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Volumn 239, Issue 1-2, 2002, Pages 45-54

Insights into binding of fatty acids by fatty acid binding proteins

Author keywords

ADIFAB; Binding; FABP; Fatty acid; Isothermal titration calorimetry; Lipidex; Tertiary structure

Indexed keywords

BILE ACID; CELL PROTEIN; FATTY ACID; FATTY ACID BINDING PROTEIN; LIGAND; MONOUNSATURATED FATTY ACID; OMEGA 3 FATTY ACID; OMEGA 6 FATTY ACID; RETINOIC ACID BINDING PROTEIN; RETINOID DERIVATIVE; RETINOL BINDING PROTEIN; CARRIER PROTEIN; FABP1 PROTEIN, HUMAN; FABP1 PROTEIN, MOUSE; FABP3 PROTEIN, HUMAN; FABP7 PROTEIN, HUMAN; TUMOR PROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 17744410109     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020502624234     Document Type: Review
Times cited : (176)

References (65)
  • 1
    • 0015496783 scopus 로고
    • A binding protein for fatty acids in cytosol of intestinal mucosa, liver, myocardium, and other tissues
    • Ockner RK, Manning JA, Poppenhausen RB, Ho WK: A binding protein for fatty acids in cytosol of intestinal mucosa, liver, myocardium, and other tissues. Science 177: 56-58, 1972
    • (1972) Science , vol.177 , pp. 56-58
    • Ockner, R.K.1    Manning, J.A.2    Poppenhausen, R.B.3    Ho, W.K.4
  • 2
    • 0023874788 scopus 로고
    • The structure of crystalline Escherichia coli-derived rat intestinal fatty acid-binding protein at 2.5-Å resolution
    • Sacchettini JC, Gordon JI, Banaszak LJ: The structure of crystalline Escherichia coli-derived rat intestinal fatty acid-binding protein at 2.5-Å resolution. J Biol Chem 263: 5815-5819, 1988
    • (1988) J. Biol. Chem. , vol.263 , pp. 5815-5819
    • Sacchettini, J.C.1    Gordon, J.I.2    Banaszak, L.J.3
  • 3
    • 0027096161 scopus 로고
    • Refinement of the structure of Escherichia coli-derived rat intestinal fatty acid binding protein with bound oleate to 1.75-Å resolution. Correlation with the structures of the apoprotein and the protein with bound palmitate
    • Sacchettini JC, Scapin G, Gopaul D, Gordon JI: Refinement of the structure of Escherichia coli-derived rat intestinal fatty acid binding protein with bound oleate to 1.75-Å resolution. Correlation with the structures of the apoprotein and the protein with bound palmitate. J Biol Chem 267: 23534-23545, 1992
    • (1992) J. Biol. Chem. , vol.267 , pp. 23534-23545
    • Sacchettini, J.C.1    Scapin, G.2    Gopaul, D.3    Gordon, J.I.4
  • 4
    • 0001089206 scopus 로고    scopus 로고
    • Fatty acid binding proteins and mammary-derived growth inhibitor
    • Hohoff C, Spener F: Fatty acid binding proteins and mammary-derived growth inhibitor. Fett Lipid 100: 252-263, 1998
    • (1998) Fett. Lipid , vol.100 , pp. 252-263
    • Hohoff, C.1    Spener, F.2
  • 5
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • Kleywegt GJ, Bergfors T, Senn H, Le Motte P, Gsell B, Shudo K, Jones TA: Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure 2: 1241-1258, 1994
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Bergfors, T.2    Senn, H.3    Le Motte, P.4    Gsell, B.5    Shudo, K.6    Jones, T.A.7
  • 6
    • 0027310780 scopus 로고
    • Crystallographic studies on a family of cellular lipophilic transport proteins. Refinement of P2 Myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol
    • Cowan SW, Newcomer ME, Jones TA: Crystallographic studies on a family of cellular lipophilic transport proteins. Refinement of P2 Myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol. J Mol Biol 230: 1225-1246, 1993
    • (1993) J. Mol. Biol. , vol.230 , pp. 1225-1246
    • Cowan, S.W.1    Newcomer, M.E.2    Jones, T.A.3
  • 7
    • 0027213028 scopus 로고
    • Crystal structures of holo- and apo-cellular retinol-binding protein II
