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Volumn 290, Issue 30, 2015, Pages 18438-18453

Fatty acid-binding proteins interact with comparative gene identification-58 linking lipolysis with lipid ligand shuttling

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CYTOLOGY; ENZYME ACTIVITY; ENZYMES; GENES; HYDROLYSIS; PROTEINS; SCAFFOLDS (BIOLOGY); TITRATION;

EID: 84937876167     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.628958     Document Type: Article
Times cited : (52)

References (65)
  • 1
    • 78650107057 scopus 로고    scopus 로고
    • Lipolysis - A highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores
    • Lass, A., Zimmermann, R., Oberer, M., and Zechner, R. (2011) Lipolysis - a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores. Prog. Lipid Res. 50, 14-27
    • (2011) Prog. Lipid Res. , vol.50 , pp. 14-27
    • Lass, A.1    Zimmermann, R.2    Oberer, M.3    Zechner, R.4
  • 2
    • 63449127032 scopus 로고    scopus 로고
    • Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores
    • Zechner, R., Kienesberger, P. C., Haemmerle, G., Zimmermann, R., and Lass, A. (2009) Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores. J. Lipid Res. 50, 3-21
    • (2009) J. Lipid Res. , vol.50 , pp. 3-21
    • Zechner, R.1    Kienesberger, P.C.2    Haemmerle, G.3    Zimmermann, R.4    Lass, A.5
  • 3
    • 79953160438 scopus 로고    scopus 로고
    • Interactions of Perilipin-5 (Plin5) with adipose triglyceride lipase
    • Granneman, J. G., Moore, H. P., Mottillo, E. P., Zhu, Z., and Zhou, L. (2011) Interactions of Perilipin-5 (Plin5) with adipose triglyceride lipase. J. Biol. Chem. 286, 5126-5135
    • (2011) J. Biol. Chem. , vol.286 , pp. 5126-5135
    • Granneman, J.G.1    Moore, H.P.2    Mottillo, E.P.3    Zhu, Z.4    Zhou, L.5
  • 4
    • 84872840929 scopus 로고    scopus 로고
    • Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover
    • Olzmann, J. A., Richter, C. M., and Kopito, R. R. (2013) Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover. Proc. Natl. Acad. Sci. U.S.A. 110, 1345-1350
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 1345-1350
    • Olzmann, J.A.1    Richter, C.M.2    Kopito, R.R.3
  • 5
    • 79959434733 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor regulates lipid metabolism via adipose triglyceride lipase
    • Borg, M. L., Andrews, Z. B., Duh, E. J., Zechner, R., Meikle, P. J., and Watt, M. J. (2011) Pigment epithelium-derived factor regulates lipid metabolism via adipose triglyceride lipase. Diabetes 60, 1458-1466
    • (2011) Diabetes , vol.60 , pp. 1458-1466
    • Borg, M.L.1    Andrews, Z.B.2    Duh, E.J.3    Zechner, R.4    Meikle, P.J.5    Watt, M.J.6
  • 6
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein/protein interactions
    • Nooren, I. M., and Thornton, J. M. (2003) Diversity of protein/protein interactions. EMBO J. 22, 3486-3492
    • (2003) EMBO J. , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 8
    • 0028968179 scopus 로고
    • Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase
    • Egloff, M. P., Sarda, L., Verger, R., Cambillau, C., and van Tilbeurgh, H. (1995) Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase. Protein Sci. 4, 44-57
    • (1995) Protein Sci. , vol.4 , pp. 44-57
    • Egloff, M.P.1    Sarda, L.2    Verger, R.3    Cambillau, C.4    Van Tilbeurgh, H.5
  • 9
    • 0034724094 scopus 로고    scopus 로고
    • Apolipoprotein C-II 39-62 activates lipoprotein lipase by direct lipid-independent
    • MacPhee, C. E., Hatters, D. M., Sawyer, W. H., and Howlett, G. J. (2000) Apolipoprotein C-II 39-62 activates lipoprotein lipase by direct lipid-independent. Biochemistry 39, 3433-3440
    • (2000) Biochemistry , vol.39 , pp. 3433-3440
    • MacPhee, C.E.1    Hatters, D.M.2    Sawyer, W.H.3    Howlett, G.J.4
  • 11
    • 68049092870 scopus 로고    scopus 로고
    • Neutral lipid storage disease: Genetic disorders caused by mutations in adipose triglyceride lipase/PNPLA2 or CGI-58/ABHD5
    • Schweiger, M., Lass, A., Zimmermann, R., Eichmann, T. O., and Zechner, R. (2009) Neutral lipid storage disease: genetic disorders caused by mutations in adipose triglyceride lipase/PNPLA2 or CGI-58/ABHD5. Am. J. Physiol. Endocrinol. Metab. 297, E289-E296
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.297 , pp. E289-E296
    • Schweiger, M.1    Lass, A.2    Zimmermann, R.3    Eichmann, T.O.4    Zechner, R.5
