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Volumn 1811, Issue 7-8, 2011, Pages 452-459

Interaction of enterocyte FABPs with phospholipid membranes: Clues for specific physiological roles

Author keywords

Fatty acid binding proteins; Intracellular fatty acid traffic; Membrane interaction; Model membranes

Indexed keywords

CYTOCHROME C; FATTY ACID BINDING PROTEIN; PHOSPHOLIPID;

EID: 79959376252     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2011.04.005     Document Type: Article
Times cited : (27)

References (50)
  • 1
    • 0022364211 scopus 로고
    • Function and regulation of hepatic and intestinal fatty acid binding proteins
    • DOI 10.1016/0009-3084(85)90060-X
    • N.M. Bass Function and regulation of hepatic and intestinal fatty-acid binding proteins Chem. Phys. Lipids 38 1985 95 114 (Pubitemid 15226750)
    • (1985) Chemistry and Physics of Lipids , vol.38 , Issue.1-2 , pp. 95-114
    • Bass, N.M.1
  • 2
    • 0030239495 scopus 로고    scopus 로고
    • Cellular fatty acid-binding proteins: Their function and physiological significance
    • DOI 10.1016/S0163-7827(96)00006-9, PII S0163782796000069
    • J.F.C. Glatz, and G.J. vanderVusse Cellular fatty acid-binding proteins: their function and physiological significance Prog. Lipid Res. 35 1996 243 282 (Pubitemid 27092444)
    • (1996) Progress in Lipid Research , vol.35 , Issue.3 , pp. 243-282
    • Glatz, J.F.C.1    Van Der Vusse, G.J.2
  • 3
    • 50949128339 scopus 로고    scopus 로고
    • The emerging functions and mechanisms of mammalian fatty acid-binding proteins
    • J. Storch, and B. Corsico The emerging functions and mechanisms of mammalian fatty acid-binding proteins Annu. Rev. Nutr. 28 2008 73 95
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 73-95
    • Storch, J.1    Corsico, B.2
  • 6
    • 0028896925 scopus 로고
    • Cytoplasmatic fatty-acid binding proteins-their structure and genes
    • J.H. Veerkamp, and R. Maatman Cytoplasmatic fatty-acid binding proteins-their structure and genes Prog. Lipid Res. 34 1995 17 52
    • (1995) Prog. Lipid Res. , vol.34 , pp. 17-52
    • Veerkamp, J.H.1    Maatman, R.2
  • 8
    • 0141884343 scopus 로고    scopus 로고
    • Intestinal-type and liver-type fatty acid-binding protein in the intestine. Tissue distribution and clinical utility
    • DOI 10.1016/S0009-9120(03)00096-1
    • M. Pelsers, Z. Namiot, W. Kisielewski, A. Namiot, M. Januszkiewicz, W.T. Hermens, and J.F.C. Glatz Intestinal-type and liver-type fatty acid-binding protein in the intestine. Tissue distribution and clinical utility Clin. Biochem. 36 2003 529 535 (Pubitemid 37244015)
    • (2003) Clinical Biochemistry , vol.36 , Issue.7 , pp. 529-535
    • Pelsers, M.M.A.L.1    Namiot, Z.2    Kisielewski, W.3    Namiot, A.4    Januszkiewicz, M.5    Hermens, W.T.6    Glatz, J.F.C.7
  • 9
    • 0027244075 scopus 로고
    • Rat intestinal fatty acid binding protein. A model system for analyzing the forces that can bind fatty acids to proteins
    • J.C. Sacchettini, and J.I. Gordon Rat intestinal fatty-acid binding protein-a model system for analyzing the forces that can bind fatty acid to proteins J. Biol. Chem. 268 1993 18399 18402 (Pubitemid 23273760)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.25 , pp. 18399-18402
    • Sacchettini, J.C.1    Gordon, J.I.2
  • 10
    • 35848954991 scopus 로고    scopus 로고
    • Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein
    • DOI 10.1021/bi701092r
    • Y. He, X. Yang, H. Wang, R. Estephan, F. Francis, S. Kodukula, J. Storch, and R.E. Stark Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein Biochemistry 46 2007 12543 12556 (Pubitemid 350060081)
