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Volumn 441, Issue 2, 2012, Pages 731-741

SRP-35, a newly identified protein of the skeletal muscle sarcoplasmic reticulum, is a retinol dehydrogenase

Author keywords

Calcium release; Excitation contraction coupling; Retinoic acid; Ryanodine receptor (RyR); Skeletal muscle

Indexed keywords

CRESOL; ENHANCED YELLOW FLUORESCENCE PROTEIN; FLUORESCENT DYE; MUSCLE PROTEIN; OXIDOREDUCTASE; PROTEIN SRP 35; RETINAL; RETINOIC ACID; RETINOL DEHYDROGENASE; RYANODINE RECEPTOR; UNCLASSIFIED DRUG;

EID: 84555189123     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111457     Document Type: Article
Times cited : (12)

References (57)
  • 1
    • 0021137066 scopus 로고
    • Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle
    • Saito, A., Seiler, S., Chu, A. and Fleischer, S. (1984) Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle. J. Cell. Biol. 99, 875-885 (Pubitemid 14043345)
    • (1984) Journal of Cell Biology , vol.99 , Issue.3 , pp. 875-885
    • Saito, A.1    Seiler, S.2    Chu, A.3    Fleischer, S.4
  • 2
    • 0015856482 scopus 로고
    • Voltage dependent charge movement of skeletal muscle: A possible step in excitation-contraction coupling
    • Schneider, M. F. and Chandler, W. K. (1972) Voltage dependent charge movement of skeletal muscle: a possible step in excitation-contraction coupling. Nature 242, 244-246
    • (1972) Nature , vol.242 , pp. 244-246
    • Schneider, M.F.1    Chandler, W.K.2
  • 4
    • 0027057958 scopus 로고
    • Long-range intramolecular linked functions in activation and inhibition of SERCA ATPases
    • Inesi, G., Canitlina, T., Yu, X., Nikic, D., Sagara, Y. and Kirtley, M. E. (1992) Long-range intramolecular linked functions in activation and inhibition of SERCA ATPases. Ann. N.Y. Acad. Sci. 671, 32-47
    • (1992) Ann. N.Y. Acad. Sci. , vol.671 , pp. 32-47
    • Inesi, G.1    Canitlina, T.2    Yu, X.3    Nikic, D.4    Sagara, Y.5    Kirtley, M.E.6
  • 5
    • 0033624484 scopus 로고    scopus 로고
    • 2+ signaling and muscle disease
    • 2+ signaling and muscle disease. Eur. J. Biochem. 267, 5291-5297
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5291-5297
    • MacLennan, D.H.1
  • 7
    • 0028349030 scopus 로고
    • Structure and development of E-C coupling units in skeletal muscle
    • Franzini-Armstrong, C. and Jorgensen, A. O. (1994) Structure and development of E-C coupling units in skeletal muscle. Annu. Rev. Physiol. 56, 509-534 (Pubitemid 24111872)
    • (1994) Annual Review of Physiology , vol.56 , pp. 509-534
    • Franzini-Armstrong, C.1    Jorgensen, A.O.2
  • 9
    • 0025809446 scopus 로고
    • Voltage sensor of excitation-contraction coupling in skeletal muscle
    • Rios, E. and Pizarro, G. (1991) Voltage sensor of excitation-contraction coupling in skeletal muscle. Physiol. Rev. 71, 849-908
    • (1991) Physiol. Rev. , vol.71 , pp. 849-908
    • Rios, E.1    Pizarro, G.2
  • 10
    • 37849031506 scopus 로고    scopus 로고
    • Immuno-proteomic approach to excitation-contraction coupling in skeletal and cardiac muscle: Molecular insights revealed by the mitsugumins
    • Weisleder, N., Takeshima, H. and Ma, J. (2008) Immuno-proteomic approach to excitation-contraction coupling in skeletal and cardiac muscle: molecular insights revealed by the mitsugumins. Cell Calcium 43, 1-8
    • (2008) Cell Calcium , vol.43 , pp. 1-8
    • Weisleder, N.1    Takeshima, H.2    Ma, J.3
  • 11
    • 67650385767 scopus 로고    scopus 로고
    • Minor sarcoplasmic reticulum membrane components that modulate excitation-contraction coupling in striated muscles
