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Volumn 412, Issue 3, 2008, Pages 553-562

Cholesterol binding is a prerequisite for the activity of the steroidogenic acute regulatory protein (StAR)

Author keywords

Cholesterol; Circular dichroism; Mitochondria; Steroidogenesis; Steroidogenic acute regulatory protein (StAR); Thermodynamics

Indexed keywords

AMINES; AMINO ACIDS; BINDING ENERGY; BINDING SITES; CELL MEMBRANES; ENZYME ACTIVITY; HEALTH; HYDROPHOBICITY; MECHANICS; MELTING POINT; MICROFLUIDICS; MOLECULES; ORGANIC ACIDS; PORT TERMINALS; SYSTEM STABILITY; THERMODYNAMIC STABILITY; THERMODYNAMICS; VOLUMETRIC ANALYSIS;

EID: 45349096923     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071264     Document Type: Article
Times cited : (43)

References (48)
  • 1
    • 0030047248 scopus 로고    scopus 로고
    • Regulation of the acute production of steroids in steroidogenic cells
    • Stocco, D. M. and Clark, B. J. (1996) Regulation of the acute production of steroids in steroidogenic cells. Endocr. Rev. 17, 221-244
    • (1996) Endocr. Rev , vol.17 , pp. 221-244
    • Stocco, D.M.1    Clark, B.J.2
  • 4
    • 0343807261 scopus 로고
    • Regulation of intramitochondrial cholesterol transfer to side-chain cleavage cytochrome P-450 in rat adrenal gland
    • Privalle, C. T., Crivello, J. F. and Jefcoate, C. R. (1983) Regulation of intramitochondrial cholesterol transfer to side-chain cleavage cytochrome P-450 in rat adrenal gland. Proc. Natl. Acad. Sci. U.S.A. 80, 702-706
    • (1983) Proc. Natl. Acad. Sci. U.S.A , vol.80 , pp. 702-706
    • Privalle, C.T.1    Crivello, J.F.2    Jefcoate, C.R.3
  • 6
    • 0029099777 scopus 로고
    • Comparison of protein phosphorylation patterns produced in adrenal cells by activation of cAMP-dependent protein kinase and Ca-dependent protein kinase
    • Hartigan, J. A., Green, E. G., Mortensen, R. M., Menachery, A., Williams, G. H. and Orme-Johnson, N. R. (1995) Comparison of protein phosphorylation patterns produced in adrenal cells by activation of cAMP-dependent protein kinase and Ca-dependent protein kinase. J. Steroid Biochem. Mol. Biol. 53, 95-101
    • (1995) J. Steroid Biochem. Mol. Biol , vol.53 , pp. 95-101
    • Hartigan, J.A.1    Green, E.G.2    Mortensen, R.M.3    Menachery, A.4    Williams, G.H.5    Orme-Johnson, N.R.6
  • 7
    • 0028868949 scopus 로고
    • Steroid production after in vitro transcription, translation, and mitochondrial processing of protein products of complementary deoxyribonucleic acid for steroidogenic acute regulatory protein
    • King, S. R., Ronen-Fuhrmann, T., Timberg, R., Clark, B. J., Orly, J. and Stocco, D. M. (1995) Steroid production after in vitro transcription, translation, and mitochondrial processing of protein products of complementary deoxyribonucleic acid for steroidogenic acute regulatory protein. Endocrinology 136, 5165-5176
    • (1995) Endocrinology , vol.136 , pp. 5165-5176
    • King, S.R.1    Ronen-Fuhrmann, T.2    Timberg, R.3    Clark, B.J.4    Orly, J.5    Stocco, D.M.6
  • 8
    • 0022895185 scopus 로고
    • Acute cAMP stimulation in Leydig cells: Rapid accumulation of a protein similar to that detected in adrenal cortex and corpus luteum
    • Pon, L. A., Epstein, L. F. and Orme-Johnson, N. R. (1986) Acute cAMP stimulation in Leydig cells: rapid accumulation of a protein similar to that detected in adrenal cortex and corpus luteum. Endocr. Res. 12, 429-446
    • (1986) Endocr. Res , vol.12 , pp. 429-446
    • Pon, L.A.1    Epstein, L.F.2    Orme-Johnson, N.R.3
  • 9
    • 0038485664 scopus 로고    scopus 로고
