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Volumn 98, Issue 1, 2014, Pages 61-70

Structure and biotechnological applications of odorant-binding proteins

Author keywords

Biosensors; Electronic nose; Fluorescence binding; Odorant binding proteins; Protein stability

Indexed keywords

ANIMALS; BIOSENSORS; BIOTECHNOLOGY; CHEMICAL DETECTION; ELECTRONIC NOSE; ODORS; VOLATILE ORGANIC COMPOUNDS;

EID: 84891890192     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-5383-y     Document Type: Review
Times cited : (135)

References (94)
  • 1
    • 0026556059 scopus 로고
    • Pheromone-binding proteins in the mouse Mus musculus
    • 1:CAS:528:DyaK38XksVGitL4%3D 1374722 10.1007/BF01923448
    • Bacchini A, Gaetani E, Cavaggioni A (1992) Pheromone-binding proteins in the mouse Mus musculus. Experientia 48:419-421
    • (1992) Experientia , vol.48 , pp. 419-421
    • Bacchini, A.1    Gaetani, E.2    Cavaggioni, A.3
  • 2
    • 84881678206 scopus 로고    scopus 로고
    • Making sense of it all: A review of olfactory biosensing
    • D. Kane A. Micolich J. Rabeau (eds) Pan Stanford Publishing Singapore
    • Bailey K (2011) Making sense of it all: a review of olfactory biosensing. In: Kane D, Micolich A, Rabeau J (eds) Nanotechnology in Australia: Showcase of Early Career Research. Pan Stanford Publishing, Singapore, pp 375-408
    • (2011) Nanotechnology in Australia: Showcase of Early Career Research , pp. 375-408
    • Bailey, K.1
  • 3
    • 79957688409 scopus 로고    scopus 로고
    • Electronic noses and tongues: Applications for the food and pharmaceutical industries
    • 22163873 10.3390/s110504744
    • Baldwin EA, Bai J, Plotto A, Dea S (2011) Electronic noses and tongues: applications for the food and pharmaceutical industries. Sensors 11:4744-4766
    • (2011) Sensors , vol.11 , pp. 4744-4766
    • Baldwin, E.A.1    Bai, J.2    Plotto, A.3    Dea, S.4
  • 4
    • 0036298269 scopus 로고    scopus 로고
    • Binding properties of a locust's chemosensory protein
    • 1:CAS:528:DC%2BD38XksVGitr4%3D 12054562 10.1016/S0006-291X(02)00185-7
    • Ban LP, Zhang L, Yan YH, Pelosi P (2002) Binding properties of a locust's chemosensory protein. Biochem Biophys Res Commun 293:50-54
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 50-54
    • Ban, L.P.1    Zhang, L.2    Yan, Y.H.3    Pelosi, P.4
  • 5
    • 0344837425 scopus 로고    scopus 로고
    • Biochemical characterisation and bacterial expression of an odorant-binding protein from Locusta migratoria
    • 1:CAS:528:DC%2BD3sXns1WksbY%3D 12678502 10.1007/s000180300032
    • Ban LP, Scaloni A, D'Ambrosio C, Zhang L, Yan YH, Pelosi P (2003) Biochemical characterisation and bacterial expression of an odorant-binding protein from Locusta migratoria. Cell Mol Life Sci 60:390-400
    • (2003) Cell Mol Life Sci , vol.60 , pp. 390-400
    • Ban, L.P.1    Scaloni, A.2    D'Ambrosio, C.3    Zhang, L.4    Yan, Y.H.5    Pelosi, P.6
  • 6
    • 84881546308 scopus 로고    scopus 로고
    • Identification of pheromone-like compounds in male reproductive organs of the oriental locust Locusta migratoria
    • 1:CAS:528:DC%2BC3sXhtFygsLbP 23867828 10.1016/j.bbrc.2013.07.015
    • Ban L, Napolitano E, Serra A, Zhou X, Iovinella I, Pelosi P (2013) Identification of pheromone-like compounds in male reproductive organs of the oriental locust Locusta migratoria. Biochem Biophys Res Commun 437:620-624
    • (2013) Biochem Biophys Res Commun , vol.437 , pp. 620-624
    • Ban, L.1    Napolitano, E.2    Serra, A.3    Zhou, X.4    Iovinella, I.5    Pelosi, P.6
  • 7
    • 80455155205 scopus 로고    scopus 로고
    • Biological senses as inspiring model for biomimetic sensors
    • 10.1109/JSEN.2011.2167321
    • Bar-Cohen Y (2011) Biological senses as inspiring model for biomimetic sensors. IEEE Sensors J 11:3194-3201
    • (2011) IEEE Sensors J , vol.11 , pp. 3194-3201
    • Bar-Cohen, Y.1
  • 8
    • 0029858390 scopus 로고    scopus 로고
    • The three dimensional structure of bovine odorant-binding protein and its mechanism of odor recognition
    • 1:CAS:528:DC%2BD38Xms1ClsLk%3D 8901871 10.1038/nsb1196-934
    • Bianchet MA, Bains G, Pelosi P, Pevsner J, Snyder SH, Monaco HL, Amzel LM (1996) The three dimensional structure of bovine odorant-binding protein and its mechanism of odor recognition. Nat Struct Biol 3:934-939
    • (1996) Nat Struct Biol , vol.3 , pp. 934-939
    • Bianchet, M.A.1    Bains, G.2    Pelosi, P.3    Pevsner, J.4    Snyder, S.H.5    Monaco, H.L.6    Amzel, L.M.7
  • 9
    • 84873684449 scopus 로고    scopus 로고
    • An innovative bovine odorant binding protein-based filtering cartridge for the removal of triazine herbicides from water
    • 1:CAS:528:DC%2BC38XhsFOksr7P 23104315 10.1007/s00216-012-6499-0
    • Bianchi F, Basini G, Grolli S, Conti V, Bianchi F, Grasselli F, Careri M, Ramoni R (2013) An innovative bovine odorant binding protein-based filtering cartridge for the removal of triazine herbicides from water. Anal Bioanal Chem 405:1067-1075
    • (2013) Anal Bioanal Chem , vol.405 , pp. 1067-1075
    • Bianchi, F.1    Basini, G.2    Grolli, S.3    Conti, V.4    Bianchi, F.5    Grasselli, F.6    Careri, M.7    Ramoni, R.8