    • Treves, S., Vukcevic, M, Maj, M., Thurnheer, R., Mosca, B. and Zorzato, F. (2009) Minor sarcoplasmic reticulum membrane components that modulate excitation-contraction coupling in striated muscles. J. Physiol. 587, 3071-3079
    • (2009) J. Physiol. , vol.587 , pp. 3071-3079
    • Treves, S.1    Vukcevic, M.2    Maj, M.3    Thurnheer, R.4    Mosca, B.5    Zorzato, F.6
  • 13
    • 58149133711 scopus 로고    scopus 로고
    • Medium- And short-chain dehydrogenase/reductase gene and protein families: The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes
    • Kavanagh, K. L., Jörnvall, H., Persson, B. and Oppermann, U. (2008) Medium- and short-chain dehydrogenase/reductase gene and protein families: the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes. Cell Mol. Life Sci. 65, 3895-3990
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 3895-3990
    • Kavanagh, K.L.1    Jörnvall, H.2    Persson, B.3    Oppermann, U.4
  • 14
    • 77952314065 scopus 로고    scopus 로고
    • From carrot to clinic: An overview of the retinoic acid signaling pathway
    • Theodosiou, M., Laudet, V. and Schubert, M. (2010) From carrot to clinic: an overview of the retinoic acid signaling pathway. Cell Mol. Life Sci. 67, 1423-1445
    • (2010) Cell Mol. Life Sci. , vol.67 , pp. 1423-1445
    • Theodosiou, M.1    Laudet, V.2    Schubert, M.3
  • 16
    • 0023483399 scopus 로고
    • A human retinoic acid receptor which belongs to the family of nuclear receptors
    • DOI 10.1038/330444a0
    • Petkovich, M., Brand, N. J., Krust, A. and Chambon, P. (1987) A human retinoic acid receptor which belongs to the family of nuclear receptors. Nature 330, 444-450 (Pubitemid 18006425)
    • (1987) Nature , vol.330 , Issue.6147 , pp. 444-450
    • Petkovich, M.1    Brand, N.J.2    Krust, A.3    Chambon, P.4
  • 18
    • 37549038650 scopus 로고    scopus 로고
    • Retinoid metabolism and nuclear receptor responses: New insights into coordinated regulation of the PPAR-RXR complex
    • DOI 10.1016/j.febslet.2007.11.081, PII S0014579307012355
    • Ziouzenkova, O. and Plutzky, J. (2008) Retinoid metabolism and nuclear receptor responses: new insights into coordinated regulation of the PPAR-RXR complex. FEBS Lett. 582, 32-38 (Pubitemid 50019948)
    • (2008) FEBS Letters , vol.582 , Issue.1 , pp. 32-38
    • Ziouzenkova, O.1    Plutzky, J.2
  • 19
    • 0029846498 scopus 로고    scopus 로고
    • Biochemical pathways of retinoid transport, metabolism and signal transduction
    • Napoli, J. L. (1996) Biochemical pathways of retinoid transport, metabolism and signal transduction. Clin. Immunol. Immunopathol. 80, S52-S62
    • (1996) Clin. Immunol. Immunopathol. , vol.80
    • Napoli, J.L.1
  • 20
    • 40149111695 scopus 로고    scopus 로고
    • Retinoic acid treatment increases lipid oxidation capacity in skeletal muscle of mice
    • DOI 10.1038/oby.2007.104, PII OBY2007104
    • Amengual, J., Ribot, J., Bonet, M. L. and Palou, A. (2008) Retinoic acid treatment increases lipid oxidation capacity in skeletal muscle of mice. Obesity 16, 585-591 (Pubitemid 351328009)
    • (2008) Obesity , vol.16 , Issue.3 , pp. 585-591
    • Amengual, J.1    Ribot, J.2    Bonet, M.L.3    Palou, A.4
  • 21
    • 0031921098 scopus 로고    scopus 로고
    • Ultrastructural localization of glycolytic enzymes on sarcoplasmic reticulum vesicles
    • Xu, K. Y. and Becker, L. C. (1998) Ultrastructural localization of glycolytic enzymes on sarcoplasmic reticulum vesicles. J. Histochem. Cytochem. 46, 419-427 (Pubitemid 28158461)
    • (1998) Journal of Histochemistry and Cytochemistry , vol.46 , Issue.4 , pp. 419-427