    • Winter NS, Bratt JM, Banaszak LJ: Crystal structures of holo- and apo-cellular retinol-binding protein II. J Mol Biol 230: 1247-1259, 1993
    • (1993) J. Mol. Biol. , vol.230 , pp. 1247-1259
    • Winter, N.S.1    Bratt, J.M.2    Banaszak, L.J.3
  • 10
    • 0030986132 scopus 로고    scopus 로고
    • The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates
    • Thompson J, Winter N, Terwey D, Bratt J, Banaszak L: The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates. J Biol Chem 272: 7140-7150, 1997
    • (1997) J. Biol. Chem. , vol.272 , pp. 7140-7150
    • Thompson, J.1    Winter, N.2    Terwey, D.3    Bratt, J.4    Banaszak, L.5
  • 11
    • 0021275901 scopus 로고
    • Fatty-acid-binding proteins. Occurrence of two fatty-acid-binding proteins in bovine liver cytosol and their binding of fatty acids, cholesterol, and other lipophilic ligands
    • Haunerland N, Jagschies G, Schulenberg H, Spener F: Fatty-acid-binding proteins. Occurrence of two fatty-acid-binding proteins in bovine liver cytosol and their binding of fatty acids, cholesterol, and other lipophilic ligands. Hoppe Seyler's Z Physiol Chem 365: 365-376, 1984
    • (1984) Hoppe Seyler's Z Physiol. Chem. , vol.365 , pp. 365-376
    • Haunerland, N.1    Jagschies, G.2    Schulenberg, H.3    Spener, F.4
  • 13
    • 0027290681 scopus 로고
    • High resolution X-ray studies of mammalian intestinal and muscle fatty acid-binding proteins provide an opportunity for defining the chemical nature of fatty acid:protein interactions
    • Scapin G, Young AC, Kromminga A, Veerkamp JH, Gordon JI, Sacchettini JC: High resolution X-ray studies of mammalian intestinal and muscle fatty acid-binding proteins provide an opportunity for defining the chemical nature of fatty acid:protein interactions. Mol Cell Biochem 123: 3-13, 1993
    • (1993) Mol. Cell Biochem. , vol.123 , pp. 3-13
    • Scapin, G.1    Young, A.C.2    Kromminga, A.3    Veerkamp, J.H.4    Gordon, J.I.5    Sacchettini, J.C.6
  • 14
    • 0039702661 scopus 로고    scopus 로고
    • Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein
    • Hohoff C, Börchers T, Rüstow B, Spener F, van Tilbeurgh H: Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein. Biochemistry 38: 12229-12239, 1999
    • (1999) Biochemistry , vol.38 , pp. 12229-12239
    • Hohoff, C.1    Börchers, T.2    Rüstow, B.3    Spener, F.4    Van Tilbeurgh, H.5
  • 17
    • 0025194826 scopus 로고
    • 19F nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol binding protein II produced in Escherichia coli. An analysis of four tryptophan substitution mutants and their interactions with all-trans-retinol
    • Li E, Qian SJ, Yang NC, d'Avignon A, Gordon JI: 19F nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol binding protein II produced in Escherichia coli. An analysis of four tryptophan substitution mutants and their interactions with all-trans-retinol. J Biol Chem 265: 11549-11554, 1990
    • (1990) J. Biol. Chem. , vol.265 , pp. 11549-11554
    • Li, E.1    Qian, S.J.2    Yang, N.C.3    d'Avignon, A.4    Gordon, J.I.5
  • 18
    • 0025907475 scopus 로고
    • Fluorine nuclear magnetic resonance analysis of the ligand binding properties of two homologous rat cellular retinol-binding proteins expressed in Escherichia coli
    • Li E, Qian SJ, Winter NS, d'Avignon A, Levin MS, Gordon.JI: Fluorine nuclear magnetic resonance analysis of the ligand binding properties of two homologous rat cellular retinol-binding proteins expressed in Escherichia coli. J Biol Chem 266: 3622-3629, 1991
    • (1991) J. Biol. Chem. , vol.266 , pp. 3622-3629
    • Li, E.1    Qian, S.J.2    Winter, N.S.3    d'Avignon, A.4    Levin, M.S.5    Gordon, J.I.6
  • 19
    • 0025132671 scopus 로고