    • (2007) Biochemistry , vol.46 , Issue.44 , pp. 12543-12556
    • He, Y.1    Yang, X.2    Wang, H.3    Estephan, R.4    Francis, F.5    Kodukula, S.6    Storch, J.7    Stark, R.E.8
  • 11
    • 33645277091 scopus 로고    scopus 로고
    • Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family
    • A.M.C. Marcelino, R.G. Smock, and L.M. Gierasch Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family Proteins 63 2006 373 384
    • (2006) Proteins , vol.63 , pp. 373-384
    • Marcelino, A.M.C.1    Smock, R.G.2    Gierasch, L.M.3
  • 12
    • 0030811918 scopus 로고    scopus 로고
    • Modelling intracellular fatty acid transport: Possible mechanistic role of cytoplasmic fatty acid-binding protein
    • M.M. Vork, J.F.C. Glatz, and G.J. VanderVusse Modelling intracellular fatty acid transport: possible mechanistic role of cytoplasmic fatty acid-binding protein Prostaglandins Leukot. Essent. Fatty Acids 57 1997 11 16
    • (1997) Prostaglandins Leukot. Essent. Fatty Acids , vol.57 , pp. 11-16
    • Vork, M.M.1    Glatz, J.F.C.2    Vandervusse, G.J.3
  • 13
    • 0036080491 scopus 로고    scopus 로고
    • Transfer of fatty acids between intracellular membranes: Roles of soluble binding proteins, distance, and time
    • R.A. Weisiger, and S.D. Zucker Transfer of fatty acids between intracellular membranes: roles of soluble binding proteins, distance, and time Am. J. Physiol. Gastrointest. Liver Physiol. 282 2002 G105 G115
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.282
    • Weisiger, R.A.1    Zucker, S.D.2
  • 14
    • 0029993073 scopus 로고    scopus 로고
    • Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms
    • DOI 10.1074/jbc.271.23.13317
    • K.T. Hsu, and J. Storch Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms J. Biol. Chem. 271 1996 13317 13323 (Pubitemid 26185369)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.23 , pp. 13317-13323
    • Hsu, K.-T.1    Storch, J.2
  • 15
    • 0034004499 scopus 로고    scopus 로고
    • Liver and intestinal fatty acid-binding proteins obtain fatty acids from phospholipid membranes by different mechanisms
    • A.E.A. Thumser, and J. Storch Liver and intestinal fatty acid-binding proteins obtain fatty acids from phospholipid membranes by different mechanisms J. Lipid Res. 41 2000 647 656 (Pubitemid 30220669)
    • (2000) Journal of Lipid Research , vol.41 , Issue.4 , pp. 647-656
    • Thumser, A.E.A.1    Storch, J.2
  • 16
    • 0035916274 scopus 로고    scopus 로고
    • Deletion of the helical motif in the intestinal fatty acid-binding protein reduces its interactions with membrane monolayers: Brewster angle microscopy, IR reflection-absorption spectroscopy, and surface pressure studies
    • DOI 10.1021/bi002252i
    • F. Wu, B. Corsico, C.R. Flach, D.P. Cistola, J. Storch, and R. Mendelsohn Deletion of the helical motif in the intestinal fatty acid-binding protein reduces its interactions with membrane monolayers: Brewster angle microscopy, IR reflection-absorption spectroscopy, and surface pressure studies Biochemistry 40 2001 1976 1983 (Pubitemid 32165666)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 1976-1983
    • Wu, F.1    Corsico, B.2    Flach, C.R.3    Cistola, D.P.4    Storch, J.5    Mendelsohn, R.6
  • 18
    • 12144289741 scopus 로고    scopus 로고
    • The α-Helical Domain of Liver Fatty Acid Binding Protein Is Responsible for the Diffusion-Mediated Transfer of Fatty Acids to Phospholipid Membranes
    • DOI 10.1021/bi0357356
