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Volumn 323, Issue 1, 2003, Pages 139-149

Identification of natural ligands of retinoic acid receptor-related orphan receptor α ligand-binding domain expressed in Sf9 cells - A mass spectrometry approach

Author keywords

Cholesterol; Electrospray ionization; Mass spectrometry; Noncovalent complex; Retinoic acid receptor related orphan receptor alpha; ROR

Indexed keywords

CHOLESTEROL; ELECTRODEPOSITION; ELECTROSPRAY IONIZATION; GAS CHROMATOGRAPHY; IONIZATION OF GASES; MASS SPECTROMETRY; SULFUR COMPOUNDS;

EID: 0242438098     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2003.08.029     Document Type: Article
Times cited : (65)

References (42)
  • 1
    • 0035976638 scopus 로고    scopus 로고
    • Nuclear receptors and lipid physiology: Opening the X-files
    • Chawla A., Repa J.J., Evans R.M., Mangelsdorf D.J. Nuclear receptors and lipid physiology: opening the X-files. Science. 294:2001;1866-1870.
    • (2001) Science , vol.294 , pp. 1866-1870
    • Chawla, A.1    Repa, J.J.2    Evans, R.M.3    Mangelsdorf, D.J.4
  • 2
    • 0035238364 scopus 로고    scopus 로고
    • The ROR nuclear orphan receptor subfamily: Critical regulators of multiple biological processes
    • Jetten A.M., Kurebayashi S., Ueda E. The ROR nuclear orphan receptor subfamily: critical regulators of multiple biological processes. Prog. Nucleic Acid Res. 69:2001;205-247.
    • (2001) Prog. Nucleic Acid Res. , vol.69 , pp. 205-247
    • Jetten, A.M.1    Kurebayashi, S.2    Ueda, E.3
  • 4
    • 0028197552 scopus 로고
    • Isoform-specific amino-terminal domains dictate DNA-binding properties of RORα, a novel family of orphan hormone nuclear receptors
    • Giguere V., Tini M., Flock G., Ong E., Evans R.M., Otulakowski G. Isoform-specific amino-terminal domains dictate DNA-binding properties of RORα, a novel family of orphan hormone nuclear receptors. Genes Dev. 8:1994;538-553.
    • (1994) Genes Dev. , vol.8 , pp. 538-553
    • Giguere, V.1    Tini, M.2    Flock, G.3    Ong, E.4    Evans, R.M.5    Otulakowski, G.6
  • 7
    • 0037144514 scopus 로고    scopus 로고
    • Identification of Reverα as a Novel RORα Target Gene
    • Delerive Ph., Chin W.W., Suen Ch.S. Identification of Reverα as a Novel RORα Target Gene. J. Biol. Chem. 277:2002;35013-35018.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35013-35018
    • Delerive, Ph.1    Chin, W.W.2    Suen, Ch.S.3
  • 8
    • 0031907862 scopus 로고    scopus 로고
    • Orphan nuclear receptor RORα-deficient mice display the cerebellar defects of staggerer
    • Dussault I., Fawcett D., Matthyssen, A., Bader J.A., Giguere V. Orphan nuclear receptor RORα-deficient mice display the cerebellar defects of staggerer. Mech. Dev. 70:1998;147-153.
    • (1998) Mech. Dev. , vol.70 , pp. 147-153
    • Dussault, I.1    Fawcett, D.2    Matthyssen, A.3    Bader, J.A.4    Giguere, V.5
  • 10
    • 0029162470 scopus 로고
    • An orphan nuclear receptor, mROR alpha, and its spatial expression in adult mouse brain
    • Matsui T., Sashihara S., Oh Y., Waxman S.G. An orphan nuclear receptor, mROR alpha, and its spatial expression in adult mouse brain. Mol. Brain Res. 33:1995;217-226.
    • (1995) Mol. Brain Res. , vol.33 , pp. 217-226
    • Matsui, T.1    Sashihara, S.2    Oh, Y.3    Waxman, S.G.4
  • 14
    • 0034254930 scopus 로고    scopus 로고
    • In vitro and in vivo evidence for orphan nuclear receptor RORalpha function in bone metabolism
    • Meyer T., Kneissel M., Mariani J., Fournier B. In vitro and in vivo evidence for orphan nuclear receptor RORalpha function in bone metabolism. Proc. Natl. Acad. Sci. USA. 97:2000;9197-9202.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9197-9202