    • Adrenocorticotropic regulation of steroidogenic acute regulatory protein
    • Lehoux, J. G., Mathieu, A., Lavigne, P. and Fleury, A. (2003) Adrenocorticotropic 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
  • 10
    • 0028973522 scopus 로고
    • T → A transversion 11 bp from a splice acceptor site in the human gene for steroidogenic acute regulatory protein causes congenital lipoid adrenal hyperplasia
    • Tee, M. K., Lin, D., Sugawara, T., Holt, J. A., Guiguen, Y., Buckingham, B., Strauss, 3rd, J. F. and Miller, W. L. (1995) T → A transversion 11 bp from a splice acceptor site in the human gene for steroidogenic acute regulatory protein causes congenital lipoid adrenal hyperplasia. Hum. Mol. Genet. 4, 2299-2305
    • (1995) Hum. Mol. Genet , vol.4 , pp. 2299-2305
    • Tee, M.K.1    Lin, D.2    Sugawara, T.3    Holt, J.A.4    Guiguen, Y.5    Buckingham, B.6    Strauss 3rd, J.F.7    Miller, W.L.8
  • 11
    • 0029855881 scopus 로고    scopus 로고
    • The pathophysiology and genetics of congenital lipoid adrenal hyperplasia. International Congenital Lipoid Adrenal Hyperplasia Consortium
    • Bose, H. S., Sugawara, T., Strauss, 3rd, J. F. and Miller, W. L. (1996) The pathophysiology and genetics of congenital lipoid adrenal hyperplasia. International Congenital Lipoid Adrenal Hyperplasia Consortium. 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 3rd, J.F.3    Miller, W.L.4
  • 12
    • 0033756526 scopus 로고    scopus 로고
    • Mutations in the steroidogenic acute regulatory protein (StAR) in six patients with congenital lipoid adrenal hyperplasia
    • Bose, H. S., Sato, S., Aisenberg, J., Shalev, S. A., Matsuo, N. and Miller, W. L. (2000) Mutations in the steroidogenic acute regulatory protein (StAR) in six patients with congenital lipoid adrenal hyperplasia. J. Clin. Endocrinol. Metab. 85, 3636-3639
    • (2000) J. Clin. Endocrinol. Metab , vol.85 , pp. 3636-3639
    • Bose, H.S.1    Sato, S.2    Aisenberg, J.3    Shalev, S.A.4    Matsuo, N.5    Miller, W.L.6
  • 13
    • 0032901292 scopus 로고    scopus 로고
    • START: A lipid-binding domain in StAR, HD-ZIP and signalling proteins
    • Ponting, C. P. and Aravind, L. (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
  • 15
    • 0030459652 scopus 로고    scopus 로고
    • Steroidogenic acute regulatory protein (StAR) retains activity in the absence of its mitochondrial import sequence: Implications for the mechanism of StAR action
    • Arakane, F., Sugawara, T., Nishino, H., Liu, Z., Holt, J. A., Pain, D., Stocco, D. M., Miller, W. L. and Strauss, 3rd, J. F. (1996) Steroidogenic acute regulatory protein (StAR) retains activity in the absence of its mitochondrial import sequence: implications for the mechanism of StAR action. Proc. Natl. Acad. Sci. U.S.A. 93, 13731-13736
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 13731-13736
    • Arakane, F.1    Sugawara, T.2    Nishino, H.3    Liu, Z.4    Holt, J.A.5    Pain, D.6    Stocco, D.M.7    Miller, W.L.8    Strauss 3rd, J.F.9
  • 16
    • 0032568819 scopus 로고    scopus 로고
    • The mechanism of action of steroidogenic acute regulatory protein (StAR). StAR acts on the outside of mitochondria to stimulate steroidogenesis
    • Arakane, F., Kallen, C. B., Watari, H., Foster, J. A., Sepuri, N. B., Pain, D., Stayrook, S. E., Lewis, M., Gerton, G. L. and Strauss, 3rd, J. F. (1998) The mechanism of action of steroidogenic acute regulatory protein (StAR). StAR acts on the outside of mitochondria to stimulate steroidogenesis. J. Biol. Chem. 273, 16339-16345
    • (1998) J. Biol. Chem , vol.273 , pp. 16339-16345
