347992917 scopus 로고    scopus 로고
    • Heterodimerization of type A and B cholecystokinin receptors enhance signaling and promote cell growth
    • Cheng, Z. J., K. G. Harikumar, E. L. Holicky, and L. J. Miller. 2003. Heterodimerization of type A and B cholecystokinin receptors enhance signaling and promote cell growth. J. Biol. Chem. 278: 52972-52979.
    • (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
  • 17
    • 0031003586 scopus 로고    scopus 로고
    • First intracellular loop of the human cholecystokinin-A receptor is essential for cyclic AMP signaling in transfected HEK-293 cells
    • DOI 10.1074/jbc.272.14.9037
    • Wu, V., M. Yang, J. A. McRoberts, J. Ren, R. Seensalu, N. Zeng, M. Dagrag, M. Birnbaumer, and J. H. Walsh. 1997. First intracellular loop of the human cholecystokinin-A receptor is essential for cyclic AMP signaling in transfected HEK-293 cells. J. Biol. Chem. 272: 9037-9042. (Pubitemid 27154904)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9037-9042
    • Wu, V.1    Yang, M.2    McRoberts, J.A.3    Ren, J.4    Seensalu, R.5    Zeng, N.6    Dagrag, M.7    Birnbaumer, M.8    Walsh, J.H.9
  • 18
    • 0033203501 scopus 로고    scopus 로고
    • Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases
    • Puri, V., R. Watanabe, M. Dominguez, X. Sun, C. L. Wheatley, D. L. Marks, and R. E. Pagano. 1999. Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases. Nat. Cell Biol. 1: 386-388. (Pubitemid 129493583)
    • (1999) Nature Cell Biology , vol.1 , Issue.6 , pp. 386-388
    • Puri, V.1    Watanabe, R.2    Dominguez, M.3    Sun, X.4    Wheatley, C.L.5    Marks, D.L.6    Pagano, R.E.7
  • 19
    • 0033016103 scopus 로고    scopus 로고
    • Fluorometric method for the enzymatic determination of cholesterol
    • DOI 10.1016/S0165-022X(98)00036-0, PII S0165022X98000360
    • Amundson, D. M., and M. Zhou. 1999. Fluorometric method for the enzymatic determination of cholesterol. J. Biochem. Biophys. Methods. 38: 43-52. (Pubitemid 29050881)
    • (1999) Journal of Biochemical and Biophysical Methods , vol.38 , Issue.1 , pp. 43-52
    • Amundson, D.M.1    Zhou, M.2
  • 20
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37: 911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 21
    • 12544254799 scopus 로고    scopus 로고
    • Distinct molecular mechanisms for agonist peptide binding to types A and B cholecystokinin receptors demonstrated using fluorescence spectroscopy
    • Harikumar, K. G., J. Clain, D. I. Pinon, M. Dong, and L. J. Miller. 2005. Distinct molecular mechanisms for agonist peptide binding to types A and B cholecystokinin receptors demonstrated using fluorescence spectroscopy. J. Biol. Chem. 280: 1044-1050.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1044-1050
    • Harikumar, K.G.1    Clain, J.2    Pinon, D.I.3    Dong, M.4    Miller, L.J.5
  • 22
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • DOI 10.1016/0003-2697(85)90442-7
    • Smith, P. K., R. I. Krohn, G. T. Hermanson, A. K. Mallia, F. H. Gartner, M. D. Provenzano, E. K. Fujimoto, N. M. Goeke, B. J. Olson, and D. C. Klenk. 1985. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150: 76-85. (Pubitemid 16258399)
    • (1985) Analytical Biochemistry , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 23
    • 66149142747 scopus 로고    scopus 로고
    • Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding
    • Flanagan, J. J., R. K. Tweten, A. E. Johnson, and A. P. Heuck. 2009. Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding. Biochemistry. 48: 3977-3987.
    • (2009) Biochemistry , vol.48 , pp. 3977-3987
    • Flanagan, J.J.1    Tweten, R.K.2    Johnson, A.E.3    Heuck, A.P.4
  • 24
    • 0033636662 scopus 로고    scopus 로고
    • Mechanism of membrane insertion of a multimeric beta-barrel protein: Perfringolysin O creates a pore using ordered and coupled conformational changes
    • Heuck, A. P., E. M. Hotze, R. K. Tweten, and A. E. Johnson. 2000. Mechanism of membrane insertion of a multimeric beta-barrel protein: perfringolysin O creates a pore using ordered and coupled conformational changes. Mol. Cell. 6: 1233-1242.