  • 12
    • 34248189053 scopus 로고    scopus 로고
    • CGI-58 facilitates lipolysis on lipid droplets but is not involved in the vesiculation of lipid droplets caused by hormonal stimulation
    • Yamaguchi, T., Omatsu, N., Morimoto, E., Nakashima, H., Ueno, K., Tanaka, T., Satouchi, K., Hirose, F., and Osumi, T. (2007) CGI-58 facilitates lipolysis on lipid droplets but is not involved in the vesiculation of lipid droplets caused by hormonal stimulation. J. Lipid Res. 48, 1078-1089
    • (2007) J. Lipid Res. , vol.48 , pp. 1078-1089
    • Yamaguchi, T.1    Omatsu, N.2    Morimoto, E.3    Nakashima, H.4    Ueno, K.5    Tanaka, T.6    Satouchi, K.7    Hirose, F.8    Osumi, T.9
  • 14
    • 79957890922 scopus 로고    scopus 로고
    • Recent insights into the structure and function of comparative gene identification-58
    • Oberer, M., Boeszoermenyi, A., Nagy, H. M., and Zechner, R. (2011) Recent insights into the structure and function of comparative gene identification-58. Curr. Opin. Lipidol. 22, 149-158
    • (2011) Curr. Opin. Lipidol. , vol.22 , pp. 149-158
    • Oberer, M.1    Boeszoermenyi, A.2    Nagy, H.M.3    Zechner, R.4
  • 15
    • 59149104232 scopus 로고    scopus 로고
    • Functional interactions between Mldp (LSDP5) and Abhd5 in the control of intracellular lipid accumulation
    • Granneman, J. G., Moore, H. P., Mottillo, E. P., and Zhu, Z. (2009) Functional interactions between Mldp (LSDP5) and Abhd5 in the control of intracellular lipid accumulation. J. Biol. Chem. 284, 3049-3057
    • (2009) J. Biol. Chem. , vol.284 , pp. 3049-3057
    • Granneman, J.G.1    Moore, H.P.2    Mottillo, E.P.3    Zhu, Z.4
  • 17
    • 77249118270 scopus 로고    scopus 로고
    • The G0/G1 switch gene 2 regulates adipose lipolysis through association with adipose triglyceride lipase
    • Yang, X., Lu, X., Lombès, M., Rha, G. B., Chi, Y. I., Guerin, T. M., Smart, E. J., and Liu, J. (2010) The G0/G1 switch gene 2 regulates adipose lipolysis through association with adipose triglyceride lipase. Cell Metab. 11, 194-205
    • (2010) Cell Metab. , vol.11 , pp. 194-205
    • Yang, X.1    Lu, X.2    Lombès, M.3    Rha, G.B.4    Chi, Y.I.5    Guerin, T.M.6    Smart, E.J.7    Liu, J.8
  • 19
    • 84868601291 scopus 로고    scopus 로고
    • The G0/G1 switch gene 2 (G0S2): Regulating metabolism and beyond
    • Heckmann, B. L., Zhang, X., Xie, X., and Liu, J. (2013) The G0/G1 switch gene 2 (G0S2): Regulating metabolism and beyond. Biochim. Biophys. Acta 1831, 276-281
    • (2013) Biochim. Biophys. Acta , vol.1831 , pp. 276-281
    • Heckmann, B.L.1    Zhang, X.2    Xie, X.3    Liu, J.4
  • 21
    • 39149141058 scopus 로고    scopus 로고
    • Anti-angiogenic pigment epithelium-derived factor regulates hepatocyte triglyceride content through adipose triglyceride lipase (ATGL)
    • Chung, C., Doll, J. A., Gattu, A. K., Shugrue, C., Cornwell, M., Fitchev, P., and Crawford, S. E. (2008) Anti-angiogenic pigment epithelium-derived factor regulates hepatocyte triglyceride content through adipose triglyceride lipase (ATGL). J. Hepatol. 48, 471-478
    • (2008) J. Hepatol. , vol.48 , pp. 471-478
    • Chung, C.1    Doll, J.A.2    Gattu, A.K.3    Shugrue, C.4    Cornwell, M.5    Fitchev, P.6    Crawford, S.E.7
  • 24
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 26
    • 0033794003 scopus 로고    scopus 로고
    • NMR spectroscopy: A multifaceted approach to macromolecular structure
    • Ferentz, A. E., and Wagner, G. (2000) NMR spectroscopy: a multifaceted approach to macromolecular structure. Q. Rev. Biophys. 33, 29-65
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 29-65
    • Ferentz, A.E.1    Wagner, G.2
  • 27
    • 77950835733 scopus 로고    scopus 로고
    • Poisson-gap sampling and forward maximum entropy reconstruction for enhancing the resolution and sensitivity of protein NMR data
    • Hyberts, S. G., Takeuchi, K., and Wagner, G. (2010) Poisson-gap sampling and forward maximum entropy reconstruction for enhancing the resolution and sensitivity of protein NMR data. J. Am. Chem. Soc. 132, 2145-2147
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2145-2147
    • Hyberts, S.G.1    Takeuchi, K.2    Wagner, G.3
  • 28
    • 84863114255 scopus 로고    scopus 로고
    • Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson gap scheduling