    • Developmental and structural studies of an intracellular lipid binding protein expressed in the ileal epithelium
    • Sacchettini JC, Hauft SM, Van Camp SL, Cistola DP, Gordon JI: Developmental and structural studies of an intracellular lipid binding protein expressed in the ileal epithelium. J Biol Chem 265: 19199-19207, 1990
    • (1990) J. Biol. Chem. , vol.265 , pp. 19199-19207
    • Sacchettini, J.C.1    Hauft, S.M.2    Van Camp, S.L.3    Cistola, D.P.4    Gordon, J.I.5
  • 20
    • 0023837979 scopus 로고
    • Interactions of oleic acid with liver fatty acid binding protein: A carbon-13 NMR study
    • Cistola DP, Walsh MT, Corey RP, Hamilton JA, Brecher P: Interactions of oleic acid with liver fatty acid binding protein: A carbon-13 NMR study. Biochemistry 27: 711-717, 1988
    • (1988) Biochemistry , vol.27 , pp. 711-717
    • Cistola, D.P.1    Walsh, M.T.2    Corey, R.P.3    Hamilton, J.A.4    Brecher, P.5
  • 21
    • 0024595766 scopus 로고
    • Fatty acid interactions with rat intestinal and liver fatty acid-binding proteins expressed in Escherichia coli. A comparative 13C NMR study
    • Cistola DP, Sacchettini JC, Banaszak LJ, Walsh MT, Gordon JI: Fatty acid interactions with rat intestinal and liver fatty acid-binding proteins expressed in Escherichia coli. A comparative 13C NMR study. J Biol Chem 264: 2700-2710, 1989
    • (1989) J. Biol. Chem. , vol.264 , pp. 2700-2710
    • Cistola, D.P.1    Sacchettini, J.C.2    Banaszak, L.J.3    Walsh, M.T.4    Gordon, J.I.5
  • 22
    • 0031113230 scopus 로고    scopus 로고
    • Solution structure of human intestinal fatty acid binding protein: Implications for ligand entry and exit
    • Zhang F, Lücke C, Baier LJ, Sacchettini JC, Hamilton JA: Solution structure of human intestinal fatty acid binding protein: Implications for ligand entry and exit. J Biomol NMR 9: 213-228, 1997
    • (1997) J. Biomol. NMR , vol.9 , pp. 213-228
    • Zhang, F.1    Lücke, C.2    Baier, L.J.3    Sacchettini, J.C.4    Hamilton, J.A.5
  • 23
    • 0032530468 scopus 로고    scopus 로고
    • NMR solution structure of type II human cellular retinoic acid binding protein: Implications for ligand binding
    • Wang L, Li Y, Abildgaard F, Markley JL, Yan H: NMR solution structure of type II human cellular retinoic acid binding protein: Implications for ligand binding. Biochemistry 37: 12727-12736, 1998
    • (1998) Biochemistry , vol.37 , pp. 12727-12736
    • Wang, L.1    Li, Y.2    Abildgaard, F.3    Markley, J.L.4    Yan, H.5
  • 24
    • 0030586026 scopus 로고    scopus 로고
    • Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein
    • Lücke C, Zhang F, Rüterjans H, Hamilton JA, Sacchettini JC: Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein. Structure 4: 785-800, 1996
    • (1996) Structure , vol.4 , pp. 785-800
    • Lücke, C.1    Zhang, F.2    Rüterjans, H.3    Hamilton, J.A.4    Sacchettini, J.C.5
  • 25
    • 0035281806 scopus 로고    scopus 로고
    • Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP)
    • Lücke C, Rademacher M, Zimmerman AW, van Moerkerk HT, Veerkamp JH, Rüterjans H: Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP). Biochem J 354: 259-266, 2001
    • (2001) Biochem. J. , vol.354 , pp. 259-266
    • Lücke, C.1    Rademacher, M.2    Zimmerman, A.W.3    Van Moerkerk, H.T.4    Veerkamp, J.H.5    Rüterjans, H.6
  • 26
    • 0031036243 scopus 로고    scopus 로고
    • Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: Implications for the mechanism of ligand entry
    • Hodsdon ME, Cistola DP: Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: Implications for the mechanism of ligand entry. Biochemistry 36: 1450-1460, 1997
    • (1997) Biochemistry , vol.36 , pp. 1450-1460
    • Hodsdon, M.E.1    Cistola, D.P.2
