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Volumn 21, Issue 5, 2008, Pages 313-323

Molecular interactions of the neuronal GPI-anchored lipocalin Lazarillo

Author keywords

Fatty acids; Grasshopper; Heme; Insect hormones; Lipid binding; Retinoic acid

Indexed keywords

HEXAPODA;

EID: 52649113377     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.902     Document Type: Article
Times cited : (13)

References (59)
  • 1
    • 34548149278 scopus 로고    scopus 로고
    • Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M
    • Ahnstrom J, Faber K, Axler O, Dahlback B. 2007. Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M. J. Lipid Res. 48: 1754-1762.
    • (2007) J. Lipid Res , vol.48 , pp. 1754-1762
    • Ahnstrom, J.1    Faber, K.2    Axler, O.3    Dahlback, B.4
  • 2
    • 52649103287 scopus 로고    scopus 로고
    • Åkerström B, Borregaard N, Flower DR, Salier J-P eds, Landes Biosciences: Georgetown, TX
    • Åkerström B, Borregaard N, Flower DR, Salier J-P (eds). 2006. CT Molecular Biology Intelligence Unit. Lipocalins. Landes Biosciences: Georgetown, TX.
    • (2006) CT Molecular Biology Intelligence Unit. Lipocalins
  • 3
    • 52649105191 scopus 로고    scopus 로고
    • 1- Microglobulin. In Lipocalins, Åkerström B, Borregaard N, Flower D, Salier J-P (eds). Landes Bioscience: Georgetown, TX.
    • 1- Microglobulin. In Lipocalins, Åkerström B, Borregaard N, Flower D, Salier J-P (eds). Landes Bioscience: Georgetown, TX.
  • 5
    • 0033594990 scopus 로고    scopus 로고
    • Binding of biliverdin, bilirubin, and thyroid hormones to lipocalin-type prostaglandin D synthase
    • Beuckmann CT, Aoyagi M, Okazaki I, Hiroike T, Toh H, Hayaishi O, Urade Y. 1999. Binding of biliverdin, bilirubin, and thyroid hormones to lipocalin-type prostaglandin D synthase. Biochemistry 38: 8006-8013.
    • (1999) Biochemistry , vol.38 , pp. 8006-8013
    • Beuckmann, C.T.1    Aoyagi, M.2    Okazaki, I.3    Hiroike, T.4    Toh, H.5    Hayaishi, O.6    Urade, Y.7
  • 6
    • 0028707893 scopus 로고
    • Analysis of cellular adhesion in cultured cells
    • Practical Uses in Cell and Molecular Biology, eds, Academic Press, Inc, San Diego;
    • Bieber AJ. 1994. Analysis of cellular adhesion in cultured cells. In Drosophila melanogaster. Practical Uses in Cell and Molecular Biology, Vol. 44, Goldstein LSB, Fyrberg EA (eds). Academic Press, Inc.: San Diego; 683-696.
    • (1994) Drosophila melanogaster , vol.44 , pp. 683-696
    • Bieber, A.J.1
  • 7
    • 0024358833 scopus 로고
    • Drosophila neuroglian: A member of the immunoglobulin superfamily with extensive homology to the vertebrate neural adhesion molecule L1
    • Bieber AJ, Snow PM, Hortsch M, Patel NH, Jacobs JR, Traquina ZR, Schilling J, Goodman CS. 1989. Drosophila neuroglian: a member of the immunoglobulin superfamily with extensive homology to the vertebrate neural adhesion molecule L1. Cell 59: 447-460.
    • (1989) Cell , vol.59 , pp. 447-460
    • Bieber, A.J.1    Snow, P.M.2    Hortsch, M.3    Patel, N.H.4    Jacobs, J.R.5    Traquina, Z.R.6    Schilling, J.7    Goodman, C.S.8
  • 8
    • 52649102253 scopus 로고    scopus 로고
    • Bacterial lipocalins: Origin, structure and function
    • Åkerström B, Borregaard N, Flower DR, Salier J-P eds, Landes Bioscience: Georgetown, TX;
    • Bishop RE, Cambillau C, Privé GG, Hsi D, Tillo D, Tillier ERM. 2006. Bacterial lipocalins: origin, structure and function. In Lipocalins, Åkerström B, Borregaard N, Flower DR, Salier J-P (eds). Landes Bioscience: Georgetown, TX; 28-40.