  • 10
    • 0021815342 scopus 로고
    • Purification and characterization of an odorant binding protein from cow nasal tissue
    • 1:CAS:528:DyaL2MXktVagsbs%3D 3996407 10.1111/j.1432-1033.1985.tb08916.x
    • Bignetti E, Cavaggioni A, Pelosi P, Persaud KC, Sorbi RT, Tirindelli R (1985) Purification and characterization of an odorant binding protein from cow nasal tissue. Eur J Biochem 149:227-231
    • (1985) Eur J Biochem , vol.149 , pp. 227-231
    • Bignetti, E.1    Cavaggioni, A.2    Pelosi, P.3    Persaud, K.C.4    Sorbi, R.T.5    Tirindelli, R.6
  • 12
    • 0036379365 scopus 로고    scopus 로고
    • Characterization of a chemosensory protein (ASP3c) from honeybee (Apis mellifera L.) as a brood pheromone carrier
    • 1:CAS:528:DC%2BD38XptlaqsLs%3D 12230571 10.1046/j.1432-1033.2002.03156.x
    • Briand L, Nespoulous C, Huet JC, Takahashi M, Pernollet JC (2002a) Characterization of a chemosensory protein (ASP3c) from honeybee (Apis mellifera L.) as a brood pheromone carrier. Eur J Biochem 269:4586-4596
    • (2002) Eur J Biochem , vol.269 , pp. 4586-4596
    • Briand, L.1    Nespoulous, C.2    Huet, J.C.3    Takahashi, M.4    Pernollet, J.C.5
  • 13
    • 0037062575 scopus 로고    scopus 로고
    • Evidence of an odorant-binding protein in the human olfactory mucus: Location, structural characterization, and odorant-binding properties
    • 1:CAS:528:DC%2BD38Xjs1Sgur8%3D 12044155 10.1021/bi015916c
    • Briand L, Eloit C, Nespoulous C, Bézirard V, Huet JC, Henry C, Blon F, Trotier D, Pernollet JC (2002b) Evidence of an odorant-binding protein in the human olfactory mucus: location, structural characterization, and odorant-binding properties. Biochemistry 41:7241-7252
    • (2002) Biochemistry , vol.41 , pp. 7241-7252
    • Briand, L.1    Eloit, C.2    Nespoulous, C.3    Bézirard, V.4    Huet, J.C.5    Henry, C.6    Blon, F.7    Trotier, D.8    Pernollet, J.C.9
  • 15
    • 0035827661 scopus 로고    scopus 로고
    • Revisiting the specificity of Mamestra brassicae and Antheraea polyphemus pheromone-binding proteins with a fluorescence binding assay
    • 1:CAS:528:DC%2BD3MXktlKns7s%3D 11274212 10.1074/jbc.M100713200
    • Campanacci V, Krieger J, Bette S, Sturgis JN, Lartigue A, Cambillau C, Breer H, Tegoni M (2001) Revisiting the specificity of Mamestra brassicae and Antheraea polyphemus pheromone-binding proteins with a fluorescence binding assay. J Biol Chem 276:20078-20084
    • (2001) J Biol Chem , vol.276 , pp. 20078-20084
    • Campanacci, V.1    Krieger, J.2    Bette, S.3    Sturgis, J.N.4    Lartigue, A.5    Cambillau, C.6    Breer, H.7    Tegoni, M.8
  • 16
    • 3343012246 scopus 로고    scopus 로고
    • Absolute configuration of 2-sec-butyl-4,5-dihydrothiazole in male mouse urine
    • 1:CAS:528:DC%2BD3sXpvVSiurk%3D 14654447 10.1093/chemse/bjg073
    • Cavaggioni A, Mucignat-Caretta C, Zagotto G (2003) Absolute configuration of 2-sec-butyl-4,5-dihydrothiazole in male mouse urine. Chem Senses 28:791-797
    • (2003) Chem Senses , vol.28 , pp. 791-797
    • Cavaggioni, A.1    Mucignat-Caretta, C.2    Zagotto, G.3
  • 17
    • 0030272827 scopus 로고    scopus 로고
    • Electronic noses - Development and future prospects
    • 1:CAS:528:DyaK28XntVKlur0%3D
    • Craven MA, Gardner JW, Bartlett PN (1996) Electronic noses - development and future prospects. Trends Anal Chem 15:486-493
    • (1996) Trends Anal Chem , vol.15 , pp. 486-493
    • Craven, M.A.1    Gardner, J.W.2    Bartlett, P.N.3
  • 18
    • 0025732668 scopus 로고
    • Purification and characterization of two odorant binding proteins from nasal tissue of rabbit and pig
    • 1:CAS:528:DyaK3MXltlShtLw%3D
    • Dal Monte M, Andreini I, Revoltella R, Pelosi P (1991) Purification and characterization of two odorant binding proteins from nasal tissue of rabbit and pig. Comp Biochem Physiol 99B:445-451
    • (1991) Comp Biochem Physiol , vol.99 , pp. 445-451
    • Dal Monte, M.1    Andreini, I.2    Revoltella, R.3    Pelosi, P.4
  • 19
    • 0027717569 scopus 로고
    • Binding of selected odorants to bovine and porcine odorant-binding proteins
    • 1:CAS:528:DyaK2cXjtFOqsrw%3D 10.1093/chemse/18.6.713
    • Dal Monte M, Centini M, Anselmi C, Pelosi P (1993) Binding of selected odorants to bovine and porcine odorant-binding proteins. Chem Senses 18:713-721
    • (1993) Chem Senses , vol.18 , pp. 713-721
    • Dal Monte, M.1    Centini, M.2    Anselmi, C.3    Pelosi, P.4
  • 20
    • 0034041910 scopus 로고    scopus 로고
    • NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori
    • 1:CAS:528:DC%2BD3cXjs12hs70%3D 10850815 10.1110/ps.9.5.1038
    • Damberger F, Nikonova L, Horst R, Peng G, Leal WS, Wuthrich K (2000) NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori. Protein Sci 9:1038-1041
    • (2000) Protein Sci , vol.9 , pp. 1038-1041
    • Damberger, F.1    Nikonova, L.2    Horst, R.3    Peng, G.4    Leal, W.S.5    Wuthrich, K.6
  • 21
    • 84874898366 scopus 로고    scopus 로고
    • Off-flavor precursors in soy protein isolate and novel strategies for their removal
    • 1:CAS:528:DC%2BC3sXntFynsL4%3D 10.1146/annurev-food-030212-182650