    • Meyer, T.1    Kneissel, M.2    Mariani, J.3    Fournier, B.4
  • 15
    • 0034518420 scopus 로고    scopus 로고
    • The role of orphan nuclear receptors in the regulation of cholesterol homeostasis
    • Repa J.J., Mangelsdorf D.J. The role of orphan nuclear receptors in the regulation of cholesterol homeostasis. Annu. Rev. Cell Dev. Biol. 16:2000;459-481.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 459-481
    • Repa, J.J.1    Mangelsdorf, D.J.2
  • 16
    • 0024102824 scopus 로고
    • Time-resolved detection of energy transfer: Theory and application to immunoassay
    • Morrison L.E. Time-resolved detection of energy transfer: theory and application to immunoassay. Anal. Biochem. 174:1988;101-120.
    • (1988) Anal. Biochem. , vol.174 , pp. 101-120
    • Morrison, L.E.1
  • 18
    • 0033711971 scopus 로고    scopus 로고
    • Structural studies on nuclear receptors
    • Renaud J.P., Moras D. Structural studies on nuclear receptors. Cell. Mol. Life Sci. 57:2000;1748-1769.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1748-1769
    • Renaud, J.P.1    Moras, D.2
  • 19
    • 0035502971 scopus 로고    scopus 로고
    • X-ray structure of the orphan nuclear receptor RORβ ligand-binding domain in the active conformation
    • Stehlin C., Wurtz J.M., Steinmetz A., Greiner E., Schüle R., Moras D., Renaud J.P. X-ray structure of the orphan nuclear receptor RORβ ligand-binding domain in the active conformation. EMBO J. 20:2001;5822-5831.
    • (2001) EMBO J. , vol.20 , pp. 5822-5831
    • Stehlin, C.1    Wurtz, J.M.2    Steinmetz, A.3    Greiner, E.4    Schüle, R.5    Moras, D.6    Renaud, J.P.7
  • 20
    • 0242484223 scopus 로고    scopus 로고
    • X-ray structure of the hRORα LBD at 1.63 .ANG.: Structural and functional data that cholesterol or a cholesterol derivative is the natural ligand of RORα
    • Kallen J., Schlaeppi J.M., Bitsch F., Geisse S., Geiser M., Delhon I., Fournier B. X-ray structure of the hRORα LBD at 1.63 .ANG.: structural and functional data that cholesterol or a cholesterol derivative is the natural ligand of RORα Structure. 10:2002;1-20.
    • (2002) Structure , vol.10 , pp. 1-20
    • Kallen, J.1    Schlaeppi, J.M.2    Bitsch, F.3    Geisse, S.4    Geiser, M.5    Delhon, I.6    Fournier, B.7
  • 21
    • 0033868825 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains
    • Bourguet W., Vivat V., Wurtz J.M., Chambon P., Gronemeyer H., Moras D. Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol. Cell. 5:2000;289-298.
    • (2000) Mol. Cell , vol.5 , pp. 289-298
    • Bourguet, W.1    Vivat, V.2    Wurtz, J.M.3    Chambon, P.4    Gronemeyer, H.5    Moras, D.6
  • 23
    • 0035831522 scopus 로고    scopus 로고
    • Crystal structure of the ligand-binding domain of the ultraspiracle protein USP, the ortholog of retinoid X receptors in insects
    • Billas I.M.L., Moulinier L., Rochel N., Moras D. Crystal structure of the ligand-binding domain of the ultraspiracle protein USP, the ortholog of retinoid X receptors in insects. J. Biol. Chem. 276:2001;7465-7474.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7465-7474
    • Billas, I.M.L.1    Moulinier, L.2    Rochel, N.3    Moras, D.4
  • 24
    • 0037063997 scopus 로고    scopus 로고
    • Crystal structure of the HNF4α ligand binding domain in complex with endogenous fatty acid ligand
    • Dhe-Paganon S., Duda K., Iwamoto M., Chi Y.I., Shoelson S.E. Crystal structure of the HNF4α ligand binding domain in complex with endogenous fatty acid ligand. J. Biol. Chem. 277:2002;37973-37976.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37973-37976