  • 27
    • 0030573021 scopus 로고    scopus 로고
    • The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: Application of a novel distance geometry algorithm
    • Hodsdon ME, Ponder JW, Cistola DP: The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: Application of a novel distance geometry algorithm. J Mol Biol 264: 585-602, 1996
    • (1996) J. Mol. Biol. , vol.264 , pp. 585-602
    • Hodsdon, M.E.1    Ponder, J.W.2    Cistola, D.P.3
  • 28
    • 0029032451 scopus 로고
    • Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy
    • Lassen D, Lücke C, Kveder M, Mesgarzadeh A, Schmidt JM, Specht B, Lezius A, Spener F, Rüterjans H: Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy. Eur J Biochem 230: 266-280, 1995
    • (1995) Eur. J. Biochem. , vol.230 , pp. 266-280
    • Lassen, D.1    Lücke, C.2    Kveder, M.3    Mesgarzadeh, A.4    Schmidt, J.M.5    Specht, B.6    Lezius, A.7    Spener, F.8    Rüterjans, H.9
  • 29
    • 0031043596 scopus 로고    scopus 로고
    • Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange
    • Hodsdon ME, Cistola DP: Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange. Biochemistry 36: 2279-2290, 1997
    • (1997) Biochemistry , vol.36 , pp. 2279-2290
    • Hodsdon, M.E.1    Cistola, D.P.2
  • 31
    • 0039165184 scopus 로고    scopus 로고
    • A comparative study of the backbone dynamics of two closely related lipid binding proteins: Bovine heart fatty acid binding protein and porcine ileal lipid binding protein
    • Lücke C, Fushman D, Ludwig C, Hamilton JA, Sacchettini JC, Rüterjans H: A comparative study of the backbone dynamics of two closely related lipid binding proteins: Bovine heart fatty acid binding protein and porcine ileal lipid binding protein. Mol Cell Biochem 192: 109 121, 1999
    • (1999) Mol. Cell Biochem. , vol.192 , pp. 109-121
    • Lücke, C.1    Fushman, D.2    Ludwig, C.3    Hamilton, J.A.4    Sacchettini, J.C.5    Rüterjans, H.6
  • 32
    • 0033525633 scopus 로고    scopus 로고
    • The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: Comparison with the X-ray structure
    • Lu J, Lin CL, Tang C, Ponder JW, Kao JL, Cistola DP, Li E: The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: Comparison with the X-ray structure. J Mol Biol 286: 1179-1195, 1999
    • (1999) J. Mol. Biol. , vol.286 , pp. 1179-1195
    • Lu, J.1    Lin, C.L.2    Tang, C.3    Ponder, J.W.4    Kao, J.L.5    Cistola, D.P.6    Li, E.7
  • 33
    • 0034647414 scopus 로고    scopus 로고
    • Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics
    • Lu J, Lin CL, Tang C, Ponder JW, Kao JL, Cistola DP, Li E: Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics. J Mol Biol 300: 619-632, 2000
    • (2000) J. Mol. Biol. , vol.300 , pp. 619-632
    • Lu, J.1    Lin, C.L.2    Tang, C.3    Ponder, J.W.4    Kao, J.L.5    Cistola, D.P.6    Li, E.7
  • 34
    • 0034622583 scopus 로고    scopus 로고
    • Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding
    • Krishnan VV, Sukumar M, Gierasch LM, Cosman M: Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding. Biochemistry 39: 9119-9129, 2000
    • (2000) Biochemistry , vol.39 , pp. 9119-9129
    • Krishnan, V.V.1    Sukumar, M.2    Gierasch, L.M.3    Cosman, M.4
  • 37
    • 0020545022 scopus 로고
    • A radiochemical procedure for the assay of fatty acid binding by proteins
    • Glatz JF, Veerkamp JH: A radiochemical procedure for the assay of fatty acid binding by proteins. Anal Biochem 132: 89-95, 1983
    • (1983) Anal Biochem. , vol.132 , pp. 89-95
    • Glatz, J.F.1    Veerkamp, J.H.2
  • 38
    • 0023664298 scopus 로고
    • Expression of rat intestinal fatty acid-binding protein in Escherichia coli. Purification and comparison of ligand binding characteristics with that of Escherichia coli-derived rat liver fatty acid-binding protein