    • Damodaran S, Arora A (2013) Off-flavor precursors in soy protein isolate and novel strategies for their removal. Ann Rev Food Sci Technol 4:327-346
    • (2013) Ann Rev Food Sci Technol , vol.4 , pp. 327-346
    • Damodaran, S.1    Arora, A.2
  • 24
    • 84870802588 scopus 로고    scopus 로고
    • Detection of odorant molecules via surface acoustic wave biosensor array based on odorant-binding proteins
    • 22981410 10.1016/j.bios.2012.08.046
    • Di Pietrantonio F, Cannatà D, Benetti M, Verona E, Varriale A, Staiano M, D'Auria S (2013) Detection of odorant molecules via surface acoustic wave biosensor array based on odorant-binding proteins. Biosens Bioelectron 41:328-334
    • (2013) Biosens Bioelectron , vol.41 , pp. 328-334
    • Di Pietrantonio, F.1    Cannatà, D.2    Benetti, M.3    Verona, E.4    Varriale, A.5    Staiano, M.6    D'Auria, S.7
  • 26
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • 1:CAS:528:DyaK28XltlKrtLc%3D 8761444
    • Flower DR (1996) The lipocalin protein family: structure and function. Biochem J 318:1-14
    • (1996) Biochem J , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 27
    • 0034684168 scopus 로고    scopus 로고
    • The lipocalin protein family: Structural and sequence overview
    • 1:CAS:528:DC%2BD3MXotFem 11058743 10.1016/S0167-4838(00)00148-5
    • Flower DR, North AC, Sansom CE (2000) The lipocalin protein family: structural and sequence overview. Biochim Biophys Acta 1482:9-24
    • (2000) Biochim Biophys Acta , vol.1482 , pp. 9-24
    • Flower, D.R.1    North, A.C.2    Sansom, C.E.3
  • 29
    • 33947424283 scopus 로고    scopus 로고
    • Mechanistic events underlying odorant binding protein chemoreception
    • 1:CAS:528:DC%2BD2sXjvVSgs78%3D 17285634 10.1002/prot.21307
    • Golebiowski J, Antonczak S, Fiorucci S, Cabrol-Bass D (2007) Mechanistic events underlying odorant binding protein chemoreception. Proteins 67:448-458
    • (2007) Proteins , vol.67 , pp. 448-458
    • Golebiowski, J.1    Antonczak, S.2    Fiorucci, S.3    Cabrol-Bass, D.4
  • 30
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • 1:CAS:528:DyaK1cXhvFaks70%3D 9504803 10.1002/elps.1150181505
    • Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 34
    • 0041819527 scopus 로고    scopus 로고
    • Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster
    • 1:CAS:528:DC%2BD3sXms1Gkt74%3D 12881720 10.1038/nsb960
    • Kruse SW, Zhao R, Smith DP, Jones DN (2003) Structure of a specific alcohol-binding site defined by the odorant binding protein LUSH from Drosophila melanogaster. Nat Struct Biol 10:694-700
    • (2003) Nat Struct Biol , vol.10 , pp. 694-700
    • Kruse, S.W.1    Zhao, R.2    Smith, D.P.3    Jones, D.N.4
  • 35
    • 84873807676 scopus 로고    scopus 로고
    • Odorant reception in insects: Roles of receptors, binding proteins, and degrading enzymes
    • 1:CAS:528:DC%2BC3sXivVWjtL4%3D 23020622 10.1146/annurev-ento-120811- 153635
    • Leal WS (2013) Odorant reception in insects: roles of receptors, binding proteins, and degrading enzymes. Annu Rev Entomol 58:373-391
    • (2013) Annu Rev Entomol , vol.58 , pp. 373-391
    • Leal, W.S.1
  • 36
    • 0033432884 scopus 로고    scopus 로고
    • Disulfide structure of the pheromone binding protein from the silkworm moth, Bombyx mori
    • 1:CAS:528:DyaK1MXotVOjsbk%3D 10611489 10.1016/S0014-5793(99)01683-X
    • Leal WS, Nikonova L, Peng G (1999) Disulfide structure of the pheromone binding protein from the silkworm moth, Bombyx mori. FEBS Lett 464:85-90
    • (1999) FEBS Lett , vol.464 , pp. 85-90
    • Leal, W.S.1    Nikonova, L.2    Peng, G.3
  • 37
    • 84857453308 scopus 로고    scopus 로고
    • Bioelectronic nose with high sensitivity and selectivity using chemically functionalized carbon nanotube combined with human olfactory receptor
    • 1:CAS:528:DC%2BC38XjtF2gur0%3D 10.1016/j.jbiotec.2011.09.011
    • Lee SH, Jin HJ, Song HS, Hong S, Park TH (2012) Bioelectronic nose with high sensitivity and selectivity using chemically functionalized carbon nanotube combined with human olfactory receptor. J Biotech 157:467-472
    • (2012) J Biotech , vol.157 , pp. 467-472
    • Lee, S.H.1    Jin, H.J.2    Song, H.S.3    Hong, S.4    Park, T.H.5
  • 38
    • 44749094974 scopus 로고    scopus 로고
    • Multiple functions of an odorant-binding protein in the mosquito Aedes aegypti
    • 1:CAS:528:DC%2BD1cXnt1Oru7s%3D 18502197 10.1016/j.bbrc.2008.05.064
    • Li S, Picimbon J-F, Ji SD, Kan YC, Qiao CL, Zhou J-J, Pelosi P (2008) Multiple functions of an odorant-binding protein in the mosquito Aedes aegypti. Biochem Biophys Res Commun 372:464-468
    • (2008) Biochem Biophys Res Commun , vol.372 , pp. 464-468
    • Li, S.1    Picimbon, J.-F.2    Ji, S.D.3    Kan, Y.C.4    Qiao, C.L.5    Zhou, J.-J.6    Pelosi, P.7
  • 39
    • 84868666069 scopus 로고    scopus 로고
    • Impedance sensing and molecular modeling of an olfactory biosensor based on chemosensory proteins of honeybee
    • 1:CAS:528:DC%2BC38Xht1emtrfI 22902534 10.1016/j.bios.2012.07.011
    • Liu Q, Wang H, Li H, Zhang J, Zhuang S, Zhang F, Hsia KJ, Wang P (2013) Impedance sensing and molecular modeling of an olfactory biosensor based on chemosensory proteins of honeybee. Biosens Bioelectron 40:174-179