    • (2006) Lipocalins , pp. 28-40
    • Bishop, R.E.1    Cambillau, C.2    Privé, G.G.3    Hsi, D.4    Tillo, D.5    Tillier, E.R.M.6
  • 9
    • 0029935233 scopus 로고    scopus 로고
    • Outlier lipocalins more than peripheral
    • Bishop RE, Weiner JH. 1996. Outlier lipocalins more than peripheral. Trends Biochem. Sci. 21: 127.
    • (1996) Trends Biochem. Sci , vol.21 , pp. 127
    • Bishop, R.E.1    Weiner, J.H.2
  • 10
    • 12844277300 scopus 로고    scopus 로고
    • The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands
    • Breustedt DA, Korndorfer IP, Redl B, Skerra A. 2005. The 1.8-A crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands. J. Biol. Chem. 280: 484-493.
    • (2005) J. Biol. Chem , vol.280 , pp. 484-493
    • Breustedt, D.A.1    Korndorfer, I.P.2    Redl, B.3    Skerra, A.4
  • 12
    • 0024284041 scopus 로고
    • Characterization and use of the Drosophila metallothionein promoter in cultured Drosophila melanogaster cells
    • Bunch TA, Grinblat Y, Goldstein LSB. 1988. Characterization and use of the Drosophila metallothionein promoter in cultured Drosophila melanogaster cells. Nucl. Acids Res. 16: 1043-1061.
    • (1988) Nucl. Acids Res , vol.16 , pp. 1043-1061
    • Bunch, T.A.1    Grinblat, Y.2    Goldstein, L.S.B.3
  • 13
    • 50849131431 scopus 로고    scopus 로고
    • Plant lipocalins
    • Åkerström B, Borregaard N, Flower DR, Salier J-P eds, Landes Bioscience: Georgetown, TX;
    • Charron J-BF, Sarhan F. 2006. Plant lipocalins. In Lipocalins, Åkerström B, Borregaard N, Flower DR, Salier J-P (eds). Landes Bioscience: Georgetown, TX; 41-48.
    • (2006) Lipocalins , pp. 41-48
    • Charron, J.-B.F.1    Sarhan, F.2
  • 14
    • 0035666914 scopus 로고    scopus 로고
    • The GPI-anchor and protein sorting
    • Chatterjee S, Mayor S. 2001.The GPI-anchor and protein sorting. Cell. Mol. Life Sci. 58: 1969-1987.
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 1969-1987
    • Chatterjee, S.1    Mayor, S.2
  • 15
    • 0027490797 scopus 로고
    • n-6 polyunsaturated fatty acids increase the neurite length of PC12 cells and embryonic chick motoneurons
    • Dehaut F, Bertrand I, Miltaud T, Pouplard-Barthelaix A, Maingault M. 1993. n-6 polyunsaturated fatty acids increase the neurite length of PC12 cells and embryonic chick motoneurons. Neurosci Lett. 161: 133-136.
    • (1993) Neurosci Lett , vol.161 , pp. 133-136
    • Dehaut, F.1    Bertrand, I.2    Miltaud, T.3    Pouplard-Barthelaix, A.4    Maingault, M.5
  • 16
    • 0037012907 scopus 로고    scopus 로고
    • Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila
    • Dobrosotskaya IY, Seegmiller AC, Brown MS, Goldstein JL, Rawson RB. 2002. Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila. Science 296: 879-883.
    • (2002) Science , vol.296 , pp. 879-883
    • Dobrosotskaya, I.Y.1    Seegmiller, A.C.2    Brown, M.S.3    Goldstein, J.L.4    Rawson, R.B.5
  • 17
    • 35649024789 scopus 로고    scopus 로고
    • Structural insight into thedual ligand specificity and mode of high density lipoprotein association of apolipoprotein D
    • Eichinger A, Nasreen A, Kim HJ, Skerra A. 2007. Structural insight into thedual ligand specificity and mode of high density lipoprotein association of apolipoprotein D. J. Biol. Chem. 282: 31068-31075.
    • (2007) J. Biol. Chem , vol.282 , pp. 31068-31075
    • Eichinger, A.1    Nasreen, A.2    Kim, H.J.3    Skerra, A.4
  • 18
    • 0037165641 scopus 로고    scopus 로고
    • Molecular and structural analyses of a novel temperature stress-induced lipocalin from wheat and Arabidopsis
    • Frenette Charron JB, Breton G, Badawi M, Sarhan F. 2002. Molecular and structural analyses of a novel temperature stress-induced lipocalin from wheat and Arabidopsis. FEBS Lett. 517: 129-132.