    • B. Corsico, H.L. Liou, and J. Storch The alpha-helical domain of liver fatty acid binding protein is responsible for the diffusion-mediated transfer of fatty acids to phospholipid membranes Biochemistry 43 2004 3600 3607 (Pubitemid 38391715)
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3600-3607
    • Corsico, B.1    Liou, H.L.2    Storch, J.3
  • 19
    • 23244434183 scopus 로고    scopus 로고
    • Fatty acid transfer from intestinal fatty acid binding protein to membranes: Electrostatic and hydrophobic interactions
    • DOI 10.1194/jlr.M500140-JLR200
    • B. Corsico, G.R. Franchini, K.T. Hsu, and J. Storch Fatty acid transfer from intestinal fatty acid binding protein to membranes: electrostatic and hydrophobic interactions J. Lipid Res. 46 2005 1765 1772 (Pubitemid 41099344)
    • (2005) Journal of Lipid Research , vol.46 , Issue.8 , pp. 1765-1772
    • Corsico, B.1    Franchini, G.R.2    Hsu, K.-T.3    Storch, J.4
  • 20
    • 33744935307 scopus 로고    scopus 로고
    • Protein-membrane interaction and fatty acid transfer from intestinal fatty acid-binding protein to membranes: Support for a multistep process
    • DOI 10.1074/jbc.M511943200
    • L.J. Falomir Lockhart, L. Laborde, P.C. Kahn, J. Storch, and B. Corsico Protein-membrane interaction and fatty acid transfer from intestinal fatty acid-binding protein to membranes-support for a multistep process J. Biol. Chem. 281 2006 13979 13989 (Pubitemid 43848324)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 13979-13989
    • Falomir-Lockhart, L.J.1    Laborde, L.2    Kahn, P.C.3    Storch, J.4    Corsico, B.5
  • 21
    • 40949143121 scopus 로고    scopus 로고
    • The integrity of the alpha-helical domain of intestinal fatty acid binding protein is essential for the collision-mediated transfer of fatty acids to phospholipid membranes
    • G.R. Franchini, J. Storch, and B. Corsico The integrity of the alpha-helical domain of intestinal fatty acid binding protein is essential for the collision-mediated transfer of fatty acids to phospholipid membranes Biochim. Biophys. Acta 1781 2008 192 199
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 192-199
    • Franchini, G.R.1    Storch, J.2    Corsico, B.3
  • 22
    • 0033592916 scopus 로고    scopus 로고
    • Binding of recombinant rat liver fatty acid-binding protein to small anionic phospholipid vesicles results in ligand release: A model for interfacial binding and fatty acid targeting
    • J.K. Davies, A.E.A. Thumser, and D.C. Wilton Binding of recombinant rat liver fatty acid-binding protein to small anionic phospholipid vesicles results in ligand release: a model for interfacial binding and fatty acid targeting Biochemistry 38 1999 16932 16940
    • (1999) Biochemistry , vol.38 , pp. 16932-16940
    • Davies, J.K.1    Thumser, A.E.A.2    Wilton, D.C.3
  • 23
    • 0037073726 scopus 로고    scopus 로고
    • Effect of charge reversal mutations on the ligand- and membrane-binding properties of liver fatty acid-binding protein
    • DOI 10.1074/jbc.M208141200
    • J.K. Davies, R.M. Hagan, and D.C. Wilton Effect of charge reversal mutations on the ligand- and membrane-binding properties of liver fatty acid-binding protein J. Biol. Chem. 277 2002 48395 48402 (Pubitemid 35470796)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48395-48402
    • Davies, J.K.1    Hagan, R.M.2    Wilton, D.C.3
  • 24
    • 39749170233 scopus 로고    scopus 로고
    • The interaction of liver fatty-acid-binding protein (FABP) with anionic phospholipid vesicles: Is there extended phospholipid anchorage under these conditions?