    • (2013) Biosens Bioelectron , vol.40 , pp. 174-179
    • Liu, Q.1    Wang, H.2    Li, H.3    Zhang, J.4    Zhuang, S.5    Zhang, F.6    Hsia, K.J.7    Wang, P.8
  • 40
    • 0036200906 scopus 로고    scopus 로고
    • Odorants of different chemical classes interact with distinct odorant binding protein subtypes
    • 11751466 10.1093/chemse/27.1.39
    • Löbel D, Jacob M, Völkner M, Breer H (2002) Odorants of different chemical classes interact with distinct odorant binding protein subtypes. Chem Senses 27:39-44
    • (2002) Chem Senses , vol.27 , pp. 39-44
    • Löbel, D.1    Jacob, M.2    Völkner, M.3    Breer, H.4
  • 41
    • 0141726803 scopus 로고    scopus 로고
    • Ligand binding to six recombinant pheromone-binding proteins of Antheraea polyphemus and Antheraea pernyi
    • 1:CAS:528:DC%2BD3sXntVKgsLo%3D 10.1007/s00360-003-0366-4
    • Maida R, Ziegelberger G, Kaissling KE (2003) Ligand binding to six recombinant pheromone-binding proteins of Antheraea polyphemus and Antheraea pernyi. J Comp Physiol 173:565-573
    • (2003) J Comp Physiol , vol.173 , pp. 565-573
    • Maida, R.1    Ziegelberger, G.2    Kaissling, K.E.3
  • 42
    • 46449107710 scopus 로고    scopus 로고
    • Mutant bovine odorant-binding protein: Temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations
    • 1:CAS:528:DC%2BD1cXnvVWhtLg%3D 18260099 10.1002/prot.21966
    • Marabotti A, Lefevre T, Staiano M, Crescenzo R, Varriale A, Rossi M, Pezolet M, D'Auria S (2008a) Mutant bovine odorant-binding protein: temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations. Proteins Struct Funct Genet 72:769-778
    • (2008) Proteins Struct Funct Genet , vol.72 , pp. 769-778
    • Marabotti, A.1    Lefevre, T.2    Staiano, M.3    Crescenzo, R.4    Varriale, A.5    Rossi, M.6    Pezolet, M.7    D'Auria, S.8
  • 43
    • 61349111425 scopus 로고    scopus 로고
    • Wild-type and mutant bovine odorant-binding proteins to probe the role of the quaternary structure organization in the protein thermal stability
    • 1:CAS:528:DC%2BD1cXhtlSnurbM 19367721 10.1021/pr800528b
    • Marabotti A, Scire A, Staiano M, Crescenzo R, Aurilla V, Tanfani F, D'Auria S (2008b) Wild-type and mutant bovine odorant-binding proteins to probe the role of the quaternary structure organization in the protein thermal stability. J Proteome Res 7:5221-5229
    • (2008) J Proteome Res , vol.7 , pp. 5221-5229
    • Marabotti, A.1    Scire, A.2    Staiano, M.3    Crescenzo, R.4    Aurilla, V.5    Tanfani, F.6    D'Auria, S.7
  • 44
    • 0032521669 scopus 로고    scopus 로고
    • Lipocalins of boar salivary glands binding odours and pheromones
    • 1:CAS:528:DyaK1cXitVWntLg%3D 9546674 10.1046/j.1432-1327.1998.2520563.x
    • Marchese S, Pes D, Scaloni A, Carbone V, Pelosi P (1998) Lipocalins of boar salivary glands binding odours and pheromones. Eur J Biochem 252:563-568
    • (1998) Eur J Biochem , vol.252 , pp. 563-568
    • Marchese, S.1    Pes, D.2    Scaloni, A.3    Carbone, V.4    Pelosi, P.5
  • 45
    • 33748971553 scopus 로고    scopus 로고
    • Synthesis of an immobilized Bombyx mori pheromone-binding protein liquid chromatography stationary phase
    • 1:CAS:528:DC%2BD28XhtVWqt73J 18970835 10.1016/j.talanta.2006.01.046
    • Margaryan A, Moaddel R, Aldrich JR, Tsuruda JM, Chen AM, Leal WS, Wainer IW (2006) Synthesis of an immobilized Bombyx mori pheromone-binding protein liquid chromatography stationary phase. Talanta 70:752-755
    • (2006) Talanta , vol.70 , pp. 752-755
    • Margaryan, A.1    Moaddel, R.2    Aldrich, J.R.3    Tsuruda, J.M.4    Chen, A.M.5    Leal, W.S.6    Wainer, I.W.7
  • 46
    • 34249011110 scopus 로고    scopus 로고
    • Odorant-binding proteins OBP57d and OBP57e affect taste perception and host-plant preference in Drosophila sechellia
    • 1854911 17456006 10.1371/journal.pbio.0050118
    • Matsuo T, Sugaya S, Yasukawa J, Aigaki T, Fuyama Y (2007) Odorant-binding proteins OBP57d and OBP57e affect taste perception and host-plant preference in Drosophila sechellia. PLoS Biol 5:e118
    • (2007) PLoS Biol , vol.5 , pp. 118
    • Matsuo, T.1    Sugaya, S.2    Yasukawa, J.3    Aigaki, T.4    Fuyama, Y.5
  • 47
    • 4944249385 scopus 로고    scopus 로고
    • Odorant binding and conformational changes of a rat odorant-binding protein
    • 1:CAS:528:DC%2BD2cXisF2ltLk%3D 15047593 10.1093/chemse/bjh017
    • Nespoulous C, Briand L, Delage MM, Tran V, Pernollet JC (2004) Odorant binding and conformational changes of a rat odorant-binding protein. Chem Senses 29:189-198
    • (2004) Chem Senses , vol.29 , pp. 189-198
    • Nespoulous, C.1    Briand, L.2    Delage, M.M.3    Tran, V.4    Pernollet, J.C.5
  • 48
    • 0031701117 scopus 로고    scopus 로고
    • Amino acid sequence, post-translational modifications, binding and labelling of porcine odorant-binding protein
    • 1:CAS:528:DyaK1MXmvVKqsA%3D%3D 9915115 10.1093/chemse/23.6.689
    • Paolini S, Scaloni A, Amoresano A, Marchese S, Napolitano E, Pelosi P (1998) Amino acid sequence, post-translational modifications, binding and labelling of porcine odorant-binding protein. Chem Senses 23:689-698
