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Volumn 53, Issue 12, 2012, Pages 2677-2689

StAR-related lipid transfer domain protein 5 binds primary bile acids

Author keywords

Bile acids; Cholesterol metabolism; Circular dichroism; Isothermal titration calorimetry; Lipid transport; NMR spectroscopy; Steroidogenic acute regulatory protein

Indexed keywords

BILE ACID; CHENODEOXYCHOLIC ACID; CHOLIC ACID; FARNESOID X RECEPTOR; LIPID TRANSFER PROTEIN; STEROIDOGENIC ACUTE REGULATORY RELATED LIPID TRANSFER DOMAIN PROTEIN 5; UNCLASSIFIED DRUG;

EID: 84869020761     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M031245     Document Type: Article
Times cited : (33)

References (70)
  • 1
    • 0028153185 scopus 로고
    • Molecular genetics and regulation of bile acid biosynthesis
    • Hylemon, P. B., R. T. Stravitz, and Z. R. Vlahcevic. 1994. Molecular genetics and regulation of bile acid biosynthesis. Prog. Liver Dis. 12: 99-120.
    • (1994) Prog. Liver Dis. , vol.12 , pp. 99-120
    • Hylemon, P.B.1    Stravitz, R.T.2    Vlahcevic, Z.R.3
  • 2
    • 0037790917 scopus 로고    scopus 로고
    • The enzymes, regulation, and genetics of bile acid synthesis
    • Russell, D. W. 2003. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72: 137-174.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 137-174
    • Russell, D.W.1
  • 4
    • 23744478870 scopus 로고    scopus 로고
    • Give lipids a START: The StAR-related lipid transfer (START) domain in mammals
    • Alpy, F., and C. Tomasetto. 2005. Give lipids a START: the StAR-related lipid transfer (START) domain in mammals. J. Cell Sci. 118: 2791-2801.
    • (2005) J. Cell Sci. , vol.118 , pp. 2791-2801
    • Alpy, F.1    Tomasetto, C.2
  • 5
    • 0032901292 scopus 로고    scopus 로고
    • START: A lipid-binding domain in StAR, HD-ZIP and signalling proteins
    • Ponting, C. P., and L. Aravind. 1999. START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins. Trends Biochem. Sci.24: 130-132.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 130-132
    • Ponting, C.P.1    Aravind, L.2
  • 7
  • 8
    • 0035342462 scopus 로고    scopus 로고
    • Adaptations of the helix-grip fold for ligand binding and catalysis in the START domain superfamily
    • Iyer, L. M., E. V. Koonin, and L. Aravind. 2001. Adaptations of the helix-grip fold for ligand binding and catalysis in the START domain superfamily. Proteins. 43: 134-144.
    • (2001) Proteins , vol.43 , pp. 134-144
    • Iyer, L.M.1    Koonin, E.V.2    Aravind, L.3
  • 9
    • 77449112767 scopus 로고    scopus 로고
    • Crystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer
    • Kudo, N., K. Kumagai, R. Matsubara, S. Kobayashi, K. Hanada, S. Wakatsuki, and R. Kato. 2010. Crystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer. J. Mol. Biol. 396: 245-251.
    • (2010) J. Mol. Biol. , vol.396 , pp. 245-251
    • Kudo, N.1    Kumagai, K.2    Matsubara, R.3    Kobayashi, S.4    Hanada, K.5    Wakatsuki, S.6    Kato, R.7
  • 11
    • 77952311395 scopus 로고    scopus 로고
    • Mammalian StAR-related lipid transfer (START) domains with specificity for cholesterol: Structural conservation and mechanism of reversible binding
    • Lavigne, P., R. Najmanivich, and J. G. Lehoux. 2010. Mammalian StAR-related lipid transfer (START) domains with specificity for cholesterol: structural conservation and mechanism of reversible binding. Subcell. Biochem. 51: 425-437.