    • Xu, K.Y.1    Becker, L.C.2
  • 23
    • 0141994764 scopus 로고    scopus 로고
    • The novel skeletal muscle sarcoplasmic reticulum JP-45 protein. Molecular cloning, tissue distribution, developmental expression, and interaction with α1.1 subunit of the voltage-gated calcium channel
    • DOI 10.1074/jbc.M305016200
    • Anderson, A. A., Treves, S., Biral, D., Betto, R., Sandonà, D., Ronjat, M. and Zorzato, F. (2003) The novel skeletal muscle sarcoplasmic reticulum JP-45 protein. Molecular cloning, tissue distribution, developmental expression, and interaction with α1.1 subunit of the voltage-gated calcium channel. J. Biol. Chem. 278, 39987-39992 (Pubitemid 37248563)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.41 , pp. 39987-39992
    • Anderson, A.A.1    Treves, S.2    Biral, D.3    Betto, R.4    Sandona, D.5    Ronjat, M.6    Zorzato, F.7
  • 24
    • 0034671917 scopus 로고    scopus 로고
    • Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane
    • DOI 10.1074/jbc.M005473200
    • Treves, S., Feriotto, G., Moccagatta, L., Gambari, R. and Zorzato, F. (2000) Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane. J. Biol. Chem. 275, 39555-39568 (Pubitemid 32058982)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 39555-39568
    • Treves, S.1    Feriotto, G.2    Moccagatta, L.3    Gambari, R.4    Zorzato, F.5
  • 25
    • 0034667521 scopus 로고    scopus 로고
    • Identification of a novel 45 kDa protein (JP-45) from rabbit sarcoplasmic-reticulum junctional-face membrane
    • Zorzato, F., Anderson, A. A., Ohlendieck, K., Froemming, G., Guerrini, R. and Treves, S. (2000) Identification of a novel 45 kDa protein (JP-45) from rabbit sarcoplasmic-reticulum junctional-face membrane. Biochem. J. 351, 537-543
    • (2000) Biochem. J. , vol.351 , pp. 537-543
    • Zorzato, F.1    Anderson, A.A.2    Ohlendieck, K.3    Froemming, G.4    Guerrini, R.5    Treves, S.6
  • 26
    • 0024386604 scopus 로고
    • Purification by Cibacron Blue dye affinity chromatography and comparison of NAD(P)H:quinone reductase (E.C.1.6.99.2) from rat liver cytosol and microsomes
    • DOI 10.1016/0006-291X(89)92617-X
    • Sharkis, D. H. and Swenson, R. P. (1989) Purification by cibacron blue F3GA dye affinity chromatography and comparison of NAD(P)H: quinone reductase (E.C.1.6.99.2) from rat liver cytosol and microsomes. Biochem. Biophys. Res. Commun. 161, 434-441 (Pubitemid 19162653)
    • (1989) Biochemical and Biophysical Research Communications , vol.161 , Issue.2 , pp. 434-441
    • Sharkis, D.H.1    Swenson, R.P.2
  • 27
    • 6344278673 scopus 로고    scopus 로고
    • Effect of ryanodine receptor mutations on interleukin-6 release and intracellular calcium homeostasis in human myotubes from malignant hyperthermia-susceptible individuals and patients affected by central core disease
    • DOI 10.1074/jbc.M403612200
    • Ducreux, S., Zorzato, F., Müller, C., Sewry, C., Muntoni, F., Quinlivan, R., Restagno, G., Girard, T. and Treves, S. (2004) Effect of ryanodine receptor mutations on interleukin-6 release and intracellular calcium homeostasis in human myotubes from malignant hyperthermia-susceptible individuals and patients affected by central core disease. J. Biol. Chem. 279, 43838-43846 (Pubitemid 39390690)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.42 , pp. 43838-43846
    • Ducreux, S.1    Zorzato, F.2    Muller, C.3    Sewry, C.4    Muntoni, F.5    Quinlivan, R.6    Restagno, G.7    Girard, T.8    Treves, S.9
  • 30
    • 0033636778 scopus 로고    scopus 로고
    • Junctophilins: A novel family of junctional membrane complex proteins