    • (1998) Chem Senses , vol.23 , pp. 689-698
    • Paolini, S.1    Scaloni, A.2    Amoresano, A.3    Marchese, S.4    Napolitano, E.5    Pelosi, P.6
  • 49
    • 0032932846 scopus 로고    scopus 로고
    • Porcine odorant-binding protein: Structural stability and ligand affinities measured by fourier-transform infrared spectroscopy and fluorescence spectroscopy
    • 1:CAS:528:DyaK1MXivFeitLY%3D 10209290 10.1016/S0167-4838(99)00037-0
    • Paolini S, Tanfani F, Fini C, Bertoli E, Pelosi P (1999) Porcine odorant-binding protein: structural stability and ligand affinities measured by fourier-transform infrared spectroscopy and fluorescence spectroscopy. Biochim Biophys Acta 1431:179-188
    • (1999) Biochim Biophys Acta , vol.1431 , pp. 179-188
    • Paolini, S.1    Tanfani, F.2    Fini, C.3    Bertoli, E.4    Pelosi, P.5
  • 50
    • 0028276387 scopus 로고
    • Odorant-binding proteins
    • 1:CAS:528:DyaK2MXjsVGhtA%3D%3D 8070277 10.3109/10409239409086801
    • Pelosi P (1994) Odorant-binding proteins. Crit Rev Biochem Mol Biol 29:199-228
    • (1994) Crit Rev Biochem Mol Biol , vol.29 , pp. 199-228
    • Pelosi, P.1
  • 51
    • 0029921089 scopus 로고    scopus 로고
    • Perireceptor events in olfaction
    • 1:CAS:528:DyaK28XislKju7g%3D 8727979 10.1002/(SICI)1097-4695(199605)30: 1<3: AID-NEU2>3.0.CO;2-A
    • Pelosi P (1996) Perireceptor events in olfaction. J Neurobiol 30:3-19
    • (1996) J Neurobiol , vol.30 , pp. 3-19
    • Pelosi, P.1
  • 52
    • 0032451671 scopus 로고    scopus 로고
    • Odorant-binding proteins: Structural aspects
    • 1:CAS:528:DyaK1MXmvFSqtg%3D%3D 9929622 10.1111/j.1749-6632.1998.tb10584.x
    • Pelosi P (1998) Odorant-binding proteins: structural aspects. Ann N Y Acad Sci 855:281-293
    • (1998) Ann N y Acad Sci , vol.855 , pp. 281-293
    • Pelosi, P.1
  • 53
    • 0035033499 scopus 로고    scopus 로고
    • The role of perireceptor events in vertebrate olfaction
    • 1:CAS:528:DC%2BD3MXktVWnsrY%3D 11361085 10.1007/PL00000875
    • Pelosi P (2001) The role of perireceptor events in vertebrate olfaction. Cell Mol Life Sci 58:503-509
    • (2001) Cell Mol Life Sci , vol.58 , pp. 503-509
    • Pelosi, P.1
  • 54
    • 0025299104 scopus 로고
    • Odorant binding proteins in vertebrates and insects: Similarities and possible common function
    • 1:CAS:528:DyaK3cXltFSqtLY%3D 10.1093/chemse/15.2.205
    • Pelosi P, Maida R (1990) Odorant binding proteins in vertebrates and insects: similarities and possible common function. Chem Senses 15:205-215
    • (1990) Chem Senses , vol.15 , pp. 205-215
    • Pelosi, P.1    Maida, R.2
  • 55
    • 0029030309 scopus 로고
    • Odorant-binding proteins in insects
    • 1:CAS:528:DyaK2MXms1emuro%3D 10.1016/0305-0491(95)00019-5
    • Pelosi P, Maida R (1995) Odorant-binding proteins in insects. Comp Biochem Physiol 111B:503-514
    • (1995) Comp Biochem Physiol , vol.111 , pp. 503-514
    • Pelosi, P.1    Maida, R.2
  • 56
    • 0019818272 scopus 로고
    • Binding of [3H]-2-isobutyl-3-methoxypyrazine to cow olfactory mucosa
    • 1:CAS:528:DyaL3MXlvVCrtbg%3D 10.1093/chemse/6.2.77
    • Pelosi P, Pisanelli AM, Baldaccini NE, Gagliardo A (1981) Binding of [3H]-2-isobutyl-3-methoxypyrazine to cow olfactory mucosa. Chem Senses 6:77-85
    • (1981) Chem Senses , vol.6 , pp. 77-85
    • Pelosi, P.1    Pisanelli, A.M.2    Baldaccini, N.E.3    Gagliardo, A.4
  • 57
    • 0019949965 scopus 로고
    • Identification of a specific olfactory receptor for 2-isobutyl-3- methoxypyrazine
    • 1:CAS:528:DyaL38Xhslylu7c%3D 7082286
    • Pelosi P, Baldaccini NE, Pisanelli AM (1982) Identification of a specific olfactory receptor for 2-isobutyl-3-methoxypyrazine. Biochem J 201:245-248
    • (1982) Biochem J , vol.201 , pp. 245-248
    • Pelosi, P.1    Baldaccini, N.E.2    Pisanelli, A.M.3
  • 58
    • 33747382424 scopus 로고    scopus 로고
    • Soluble proteins in insect chemical communication
    • 1:CAS:528:DC%2BD28Xos1Kku74%3D 16786224 10.1007/s00018-005-5607-0
    • Pelosi P, Zhou J-J, Ban LP, Calvello M (2006) Soluble proteins in insect chemical communication. Cell Mol Life Sci 63:1658-1676
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1658-1676
    • Pelosi, P.1    Zhou, J.-J.2    Ban, L.P.3    Calvello, M.4
  • 59
    • 84867699605 scopus 로고    scopus 로고
    • Odorant binding proteins and mouse urinary proteins: Potential biomimetic sensing systems
    • Persaud KC, Ng SM, Mucignat C, Pelosi P (2009) Odorant binding proteins and mouse urinary proteins: potential biomimetic sensing systems. Chem Senses 34:E36-E37
    • (2009) Chem Senses , vol.34
    • Persaud, K.C.1    Ng, S.M.2    Mucignat, C.3    Pelosi, P.4
  • 60
    • 0025259871 scopus 로고
    • Odorant-binding protein. Characterization of ligand binding
    • 1:CAS:528:DyaK3cXksFCmt7g%3D 2318850
    • Pevsner J, Hou V, Snowman AM, Snyder SH (1990) Odorant-binding protein. Characterization of ligand binding. J Biol Chem 265:6118-6125
    • (1990) J Biol Chem , vol.265 , pp. 6118-6125
    • Pevsner, J.1    Hou, V.2    Snowman, A.M.3    Snyder, S.H.4
  • 61
    • 0034254740 scopus 로고    scopus 로고