    • DOI 10.1042/BJ20071109
    • R.M. Hagan, J. Worner-Gibbs, and D.C. Wilton The interaction of liver fatty-acid-binding protein (FABP) with anionic phospholipid vesicles: is there extended phospholipid anchorage under these conditions? Biochem. J. 410 2008 123 129 (Pubitemid 351300331)
    • (2008) Biochemical Journal , vol.410 , Issue.1 , pp. 123-129
    • Hagan, R.M.1    Worner-Gibbs, J.2    Wilton, D.C.3
  • 25
    • 0028905325 scopus 로고
    • 2-(Tributylstannyl)-4-[3-(trifluoromethyl)-3H-diazirin-3-yl] benzyl alcohol-a building-block for photolabeling and cross-linking reagents of very high specific radioactivity
    • T. Weber, and J. Brunner 2-(Tributylstannyl)-4-[3-(trifluoromethyl)-3H- diazirin-3-yl] benzyl alcohol-a building-block for photolabeling and cross-linking reagents of very high specific radioactivity J. Am. Chem. Soc. 117 1995 3084 3095
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3084-3095
    • Weber, T.1    Brunner, J.2
  • 26
    • 0035907295 scopus 로고    scopus 로고
    • Evidence for a central apolipoprotein A-I domain loosely bound to lipids in discoidal lipoproteins that is capable of penetrating the bilayer of phospholipid vesicles
    • B. Corsico, J.D. Toledo, and H.A. Garda Evidence for a central apolipoprotein A-I domain loosely bound to lipids in discoidal lipoproteins that is capable of penetrating the bilayer of phospholipid vesicles J. Biol. Chem. 276 2001 16978 16985
    • (2001) J. Biol. Chem. , vol.276 , pp. 16978-16985
    • Corsico, B.1    Toledo, J.D.2    Garda, H.A.3
  • 27
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential
    • DOI 10.1016/0005-2736(85)90521-8
    • M.J. Hope, M.B. Bally, G. Webb, and P.R. Cullis Production of large unilamellar vesicles by rapid extrusion procedure-characterization of size distribution, trapped volume and ability to maintain a membrane-potential Biochim. Biophys. Acta 812 1985 55 65 (Pubitemid 15159822)
    • (1985) Biochimica et Biophysica Acta - Biomembranes , vol.812 , Issue.1 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 28
    • 0016360614 scopus 로고
    • Preparation of homogeneous, single-walled phosphatidylcholine vesicles
    • C. Huang, and T.E. Thompson Preparation of homogeneous, single-walled phosphatidylcholine vesicles Methods Enzymol. 32 1974 5
    • (1974) Methods Enzymol. , vol.32 , pp. 5
    • Huang, C.1    Thompson, T.E.2
  • 29
    • 79959379270 scopus 로고
    • Interaction of fatty-acid binding protein (FABP) with fluorescent analogs of free fatty acids
    • J. Storch, A.M. Kleinfeld, N.M. Bass, and H. Shields Interaction of fatty-acid binding protein (FABP) with fluorescent analogs of free fatty acids Biophys. J. 49 1986 A106 A
    • (1986) Biophys. J. , vol.49
    • Storch, J.1    Kleinfeld, A.M.2    Bass, N.M.3    Shields, H.4
  • 30
    • 0019331570 scopus 로고
    • Studies on the mechanism of membrane-fusion-kinetics of calcium-ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicle content
    • J. Wilschut, N. Duzgunes, R. Fraley, and D. Papahadjopoulos Studies on the mechanism of membrane-fusion-kinetics of calcium-ion induced fusion of phosphatidylserine vesicles followed by a new assay for mixing of aqueous vesicle content Biochemistry 19 1980 6011 6021
    • (1980) Biochemistry , vol.19 , pp. 6011-6021
    • Wilschut, J.1    Duzgunes, N.2    Fraley, R.3    Papahadjopoulos, D.4
  • 31
    • 0001022995 scopus 로고
    • A modification of the colorimetric phosphorus determination for use with the photoelectric colorimeter