    • (2000) Mol. Cell , vol.6 , pp. 1233-1242
    • Heuck, A.P.1    Hotze, E.M.2    Tweten, R.K.3    Johnson, A.E.4
  • 25
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn, J., S. C. Feil, W. J. McKinstry, R. K. Tweten, and M. W. Parker. 1997. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell. 89: 685-692. (Pubitemid 27516171)
    • (1997) Cell , vol.89 , Issue.5 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 26
    • 18744391355 scopus 로고    scopus 로고
    • The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains
    • DOI 10.1046/j.1432-1033.2002.03338.x
    • Shimada, Y., M. Maruya, S. Iwashita, and Y. Ohno-Iwashita. 2002. The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains. Eur. J. Biochem. 269: 6195-6203. (Pubitemid 35461832)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.24 , pp. 6195-6203
    • Shimada, Y.1    Maruya, M.2    Iwashita, S.3    Ohno-Iwashita, Y.4
  • 27
    • 0030746612 scopus 로고    scopus 로고
    • A biotinylated perfringolysin O derivative: A new probe for detection of cell surface cholesterol
    • DOI 10.1016/S0005-2736(97)00061-8, PII S0005273697000618
    • Iwamoto, M., I. Morita, M. Fukuda, S. Murota, S. Ando, and Y. Ohno-Iwashita. 1997. A biotinylated perfringolysin O derivative: a new probe for detection of cell surface cholesterol. Biochim. Biophys. Acta. 1327: 222-230. (Pubitemid 27300139)
    • (1997) Biochimica et Biophysica Acta - Biomembranes , vol.1327 , Issue.2 , pp. 222-230
    • Iwamoto, M.1    Morita, I.2    Fukuda, M.3    Murota, S.-I.4    Ando, S.5    Ohno-Iwashita, Y.6
  • 29
    • 0019061918 scopus 로고
    • Ligand: A versatile computerized approach for characterization of ligand-binding systems
    • Munson, P. J., and D. Rodbard. 1980. Ligand: a versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem. 107: 220-239.
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 30
    • 0026755609 scopus 로고
    • Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains
    • Ballesteros, J. A., and H. Weinstein. 1992. Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains. Biophys. J. 62: 107-109.
    • (1992) Biophys. J. , vol.62 , pp. 107-109
    • Ballesteros, J.A.1    Weinstein, H.2
  • 32
    • 0029085939 scopus 로고
    • Abnormal processing of the human cholecystokinin receptor gene in association with gallstones and obesity
    • Miller, L. J., E. L. Holicky, C. D. Ulrich, and E. D. Wieben. 1995. Abnormal processing of the human cholecystokinin receptor gene in association with gallstones and obesity. Gastroenterology. 109: 1375-1380.
    • (1995) Gastroenterology , vol.109 , pp. 1375-1380
    • Miller, L.J.1    Holicky, E.L.2    Ulrich, C.D.3    Wieben, E.D.4
  • 33
    • 0028907072 scopus 로고
    • A truncated isoform of human CCK-B/gastrin receptor generated by alternative usage of a novel exon
    • Miyake, A. 1995. A truncated isoform of human CCK-B/gastrin receptor generated by alternative usage of a novel exon. Biochem. Biophys. Res. Commun. 208: 230-237.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 230-237
    • Miyake, A.1
  • 35
    • 69249115724 scopus 로고    scopus 로고
    • Differential effect of membrane cholesterol removal on mu- and delta-opioid receptors: A parallel comparison of acute and chronic signaling to adenylyl cyclase
    • Levitt, E. S., M. J. Clark, P. M. Jenkins, J. R. Martens, and J. R. Traynor. 2009. Differential effect of membrane cholesterol removal on mu- and delta-opioid receptors: a parallel comparison of acute and chronic signaling to adenylyl cyclase. J. Biol. Chem. 284: 22108-22122.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22108-22122
    • Levitt, E.S.1    Clark, M.J.2    Jenkins, P.M.3    Martens, J.R.4    Traynor, J.R.5
  • 36
    • 0037036457 scopus 로고    scopus 로고
    • Manipulation of cholesterol levels in rod disk membranes by methyl-beta-cyclodextrin: Effects on receptor activation
    • Niu, S. L., D. C. Mitchell, and B. J. Litman. 2002. Manipulation of cholesterol levels in rod disk membranes by methyl-beta-cyclodextrin: effects on receptor activation. J. Biol. Chem. 277: 20139-20145.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20139-20145
    • Niu, S.L.1    Mitchell, D.C.2    Litman, B.J.3
  • 37
    • 54049106162 scopus 로고    scopus 로고
    • Cholesterol-dependent separation of the beta2-adrenergic receptor from its partners determines signaling efficacy: Insight into nanoscale organization of signal transduction
    • Pontier, S. M., Y. Percherancier, S. Galandrin, A. Breit, C. Gales, and M. Bouvier. 2008. Cholesterol-dependent separation of the beta2-adrenergic receptor from its partners determines signaling efficacy: insight into nanoscale organization of signal transduction. J. Biol. Chem. 283: 24659-24672.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24659-24672
    • Pontier, S.M.1    Percherancier, Y.2    Galandrin, S.3    Breit, A.4    Gales, C.5    Bouvier, M.6
  • 38
    • 0242270621 scopus 로고    scopus 로고
    • Inhibition of chemokine receptor function by membrane cholesterol oxidation
    • DOI 10.1016/S0014-4827(03)00345-8
    • Nguyen, D. H., and D. D. Taub. 2003. Inhibition of chemokine receptor function by membrane cholesterol oxidation. Exp. Cell Res. 291: 36-45. (Pubitemid 37338681)
    • (2003) Experimental Cell Research , vol.291 , Issue.1 , pp. 36-45
    • Nguyen, D.H.1    Taub, D.D.2
  • 39
    • 0033554397 scopus 로고    scopus 로고
    • Membrane cholesterol modulates galanin-GalR2 interaction
    • Pang, L., M. Graziano, and S. Wang. 1999. Membrane cholesterol modulates galanin-GalR2 interaction. Biochemistry. 38: 12003-12011.