    • Hyberts, S. G., Milbradt, A. G., Wagner, A. B., Arthanari, H., and Wagner, G. (2012) Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson gap scheduling. J. Biomol. NMR 52, 315-327
    • (2012) J. Biomol. NMR , vol.52 , pp. 315-327
    • Hyberts, S.G.1    Milbradt, A.G.2    Wagner, A.B.3    Arthanari, H.4    Wagner, G.5
  • 35
    • 10644275883 scopus 로고    scopus 로고
    • Physical association between the adipocyte fatty acid-binding protein and hormone-sensitive lipase: A fluorescence resonance energy transfer analysis
    • Smith, A. J., Sanders, M. A., Thompson, B. R., Londos, C., Kraemer, F. B., and Bernlohr, D. A. (2004) Physical association between the adipocyte fatty acid-binding protein and hormone-sensitive lipase: a fluorescence resonance energy transfer analysis. J. Biol. Chem. 279, 52399-52405
    • (2004) J. Biol. Chem. , vol.279 , pp. 52399-52405
    • Smith, A.J.1    Sanders, M.A.2    Thompson, B.R.3    Londos, C.4    Kraemer, F.B.5    Bernlohr, D.A.6
  • 36
    • 36148956577 scopus 로고    scopus 로고
    • Interaction of the adipocyte fatty acid-binding protein with the hormone-sensitive lipase: Regulation by fatty acids and phosphorylation
    • Smith, A. J., Thompson, B. R., Sanders, M. A., and Bernlohr, D. A. (2007) Interaction of the adipocyte fatty acid-binding protein with the hormone-sensitive lipase: regulation by fatty acids and phosphorylation. J. Biol. Chem. 282, 32424-32432
    • (2007) J. Biol. Chem. , vol.282 , pp. 32424-32432
    • Smith, A.J.1    Thompson, B.R.2    Sanders, M.A.3    Bernlohr, D.A.4
  • 37
    • 57749116294 scopus 로고    scopus 로고
    • Mapping of the hormone-sensitive lipase binding site on the adipocyte fatty acid-binding protein (AFABP): Identification of the charge quartet on the AFabp/aP2 helix-turn-helix domain
    • Smith, A. J., Sanders, M. A., Juhlmann, B. E., Hertzel, A. V., and Bernlohr, D. A. (2008) Mapping of the hormone-sensitive lipase binding site on the adipocyte fatty acid-binding protein (AFABP): identification of the charge quartet on the AFabp/aP2 helix-turn-helix domain. J. Biol. Chem. 283, 33536-33543
    • (2008) J. Biol. Chem. , vol.283 , pp. 33536-33543
    • Smith, A.J.1    Sanders, M.A.2    Juhlmann, B.E.3    Hertzel, A.V.4    Bernlohr, D.A.5
  • 41
    • 33645974312 scopus 로고    scopus 로고
    • Adipocyte-type fatty acid-binding protein as inter-compartmental shuttle for peroxisome proliferator activated receptor γ agonists in cultured cell
    • Adida, A., and Spener, F. (2006) Adipocyte-type fatty acid-binding protein as inter-compartmental shuttle for peroxisome proliferator activated receptor γ agonists in cultured cell. Biochim. Biophys. Acta 1761, 172-181
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 172-181
    • Adida, A.1    Spener, F.2
  • 42
    • 84882606619 scopus 로고    scopus 로고
    • Interactions between human liver fatty acid binding protein and peroxisome proliferator activated receptor selective drugs
    • Velkov, T. (2013) Interactions between human liver fatty acid binding protein and peroxisome proliferator activated receptor selective drugs. PPAR Res. 2013, 938401
    • (2013) PPAR Res. , vol.2013
    • Velkov, T.1
  • 43
    • 0035956863 scopus 로고    scopus 로고
    • Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors α- and γ-mediated gene expression via liver fatty acid binding protein: A signaling path to the nucleus
    • Wolfrum, C., Borrmann, C. M., Borchers, T., and Spener, F. (2001) Fatty acids and hypolipidemic drugs regulate peroxisome proliferator-activated receptors α- and γ-mediated gene expression via liver fatty acid binding protein: a signaling path to the nucleus. Proc. Natl. Acad. Sci. U.S.A. 98, 2323-2328
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2323-2328
    • Wolfrum, C.1    Borrmann, C.M.2    Borchers, T.3    Spener, F.4
  • 45
    • 65349165784 scopus 로고    scopus 로고
    • Characterization of pedf: A multi-functional serpin family protein
    • Filleur, S., Nelius, T., de Riese, W., and Kennedy, R. C. (2009) Characterization of pedf: A multi-functional serpin family protein. J. Cell. Biochem. 106, 769-775
    • (2009) J. Cell. Biochem. , vol.106 , pp. 769-775
    • Filleur, S.1    Nelius, T.2    De Riese, W.3    Kennedy, R.C.4
  • 47
    • 84897025645 scopus 로고    scopus 로고
    • Comparative gene identification-58/α/β hydrolase domain 5: More than just an adipose triglyceride lipase activator?