    • Arakane, F.1    Kallen, C.B.2    Watari, H.3    Foster, J.A.4    Sepuri, N.B.5    Pain, D.6    Stayrook, S.E.7    Lewis, M.8    Gerton, G.L.9    Strauss 3rd, J.F.10
  • 17
    • 0035824668 scopus 로고    scopus 로고
    • Mitochondrial processing of newly synthesized steroidogenic acute regulatory protein (StAR), but not total StAR, mediates cholesterol transfer to cytochrome P450 side chain cleavage enzyme in adrenal cells
    • Artemenko, I. P., Zhao, D., Hales, D. B., Hales, K. H. and Jefcoate, C. R. (2001) Mitochondrial processing of newly synthesized steroidogenic acute regulatory protein (StAR), but not total StAR, mediates cholesterol transfer to cytochrome P450 side chain cleavage enzyme in adrenal cells. J. Biol. Chem. 276, 46583-46596
    • (2001) J. Biol. Chem , vol.276 , pp. 46583-46596
    • Artemenko, I.P.1    Zhao, D.2    Hales, D.B.3    Hales, K.H.4    Jefcoate, C.R.5
  • 18
    • 0037007628 scopus 로고    scopus 로고
    • Rapid regulation of steroidogenesis by mitochondrial protein import
    • Bose, H., Lingappa, V. R. and Miller, W. L. (2002) Rapid regulation of steroidogenesis by mitochondrial protein import. Nature 417, 87-91
    • (2002) Nature , vol.417 , pp. 87-91
    • Bose, H.1    Lingappa, V.R.2    Miller, W.L.3
  • 19
    • 0034672689 scopus 로고    scopus 로고
    • Steroidogenic acute regulatory protein (StAR) and the intramitochondrial translocation of cholesterol
    • Christenson, L. K. and Strauss, 3rd, J. F. (2000) Steroidogenic acute regulatory protein (StAR) and the intramitochondrial translocation of cholesterol. Biochim. Biophys. Acta 1529, 175-187
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 175-187
    • Christenson, L.K.1    Strauss 3rd, J.F.2
  • 20
    • 0033594958 scopus 로고    scopus 로고
    • The active form of the steroidogenic acute regulatory protein, StAR, appears to be a molten globule
    • Bose, H. S., Whittal, R. M., Baldwin, M. A. and Miller, W. L. (1999) The active form of the steroidogenic acute regulatory protein, StAR, appears to be a molten globule. Proc. Natl. Acad. Sci. U.S.A. 96, 7250-7255
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 7250-7255
    • Bose, H.S.1    Whittal, R.M.2    Baldwin, M.A.3    Miller, W.L.4
  • 21
    • 0034064138 scopus 로고    scopus 로고
    • Structure and lipid transport mechanism of a StAR-related domain
    • Tsujishita, Y. and Hurley, J. H. (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
  • 22
    • 0036918153 scopus 로고    scopus 로고
    • Insights into steroidogenic acute regulatory protein (StAR)-dependent cholesterol transfer in mitochondria: Evidence from molecular modeling and structure-based thermodynamics supporting the existence of partially unfolded states of StAR
    • Mathieu, A. P., Fleury, A., Ducharme, L., Lavigne, P. and LeHoux, J. G. (2002) Insights into steroidogenic acute regulatory protein (StAR)-dependent cholesterol transfer in mitochondria: evidence from molecular modeling and structure-based thermodynamics supporting the existence of partially unfolded states of StAR. J. Mol. Endocrinol. 29, 327-345
    • (2002) J. Mol. Endocrinol , vol.29 , pp. 327-345
    • Mathieu, A.P.1    Fleury, A.2    Ducharme, L.3    Lavigne, P.4    LeHoux, J.G.5
  • 23
    • 0022993214 scopus 로고
    • Preparation and characterization of submitochondrial fractions from adrenal cells
    • della-Cioppa, G., Muffly, K. E., Yanagibashi, K. and Hall, P. F. (1986) Preparation and characterization of submitochondrial fractions from adrenal cells. Mol. Cell. Endocrinol. 48, 111-120
    • (1986) Mol. Cell. Endocrinol , vol.48 , pp. 111-120
    • della-Cioppa, G.1    Muffly, K.E.2    Yanagibashi, K.3    Hall, P.F.4