    • Lowe JB, Sacchettini JC, Laposata M, McQuillan JJ, Gordon JI: Expression of rat intestinal fatty acid-binding protein in Escherichia coli. Purification and comparison of ligand binding characteristics with that of Escherichia coli-derived rat liver fatty acid-binding protein. J Biol Chem 262: 5931-5937, 1987
    • (1987) J. Biol. Chem. , vol.262 , pp. 5931-5937
    • Lowe, J.B.1    Sacchettini, J.C.2    Laposata, M.3    McQuillan, J.J.4    Gordon, J.I.5
  • 39
    • 0023774566 scopus 로고
    • Characterization and binding properties of fatty acid-binding proteins from human, pig, and rat heart
    • Paulussen RJ, van der Logt CP, Veerkamp JH: Characterization and binding properties of fatty acid-binding proteins from human, pig, and rat heart. Arch Biochem Biophys 264: 533-545, 1988
    • (1988) Arch. Biochem. Biophys. , vol.264 , pp. 533-545
    • Paulussen, R.J.1    Van der Logt, C.P.2    Veerkamp, J.H.3
  • 40
    • 0025170934 scopus 로고
    • Assay of the binding of fatty acids by proteins: Evaluation of the Lipidex 1000 procedure
    • Vork MM, Glatz JF, Surtel DA, van der Vusse GJ: Assay of the binding of fatty acids by proteins: Evaluation of the Lipidex 1000 procedure. Mol Cell Biochem 98: 111-117, 1990
    • (1990) Mol. Cell Biochem. , vol.98 , pp. 111-117
    • Vork, M.M.1    Glatz, J.F.2    Surtel, D.A.3    Van der Vusse, G.J.4
  • 41
    • 0025783264 scopus 로고
    • Interaction of fatty acids with recombinant rat intestinal and liver fatty acid-binding proteins
    • Nemecz G, Hubbell T, Jefferson JR, Lowe JB, Schroeder F: Interaction of fatty acids with recombinant rat intestinal and liver fatty acid-binding proteins. Arch Biochem Biophys 286: 300-309, 1991
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 300-309
    • Nemecz, G.1    Hubbell, T.2    Jefferson, J.R.3    Lowe, J.B.4    Schroeder, F.5
  • 42
    • 0027194345 scopus 로고
    • Purification and characterization of fatty acid-binding proteins from brown adipose tissue of the rat
    • 1169
    • Dutta-Roy AK, Huang Y, Dunbar B, Trayhurn P: Purification and characterization of fatty acid-binding proteins from brown adipose tissue of the rat. Biochim Biophys Acta 1169: 73-79, 1993
    • (1993) Biochim. Biophys. Acta , pp. 73-79
    • Dutta-Roy, A.K.1    Huang, Y.2    Dunbar, B.3    Trayhurn, P.4
  • 45
    • 17544371709 scopus 로고    scopus 로고
    • Kinetics of fatty acid interactions with fatty acid binding proteins from adipocyte, heart, and intestine
    • Richieri GV, Ogata RT, Kleinfeld AM: Kinetics of fatty acid interactions with fatty acid binding proteins from adipocyte, heart, and intestine. J Biol Chem 271: 11291-11300, 1996
    • (1996) J. Biol. Chem. , vol.271 , pp. 11291-11300
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 46
    • 0027089776 scopus 로고
    • A fluorescently labeled intestinal fatty acid binding protein. Interactions with fatty acids and its use in monitoring free fatty acids
    • Richieri GV, Ogata RT, Kleinfeld AM: A fluorescently labeled intestinal fatty acid binding protein. Interactions with fatty acids and its use in monitoring free fatty acids. J Biol Chem 267: 23495-23501, 1992
    • (1992) J. Biol. Chem. , vol.267 , pp. 23495-23501
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 47
    • 0029859741 scopus 로고    scopus 로고
    • Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein
    • Richicri GV, Ogata RT, Kleinfeld AM: Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein. J Biol Chem 271: 31069-31074, 1996
    • (1996) J. Biol. Chem. , vol.271 , pp. 31069-31074
    • Richicri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 48
    • 0028076831 scopus 로고