    • (2002) FEBS Lett , vol.517 , pp. 129-132
    • Frenette Charron, J.B.1    Breton, G.2    Badawi, M.3    Sarhan, F.4
  • 19
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson T, Kurzchalia TV. 1998. Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 394: 802-805.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 20
    • 47349099698 scopus 로고    scopus 로고
    • Ganfornina MD, Carmo SD, Lora JM, Torres-Schumann S, Vogel M, Allhorn M, Gonzalez C, Bastiani MJ, Rassart E, Sanchez D. 2008. Apolipoprotein D is involved in the mechanisms regulating protection from oxidative stress. Aging Cell 2008 Apr 14; [Epub ahead of print] PMID: 18419796.
    • Ganfornina MD, Carmo SD, Lora JM, Torres-Schumann S, Vogel M, Allhorn M, Gonzalez C, Bastiani MJ, Rassart E, Sanchez D. 2008. Apolipoprotein D is involved in the mechanisms regulating protection from oxidative stress. Aging Cell 2008 Apr 14; [Epub ahead of print] PMID: 18419796.
  • 22
    • 0028796918 scopus 로고
    • Lazarillo, a new GPI-linked surface lipocalin, is restricted to a subset of neurons in the grasshopper embryo
    • Ganfornina MD, Sanchez D, Bastiani MJ. 1995. Lazarillo, a new GPI-linked surface lipocalin, is restricted to a subset of neurons in the grasshopper embryo. Development 121: 123-134.
    • (1995) Development , vol.121 , pp. 123-134
    • Ganfornina, M.D.1    Sanchez, D.2    Bastiani, M.J.3
  • 23
    • 34247602215 scopus 로고    scopus 로고
    • The lipocalin protein family: Protein sequence, structure and relationships to the calycin superfamily
    • Åkerström B, Borregaard N, Flower DR, Salier J-P eds, Landes Bioscience: Georgetown, TX;
    • Ganfornina MD, Sanchez D, Greene LH, Flower DR. 2006. The lipocalin protein family: protein sequence, structure and relationships to the calycin superfamily. In Lipocalins, Åkerström B, Borregaard N, Flower DR, Salier J-P (eds). Landes Bioscience: Georgetown, TX; 17-27.
    • (2006) Lipocalins , pp. 17-27
    • Ganfornina, M.D.1    Sanchez, D.2    Greene, L.H.3    Flower, D.R.4
  • 25
    • 0023352067 scopus 로고
    • The molecular structure of insecticyanin from the tobacco hornworm Manduca sexta L. at 2.6 Å resolution
    • Holden HM, Rypniewski WR, Law JH, Rayment I. 1987. The molecular structure of insecticyanin from the tobacco hornworm Manduca sexta L. at 2.6 Å resolution. EMBO J. 6: 1565-1570.
    • (1987) EMBO J , vol.6 , pp. 1565-1570
    • Holden, H.M.1    Rypniewski, W.R.2    Law, J.H.3    Rayment, I.4
  • 27
    • 34247885894 scopus 로고    scopus 로고
    • Induction of neurite outgrowth in PC12 cells by the medium-chain fatty acid octanoic acid
    • Kamata Y, Shiraga H, Tai A, Kawamoto Y, Gohda E. 2007. Induction of neurite outgrowth in PC12 cells by the medium-chain fatty acid octanoic acid. Neuroscience 146: 1073-1081.
    • (2007) Neuroscience , vol.146 , pp. 1073-1081
    • Kamata, Y.1    Shiraga, H.2    Tai, A.3    Kawamoto, Y.4    Gohda, E.5
  • 28
    • 0028168283 scopus 로고
    • Tryptophan-19 of β-lactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure
    • Katakura Y, Totsuka M, Ametani A, Kaminogawa S. 1994. Tryptophan-19 of β-lactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure. Biochim. Biophys. Acta 1207: 58-67.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 58-67
    • Katakura, Y.1    Totsuka, M.2    Ametani, A.3    Kaminogawa, S.4
  • 30
    • 40649091053 scopus 로고    scopus 로고
    • Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins
    • Kolodziejczyk R, Bujacz G, Jakób M, Ozyhar A, Jaskolski M, Kochman M. 2008. Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins. J. Mol. Biol. 377: 870-881.
    • (2008) J. Mol. Biol , vol.377 , pp. 870-881
    • Kolodziejczyk, R.1    Bujacz, G.2    Jakób, M.3    Ozyhar, A.4    Jaskolski, M.5    Kochman, M.6
  • 31
    • 0024316809 scopus 로고
    • The glycosyl-phosphatidylinositol anchor of membrane proteins
    • Low MG. 1989. The glycosyl-phosphatidylinositol anchor of membrane proteins. Biochim. Biophys. Acta 988: 427-454.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 427-454
    • Low, M.G.1
  • 32
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan P, Johnson WC. 1987. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167: 76-85.