  • 24
    • 34547523811 scopus 로고
    • Freezing damage to isolated tomato fruit mitochondria as modified by cryoprotective agents and storage temperature
    • Dickinson, D. B., Misch, M. J. and Drury, R. E. (1970) Freezing damage to isolated tomato fruit mitochondria as modified by cryoprotective agents and storage temperature. Plant Physiol. 46, 200-203
    • (1970) Plant Physiol , vol.46 , pp. 200-203
    • Dickinson, D.B.1    Misch, M.J.2    Drury, R.E.3
  • 26
    • 0016274599 scopus 로고
    • Interaction of gelatin with stereospecific binding proteins and its enhancement of competitive binding assays
    • Murphy, B. E. and Marvin, M. (1974) Interaction of gelatin with stereospecific binding proteins and its enhancement of competitive binding assays. J. Clin. Pathol. 27, 687-692
    • (1974) J. Clin. Pathol , vol.27 , pp. 687-692
    • Murphy, B.E.1    Marvin, M.2
  • 27
    • 0029563395 scopus 로고
    • Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc leucine zippers: A description of putative electrostatic interactions responsible for the specificity of heterodimerization
    • Lavigne, P., Kondejewski, L. H., Houston, Jr, M. E., Sonnichsen, F. D., Lix, B., Skyes, B. D., Hodges, R. S. and Kay, C. M. (1995) Preferential heterodimeric parallel coiled-coil formation by synthetic Max and c-Myc leucine zippers: a description of putative electrostatic interactions responsible for the specificity of heterodimerization. J. Mol. Biol. 254, 505-520
    • (1995) J. Mol. Biol , vol.254 , pp. 505-520
    • Lavigne, P.1    Kondejewski, L.H.2    Houston Jr, M.E.3    Sonnichsen, F.D.4    Lix, B.5    Skyes, B.D.6    Hodges, R.S.7    Kay, C.M.8
  • 28
    • 0032493843 scopus 로고    scopus 로고
    • Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper
    • Lavigne, P., Crump, M. P., Gagne, S. M., Hodges, R. S., Kay, C. M. and Sykes, B. D. (1998) Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper. J. Mol. Biol. 281, 165-181
    • (1998) J. Mol. Biol , vol.281 , pp. 165-181
    • Lavigne, P.1    Crump, M.P.2    Gagne, S.M.3    Hodges, R.S.4    Kay, C.M.5    Sykes, B.D.6
  • 29
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 30
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P. L. (1979) Stability of proteins: small globular proteins. Adv. Protein Chem. 33, 167-241
    • (1979) Adv. Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 31
    • 25444455861 scopus 로고    scopus 로고
    • Naud, J. F., McDuff, F. O., Sauve, S., Montagne, M., Webb, B. A., Smith, S. P., Chabot, B. and Lavigne, P. (2005) Structural and thermodynamical characterization of the complete p21 gene product of Max. Biochemistry 44, 12746-12758
    • Naud, J. F., McDuff, F. O., Sauve, S., Montagne, M., Webb, B. A., Smith, S. P., Chabot, B. and Lavigne, P. (2005) Structural and thermodynamical characterization of the complete p21 gene product of Max. Biochemistry 44, 12746-12758
  • 32
    • 33845747803 scopus 로고    scopus 로고
    • The mechanism of discrimination between cognate and non-specific DNA by dimeric b/HLH/LZ transcription factors
    • Sauve, S., Naud, J. F. and Lavigne, P. (2007) The mechanism of discrimination between cognate and non-specific DNA by dimeric b/HLH/LZ transcription factors. J. Mol. Biol. 365, 1163-1175
    • (2007) J. Mol. Biol , vol.365 , pp. 1163-1175
    • Sauve, S.1    Naud, J.F.2    Lavigne, P.3
  • 33
    • 0015870378 scopus 로고
    • Circular dichroism and optical rotatory dispersion of proteins and polypeptides
    • Adler, A. J., Greenfield, N. J. and Fasman, G. D. (1973) Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol. 27, 675-735