    • Discrimination of pheromone enantiomers by two pheromone binding proteins from the gypsy moth Lymantria dispar
    • 1:CAS:528:DC%2BD3cXksFOru7k%3D 10913308 10.1021/bi000461x
    • Plettner E, Lazar J, Prestwich EG, Prestwich GD (2000) Discrimination of pheromone enantiomers by two pheromone binding proteins from the gypsy moth Lymantria dispar. Biochemistry 39:8953-8962
    • (2000) Biochemistry , vol.39 , pp. 8953-8962
    • Plettner, E.1    Lazar, J.2    Prestwich, E.G.3    Prestwich, G.D.4
  • 62
    • 0036866336 scopus 로고    scopus 로고
    • Encapsulation of flavors using cyclodextrins: Comparisonof flavor retention in alpha, beta, and gamma types
    • 1:CAS:528:DC%2BD3sXjs1Gg 10.1111/j.1365-2621.2002.tb09577.x
    • Reineccius TA, Reineccius GA, Peppard TL (2002) Encapsulation of flavors using cyclodextrins: comparisonof flavor retention in alpha, beta, and gamma types. J Food Sci 67:3271-3279
    • (2002) J Food Sci , vol.67 , pp. 3271-3279
    • Reineccius, T.A.1    Reineccius, G.A.2    Peppard, T.L.3
  • 63
    • 0038640587 scopus 로고    scopus 로고
    • A pheromone-binding protein from the cockroach Leucophaea maderae: Cloning, expression and pheromone binding
    • 1:CAS:528:DC%2BD3sXisleqsL4%3D 12529170 10.1042/BJ20021877
    • Riviere S, Lartigue A, Quennedey B, Campanacci V, Farine JP, Tegoni M, Cambillau C, Brossut R (2003) A pheromone-binding protein from the cockroach Leucophaea maderae: cloning, expression and pheromone binding. Biochem J 371:573-579
    • (2003) Biochem J , vol.371 , pp. 573-579
    • Riviere, S.1    Lartigue, A.2    Quennedey, B.3    Campanacci, V.4    Farine, J.P.5    Tegoni, M.6    Cambillau, C.7    Brossut, R.8
  • 64
    • 80052935359 scopus 로고    scopus 로고
    • Lipocalin based biosensors for low mass hydrophobic analytes; Development of a novel SAM for polyhistidine tagged proteins
    • 1:CAS:528:DC%2BC3cXhtFChsLfN 10.1016/j.snb.2010.07.053
    • Rodgers M, Findlay J, Millner P (2010) Lipocalin based biosensors for low mass hydrophobic analytes; development of a novel SAM for polyhistidine tagged proteins. Sensors Actuators B Chem 150:12-18
    • (2010) Sensors Actuators B Chem , vol.150 , pp. 12-18
    • Rodgers, M.1    Findlay, J.2    Millner, P.3
  • 65
    • 0034141728 scopus 로고    scopus 로고
    • Sexual attraction in the silkworm moth: Structure of the pheromone-binding-protein-bombykol complex
    • 1:CAS:528:DC%2BD3cXht1ynurw%3D 10662696 10.1016/S1074-5521(00)00078-8
    • Sandler BH, Nikonova L, Leal WS, Clardy J (2000) Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex. Chem Biol 7:143-151
    • (2000) Chem Biol , vol.7 , pp. 143-151
    • Sandler, B.H.1    Nikonova, L.2    Leal, W.S.3    Clardy, J.4
  • 66
    • 79951724092 scopus 로고    scopus 로고
    • Odorant binding protein based biomimetic sensors for detection of alcohols associated with Salmonella contamination in packaged beef
    • 1:CAS:528:DC%2BC3MXit1ynsrw%3D 21227678 10.1016/j.bios.2010.07.122
    • Sankaran S, Panigrahi S, Mallik S (2011) Odorant binding protein based biomimetic sensors for detection of alcohols associated with Salmonella contamination in packaged beef. Biosens Bioelectron 26:3103-3109
    • (2011) Biosens Bioelectron , vol.26 , pp. 3103-3109
    • Sankaran, S.1    Panigrahi, S.2    Mallik, S.3
  • 67
    • 0033590202 scopus 로고    scopus 로고
    • Structural analyses and disulfide-bridge pairing of two odorant-binding proteins from Bombyx mori
    • 1:CAS:528:DyaK1MXnvFeku7g%3D 10600513 10.1006/bbrc.1999.1791
    • Scaloni A, Monti M, Angeli S, Pelosi P (1999) Structural analyses and disulfide-bridge pairing of two odorant-binding proteins from Bombyx mori. Biochem Biophys Res Commun 266:386-391
    • (1999) Biochem Biophys Res Commun , vol.266 , pp. 386-391
    • Scaloni, A.1    Monti, M.2    Angeli, S.3    Pelosi, P.4
  • 70
    • 0032474475 scopus 로고    scopus 로고
    • The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism
    • 1:CAS:528:DyaK1cXivFCisrc%3D 9609684 10.1021/bi980179e
    • Spinelli S, Ramoni R, Grolli S, Bonicel J, Cambillau C, Tegoni M (1998) The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism. Biochemistry 37:7913-7918
    • (1998) Biochemistry , vol.37 , pp. 7913-7918
    • Spinelli, S.1    Ramoni, R.2    Grolli, S.3    Bonicel, J.4    Cambillau, C.5    Tegoni, M.6
  • 71
    • 0036113683 scopus 로고    scopus 로고
    • Boar salivary lipocalin. Three-dimensional X-ray structure and androsterol/androstenone docking simulations
    • 1:CAS:528:DC%2BD38XksVWrsr4%3D 12027882 10.1046/j.1432-1033.2002.02901.x
    • Spinelli S, Vincent F, Pelosi P, Tegoni M, Cambillau C (2002) Boar salivary lipocalin. Three-dimensional X-ray structure and androsterol/ androstenone docking simulations. Eur J Biochem 269:2449-2456
    • (2002) Eur J Biochem , vol.269 , pp. 2449-2456
    • Spinelli, S.1    Vincent, F.2    Pelosi, P.3    Tegoni, M.4    Cambillau, C.5
  • 72
    • 0032466927 scopus 로고    scopus 로고
    • Odorant-binding proteins: Expression and function
    • 1:CAS:528:DyaK1MXmvFWjsw%3D%3D 10049226 10.1111/j.1749-6632.1998.tb10591. x
    • Steinbrecht RA (1998) Odorant-binding proteins: expression and function. Ann N Y Acad Sci 855:323-332