    • G. Gomori A modification of the colorimetric phosphorus determination for use with the photoelectric colorimeter J. Lab. Clin. Med. 27 1942 955 960
    • (1942) J. Lab. Clin. Med. , vol.27 , pp. 955-960
    • Gomori, G.1
  • 32
    • 0023228875 scopus 로고
    • Binding of cytochrome c to liposomes as revealed by the quenching of fluorescence from pyrene-labeled phospholipids
    • DOI 10.1021/bi00385a006
    • P. Mustonen, J.A. Virtanen, P.J. Somerharju, and P.K.J. Kinnunen Binding of cytochrome-c to liposomes as revealed by the quenching of fluorescence from pyrene-labeled phospholipids Biochemistry 26 1987 2991 2997 (Pubitemid 17087827)
    • (1987) Biochemistry , vol.26 , Issue.11 , pp. 2991-2997
    • Mustonen, P.1    Virtanen, J.A.2    Somerharju, P.J.3    Kinnunen, P.K.J.4
  • 33
    • 0033544881 scopus 로고    scopus 로고
    • The adipocyte fatty acid-binding protein binds to membranes by electrostatic interactions
    • E.R. Smith, and J. Storch The adipocyte fatty acid-binding protein binds to membranes by electrostatic interactions J. Biol. Chem. 274 1999 35325 35330 (Pubitemid 129512819)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.50 , pp. 35325-35330
    • Smith, E.R.1    Storch, J.2
  • 34
    • 0027050183 scopus 로고
    • 1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4,5-bisphosphate
    • DOI 10.1021/bi00166a005
    • M. Rebecchi, A. Peterson, and S. McLaughlin Phosphoinositide-specific phospholipase c-delta-1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4,5-biphosphate Biochemistry 31 1992 12742 12747 (Pubitemid 23027052)
    • (1992) Biochemistry , vol.31 , Issue.51 , pp. 12742-12747
    • Rebecchi, M.1    Peterson, A.2    McLaughlin, S.3
  • 35
    • 0028004486 scopus 로고
    • 2 terminus of Src
    • DOI 10.1021/bi00248a019
    • C.A. Buser, C.T. Sigal, M.D. Resh, and S. McLaughlin Membrane-binding of myristylated peptides corresponding to the NH2-terminus of Src Biochemistry 33 1994 13093 13101 (Pubitemid 24364757)
    • (1994) Biochemistry , vol.33 , Issue.44 , pp. 13093-13101
    • Buser, C.A.1    Sigal, C.T.2    Resh, M.D.3    McLaughlin, S.4
  • 36
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • DOI 10.1016/0003-2697(87)90587-2
    • H. Schagger, and G. Vonjagow Tricine sodium dodecyl-sulfate polyamide-gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa Anal. Biochem. 166 1987 368 379 (Pubitemid 18004907)
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 37
    • 0025262186 scopus 로고
    • In situ chemical cleavage of proteins immobilized to glass-fiver and polyvinylidenedifluoride membranes: Cleavage at tryptophan residues with 2-(2'-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine to obtain internal amino acid sequence
    • DOI 10.1016/0003-2697(90)90412-3
    • D.L. Crimmins, D.W. McCourt, R.S. Thoma, M.G. Scott, K. Macke, and B.D. Schwartz In situ chemical cleavage of proteins immobilized to glass-fiber and polyvinylidenedifluoride membranes: cleavage at tryptophan residues with 2-(2′-nitrophenylsulfenyl)-3-methyl-3′-bromoindolenine to obtain internal amino-acid sequence Anal. Biochem. 187 1990 27 38 (Pubitemid 20157511)
    • (1990) Analytical Biochemistry , vol.187 , Issue.1 , pp. 27-38
    • Crimmins, D.L.1    McCourt, D.W.2    Thoma, R.S.3    Scott, M.G.4    Macke, K.5    Schwartz, B.D.6
  • 38
    • 0028057721 scopus 로고
    • Evidence for two distinct acidic phospholipid-binding sites in cytochrome c
    • M. Rytomaa, and P.K.J. Kinnunen Evidence for 2 distinct acidic phospholipid-binding sites in cytochrome-c J. Biol. Chem. 269 1994 1770 1774 (Pubitemid 24035373)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.3 , pp. 1770-1774