    • Takeshima, H., Komazaki, S., Nishi, M., Iino, M. and Kangawa, K. (2002) Junctophilins: a novel family of junctional membrane complex proteins. Mol. Cell 6, 11-22
    • (2002) Mol. Cell , vol.6 , pp. 11-22
    • Takeshima, H.1    Komazaki, S.2    Nishi, M.3    Iino, M.4    Kangawa, K.5
  • 31
    • 0025883535 scopus 로고
    • Characteristics of short-chain alcohol dehydrogenases and related enzymes
    • Persson, B., Krook, M. and Jörnvall, H. (1991) Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 200, 537-543
    • (1991) Eur. J. Biochem. , vol.200 , pp. 537-543
    • Persson, B.1    Krook, M.2    Jörnvall, H.3
  • 32
    • 0036183076 scopus 로고    scopus 로고
    • Short-chain dehydrogenase/reductase (SDR) relationships: A large family with eight clusters common to human, animal, and plant genomes
    • DOI 10.1110/ps.26902
    • Kallberg, Y., Oppermann, U., Jörnvall, H. and Persson, B. (2002) Short-chain dehydrogenase/reductase (SDR) relationships: a large family with eight clusters common to human, animal, and plant genomes. Protein Sci. 11, 636-641 (Pubitemid 34173025)
    • (2002) Protein Science , vol.11 , Issue.3 , pp. 636-641
    • Kallberg, Y.1    Oppermann, U.2    Jornvall, H.3    Persson, B.4
  • 33
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/ reductases (SDRs)
    • DOI 10.1016/S0009-2797(02)00223-5, PII S0009279702002235
    • Persson, B., Kallberg, Y., Oppermann, U. and Jörnvall, H. (2003) Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 143, 271-278 (Pubitemid 36253590)
    • (2003) Chemico-Biological Interactions , vol.143-144 , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jornvall, H.4
  • 34
    • 0029778148 scopus 로고    scopus 로고
    • Involvement of alcohol dehydrogenase, short-chain dehydrogenase/ reductase, aldehyde dehydrogenase, and cytochrome P450 in the control of retinoid signaling by activation of retinoic acid synthesis
    • Duester, G. (1996) Involvement of alcohol dehydrogenase, short-chain dehydrogenase/reductase, aldehyde dehydrogenase, and cytochrome P450 in the control of retinoid signaling by activation of retinoic acid synthesis. Biochemistry 35, 12221-12227
    • (1996) Biochemistry , vol.35 , pp. 12221-12227
    • Duester, G.1
  • 35
    • 58149133711 scopus 로고    scopus 로고
    • Medium- And short-chain dehydrogenase/reductase gene and protein families: The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes
    • Parés, X., Farrés, J., Kedishvili, N. and Duester, G. (2009) Medium- and short-chain dehydrogenase/reductase gene and protein families: the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes. Cell Mol. Life Sci. 65, 3895-3906
    • (2009) Cell Mol. Life Sci. , vol.65 , pp. 3895-3906
    • Parés, X.1    Farrés, J.2    Kedishvili, N.3    Duester, G.4
  • 36
    • 0027223007 scopus 로고
    • The mouse retinoid-X receptor-γ gene: Genomic organization and evidence for functional isoforms
    • DOI 10.1210/me.7.5.651
    • Liu, Q. and Linney, E. (1993) The mouse retinoid-X receptor-γ gene: genomc organization and evidence for functional isoforms. Mol. Endocrinol. 7, 651-658 (Pubitemid 23157743)
    • (1993) Molecular Endocrinology , vol.7 , Issue.5 , pp. 651-658
    • Liu, Q.1    Linney, E.2
  • 37
    • 23944459079 scopus 로고    scopus 로고
    • Skeletal muscle and nuclear hormone receptors: Implications for cardiovascular and metabolic disease
    • DOI 10.1016/j.biocel.2005.03.002, PII S135727250500110X
    • Smith, A. G. and Muscat, G.E.O. (2005) Skeletal muscle and nuclear hormone receptors: implications for cardiovascular and metabolic disease. Int. J. Biochem. Cell Biol. 37, 2047-2063 (Pubitemid 41206820)