    • (1987) Anal. Biochem , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson, W.C.2
  • 33
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • Mayor S, Rothberg KG, Maxfield FR. 1994. Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science 264: 1948-1951.
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 35
    • 52649157484 scopus 로고    scopus 로고
    • Retinol Jainding protein and its interaction with transthyretin
    • Åkerström B, Borregaard N, Flower DR, Salier J-P eds, Landes Bioscience: Georgetown, TX;
    • Newcomer ME, Ong DE. 2006. Retinol Jainding protein and its interaction with transthyretin. In Lipocalins, Åkerström B, Borregaard N, Flower DR, Salier J-P (eds). Landes Bioscience: Georgetown, TX; 75-82.
    • (2006) Lipocalins , pp. 75-82
    • Newcomer, M.E.1    Ong, D.E.2
  • 37
    • 33749472529 scopus 로고    scopus 로고
    • Influence of oxidative stress on fusion of pre-synaptic plasma membranes of the rat brain with phosphatidyl choline liposomes, and protective effect of vitamin E
    • Omoi NO, Arai M, Saito M, Takatsu H, Shibata A, Fukuzawa K, Sato K, Abe K, Fukui K, Urano S. 2006. Influence of oxidative stress on fusion of pre-synaptic plasma membranes of the rat brain with phosphatidyl choline liposomes, and protective effect of vitamin E. J. Nutr. Sci. Vitaminol. (Tokyo) 52: 248-255.
    • (2006) J. Nutr. Sci. Vitaminol. (Tokyo) , vol.52 , pp. 248-255
    • Omoi, N.O.1    Arai, M.2    Saito, M.3    Takatsu, H.4    Shibata, A.5    Fukuzawa, K.6    Sato, K.7    Abe, K.8    Fukui, K.9    Urano, S.10
  • 38
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • Paladino S, Sarnataro D, Pillich R, Tivodar S, Nitsch L, Zurzolo C. 2004. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J. Cell Biol. 167: 699-709.
    • (2004) J. Cell Biol , vol.167 , pp. 699-709
    • Paladino, S.1    Sarnataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 39
    • 0029147426 scopus 로고
    • Digging into caveolae
    • Parton RG, Simons K. 1995. Digging into caveolae. Science 269: 1398-1399.
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 40
    • 0025298322 scopus 로고
    • Is apolipoprotein D a mammalian bilin-binding protein?
    • Peitsch MC, Boguski MS. 1990. Is apolipoprotein D a mammalian bilin-binding protein? New Biol. 2: 197-206.
    • (1990) New Biol , vol.2 , pp. 197-206
    • Peitsch, M.C.1    Boguski, M.S.2
  • 43
    • 0028796919 scopus 로고
    • Developmental expression of the lipocalin Lazarillo and its role in axonal pathfinding in the grasshopper embryo
    • Sanchez D, Ganfornina MD, Bastiani MJ. 1995. Developmental expression of the lipocalin Lazarillo and its role in axonal pathfinding in the grasshopper embryo. Development 121: 135-147.
    • (1995) Development , vol.121 , pp. 135-147
    • Sanchez, D.1    Ganfornina, M.D.2    Bastiani, M.J.3
  • 44
    • 0034684270 scopus 로고    scopus 로고
    • Lazarillo, a neuronal lipocalin in grasshoppers with a role in axon guidance
    • Sanchez D, Ganfornina MD, Bastiani MJ. 2000. Lazarillo, a neuronal lipocalin in grasshoppers with a role in axon guidance. Biochim. Biophys. Acta 1482: 102-109.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 102-109
    • Sanchez, D.1    Ganfornina, M.D.2    Bastiani, M.J.3
  • 46
    • 33645864333 scopus 로고    scopus 로고
    • Loss of glial Lazarillo, a homolog of apolipoprotein D, reduces lifespan and stress resistance in Drosophila
    • Sanchez D, Lopez-Arias B, Torroja L, Canal I, Wang X, Bastiani MJ, Ganfornina MD. 2006. Loss of glial Lazarillo, a homolog of apolipoprotein D, reduces lifespan and stress resistance in Drosophila. Curr. Biol. 16: 680-686.
    • (2006) Curr. Biol , vol.16 , pp. 680-686
    • Sanchez, D.1    Lopez-Arias, B.2    Torroja, L.3    Canal, I.4    Wang, X.5    Bastiani, M.J.6    Ganfornina, M.D.7
  • 48
    • 0016160429 scopus 로고
    • Measurement of protein by spectrophotometry at 205 nm
    • Scopes RK. 1974. Measurement of protein by spectrophotometry at 205 nm. Anal. Biochem. 59: 277-282.