    • (1998) Ann N y Acad Sci , vol.855 , pp. 323-332
    • Steinbrecht, R.A.1
  • 73
    • 84856090037 scopus 로고    scopus 로고
    • Expression in antennae and reproductive organs suggests a dual role of an odorant-binding protein in two sibling Helicoverpa species
    • 1:CAS:528:DC%2BC38Xit1ChsLY%3D 3264552 22291900 10.1371/journal.pone. 0030040
    • Sun YL, Huang LQ, Pelosi P, Wang CZ (2012a) Expression in antennae and reproductive organs suggests a dual role of an odorant-binding protein in two sibling Helicoverpa species. PLoS One 7:e30040
    • (2012) PLoS One , vol.7 , pp. 30040
    • Sun, Y.L.1    Huang, L.Q.2    Pelosi, P.3    Wang, C.Z.4
  • 74
    • 84863297389 scopus 로고    scopus 로고
    • Two odorant-binding proteins mediate the behavioural response of aphids to the alarm pheromone (E)-β-farnesene and structural analogues
    • 1:CAS:528:DC%2BC38XksFGlurw%3D 3299684 22427877 10.1371/journal.pone. 0032759
    • Sun YF, De Biasio F, Qiao HL, Iovinella I, Yang SX, Ling Y, Riviello L, Battaglia D, Falabella P, Yang XL, Pelosi P (2012b) Two odorant-binding proteins mediate the behavioural response of aphids to the alarm pheromone (E)-β-farnesene and structural analogues. PLoS One 7:e32759
    • (2012) PLoS One , vol.7 , pp. 32759
    • Sun, Y.F.1    De Biasio, F.2    Qiao, H.L.3    Iovinella, I.4    Yang, S.X.5    Ling, Y.6    Riviello, L.7    Battaglia, D.8    Falabella, P.9    Yang, X.L.10    Pelosi, P.11
  • 75
    • 79961026622 scopus 로고    scopus 로고
    • Functional dissection of odorant binding protein genes in Drosophila melanogaster
    • 1:STN:280:DC%2BC3MjjsVOhsw%3D%3D 3150612 21605338 10.1111/j.1601-183X. 2011.00704.x
    • Swarup S, Williams TI, Anholt RR (2011) Functional dissection of odorant binding protein genes in Drosophila melanogaster. Genes Brain Behav 10:648-657
    • (2011) Genes Brain Behav , vol.10 , pp. 648-657
    • Swarup, S.1    Williams, T.I.2    Anholt, R.R.3
  • 76
    • 33645221480 scopus 로고    scopus 로고
    • A single lysyl residue defines the binding specificity of a human odorant-binding protein for aldehydes
    • 1:CAS:528:DC%2BD28XivV2qt74%3D 16546182 10.1016/j.febslet.2006.03.017
    • Tcatchoff L, Nespoulous C, Pernollet JC, Briand L (2006) A single lysyl residue defines the binding specificity of a human odorant-binding protein for aldehydes. FEBS Lett 580(8):2102-2108
    • (2006) FEBS Lett , vol.580 , Issue.8 , pp. 2102-2108
    • Tcatchoff, L.1    Nespoulous, C.2    Pernollet, J.C.3    Briand, L.4
  • 77
    • 0029760325 scopus 로고    scopus 로고
    • Domain swapping creates a third putative combining site in bovine odorant binding protein dimer
    • 1:CAS:528:DyaK28XmtFCrsLc%3D 8836103 10.1038/nsb1096-863
    • 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
  • 79
    • 2342617588 scopus 로고    scopus 로고
    • Structural aspects of sexual attraction and chemical communication in insects
    • 1:CAS:528:DC%2BD2cXjvVemur8%3D 15130562 10.1016/j.tibs.2004.03.003
    • Tegoni M, Campanacci V, Cambillau C (2004) Structural aspects of sexual attraction and chemical communication in insects. Trends Biochem Sci 29:257-264
    • (2004) Trends Biochem Sci , vol.29 , pp. 257-264
    • Tegoni, M.1    Campanacci, V.2    Cambillau, C.3
  • 80
    • 0021984229 scopus 로고
    • Specificity of a pyrazine binding protein from cow olfactory mucosa
    • 1:CAS:528:DyaL2MXkt1SnsbY%3D 10.1093/chemse/10.1.45
    • Topazzini A, Pelosi P, Pasqualetto PL, Baldaccini NE (1985) Specificity of a pyrazine binding protein from cow olfactory mucosa. Chem Senses 10:45-49
    • (1985) Chem Senses , vol.10 , pp. 45-49
    • Topazzini, A.1    Pelosi, P.2    Pasqualetto, P.L.3    Baldaccini, N.E.4
  • 81
    • 0034733389 scopus 로고    scopus 로고
    • Complexes of porcine odorant binding protein with odorant molecules belonging to different chemical classes
    • 1:CAS:528:DC%2BD3cXktFehurk%3D 10864504 10.1006/jmbi.2000.3820
    • Vincent F, Spinelli S, Ramoni R, Grolli S, Pelosi P, Cambillau C, Tegoni M (2000) Complexes of porcine odorant binding protein with odorant molecules belonging to different chemical classes. J Mol Biol 300:127-139
    • (2000) J Mol Biol , vol.300 , pp. 127-139
    • Vincent, F.1    Spinelli, S.2    Ramoni, R.3    Grolli, S.4    Pelosi, P.5    Cambillau, C.6    Tegoni, M.7
  • 83
    • 84858339838 scopus 로고    scopus 로고
    • Mammalian lipocalin allergens-insights into their enigmatic allergenicity
    • 1:CAS:528:DC%2BC38XmvVent7k%3D 22093088 10.1111/j.1365-2222.2011.03903.x
    • Virtanen T, Kinnunen T, Rytkönen-Nissinen M (2012) Mammalian lipocalin allergens-insights into their enigmatic allergenicity. Clin Exp Allergy 42:494-504
    • (2012) Clin Exp Allergy , vol.42 , pp. 494-504
    • Virtanen, T.1    Kinnunen, T.2    Rytkönen-Nissinen, M.3
  • 84
    • 84902643488 scopus 로고    scopus 로고
    • Biochemical diversity of odor detection: OBPs, ODEs and SNMPs
    • G.J. Blomquist R.G. Vogt (eds) Elsevier Academic London 10.1016/B978-012107151-6/50016-5
    • Vogt RG (2003) Biochemical diversity of odor detection: OBPs, ODEs and SNMPs. In: Blomquist GJ, Vogt RG (eds) Insect pheromone biochemistry and molecular biology. Elsevier Academic, London, pp 391-446