    • (2010) Subcell. Biochem. , vol.51 , pp. 425-437
    • Lavigne, P.1    Najmanivich, R.2    Lehoux, J.G.3
  • 12
    • 12244288339 scopus 로고    scopus 로고
    • Molecular modeling and structure-based thermodynamic analysis of the StAR protein
    • Mathieu, A. P., P. Lavigne, and J. G. LeHoux. 2002. Molecular modeling and structure-based thermodynamic analysis of the StAR protein. Endocr. Res. 28: 419-423.
    • (2002) Endocr. Res. , vol.28 , pp. 419-423
    • Mathieu, A.P.1    Lavigne, P.2    LeHoux, J.G.3
  • 14
    • 0037076327 scopus 로고    scopus 로고
    • Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain
    • Romanowski, M. J., R. E. Soccio, J. L. Breslow, and S. K. Burley. 2002. Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain. Proc. Natl. Acad. Sci. USA. 99: 6949-6954.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6949-6954
    • Romanowski, M.J.1    Soccio, R.E.2    Breslow, J.L.3    Burley, S.K.4
  • 16
    • 0034064138 scopus 로고    scopus 로고
    • Structure and lipid transport mechanism of a StAR-related domain
    • Tsujishita, Y., and J. H. Hurley. 2000. Structure and lipid transport mechanism of a StAR-related domain. Nat. Struct. Biol. 7: 408-414.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 408-414
    • Tsujishita, Y.1    Hurley, J.H.2
  • 17
    • 84857854776 scopus 로고    scopus 로고
    • The mammalian START domain protein family in lipid transport in health and disease
    • Clark, B. J. 2012. The mammalian START domain protein family in lipid transport in health and disease. J. Endocrinol. 212: 257-275.
    • (2012) J. Endocrinol. , vol.212 , pp. 257-275
    • Clark, B.J.1
  • 18
    • 0037076275 scopus 로고    scopus 로고
    • The cholesterol-regulated StarD4 gene encodes a StAR-related lipid transfer protein with two closely related homologues, StarD5 and StarD6
    • Soccio, R. E., R. M. Adams, M. J. Romanowski, E. Sehayek, S. K. Burley, and J. L. Breslow. 2002. The cholesterol-regulated StarD4 gene encodes a StAR-related lipid transfer protein with two closely related homologues, StarD5 and StarD6. Proc. Natl. Acad. Sci. USA.99: 6943-6948.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6943-6948
    • Soccio, R.E.1    Adams, R.M.2    Romanowski, M.J.3    Sehayek, E.4    Burley, S.K.5    Breslow, J.L.6
  • 21
    • 0029855881 scopus 로고    scopus 로고
    • The pathophysiology and genetics of congenital lipoid adrenal hyperplasia
    • Bose, H. S., T. Sugawara, J. F. Strauss 3rd, and W. L. Miller. 1996. The pathophysiology and genetics of congenital lipoid adrenal hyperplasia. N. Engl. J. Med. 335: 1870-1878.
    • (1996) N. Engl. J. Med. , vol.335 , pp. 1870-1878
    • Bose, H.S.1    Sugawara, T.2    Strauss III, J.F.3    Miller, W.L.4
  • 22
    • 14044251615 scopus 로고    scopus 로고
    • A genetic isolate of congenital lipoid adrenal hyperplasia with atypical clinical findings
    • Chen, X., B. Y. Baker, M. A. Abduljabbar, and W. L. Miller. 2005. A genetic isolate of congenital lipoid adrenal hyperplasia with atypical clinical findings. J. Clin. Endocrinol. Metab. 90: 835-840.