    • (1973) Methods Enzymol , vol.27 , pp. 675-735
    • Adler, A.J.1    Greenfield, N.J.2    Fasman, G.D.3
  • 34
    • 24344436769 scopus 로고    scopus 로고
    • A novel mutation L260P of the steroidogenic acute regulatory protein gene in three unrelated patients of Swiss ancestry with congenital lipoid adrenal hyperplasia
    • Flück, C. E., Maret, A., Mallet, D., Portrat-Doyen, S., Achermann, J. C., Leheup, B., Theintz, G. E., Mullis, P. E. and Morel, Y. (2005) A novel mutation L260P of the steroidogenic acute regulatory protein gene in three unrelated patients of Swiss ancestry with congenital lipoid adrenal hyperplasia. J. Clin. Endocrinol. Metab. 90, 5304-5308
    • (2005) J. Clin. Endocrinol. Metab , vol.90 , pp. 5304-5308
    • Flück, C.E.1    Maret, A.2    Mallet, D.3    Portrat-Doyen, S.4    Achermann, J.C.5    Leheup, B.6    Theintz, G.E.7    Mullis, P.E.8    Morel, Y.9
  • 35
    • 33845571063 scopus 로고    scopus 로고
    • Modeling the structure of the StART domains of MLN64 and StAR proteins in complex with cholesterol
    • Murcia, M., Faraldo-Gomez, J. D., Maxfield, F. R. and Roux, B. (2006) Modeling the structure of the StART domains of MLN64 and StAR proteins in complex with cholesterol. J. Lipid Res. 47, 2614-2630
    • (2006) J. Lipid Res , vol.47 , pp. 2614-2630
    • Murcia, M.1    Faraldo-Gomez, J.D.2    Maxfield, F.R.3    Roux, B.4
  • 36
    • 0025779077 scopus 로고
    • Number and placement of hydrophobic residues in a longitudinal strip governs helix formation of peptides in the presence of lipid vesicles
    • Lu, S., Ciardelli, T., Reyes, V. E. and Humphreys, R. E. (1991) Number and placement of hydrophobic residues in a longitudinal strip governs helix formation of peptides in the presence of lipid vesicles. J. Biol. Chem. 266, 10054-10057
    • (1991) J. Biol. Chem , vol.266 , pp. 10054-10057
    • Lu, S.1    Ciardelli, T.2    Reyes, V.E.3    Humphreys, R.E.4
  • 37
    • 0032493328 scopus 로고    scopus 로고
    • Incorrect folding of steroidogenic acute regulatory protein (StAR) in congenital lipoid adrenal hyperplasia
    • Bose, H. S., Baldwin, M. A. and Miller, W. L. (1998) Incorrect folding of steroidogenic acute regulatory protein (StAR) in congenital lipoid adrenal hyperplasia. Biochemistry (Moscow) 37, 9768-9775
    • (1998) Biochemistry (Moscow) , vol.37 , pp. 9768-9775
    • Bose, H.S.1    Baldwin, M.A.2    Miller, W.L.3
  • 38
    • 0027078034 scopus 로고
    • Rod-like cholesterol micelles in agueous solution studied using polarized and depolarized dynamic light scattering
    • Castanho, M. A., Brown, W. and Prieto, M. J. (1992) Rod-like cholesterol micelles in agueous solution studied using polarized and depolarized dynamic light scattering. Biophys. J. 63, 1455-1461
    • (1992) Biophys. J , vol.63 , pp. 1455-1461
    • Castanho, M.A.1    Brown, W.2    Prieto, M.J.3
  • 39
    • 12244288339 scopus 로고    scopus 로고
    • Molecular modeling and structure-based thermodynamic analysis of the StAR protein
    • Mathieu, A. P., Lavigne, P. and LeHoux, J. G. (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
  • 40
    • 33845504474 scopus 로고    scopus 로고
    • Nonclassic congenital lipoid adrenal hyperplasia: A new disorder of the steroidogenic acute regulatory protein with very late presentation and normal male genitalia
    • Baker, B. Y., Lin, L., Kim, C. J., Raza, J., Smith, C. P., Miller, W. L. and Achermann, J. C. (2006) Nonclassic congenital lipoid adrenal hyperplasia: a new disorder of the steroidogenic acute regulatory protein with very late presentation and normal male genitalia. J. Clin. Endocrinol. Metab. 91, 4781-4785