    • Dhe-Paganon, S.1    Duda, K.2    Iwamoto, M.3    Chi, Y.I.4    Shoelson, S.E.5
  • 26
    • 0031795334 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry for the study of non-covalent complexes: An emerging technology
    • Pramanik B.N., Bartner P.L., Mirza U.A., Liu Y.H., Ganguly A.K. Electrospray ionization mass spectrometry for the study of non-covalent complexes: an emerging technology. J. Mass Spectrom. 33:1998;911-920.
    • (1998) J. Mass Spectrom. , vol.33 , pp. 911-920
    • Pramanik, B.N.1    Bartner, P.L.2    Mirza, U.A.3    Liu, Y.H.4    Ganguly, A.K.5
  • 28
    • 0033532556 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry in the study of biomolecular non-covalent interactions
    • Veenstra T.D. Electrospray ionization mass spectrometry in the study of biomolecular non-covalent interactions. Biophys. Chem. 79:1999;63-79.
    • (1999) Biophys. Chem. , vol.79 , pp. 63-79
    • Veenstra, T.D.1
  • 31
    • 0036187372 scopus 로고    scopus 로고
    • Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3
    • Greschik H., Wurtz J.M., Sanglier S., Bourguet W., Van Dorsselaer A., Moras D., Renaud J.P. Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol. Cell. 9:2002;303-313.
    • (2002) Mol. Cell , vol.9 , pp. 303-313
    • Greschik, H.1    Wurtz, J.M.2    Sanglier, S.3    Bourguet, W.4    Van Dorsselaer, A.5    Moras, D.6    Renaud, J.P.7
  • 34
    • 0035870191 scopus 로고    scopus 로고
    • Stabilization of gas-phase noncovalent macromolecular complexes in electrospray mass spectrometry using aqueous triethylammonium bicarbonate buffer
    • Lemaire D., Marie G., Serani L., Laprevote O. Stabilization of gas-phase noncovalent macromolecular complexes in electrospray mass spectrometry using aqueous triethylammonium bicarbonate buffer. Anal. Chem. 73:2001;1699-1706.
    • (2001) Anal. Chem. , vol.73 , pp. 1699-1706
    • Lemaire, D.1    Marie, G.2    Serani, L.3    Laprevote, O.4
  • 38
    • 0036006850 scopus 로고    scopus 로고
    • Control and biochemical nature of the ecdysteroidogenic pathway
    • Gilbert L.I., Rybczynski R., Warren J.T. Control and biochemical nature of the ecdysteroidogenic pathway. Annu. Rev. Entomol. 47:2002;883-916.
    • (2002) Annu. Rev. Entomol. , vol.47 , pp. 883-916
    • Gilbert, L.I.1    Rybczynski, R.2    Warren, J.T.3
  • 40
    • 0342316532 scopus 로고    scopus 로고
    • Oxysterols: Modulators of cholesterol metabolism and other processes
    • Schroepfer G.J. Jr. Oxysterols: modulators of cholesterol metabolism and other processes. Physiol. Rev. 80:2000;361-554.
    • (2000) Physiol. Rev. , vol.80 , pp. 361-554
    • Schroepfer, G.J.Jr.1
  • 41
    • 0034793082 scopus 로고    scopus 로고
    • Genetic disorders of cholesterol biosynthesis in mice and humans
    • Nwokoro N.A., Wassif C.A., Porter F.D. Genetic disorders of cholesterol biosynthesis in mice and humans. Mol. Genet. Metabol. 74:2001;105-119.
    • (2001) Mol. Genet. Metabol. , vol.74 , pp. 105-119
    • Nwokoro, N.A.1    Wassif, C.A.2    Porter, F.D.3
  • 42
    • 0036786432 scopus 로고    scopus 로고
    • Novel mechanism of nuclear receptor co-repressor interaction dictated by activation function 2 helix determinants
    • Moraitis A.N., Giguère V., Thomson C.C. Novel mechanism of nuclear receptor co-repressor interaction dictated by activation function 2 helix determinants. Mol. Cell. Biol. 22:2002;6831-6841.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6831-6841
    • Moraitis, A.N.1    Giguère, V.2    Thomson, C.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.