    • (1974) Anal. Biochem , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 49
    • 0027499708 scopus 로고
    • The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment
    • Schmidt TGM, Skerra A. 1993. The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment. Protein Eng. 6: 109-122.
    • (1993) Protein Eng , vol.6 , pp. 109-122
    • Schmidt, T.G.M.1    Skerra, A.2
  • 50
    • 0027991404 scopus 로고
    • One-step affinity purification of bacterially produced protein by means of the Strep tag and immobilized recombinant core streptavidin
    • Schmidt TGM, Skerra A. 1994. One-step affinity purification of bacterially produced protein by means of the Strep tag and immobilized recombinant core streptavidin. J. Chromatogr. 676: 337-345.
    • (1994) J. Chromatogr , vol.676 , pp. 337-345
    • Schmidt, T.G.M.1    Skerra, A.2
  • 51
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • Schmidt TGM, Skerra A. 2007. The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat. Protoc. 2: 1528-1535.
    • (2007) Nat. Protoc , vol.2 , pp. 1528-1535
    • Schmidt, T.G.M.1    Skerra, A.2
  • 52
    • 0022498720 scopus 로고
    • A chick neural retina adhesion and survival molecule is a retinol-binding protein
    • Schubert D, LaCorbiere M, Esch F. 1986. A chick neural retina adhesion and survival molecule is a retinol-binding protein. J. Cell Biol. 102: 2295-2301.
    • (1986) J. Cell Biol , vol.102 , pp. 2295-2301
    • Schubert, D.1    LaCorbiere, M.2    Esch, F.3
  • 54
    • 0028555357 scopus 로고
    • Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli
    • Skerra A. 1994. Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli. Gene 151: 131-135.
    • (1994) Gene , vol.151 , pp. 131-135
    • Skerra, A.1
  • 55
    • 0033814033 scopus 로고    scopus 로고
    • Use of the Strep-tag and streptavidin for detection and purification of recombinant proteins
    • Skerra A, Schmidt TGM. 2000. Use of the Strep-tag and streptavidin for detection and purification of recombinant proteins. Meth. Enzymol. 326: 271-304.
    • (2000) Meth. Enzymol , vol.326 , pp. 271-304
    • Skerra, A.1    Schmidt, T.G.M.2
  • 56
    • 0029760325 scopus 로고    scopus 로고
    • Domain swapping creates a third putative combining site in bovine odorant binding protein dimer
    • Tegoni M, Ramoni R, Bignetti E, Spinelli S, Cambillau C 1996. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nat. Struct. Biol. 3: 863-867.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 863-867
    • Tegoni, M.1    Ramoni, R.2    Bignetti, E.3    Spinelli, S.4    Cambillau, C.5
  • 57
    • 0028893390 scopus 로고
    • Structural and functional significance of cysteine residues of glutathione-independent prostaglandin D synthase
    • Urade Y, Tanaka T, Eguchi N, Kikuchi M, Kimura H, Toh H, Hayaishi O. 1995. Structural and functional significance of cysteine residues of glutathione-independent prostaglandin D synthase. J. Biol. Chem. 270.
    • (1995) J. Biol. Chem , pp. 270
    • Urade, Y.1    Tanaka, T.2    Eguchi, N.3    Kikuchi, M.4    Kimura, H.5    Toh, H.6    Hayaishi, O.7
  • 58
    • 33845990292 scopus 로고    scopus 로고
    • Lipocalins and insulin resistance: Etiological role of retinol-binding protein 4 and lipocalin-2?
    • van Dam RM, Hu FB. 2007. Lipocalins and insulin resistance: etiological role of retinol-binding protein 4 and lipocalin-2? Clin. Chem. 53: 5-7.
    • (2007) Clin. Chem , vol.53 , pp. 5-7
    • van Dam, R.M.1    Hu, F.B.2
  • 59
    • 33645882217 scopus 로고    scopus 로고
    • Overexpression of a Drosophila homolog of apolipoprotein D leads to increased stress resistance and extended lifespan
    • Walker DW, Muffat J, Rundel C, Benzer S. 2006. Overexpression of a Drosophila homolog of apolipoprotein D leads to increased stress resistance and extended lifespan. Curr. Biol. 16: 674-679.
    • (2006) Curr. Biol , vol.16 , pp. 674-679
    • Walker, D.W.1    Muffat, J.2    Rundel, C.3    Benzer, S.4


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