    • (2006) J. Clin. Endocrinol. Metab , vol.91 , pp. 4781-4785
    • Baker, B.Y.1    Lin, L.2    Kim, C.J.3    Raza, J.4    Smith, C.P.5    Miller, W.L.6    Achermann, J.C.7
  • 41
    • 0035813102 scopus 로고    scopus 로고
    • Steroidogenic acute regulatory protein binds cholesterol and modulates mitochondrial membrane sterol domain dynamics
    • Petrescu, A. D., Gallegos, A. M., Okamura, Y., Strauss, 3rd, J. F. and Schroeder, F. (2001) Steroidogenic acute regulatory protein binds cholesterol and modulates mitochondrial membrane sterol domain dynamics. J. Biol. Chem. 276, 36970-36982
    • (2001) J. Biol. Chem , vol.276 , pp. 36970-36982
    • Petrescu, A.D.1    Gallegos, A.M.2    Okamura, Y.3    Strauss 3rd, J.F.4    Schroeder, F.5
  • 42
    • 34249811452 scopus 로고    scopus 로고
    • Cholesterol binding does not predict activity of the steroidogenic acute regulatory protein, StAR
    • Baker, B. Y., Epand, R. F., Epand, R. M. and Miller, W. L. (2007) Cholesterol binding does not predict activity of the steroidogenic acute regulatory protein, StAR. J. Biol. Chem. 282, 10223-10232
    • (2007) J. Biol. Chem , vol.282 , pp. 10223-10232
    • Baker, B.Y.1    Epand, R.F.2    Epand, R.M.3    Miller, W.L.4
  • 43
    • 33845977384 scopus 로고    scopus 로고
    • Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis
    • Liu, J., Rone, M. B. and Papadopoulos, V. (2006) Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis. J. Biol. Chem. 281, 38879-38893
    • (2006) J. Biol. Chem , vol.281 , pp. 38879-38893
    • Liu, J.1    Rone, M.B.2    Papadopoulos, V.3
  • 44
    • 0034934281 scopus 로고    scopus 로고
    • Solvent entropy-driven searching for protein modeling examined and tested in simplified models
    • König, R. and Dandekar, T. (2001) Solvent entropy-driven searching for protein modeling examined and tested in simplified models. Protein Eng. 14, 329-335
    • (2001) Protein Eng , vol.14 , pp. 329-335
    • König, R.1    Dandekar, T.2
  • 45
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • Ross, P. D. and Subramanian, S. (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry (Moscow) 20, 3096-3102
    • (1981) Biochemistry (Moscow) , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 46
    • 73849163221 scopus 로고
    • The contribution of hydrophobic bonds to the thermal stability of protein conformations
    • Scheraga, H. A., Nemethy, G. and Steinberg, I. Z. (1962) The contribution of hydrophobic bonds to the thermal stability of protein conformations. J. Biol. Chem. 237, 2506-2508
    • (1962) J. Biol. Chem , vol.237 , pp. 2506-2508
    • Scheraga, H.A.1    Nemethy, G.2    Steinberg, I.Z.3
  • 47
    • 0000434932 scopus 로고    scopus 로고
    • Critical micellization concentration of surfactants in aqueous solutions and free energy of micellization
    • Zana, R. (1996) Critical micellization concentration of surfactants in aqueous solutions and free energy of micellization. Langmuir 12, 1208-1211
    • (1996) Langmuir , vol.12 , pp. 1208-1211
    • Zana, R.1
  • 48
    • 0037389276 scopus 로고    scopus 로고
    • Transport of plasma membrane-derived cholesterol and the function of Niemann-Pick C1 protein
    • Wiegand, V., Chang, T. Y., Strauss, 3rd, J. F., Fahrenholz, F. and Gimpl, G. (2003) Transport of plasma membrane-derived cholesterol and the function of Niemann-Pick C1 protein. FASEB J. 17, 782-784
    • (2003) FASEB J , vol.17 , pp. 782-784
    • Wiegand, V.1    Chang, T.Y.2    Strauss 3rd, J.F.3    Fahrenholz, F.4    Gimpl, G.5


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