    • (2005) International Journal of Biochemistry and Cell Biology , vol.37 , Issue.10 SPEC. ISS. , pp. 2047-2063
    • Smith, A.G.1    Muscat, G.E.O.2
  • 38
    • 0028361264 scopus 로고
    • Activation of myoD gene transcription by 3,5,3′-triodo-L-thyronine: A direct role for the thyroid hormone and retinoid X receptors
    • Muscat, G.E, Mynett-Johnson, L., Dowhan, D., Downes, M. and Griggs, R. (1994) Activation of myoD gene transcription by 3,5,3′-triodo-L-thyronine: a direct role for the thyroid hormone and retinoid X receptors. Nucleic Acids Res. 22, 583-591
    • (1994) Nucleic Acids Res. , vol.22 , pp. 583-591
    • Muscat, G.E.1    Mynett-Johnson, L.2    Dowhan, D.3    Downes, M.4    Griggs, R.5
  • 39
    • 0027410189 scopus 로고
    • Retinoic acid induces adult muscle cell differentiation mediated by the retinoic acid receptor-α
    • Halevy, O. and Lerman, O. (1993) Retinoic acid induces adult muscle cell differentiation mediated by the retinoic acid receptor α. J. Cell Physiol. 154, 566-572 (Pubitemid 23076325)
    • (1993) Journal of Cellular Physiology , vol.154 , Issue.3 , pp. 566-572
    • Halevy, O.1    Lerman, O.2
  • 40
    • 70350225306 scopus 로고    scopus 로고
    • Activation of RXR and RAR signaling promotes myogenic differentiation of myoblastic C2C12 cells
    • Zhu, G. H., Huang, J., Bi, Y., Su, Y., Tang, Y., He, B. C., He, Y., Luo, J., Wang, Y., Chen, L. et al. (2009) Activation of RXR and RAR signaling promotes myogenic differentiation of myoblastic C2C12 cells. Differentiation 78, 195-204
    • (2009) Differentiation , vol.78 , pp. 195-204
    • Zhu, G.H.1    Huang, J.2    Bi, Y.3    Su, Y.4    Tang, Y.5    He, B.C.6    He, Y.7    Luo, J.8    Wang, Y.9    Chen, L.10
  • 42
    • 0029619420 scopus 로고
    • The subcellular localization of 17β-hydroxysteroid dehydrogenase type 4 and its interaction with actin
    • DOI 10.1016/0960-0760(95)00213-8
    • Markus, M., Husen, B. and Adamski, J. (1995) The subcellular localization of 17β-hydroxysteroid dehydrogenase type 4 and its interaction with actin. J. Steroid Biochem. Molec. Biol. 55, 617-621 (Pubitemid 26022388)
    • (1995) Journal of Steroid Biochemistry and Molecular Biology , vol.55 , Issue.5-6 , pp. 617-621
    • Markus, M.1    Husen, B.2    Adamski, J.3
  • 43
    • 0015160695 scopus 로고
    • Changes in the sarcoplasmic reticulum and transverse tubular system of fast and slow skeletal muscles of the mouse during postnatal development
    • Luff, A. R. and Atwood, H. L. (1971) Changes in the sarcoplasmic reticulum and transverse tubular system of fast and slow skeletal muscles of the mouse during postnatal development. J. Cell Biol. 51, 369-383
    • (1971) J. Cell Biol. , vol.51 , pp. 369-383
    • Luff, A.R.1    Atwood, H.L.2
  • 44
    • 0015963187 scopus 로고
    • Stereological analysis of mammalian skeletal muscle. I. Soleus muscle of the adult guinea pig
    • Eisenberg, B. R., Kuda, A. M. and Peter, J. B. (1974) Stereological analysis of mammalian skeletal muscle. I. Soleus muscle of the adult guinea pig. J. Cell Biol. 60, 732-754
    • (1974) J. Cell Biol. , vol.60 , pp. 732-754
    • Eisenberg, B.R.1    Kuda, A.M.2    Peter, J.B.3
  • 45
    • 0019847353 scopus 로고
    • Striated muscle contractile and control mechanisms
    • Franzini-Armstrong, C. and Peachey, L. D. (1981) Striated muscle contractile and control mechanisms. J. Cell Biol. 91, 166-186
    • (1981) J. Cell Biol. , vol.91 , pp. 166-186
    • Franzini-Armstrong, C.1    Peachey, L.D.2
  • 46
    • 0021100150 scopus 로고
    • 2+ -dependent elution from phenyl-sepharose
