Publications
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“A genome-wide analysis of the ERF gene family in sorghum”, vol. 12, pp. 2038-2055, 2013.
, “Genome-wide identification, classification, and analysis of two-component signal system genes in maize”, vol. 10, pp. 3316-3330, 2011.
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Aoyama T and Oka A (2003). Cytokinin signal transduction in plant cells. J. Plant Res. 116: 221-231.
http://dx.doi.org/10.1007/s10265-003-0094-6
PMid:12836044
Asakura Y, Hagino T, Ohta Y, Aoki K, et al. (2003). Molecular characterization of His-Asp phosphorelay signaling factors in maize leaves: implications of the signal divergence by cytokinin-inducible response regulators in the cytosol and the nuclei. Plant Mol. Biol. 52: 331-341.
http://dx.doi.org/10.1023/A:1023971315108
PMid:12856940
Bailey TL, Williams N, Misleh C and Li WW (2006). MEME: discovering and analyzing DNA and protein sequence motifs. Nucleic Acids Res. 34: W369-W373.
http://dx.doi.org/10.1093/nar/gkl198
PMid:16845028 PMCid:1538909
Brandstatter I and Kieber JJ (1998). Two genes with similarity to bacterial response regulators are rapidly and specifically induced by cytokinin in Arabidopsis. Plant Cell 10: 1009-1019.
PMid:9634588 PMCid:144033
D'Agostino IB and Kieber JJ (1999). Phosphorelay signal transduction: the emerging family of plant response regulators. Trends Biochem. Sci. 24: 452-456.
http://dx.doi.org/10.1016/S0968-0004(99)01465-6
D'Agostino IB, Deruere J and Kieber JJ (2000). Characterization of the response of the Arabidopsis response regulator gene family to cytokinin. Plant Physiol. 124: 1706-1717.
http://dx.doi.org/10.1104/pp.124.4.1706
PMid:11115887 PMCid:59868
Du L, Jiao F, Chu J, Jin G, et al. (2007). The two-component signal system in rice (Oryza sativa L.): a genome-wide study of cytokinin signal perception and transduction. Genomics 89: 697-707.
http://dx.doi.org/10.1016/j.ygeno.2007.02.001
PMid:17408920
Forde BG (2002). Local and long-range signaling pathways regulating plant responses to nitrate. Annu. Rev. Plant Biol. 53: 203-224.
http://dx.doi.org/10.1146/annurev.arplant.53.100301.135256
PMid:12221973
Grefen C and Harter K (2004). Plant two-component systems: principles, functions, complexity and cross talk. Planta 219: 733-742.
http://dx.doi.org/10.1007/s00425-004-1316-4
PMid:15232695
Gu Z, Cavalcanti A, Chen FC, Bouman P, et al. (2002). Extent of gene duplication in the genomes of Drosophila, nematode, and yeast. Mol. Biol. Evol. 19: 256-262.
http://dx.doi.org/10.1093/oxfordjournals.molbev.a004079
PMid:11861885
Hass C, Lohrmann J, Albrecht V, Sweere U, et al. (2004). The response regulator 2 mediates ethylene signalling and hormone signal integration in Arabidopsis. EMBO J. 23: 3290-3302.
http://dx.doi.org/10.1038/sj.emboj.7600337
PMid:15282545 PMCid:514511
Hutchison CE and Kieber JJ (2002). Cytokinin signaling in Arabidopsis. Plant Cell 14: S47-S59.
PMid:12045269 PMCid:151247
Hwang I and Sheen J (2001). Two-component circuitry in Arabidopsis cytokinin signal transduction. Nature 413: 383-389.
http://dx.doi.org/10.1038/35096500
PMid:11574878
Hwang I, Chen HC and Sheen J (2002). Two-component signal transduction pathways in Arabidopsis. Plant Physiol. 129: 500-515.
http://dx.doi.org/10.1104/pp.005504
PMid:12068096 PMCid:161668
Ildoo H, Huei-Chi C and Jen S (2002). Two-component signal transduction pathways in Arabidopsis. Plant Physiol. 129: 500-515.
http://dx.doi.org/10.1104/pp.005504
PMid:12068096 PMCid:161668
Inoue T, Higuchi M, Hashimoto Y, Seki M, et al. (2001). Identification of CRE1 as a cytokinin receptor from Arabidopsis. Nature 409: 1060-1063.