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , pp. 835-840
    • Chen, X.1    Baker, B.Y.2    Abduljabbar, M.A.3    Miller, W.L.4
  • 23
    • 0028104418 scopus 로고
    • The purification, cloning, and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 mouse Leydig tumor cells. Characterization of the steroidogenic acute regulatory protein (StAR)
    • Clark, B. J., J. Wells, S. R. King, and D. M. Stocco. 1994. The purification, cloning, and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 mouse Leydig tumor cells. Characterization of the steroidogenic acute regulatory protein (StAR). J. Biol. Chem. 269: 28314-28322.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28314-28322
    • Clark, B.J.1    Wells, J.2    King, S.R.3    Stocco, D.M.4
  • 26
    • 0033306854 scopus 로고    scopus 로고
    • A novel compound heterozygous mutation in the steroidogenic acute regulatory protein gene in a patient with congenital lipoid adrenal hyperplasia
    • Katsumata, N., Y. Kawada, Y. Yamamoto, M. Noda, A. Nimura, R. Horikawa, and T. Tanaka. 1999. A novel compound heterozygous mutation in the steroidogenic acute regulatory protein gene in a patient with congenital lipoid adrenal hyperplasia. J. Clin. Endocrinol. Metab. 84: 3983-3987.
    • (1999) J. Clin. Endocrinol. Metab. , vol.84 , pp. 3983-3987
    • Katsumata, N.1    Kawada, Y.2    Yamamoto, Y.3    Noda, M.4    Nimura, A.5    Horikawa, R.6    Tanaka, T.7
  • 27
    • 59649120936 scopus 로고    scopus 로고
    • Evidence for impaired physiological decrease in the uteroplacental vascular resistance in pregnant women with familial hypercholesterolemia
    • Khoury, J., A. L. Amundsen, S. Tonstad, T. Henriksen, L. Ose, K. Retterstol, and P. O. Iversen. 2009. Evidence for impaired physiological decrease in the uteroplacental vascular resistance in pregnant women with familial hypercholesterolemia. Acta Obstet. Gynecol. Scand. 88: 222-226.
    • (2009) Acta Obstet. Gynecol. Scand. , vol.88 , pp. 222-226
    • Khoury, J.1    Amundsen, A.L.2    Tonstad, S.3    Henriksen, T.4    Ose, L.5    Retterstol, K.6    Iversen, P.O.7
  • 28
    • 0038485664 scopus 로고    scopus 로고
    • Adrenocorticotropin regulation of steroidogenic acute regulatory protein
    • Lehoux, J. G., A. Mathieu, P. Lavigne, and A. Fleury. 2003. Adrenocorticotropin regulation of steroidogenic acute regulatory protein. Microsc. Res. Tech. 61: 288-299.
    • (2003) Microsc. Res. Tech. , vol.61 , pp. 288-299
    • Lehoux, J.G.1    Mathieu, A.2    Lavigne, P.3    Fleury, A.4
  • 32
    • 0037073676 scopus 로고    scopus 로고
    • Transport of cholesterol into mitochondria is rate-limiting for bile acid synthesis via the alternative pathway in primary rat hepatocytes
    • Pandak, W. M., S. Ren, D. Marques, E. Hall, K. Redford, D. Mallonee, P. Bohdan, D. Heuman, G. Gil, and P. Hylemon. 2002. Transport of cholesterol into mitochondria is rate-limiting for bile acid synthesis via the alternative pathway in primary rat hepatocytes. J. Biol. Chem. 277: 48158-48164.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48158-48164
    • Pandak, W.M.1    Ren, S.2    Marques, D.3    Hall, E.4    Redford, K.5    Mallonee, D.6    Bohdan, P.7    Heuman, D.8    Gil, G.9    Hylemon, P.10
  • 33
    • 0028819993 scopus 로고
    • Structure of the human steroidogenic acute regulatory protein (StAR) gene: StAR stimulates mitochondrial cholesterol 27-hydroxylase activity
    • Sugawara, T., D. Lin, J. A. Holt, K. O. Martin, N. B. Javitt, W. L. Miller, and J. F. Strauss 3rd. 1995. Structure of the human steroidogenic acute regulatory protein (StAR) gene: StAR stimulates mitochondrial cholesterol 27-hydroxylase activity. Biochemistry. 34: 12506-12512.