    • Equilibrium constants for the binding of fatty acids with fatty acid-binding proteins from adipocyte, intestine, heart, and liver measured with the fluorescent probe ADIFAB
    • Richieri GV, Ogata RT, Kleinfeld AM: Equilibrium constants for the binding of fatty acids with fatty acid-binding proteins from adipocyte, intestine, heart, and liver measured with the fluorescent probe ADIFAB. J Biol Chem 269: 23919-23930, 1994
    • (1994) J. Biol. Chem. , vol.269 , pp. 23919-23930
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 49
    • 0034691282 scopus 로고    scopus 로고
    • Fatty acid binding proteins from different tissues show distinct patterns of fatty acid interactions
    • Richieri GV, Ogata RT, Zimmerman AW, Veerkamp JH, Kleinfeld AM: Fatty acid binding proteins from different tissues show distinct patterns of fatty acid interactions. Biochemistry 39: 7197-7204, 2000
    • (2000) Biochemistry , vol.39 , pp. 7197-7204
    • Richieri, G.V.1    Ogata, R.T.2    Zimmerman, A.W.3    Veerkamp, J.H.4    Kleinfeld, A.M.5
  • 50
    • 0030757235 scopus 로고    scopus 로고
    • Mutants of rat intestinal fatty acid-binding protein illustrate the critical role played by enthalpy-entropy compensation in ligand binding
    • Richieri GV, Low PJ, Ogata RT, Kleinfeld AM: Mutants of rat intestinal fatty acid-binding protein illustrate the critical role played by enthalpy-entropy compensation in ligand binding. J Biol Chem 272: 16737-16740, 1997
    • (1997) J. Biol. Chem. , vol.272 , pp. 16737-16740
    • Richieri, G.V.1    Low, P.J.2    Ogata, R.T.3    Kleinfeld, A.M.4
  • 51
    • 0032959121 scopus 로고    scopus 로고
    • Fatty acid interactions with native and mutant fatty acid binding proteins 4
    • Richieri GV, Ogata RT, Kleinfeld AM: Fatty acid interactions with native and mutant fatty acid binding proteins. Mol Cell Biochem 192: 77-85, 1999
    • (1999) Mol. Cell Biochem. , vol.192 , pp. 77-85
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 52
    • 0032571327 scopus 로고    scopus 로고
    • Thermodynamics of fatty acid binding to engineered mutants of the adipocyte and intestinal fatty acid-binding proteins
    • Richieri GV, Low PJ, Ogata RT, Kleinfeld AM: Thermodynamics of fatty acid binding to engineered mutants of the adipocyte and intestinal fatty acid-binding proteins. J Biol Chem 273: 7397-7405, 1998
    • (1998) J. Biol. Chem. , vol.273 , pp. 7397-7405
    • Richieri, G.V.1    Low, P.J.2    Ogata, R.T.3    Kleinfeld, A.M.4
  • 53
    • 0029930226 scopus 로고    scopus 로고
    • Affinity of fatty acid for rat intestinal fatty acid binding protein: Further examination
    • Kurian E, Kirk WR, Prendergast FG: Affinity of fatty acid for rat intestinal fatty acid binding protein: Further examination. Biochemistry 35: 3865-3874, 1996
    • (1996) Biochemistry , vol.35 , pp. 3865-3874
    • Kurian, E.1    Kirk, W.R.2    Prendergast, F.G.3
  • 54
    • 0027506984 scopus 로고
    • Membrane partition of fatty acids and inhibition of T cell function
    • Anel A, Richieri GV, Kleinfeld AM: Membrane partition of fatty acids and inhibition of T cell function. Biochemistry 32: 530-536, 1993
    • (1993) Biochemistry , vol.32 , pp. 530-536
    • Anel, A.1    Richieri, G.V.2    Kleinfeld, A.M.3
  • 55
    • 0017884417 scopus 로고
    • The hydrophobic effect and the organization of living matter
    • Tanford C: The hydrophobic effect and the organization of living matter. Science 200: 1012-1018, 1978
    • (1978) Science , vol.200 , pp. 1012-1018
    • Tanford, C.1
  • 56
    • 0027282014 scopus 로고
    • Titration calorimetry as a binding assay for lipid-binding proteins
    • Miller KR, Cistola DP: Titration calorimetry as a binding assay for lipid-binding proteins. Mol Cell Biochem 123: 29-37, 1993