    • Zierler, K. A., Zechner, R., and Haemmerle, G. (2014) Comparative gene identification-58/α/β hydrolase domain 5: more than just an adipose triglyceride lipase activator? Curr. Opin. Lipidol. 25, 102-109
    • (2014) Curr. Opin. Lipidol. , vol.25 , pp. 102-109
    • Zierler, K.A.1    Zechner, R.2    Haemmerle, G.3
  • 48
    • 84911458356 scopus 로고    scopus 로고
    • Comparative gene identification-58 (CGI-58) promotes autophagy as a putative lysophosphatidylglycerol acyltransferase
    • Zhang, J., Xu, D., Nie, J., Han, R., Zhai, Y., and Shi, Y. (2014) Comparative gene identification-58 (CGI-58) promotes autophagy as a putative lysophosphatidylglycerol acyltransferase. J. Biol. Chem. 289, 33044-33053
    • (2014) J. Biol. Chem. , vol.289 , pp. 33044-33053
    • Zhang, J.1    Xu, D.2    Nie, J.3    Han, R.4    Zhai, Y.5    Shi, Y.6
  • 50
    • 3242669109 scopus 로고    scopus 로고
    • Fatty acid-binding proteins-insights from genetic manipulations
    • Haunerland, N. H., and Spener, F. (2004) Fatty acid-binding proteins-insights from genetic manipulations. Prog. Lipid Res. 43, 328-349
    • (2004) Prog. Lipid Res. , vol.43 , pp. 328-349
    • Haunerland, N.H.1    Spener, F.2
  • 51
    • 50949128339 scopus 로고    scopus 로고
    • The emerging functions and mechanisms of mammalian fatty acid-binding proteins
    • Storch, J., and Corsico, B. (2008) The emerging functions and mechanisms of mammalian fatty acid-binding proteins. Annu. Rev. Nutr. 28, 73-95
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 73-95
    • Storch, J.1    Corsico, B.2
  • 53
    • 33645277091 scopus 로고    scopus 로고
    • Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family
    • Marcelino, A. M., Smock, R. G., and Gierasch, L. M. (2006) Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family. Proteins Struct. Funct. Genet. 63, 373-384
    • (2006) Proteins Struct. Funct. Genet. , vol.63 , pp. 373-384
    • Marcelino, A.M.1    Smock, R.G.2    Gierasch, L.M.3
  • 54
    • 0033545915 scopus 로고    scopus 로고
    • Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein
    • Shen, W. J., Sridhar, K., Bernlohr, D. A., and Kraemer, F. B. (1999) Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein. Proc. Natl. Acad. Sci. U.S.A. 96, 5528-5532
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 5528-5532
    • Shen, W.J.1    Sridhar, K.2    Bernlohr, D.A.3    Kraemer, F.B.4
  • 56
    • 0035966072 scopus 로고    scopus 로고
    • Characterization of the functional interaction of adipocyte lipid-binding protein with hormone-sensitive lipase
    • Shen, W. J., Liang, Y., Hong, R., Patel, S., Natu, V., Sridhar, K., Jenkins, A., Bernlohr, D. A., and Kraemer, F. B. (2001) Characterization of the functional interaction of adipocyte lipid-binding protein with hormone-sensitive lipase. J. Biol. Chem. 276, 49443-49448
    • (2001) J. Biol. Chem. , vol.276 , pp. 49443-49448
    • Shen, W.J.1    Liang, Y.2    Hong, R.3    Patel, S.4    Natu, V.5    Sridhar, K.6    Jenkins, A.7    Bernlohr, D.A.8    Kraemer, F.B.9
  • 58
    • 0032895839 scopus 로고    scopus 로고
    • Targeted disruption of the adipocyte lipid-binding protein (aP2 protein) gene impairs fat cell lipolysis and increases cellular fatty acid levels