    • (2003) Insect Pheromone Biochemistry and Molecular Biology , pp. 391-446
    • Vogt, R.G.1
  • 85
    • 85069931256 scopus 로고    scopus 로고
    • Molecular basis of pheromone detection in insects
    • L.I. Gilbert K. Iatrou S. Gill (eds) Endocrinology 3 Elsevier London
    • Vogt RG (2005) Molecular basis of pheromone detection in insects. In: Gilbert LI, Iatrou K, Gill S (eds) Comprehensive insect physiology, biochemistry, pharmacology and molecular biology, vol 3, Endocrinology. Elsevier, London, pp 753-804
    • (2005) Comprehensive Insect Physiology, Biochemistry, Pharmacology and Molecular Biology , pp. 753-804
    • Vogt, R.G.1
  • 86
    • 0019489601 scopus 로고
    • Pheromone binding and inactivation by moth antennae
    • 1:CAS:528:DyaL38XjtF2jsA%3D%3D 18074618 10.1038/293161a0
    • Vogt RG, Riddiford LM (1981) Pheromone binding and inactivation by moth antennae. Nature 293:161-163
    • (1981) Nature , vol.293 , pp. 161-163
    • Vogt, R.G.1    Riddiford, L.M.2
  • 88
    • 40849135476 scopus 로고    scopus 로고
    • Binding of polyclycic aromatic hydrocarbons to mutants of odorant-binding protein: A first step towards biosensors for environmental monitoring
    • 1:CAS:528:DC%2BD1cXjtlChurY%3D 18284927 10.1016/j.bbapap.2008.01.012
    • Wei Y, Brandazza A, Pelosi P (2008) Binding of polyclycic aromatic hydrocarbons to mutants of odorant-binding protein: a first step towards biosensors for environmental monitoring. Biochim Biophys Acta 1784:666-671
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 666-671
    • Wei, Y.1    Brandazza, A.2    Pelosi, P.3
  • 89
    • 67649289011 scopus 로고    scopus 로고
    • Linking biological and artificial olfaction: Biomimetic quartz crystal microbalance odor sensors
    • 1:CAS:528:DC%2BD1MXmsFKjs7s%3D 10.1002/tee.20414
    • Wyszynski B, Nakamoto T (2009) Linking biological and artificial olfaction: biomimetic quartz crystal microbalance odor sensors. IEEJ Trans Electr Electron Eng 4:334-338
    • (2009) IEEJ Trans Electr Electron Eng , vol.4 , pp. 334-338
    • Wyszynski, B.1    Nakamoto, T.2
  • 90
    • 12344262334 scopus 로고    scopus 로고
    • Drosophila OBP LUSH is required for activity of pheromone-sensitive neurons
    • 1:CAS:528:DC%2BD2MXhtFOrt7w%3D 15664171 10.1016/j.neuron.2004.12.031
    • Xu P, Atkinson R, Jones DN, Smith DP (2005) Drosophila OBP LUSH is required for activity of pheromone-sensitive neurons. Neuron 45:193-200
    • (2005) Neuron , vol.45 , pp. 193-200
    • Xu, P.1    Atkinson, R.2    Jones, D.N.3    Smith, D.P.4
  • 91
    • 80051707868 scopus 로고    scopus 로고
    • Dynamics of odorant binding to thin aqueous films of rat-OBP3
    • 1:CAS:528:DC%2BC3MXhtVeitbbN 21536621 10.1093/chemse/bjr037
    • Yabuki M, Scott DJ, Briand L, Taylor AJ (2011) Dynamics of odorant binding to thin aqueous films of rat-OBP3. Chem Senses 36:659-671
    • (2011) Chem Senses , vol.36 , pp. 659-671
    • Yabuki, M.1    Scott, D.J.2    Briand, L.3    Taylor, A.J.4
  • 92
    • 70349782324 scopus 로고    scopus 로고
    • Polypyrrole nanotubes conjugated with human olfactory receptors: High-performance transducers for FET-type bioelectronic noses
    • 1:CAS:528:DC%2BD1MXks1Crsrc%3D 10.1002/anie.200805171
    • Yoon H, Lee SH, Kwon OS, Song HS, Oh EH, Park TH, Jang J (2009) Polypyrrole nanotubes conjugated with human olfactory receptors: high-performance transducers for FET-type bioelectronic noses. Angew Chem Int Ed 48:2755-2758
    • (2009) Angew Chem Int Ed , vol.48 , pp. 2755-2758
    • Yoon, H.1    Lee, S.H.2    Kwon, O.S.3    Song, H.S.4    Oh, E.H.5    Park, T.H.6    Jang, J.7
  • 93
    • 0842281552 scopus 로고    scopus 로고
    • Revisiting the odorant-binding protein LUSH of Drosophila melanogaster: Evidence for odour recognition and discrimination
    • 1:CAS:528:DC%2BD2cXpsV2htQ%3D%3D 14759510 10.1016/S0014-5793(03)01521-7
    • Zhou J-J, Zhang G-A, Huang W, Birkett MA, Field LM, Pickett JA, Pelosi P (2004) Revisiting the odorant-binding protein LUSH of Drosophila melanogaster: evidence for odour recognition and discrimination. FEBS Lett 558:23-26
    • (2004) FEBS Lett , vol.558 , pp. 23-26
    • Zhou, J.-J.1    Zhang, G.-A.2    Huang, W.3    Birkett, M.A.4    Field, L.M.5    Pickett, J.A.6    Pelosi, P.7
  • 94
    • 84876549103 scopus 로고    scopus 로고
    • Diversity, abundance and sex-specific expression of chemosensory proteins in the reproductive organs of the locust Locusta migratoria manilensis
    • 1:CAS:528:DC%2BC3sXhsVekt74%3D 23096575 10.1515/hsz-2012-0114
    • Zhou XH, Ban LP, Iovinella I, Zhao LJ, Gao Q, Felicioli A, Sagona S, Pieraccini G, Pelosi P, Zhang L, Dani FR (2013) Diversity, abundance and sex-specific expression of chemosensory proteins in the reproductive organs of the locust Locusta migratoria manilensis. Biol Chem 394:43-54
    • (2013) Biol Chem , vol.394 , pp. 43-54
    • Zhou, X.H.1    Ban, L.P.2    Iovinella, I.3    Zhao, L.J.4    Gao, Q.5    Felicioli, A.6    Sagona, S.7    Pieraccini, G.8    Pelosi, P.9    Zhang, L.10    Dani, F.R.11


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