    • (1995) Biochemistry , vol.34 , pp. 12506-12512
    • Sugawara, T.1    Lin, D.2    Holt, J.A.3    Martin, K.O.4    Javitt, N.B.5    Miller, W.L.6    Strauss III, J.F.7
  • 34
    • 33745472965 scopus 로고    scopus 로고
    • MLN64 and MENTHO, two mediators of endosomal cholesterol transport
    • Alpy, F., and C. Tomasetto. 2006. MLN64 and MENTHO, two mediators of endosomal cholesterol transport. Biochem. Soc. Trans. 34: 343-345.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 343-345
    • Alpy, F.1    Tomasetto, C.2
  • 35
    • 50949123980 scopus 로고    scopus 로고
    • Intracellular cholesterol transporter StarD4 binds free cholesterol and increases cholesteryl ester formation
    • Rodriguez-Agudo, D., S. Ren, E. Wong, D. Marques, K. Redford, G. Gil, P. Hylemon, and W. M. Pandak. 2008. Intracellular cholesterol transporter StarD4 binds free cholesterol and increases cholesteryl ester formation. J. Lipid Res. 49: 1409-1419.
    • (2008) J. Lipid Res. , vol.49 , pp. 1409-1419
    • Rodriguez-Agudo, D.1    Ren, S.2    Wong, E.3    Marques, D.4    Redford, K.5    Gil, G.6    Hylemon, P.7    Pandak, W.M.8
  • 36
    • 67651095693 scopus 로고    scopus 로고
    • The changed immunoreactivity of StarD6 after pilocarpine-induced epilepsy
    • Chang, I. Y., J. K. Kim, S. M. Lee, J. N. Kim, J. Soh, J. W. Kim, and S. P. Yoon. 2009. The changed immunoreactivity of StarD6 after pilocarpine-induced epilepsy. Neuroreport. 20: 963-967.
    • (2009) Neuroreport , vol.20 , pp. 963-967
    • Chang, I.Y.1    Kim, J.K.2    Lee, S.M.3    Kim, J.N.4    Soh, J.5    Kim, J.W.6    Yoon, S.P.7
  • 37
    • 34250724415 scopus 로고    scopus 로고
    • The changed immunolocalization of START-domain-containing 6 (StarD6) during the development of testes in rat perinatal hypothyroidism
    • Chang, I. Y., S. Y. Shin, J. W. Kim, J. M. Yu, J. S. Kim, P. I. Song, and S. P. Yoon. 2007. The changed immunolocalization of START-domain-containing 6 (StarD6) during the development of testes in rat perinatal hypothyroidism. Acta Histochem. 109: 315-321.
    • (2007) Acta Histochem. , vol.109 , pp. 315-321
    • Chang, I.Y.1    Shin, S.Y.2    Kim, J.W.3    Yu, J.M.4    Kim, J.S.5    Song, P.I.6    Yoon, S.P.7
  • 38
    • 14044250161 scopus 로고    scopus 로고
    • Expression of the putative sterol binding protein Stard6 gene is male germ cell specific
    • Gomes, C., S. D. Oh, J. W. Kim, S. Y. Chun, K. Lee, H. B. Kwon, and J. Soh. 2005. Expression of the putative sterol binding protein Stard6 gene is male germ cell specific. Biol. Reprod. 72: 651-658.
    • (2005) Biol. Reprod. , vol.72 , pp. 651-658
    • Gomes, C.1    Oh, S.D.2    Kim, J.W.3    Chun, S.Y.4    Lee, K.5    Kwon, H.B.6    Soh, J.7
  • 41
    • 84856541540 scopus 로고    scopus 로고
    • Immunolocalization of steroidogenic acute regulatory protein-related lipid transfer (START) domain-containing proteins in the developing cerebellum of normal and hypothyroid rats
    • Chang, I. Y., T. Ohn, G. S. Ko, Y. Yoon, J. W. Kim, and S. P. Yoon. 2012. Immunolocalization of steroidogenic acute regulatory protein-related lipid transfer (START) domain-containing proteins in the developing cerebellum of normal and hypothyroid rats. J. Chem. Neuroanat. 43: 28-33.