    • Coe, N. R., Simpson, M. A., and Bernlohr, D. A. (1999) Targeted disruption of the adipocyte lipid-binding protein (aP2 protein) gene impairs fat cell lipolysis and increases cellular fatty acid levels. J. Lipid Res. 40, 967-972
    • (1999) J. Lipid Res. , vol.40 , pp. 967-972
    • Coe, N.R.1    Simpson, M.A.2    Bernlohr, D.A.3
  • 59
    • 78650317248 scopus 로고    scopus 로고
    • Endogenous ligands for nuclear receptors: Digging deeper
    • Schupp, M., and Lazar, M. A. (2010) Endogenous ligands for nuclear receptors: digging deeper. J. Biol. Chem. 285, 40409-40415
    • (2010) J. Biol. Chem. , vol.285 , pp. 40409-40415
    • Schupp, M.1    Lazar, M.A.2
  • 60
    • 0036291635 scopus 로고    scopus 로고
    • Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating T
    • Tan, N. S., Shaw, N. S., Vinckenbosch, N., Liu, P., Yasmin, R., Desvergne, B., Wahli, W., and Noy, N. (2002) Selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating transcription selective cooperation between fatty acid binding proteins and peroxisome proliferator-activated receptors in regulating T. Mol. Cell. Biol. 22, 5114-5127
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5114-5127
    • Tan, N.S.1    Shaw, N.S.2    Vinckenbosch, N.3    Liu, P.4    Yasmin, R.5    Desvergne, B.6    Wahli, W.7    Noy, N.8
  • 61
    • 34250201866 scopus 로고    scopus 로고
    • Continuous nucleocytoplasmic shuttling underlies transcriptional activation of PPAR?? by FABP4
    • Ayers, S. D., Nedrow, K. L., Gillilan, R. E., and Noy, N. (2007) Continuous nucleocytoplasmic shuttling underlies transcriptional activation of PPAR?? by FABP4. Biochemistry 46, 6744-6752
    • (2007) Biochemistry , vol.46 , pp. 6744-6752
    • Ayers, S.D.1    Nedrow, K.L.2    Gillilan, R.E.3    Noy, N.4
  • 62
    • 34548515270 scopus 로고    scopus 로고
    • Structural basis for activation of fatty acid-binding protein 4
    • Gillilan, R. E., Ayers, S. D., and Noy, N. (2007) Structural basis for activation of fatty acid-binding protein 4. J. Mol. Biol. 372, 1246-1260
    • (2007) J. Mol. Biol. , vol.372 , pp. 1246-1260
    • Gillilan, R.E.1    Ayers, S.D.2    Noy, N.3
  • 63
    • 84901449113 scopus 로고    scopus 로고
    • Structural basis for ligand regulation of the fatty acid-binding protein 5, peroxisome proliferator-activated receptor β/δ (FABP5-PPARβ/δ) signaling pathway
    • Armstrong, E. H., Goswami, D., Griffin, P. R., Noy, N., and Ortlund, E. A. (2014) Structural basis for ligand regulation of the fatty acid-binding protein 5, peroxisome proliferator-activated receptor β/δ (FABP5-PPARβ/δ) signaling pathway. J. Biol. Chem. 289, 14941-54
    • (2014) J. Biol. Chem. , vol.289 , pp. 14941-14954
    • Armstrong, E.H.1    Goswami, D.2    Griffin, P.R.3    Noy, N.4    Ortlund, E.A.5
  • 65
    • 84894475571 scopus 로고    scopus 로고
    • FABP4 attenuates PPARγ and adipogenesis and is inversely correlated with PPARγ in adipose tissues
    • Garin-Shkolnik, T., Rudich, A., Hotamisligil, G. S., and Rubinstein, M. (2014) FABP4 attenuates PPARγ and adipogenesis and is inversely correlated with Pparγ in adipose tissues. Diabetes 63, 900-911
    • (2014) Diabetes , vol.63 , pp. 900-911
    • Garin-Shkolnik, T.1    Rudich, A.2    Hotamisligil, G.S.3    Rubinstein, M.4


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