    • 2+ -dependent elution from phenyl-sepharose. J. Biol. Chem. 258, 11932-11936
    • (1983) J. Biol. Chem. , vol.258 , pp. 11932-11936
    • Cala, S.E.1    Jones, L.R.2
  • 47
    • 0004053611 scopus 로고    scopus 로고
    • John Wiley & Sons, New York
    • Voet, D. and Voet, J. G. (2004) Biochemistry, pp. 800-802, John Wiley & Sons, New York
    • (2004) Biochemistry , pp. 800-802
    • Voet, D.1    Voet, J.G.2
  • 48
    • 1542373629 scopus 로고    scopus 로고
    • NADH Oxidase Activity of Rat Cardiac Sarcoplasmic Reticulum Regulates Calcium-Induced Calcium Release
    • DOI 10.1161/01.RES.0000115554.65513.7C
    • Cherednichenko, G., Zima, A. V., Feng, W., Schafer, S., Blatter, L. A. and Pessah, I. N. (2004) NADH oxidase activity of rat cardiac sarcoplasmic reticulum regulates calcium induced calcium-release. Circ. Res. 94, 478-486 (Pubitemid 38326283)
    • (2004) Circulation Research , vol.94 , Issue.4 , pp. 478-486
    • Cherednichenko, G.1    Zima, A.V.2    Feng, W.3    Schaefer, S.4    Blatter, L.A.5    Pessah, I.N.6
  • 49
    • 0038643831 scopus 로고    scopus 로고
    • Differential modulation of cardiac and skeletal muscle ryanodine receptors by NADH
    • DOI 10.1016/S0014-5793(03)00664-1
    • Zima, A. V., Copello, J. A. and Blatter, L. A. (2003) Differential modulation of cardiac and skeletal muscle ryanodine receptors by NADH. FEBS Lett. 547, 32-36 (Pubitemid 36829374)
    • (2003) FEBS Letters , vol.547 , Issue.1-3 , pp. 32-36
    • Zima, A.V.1    Copello, J.A.2    Blatter, L.A.3
  • 53
    • 73549121713 scopus 로고    scopus 로고
    • The cell boundary theorem: A simple law of the control of cytosolic calcium concentration
    • Rios, E. (2010) The cell boundary theorem: a simple law of the control of cytosolic calcium concentration. J. Physiol. Sci. 60, 81-84
    • (2010) J. Physiol. Sci. , vol.60 , pp. 81-84
    • Rios, E.1
  • 55
    • 0032579324 scopus 로고    scopus 로고
    • The isolation and characterization of the promoter of the human type 1 inositol 1,4,5-trisphosphate receptor
    • DOI 10.1016/S0378-1119(97)00630-6, PII S0378111997006306
    • Deelman, L. E., Jonk, L.J.C. and Henning, R. H. (1998) The isolation and characterization of the promoter of the human type I inositol 1,4,5-trisphosphate receptor. Gene 207, 219-225 (Pubitemid 28085352)
    • (1998) Gene , vol.207 , Issue.2 , pp. 219-225
    • Deelman, L.E.1    Jonk, L.J.C.2    Henning, R.H.3
  • 56
    • 3843117675 scopus 로고    scopus 로고
    • Retinoid X receptor γ-deficient mice have increased skeletal muscle lipoprotein lipase activity and less weight gain when fed a high-fat diet
    • DOI 10.1210/en.2003-1401
    • Haugen, B., Jensen, D. R., Sharma, V., Pulawa, L. K., Hays, W. R., Krezel, W., Chambon, P. and Eckel, R. H. (2004) Retinoid X receptor γ-deficient mice have increased skeletal muscle lipoprotein lipase activity and less weight gain when fed a high-fat diet. Endocrinology 145, 3679-3685 (Pubitemid 39037553)
    • (2004) Endocrinology , vol.145 , Issue.8 , pp. 3679-3685
    • Haugen, B.R.1    Jensen, D.R.2    Sharma, V.3    Pulawa, L.K.4    Hays, W.R.5    Krezel, W.6    Chambon, P.7    Eckel, R.H.8
  • 57
    • 0028948510 scopus 로고
    • Retinoic acid stimulates glucose transporter expression in L6 muscle cells
    • Sleeman, M. W., Zhou, H., Rogers, S., Ng, K. W. and Best, J. D. (1995) Retinoic acid stimulates glucose transporter expression in L6 muscle cells. Mol. Cell. Endocrinol. 27, 161-167
    • (1995) Mol. Cell. Endocrinol. , vol.27 , pp. 161-167
    • Sleeman, M.W.1    Zhou, H.2    Rogers, S.3    Ng, K.W.4    Best, J.D.5


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