    • (2012) J. Chem. Neuroanat. , vol.43 , pp. 28-33
    • Chang, I.Y.1    Ohn, T.2    Ko, G.S.3    Yoon, Y.4    Kim, J.W.5    Yoon, S.P.6
  • 42
    • 79952365168 scopus 로고    scopus 로고
    • Cytosolic StAR-related lipid transfer domain 4 (STARD4) protein influences keratinocyte lipid phenotype and differentiation status
    • Elbadawy, H. M., F. Borthwick, C. Wright, P. E. Martin, and A. Graham. 2011. Cytosolic StAR-related lipid transfer domain 4 (STARD4) protein influences keratinocyte lipid phenotype and differentiation status. Br. J. Dermatol. 164: 628-632.
    • (2011) Br. J. Dermatol. , vol.164 , pp. 628-632
    • Elbadawy, H.M.1    Borthwick, F.2    Wright, C.3    Martin, P.E.4    Graham, A.5
  • 47
    • 21444455252 scopus 로고    scopus 로고
    • Differential gene regulation of StarD4 and StarD5 cholesterol transfer proteins. Activation of StarD4 by sterol regulatory element-binding protein-2 and StarD5 by endoplasmic reticulum stress
    • Soccio, R. E., R. M. Adams, K. N. Maxwell, and J. L. Breslow. 2005. Differential gene regulation of StarD4 and StarD5 cholesterol transfer proteins. Activation of StarD4 by sterol regulatory element-binding protein-2 and StarD5 by endoplasmic reticulum stress. J. Biol. Chem. 280: 19410-19418.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19410-19418
    • Soccio, R.E.1    Adams, R.M.2    Maxwell, K.N.3    Breslow, J.L.4
  • 48
    • 45349096923 scopus 로고    scopus 로고
    • Cholesterol binding is a prerequisite for the activity of the steroidogenic acute regulatory protein (StAR)
    • Roostaee, A., E. Barbar, J. G. Lehoux, and P. Lavigne. 2008. Cholesterol binding is a prerequisite for the activity of the steroidogenic acute regulatory protein (StAR). Biochem. J. 412: 553-562.
    • (2008) Biochem. J. , vol.412 , pp. 553-562
    • Roostaee, A.1    Barbar, E.2    Lehoux, J.G.3    Lavigne, P.4
  • 52
    • 0031027910 scopus 로고    scopus 로고
    • Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR
    • Gardner, K. H., M. K. Rosen, and L. E. Kay. 1997. Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. Biochemistry. 36: 1389-1401.
    • (1997) Biochemistry , vol.36 , pp. 1389-1401
    • Gardner, K.H.1    Rosen, M.K.2    Kay, L.E.3
  • 53
    • 35948942349 scopus 로고    scopus 로고
    • NMR methods for the determination of protein-ligand dissociation constants
    • Fielding, L. 2007. NMR methods for the determination of protein-ligand dissociation constants. Prog. Nucl. Magn. Reson. Spectrosc. 51: 219-242.
    • (2007) Prog. Nucl. Magn. Reson. Spectrosc. , vol.51 , pp. 219-242
    • Fielding, L.1
  • 54
    • 79951996670 scopus 로고    scopus 로고
    • Assessing the performance of the molecular mechanics/Poisson Boltzmann surface area and molecular mechanics/generalized Born surface area methods. II. The accuracy of ranking poses generated from docking
    • Hou, T., J. Wang, Y. Li, and W. Wang. 2011. Assessing the performance of the molecular mechanics/Poisson Boltzmann surface area and molecular mechanics/generalized Born surface area methods. II. The accuracy of ranking poses generated from docking. J. Comput. Chem. 32: 866-877.