    • (1993) Mol. Cell Biochem. , vol.123 , pp. 29-37
    • Miller, K.R.1    Cistola, D.P.2
  • 57
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T, Williston S, Brandts JF, Lin LN: Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 179: 131-137, 1989
    • (1989) Anal Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 58
    • 0028090521 scopus 로고
    • Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and X-ray crystallographic studies
    • LaLonde JM, Levenson MA, Roe JJ, Bernlohr DA, Banaszak LJ: Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and X-ray crystallographic studies. J Biol Chem 269: 25339-25347, 1994
    • (1994) J. Biol. Chem. , vol.269 , pp. 25339-25347
    • LaLonde, J.M.1    Levenson, M.A.2    Roe, J.J.3    Bernlohr, D.A.4    Banaszak, L.J.5
  • 59
    • 0039250873 scopus 로고    scopus 로고
    • Binding of fatty acids and peroxisome proliferators to orthologous fatty acid binding proteins from human, murine, and bovine liver
    • Wolfrum C, Börchers T, Sacchettini JC, Spener F: Binding of fatty acids and peroxisome proliferators to orthologous fatty acid binding proteins from human, murine, and bovine liver. Biochemistry 39: 1469-1474, 2000
    • (2000) Biochemistry , vol.39 , pp. 1469-1474
    • Wolfrum, C.1    Börchers, T.2    Sacchettini, J.C.3    Spener, F.4
  • 60
    • 0000513014 scopus 로고    scopus 로고
    • Ligand specificity of brain lipid-binding protein
    • Xu LZ, Sanchez R, Sali A, Heintz N: Ligand specificity of brain lipid-binding protein. J Biol Chem 271: 24711-24719, 1996
    • (1996) J. Biol. Chem. , vol.271 , pp. 24711-24719
    • Xu, L.Z.1    Sanchez, R.2    Sali, A.3    Heintz, N.4
  • 61
    • 0029034233 scopus 로고
    • Thermodynamics of fatty acid binding to fatty acid-binding proteins and fatty acid partition between water and membranes measured using the fluorescent probe ADIFAB
    • Richieri GV, Ogata RT, Kleinfeld AM: Thermodynamics of fatty acid binding to fatty acid-binding proteins and fatty acid partition between water and membranes measured using the fluorescent probe ADIFAB. J Biol Chem 270: 15076-15084, 1995
    • (1995) J. Biol. Chem. , vol.270 , pp. 15076-15084
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 62
    • 0028773645 scopus 로고
    • Structural studies on human muscle fatty acid binding protein at 1.4 Å resolution: Binding interactions with three C18 fatty acids
    • Young AC, Scapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC: Structural studies on human muscle fatty acid binding protein at 1.4 Å resolution: Binding interactions with three C18 fatty acids. Structure 2: 523-534, 1994
    • (1994) Structure , vol.2 , pp. 523-534
    • Young, A.C.1    Scapin, G.2    Kromminga, A.3    Patel, S.B.4    Veerkamp, J.H.5    Sacchettini, J.C.6
  • 63
    • 0032502246 scopus 로고    scopus 로고
    • Bovine epidermal fatty acid-binding protein: Determination of ligand specificity and cellular localization in retina and testis
    • Kingma PB, Bok D, Ong DE: Bovine epidermal fatty acid-binding protein: Determination of ligand specificity and cellular localization in retina and testis. Biochemistry 37: 3250-3257, 1998
    • (1998) Biochemistry , vol.37 , pp. 3250-3257
    • Kingma, P.B.1    Bok, D.2    Ong, D.E.3
  • 64
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ: MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24: 946-950, 1991
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 65
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt EA, Bacon DJ: Raster3D: Photorealistic molecular graphics. Methods Enzymol 277: 505-524, 1997
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


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