    • Rytomaa, M.1    Kinnunen, P.K.J.2
  • 40
    • 0032489363 scopus 로고    scopus 로고
    • Conformation of apolipoprotein AI in reconstituted lipoprotein particles and particle-membrane interaction: Effect of cholesterol
    • DOI 10.1016/S0005-2760(97)00187-2, PII S0005276097001872
    • A. Tricerri, B. Corsico, J.D. Toledo, H.A. Garda, and R.R. Brenner Conformation of apolipoprotein AI in reconstituted lipoprotein particles and particle-membrane interaction: effect of cholesterol Biochim. Biophys. Acta 1391 1998 67 78 (Pubitemid 28143975)
    • (1998) Biochimica et Biophysica Acta - Lipids and Lipid Metabolism , vol.1391 , Issue.1 , pp. 67-78
    • Tricerri, A.1    Corsico, B.2    Toledo, J.D.3    Garda, H.A.4    Brenner, R.R.5
  • 42
    • 43849106790 scopus 로고    scopus 로고
    • Binding and interactions of L-BABP to lipid membranes studied by molecular dynamic simulations
    • DOI 10.1016/j.bbamem.2008.02.015, PII S0005273608000849
    • M.A. Villarreal, M. Perduca, H.L. Monaco, and G.G. Montich Binding and interactions of L-BABP to lipid membranes studied by molecular dynamic simulations Biochim. Biophys. Acta 1778 2008 1390 1397 (Pubitemid 351695496)
    • (2008) Biochimica et Biophysica Acta - Biomembranes , vol.1778 , Issue.6 , pp. 1390-1397
    • Villarreal, M.A.1    Perduca, M.2    Monaco, H.L.3    Montich, G.G.4
  • 43
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • DOI 10.1016/S0163-7827(00)00005-9, PII S0163782700000059
    • M. Schlame, D. Rua, and M.L. Greenberg The biosynthesis and functional role of cardiolipin Prog. Lipid Res. 39 2000 257 288 (Pubitemid 30224706)
    • (2000) Progress in Lipid Research , vol.39 , Issue.3 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 44
    • 50249148905 scopus 로고    scopus 로고
    • Cardiolipin, the heart of mitochondrial metabolism
    • R.H. Houtkooper, and F.M. Vaz Cardiolipin, the heart of mitochondrial metabolism Cell. Mol. Life Sci. 65 2008 2493 2506
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2493-2506
    • Houtkooper, R.H.1    Vaz, F.M.2
  • 46
    • 69249217642 scopus 로고    scopus 로고
    • Melatonin inhibits cardiolipin peroxidation in mitochondria and prevents the mitochondrial permeability transition and cytochrome c release
    • G. Petrosillo, N. Moro, F.M. Ruggiero, and G. Paradies Melatonin inhibits cardiolipin peroxidation in mitochondria and prevents the mitochondrial permeability transition and cytochrome c release Free Radic. Biol. Med. 47 2009 969 974
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 969-974
    • Petrosillo, G.1    Moro, N.2    Ruggiero, F.M.3    Paradies, G.4
  • 48
    • 79959377979 scopus 로고    scopus 로고
    • Intestinal lipid metabolism is altered in liver fatty acid-binding protein-null mice (LFABP-/-)
    • W. Lagakos, Y.X. Zhou, B. Mandap, B. Binas, and J. Storch Intestinal lipid metabolism is altered in liver fatty acid-binding protein-null mice (LFABP-/-) FASEB J. 21 2007 21:A109
    • (2007) FASEB J. , vol.21
    • Lagakos, W.1    Zhou, Y.X.2    Mandap, B.3    Binas, B.4    Storch, J.5
  • 49
    • 34548451229 scopus 로고    scopus 로고
    • Modeling fatty acid delivery from intestinal fatty acid binding protein to a membrane
    • DOI 10.1110/ps.072875307
    • M. Mihajlovic, and T. Lazaridis Modeling fatty acid delivery from intestinal fatty acid binding protein to a membrane Protein Sci. 16 2007 2042 2055 (Pubitemid 47367127)
    • (2007) Protein Science , vol.16 , Issue.9 , pp. 2042-2055
    • Mihajlovic, M.1    Lazaridis, T.2


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