    • (1999) Biochemistry , vol.38 , pp. 12003-12011
    • Pang, L.1    Graziano, M.2    Wang, S.3
  • 45
    • 0035130154 scopus 로고    scopus 로고
    • Gallbladder muscle dysfunction in patients with chronic acalculous disease
    • Amaral, J., Z. L. Xiao, Q. Chen, P. Yu, P. Biancani, and J. Behar. 2001. Gallbladder muscle dysfunction in patients with chronic acalculous disease. Gastroenterology. 120: 506-511. (Pubitemid 32147648)
    • (2001) Gastroenterology , vol.120 , Issue.2 , pp. 506-511
    • Amaral, J.1    Xiao, Z.-L.2    Chen, Q.3    Yu, P.4    Biancani, P.5    Behar, J.6
  • 46
    • 0033044627 scopus 로고    scopus 로고
    • Excess membrane cholesterol alters human gallbladder muscle contractility and membrane fluidity
    • Chen, Q., J. Amaral, P. Biancani, and J. Behar. 1999. Excess membrane cholesterol alters human gallbladder muscle contractility and membrane fluidity. Gastroenterology. 116: 678-685. (Pubitemid 29106776)
    • (1999) Gastroenterology , vol.116 , Issue.3 , pp. 678-685
    • Chen, Q.1    Amaral, J.2    Biancani, P.3    Behar, J.4
  • 47
    • 0030823668 scopus 로고    scopus 로고
    • Gallbladder relaxation in patients with pigment and cholesterol stones
    • DOI 10.1016/S0016-5085(97)70189-6
    • Chen, Q., J. Amaral, S. Oh, P. Biancani, and J. Behar. 1997. Gallbladder relaxation in patients with pigment and cholesterol stones. Gastroenterology. 113: 930-937. (Pubitemid 27381154)
    • (1997) Gastroenterology , vol.113 , Issue.3 , pp. 930-937
    • Chen, Q.1    Amaral, J.2    Oh, S.3    Biancani, P.4    Behar, J.5
  • 50
    • 0028784179 scopus 로고
    • Direct G protein activation reverses impaired CCK signaling in human gallbladders with cholesterol stones
    • Yu, P., Q. Chen, K. M. Harnett, J. Amaral, P. Biancani, and J. Behar. 1995. Direct G protein activation reverses impaired CCK signaling in human gallbladders with cholesterol stones. Am. J. Physiol. 269: G659-G665.
    • (1995) Am. J. Physiol. , vol.269
    • Yu, P.1    Chen, Q.2    Harnett, K.M.3    Amaral, J.4    Biancani, P.5    Behar, J.6
  • 51
    • 0141811657 scopus 로고    scopus 로고
    • 1 angiotensin receptor activation and signaling
    • DOI 10.1210/en.2002-0135
    • Gáborik, Z., G. Jagadeesh, M. Zhang, A. Spat, K. J. Catt, and L. Hunyady. 2003. The role of a conserved region of the second intracellular loop in AT1 angiotensin receptor activation and signaling. Endocrinology. 144: 2220-2228. (Pubitemid 36629870)
    • (2003) Endocrinology , vol.144 , Issue.6 , pp. 2220-2228
    • Gaborik, Z.1    Jagadeesh, G.2    Zhang, M.3    Spat, A.4    Catt, K.J.5    Hunyady, L.6
  • 53
    • 50449100012 scopus 로고    scopus 로고
    • Mutational analysis of the conserved Asp2.50 and ERY motif reveals signaling bias of the urotensin II receptor
    • Proulx, C. D., B. J. Holleran, A. A. Boucard, E. Escher, G. Guillemette, and R. Leduc. 2008. Mutational analysis of the conserved Asp2.50 and ERY motif reveals signaling bias of the urotensin II receptor. Mol. Pharmacol. 74: 552-561.