    • (2011) J. Comput. Chem. , vol.32 , pp. 866-877
    • Hou, T.1    Wang, J.2    Li, Y.3    Wang, W.4
  • 55
    • 84874974074 scopus 로고    scopus 로고
    • (1)H, (13)C, and (15)N backbone chemical shift assignments of StAR-related lipid transfer domain protein 5 (STARD5)
    • Epub ahead of print. March 6, 2012; doi:10.1007/s12104-012-9368-z
    • Lorin, A., D. Letourneau, A. Lefebvre, J. G. Lehoux, and P. Lavigne. 2012. (1)H, (13)C, and (15)N backbone chemical shift assignments of StAR-related lipid transfer domain protein 5 (STARD5). Biomol. NMR Assign. Epub ahead of print. March 6, 2012; doi:10.1007/s12104-012-9368-z.
    • (2012) Biomol. NMR Assign.
    • Lorin, A.1    Letourneau, D.2    Lefebvre, A.3    Lehoux, J.G.4    Lavigne, P.5
  • 56
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart, D. S., and B. D. Sykes. 1994. Chemical shifts as a tool for structure determination. Methods Enzymol. 239: 363-392.
    • (1994) Methods Enzymol. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 57
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart, D. S., and B. D. Sykes. 1994. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR. 4: 171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 60
    • 0033026760 scopus 로고    scopus 로고
    • Endogenous bile acids are ligands for the nuclear receptor FXR/BAR
    • Wang, H., J. Chen, K. Hollister, L. C. Sowers, and B. M. Forman. 1999. Endogenous bile acids are ligands for the nuclear receptor FXR/BAR. Mol. Cell. 3: 543-553.
    • (1999) Mol. Cell. , vol.3 , pp. 543-553
    • Wang, H.1    Chen, J.2    Hollister, K.3    Sowers, L.C.4    Forman, B.M.5
  • 64
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • Sreerama, N., and R. W. Woody. 2004. Computation and analysis of protein circular dichroism spectra. Methods Enzymol. 383: 318-351.
    • (2004) Methods Enzymol. , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 65
    • 78650485354 scopus 로고    scopus 로고
    • Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-throughput determination of ligand affinities with extrinsic fluorescent dyes
    • Layton, C. J., and H. W. Hellinga. 2010. Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-throughput determination of ligand affinities with extrinsic fluorescent dyes. Biochemistry. 49: 10831-10841.
    • (2010) Biochemistry , vol.49 , pp. 10831-10841
    • Layton, C.J.1    Hellinga, H.W.2
  • 66
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S. B., P. J. Hajduk, R. P. Meadows, and S. W. Fesik. 1996. Discovering high-affinity ligands for proteins: SAR by NMR. Science.274: 1531-1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 67
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. 2002. Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry. 41: 1-7.
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 68
    • 1542275425 scopus 로고    scopus 로고
    • The farnesoid X receptor controls gene expression in a ligand- And promoter-selective fashion
    • Lew, J. L., A. Zhao, J. Yu, L. Huang, N. De Pedro, F. Pelaez, S. D. Wright, and J. Cui. 2004. The farnesoid X receptor controls gene expression in a ligand- and promoter-selective fashion. J. Biol. Chem.279: 8856-8861.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8856-8861
    • Lew, J.L.1    Zhao, A.2    Yu, J.3    Huang, L.4    De Pedro, N.5    Pelaez, F.6    Wright, S.D.7    Cui, J.8
  • 70
    • 0029094346 scopus 로고
    • Enthalpic contribution to protein stability: Insights from atom-based calculations and statistical mechanics
    • Lazaridis, T., G. Archontis, and M. Karplus. 1995. Enthalpic contribution to protein stability: insights from atom-based calculations and statistical mechanics. Adv. Protein Chem. 47: 231-306.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 231-306
    • Lazaridis, T.1    Archontis, G.2    Karplus, M.3


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