    • (2008) Mol. Pharmacol. , vol.74 , pp. 552-561
    • Proulx, C.D.1    Holleran, B.J.2    Boucard, A.A.3    Escher, E.4    Guillemette, G.5    Leduc, R.6
  • 54
    • 16844374531 scopus 로고    scopus 로고
    • Lipid rafts control signaling of type-1 cannabinoid receptors in neuronal cells. Implications for anandamide-induced apoptosis
    • Bari, M., N. Battista, F. Fezza, A. Finazzi-Agro, and M. Maccarrone. 2005. Lipid rafts control signaling of type-1 cannabinoid receptors in neuronal cells. Implications for anandamide-induced apoptosis. J. Biol. Chem. 280: 12212-12220.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12212-12220
    • Bari, M.1    Battista, N.2    Fezza, F.3    Finazzi-Agro, A.4    Maccarrone, M.5
  • 55
    • 23844482784 scopus 로고    scopus 로고
    • Cholesterol-dependent modulation of type 1 cannabinoid receptors in nerve cells
    • DOI 10.1002/jnr.20546
    • Bari, M., A. Paradisi, N. Pasquariello, and M. Maccarrone. 2005. Cholesterol-dependent modulation of type 1 cannabinoid receptors in nerve cells. J. Neurosci. Res. 81: 275-283. (Pubitemid 41153342)
    • (2005) Journal of Neuroscience Research , vol.81 , Issue.2 , pp. 275-283
    • Bari, M.1    Paradisi, A.2    Pasquariello, N.3    Maccarrone, M.4
  • 56
  • 57
    • 17844390997 scopus 로고    scopus 로고
    • Differential docking of high-affinity peptide ligands to type A and B cholecystokinin receptors demonstrated by photoaffinity labeling
    • DOI 10.1021/bi050130q
    • Dong, M., G. Liu, D. I. Pinon, and L. J. Miller. 2005. Differential docking of high-affinity peptide ligands to type A and B cholecystokinin receptors demonstrated by photoaffinity labeling. Biochemistry. 44: 6693-6700. (Pubitemid 40593820)
    • (2005) Biochemistry , vol.44 , Issue.17 , pp. 6693-6700
    • Dong, M.1    Liu, G.2    Pinon, D.I.3    Miller, L.J.4
  • 58
    • 17544375784 scopus 로고    scopus 로고
    • A segment of five amino acids in the second extracellular loop of the cholecystokinin-B receptor is essential for selectivity of the peptide agonist gastrin
    • DOI 10.1074/jbc.271.25.14698
    • Silvente-Poirot, S., and S. A. Wank. 1996. A segment of five amino acids in the second extracellular loop of the cholecystokinin-B receptor is essential for selectivity of the peptide agonist gastrin. J. Biol. Chem. 271: 14698-14706. (Pubitemid 26194945)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.25 , pp. 14698-14706
    • Silvente-Poirot, S.1    Wank, S.A.2
  • 59
    • 33748754344 scopus 로고    scopus 로고
    • Fluorescent indicators distributed throughout the pharmacophore of cholecystokinin provide insights into distinct modes of binding and activation of type A and B cholecystokinin receptors
    • DOI 10.1074/jbc.M605098200
    • Harikumar, K. G., D. I. Pinon, and L. J. Miller. 2006. Fluorescent indicators distributed throughout the pharmacophore of cholecystokinin provide insights into distinct modes of binding and activation of type A and B cholecystokinin receptors. J. Biol. Chem. 281: 27072-27080. (Pubitemid 44401736)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.37 , pp. 27072-27080
    • Harikumar, K.G.1    Pinon, D.I.2    Miller, L.J.3
  • 60
    • 0029122636 scopus 로고
    • Insulation of a G protein-coupled receptor on the plasmalemmal surface of the pancreatic acinar cell
    • Roettger, B. F., R. U. Rentsch, E. M. Hadac, E. H. Hellen, T. P. Burghardt, and L. J. Miller. 1995. Insulation of a G protein-coupled receptor on the plasmalemmal surface of the pancreatic acinar cell. J. Cell Biol. 130: 579-590.
    • (1995) J. Cell Biol. , vol.130 , pp. 579-590
    • Roettger, B.F.1    Rentsch, R.U.2    Hadac, E.M.3    Hellen, E.H.4    Burghardt, T.P.5    Miller, L.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.