http://dx.doi.org/10.1038/35059117
PMid:11234017
Lohrmann J, Buchholz G, Keitel C, Sweere U, et al. (1999). Differential expression and nuclear localization of response regulator-like proteins from Arabidopsis thaliana. Plant Biol. 1: 495-505.
http://dx.doi.org/10.1111/j.1438-8677.1999.tb00775.x
Lohrmann J, Sweere U, Zabaleta E, Baurle I, et al. (2001). The response regulator ARR2: a pollen-specific transcription factor involved in the expression of nuclear genes for components of mitochondrial complex I in Arabidopsis. Mol. Genet. Genomics 265: 2-13.
http://dx.doi.org/10.1007/s004380000400
PMid:11370868
Mahonen AP, Bonke M, Kauppinen L, Riikonen M, et al. (2000). A novel two-component hybrid molecule regulates vascular morphogenesis of the Arabidopsis root. Genes Dev. 14: 2938-2943.
http://dx.doi.org/10.1101/gad.189200
PMid:11114883 PMCid:317089
Martín AC, del Pozo JC, Iglesias J, Rubio V, et al. (2000). Influence of cytokinins on the expression of phosphate starvation responsive genes in Arabidopsis. Plant J. 24: 559-567.
http://dx.doi.org/10.1046/j.1365-313x.2000.00893.x
PMid:11123795
Mason MG, Mathews DE, Argyros DA, Maxwell BB, et al. (2005). Multiple type-B response regulators mediate cytokinin signal transduction in Arabidopsis. Plant Cell 17: 3007-3018.
http://dx.doi.org/10.1105/tpc.105.035451
PMid:16227453 PMCid:1276026
Mok DW and Mok MC (2001). Cytokinin metabolism and action. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52: 89-118.
http://dx.doi.org/10.1146/annurev.arplant.52.1.89
PMid:11337393
Pischke MS, Jones LG, Otsuga D, Fernandez DE, et al. (2002). An Arabidopsis histidine kinase is essential for megagametogenesis. Proc. Natl. Acad. Sci. U. S. A. 99: 15800-15805.
http://dx.doi.org/10.1073/pnas.232580499
PMid:12426401 PMCid:137796
Riechmann JL, Heard J, Martin G, Reuber L, et al. (2000). Arabidopsis transcription factors: genome-wide comparative analysis among eukaryotes. Science 290: 2105-2110.
http://dx.doi.org/10.1126/science.290.5499.2105
PMid:11118137
Riefler M, Novak O, Strnad M and Schmulling T (2006). Arabidopsis cytokinin receptor mutants reveal functions in shoot growth, leaf senescence, seed size, germination, root development, and cytokinin metabolism. Plant Cell 18: 40-54.
http://dx.doi.org/10.1105/tpc.105.037796
PMid:16361392 PMCid:1323483
Romanov GA, Kieber JJ and Schmulling T (2002). A rapid cytokinin response assay in Arabidopsis indicates a role for phospholipase D in cytokinin signalling. FEBS Lett. 515: 39-43.
http://dx.doi.org/10.1016/S0014-5793(02)02415-8
Sakai H, Aoyama T and Oka A (2000). Arabidopsis ARR1 and ARR2 response regulators operate as transcriptional activators. Plant J. 24: 703-711.
http://dx.doi.org/10.1046/j.1365-313x.2000.00909.x
PMid:11135105
Schaller GE, Mathews DE, Gribskov M and Walker JC (2002). Two-Component Signalling Elements and Histidyl-Aspartyl Phosphorelays. In: The Arabidopsis book American Society of Plant Biologists (Somerville C and Meyerowitz E, eds.). DOI/10.1199/tab.0086, Available at [http:/www.aspb.org/publications/Arabidopsis]. Accessed...... Schnable PS, Ware D, Fulton RS, Stein JC, et al. (2009). The B73 maize genome: complexity, diversity, and dynamics. Science 326: 1112-1115.
Stock AM, Robinson VL and Goudreau PN (2000). Two-component signal transduction. Annu. Rev. Biochem. 69: 183-215.
http://dx.doi.org/10.1146/annurev.biochem.69.1.183
PMid:10966457
Suzuki T, Miwa K, Ishikawa K, Yamada H, et al. (2001). The Arabidopsis sensor His-kinase, AHk4, can respond to cytokinins. Plant Cell Physiol. 42: 107-113.
http://dx.doi.org/10.1093/pcp/pce037
PMid:11230563
Thomason P and Kay R (2000). Eukaryotic signal transduction via histidine-aspartate phosphorelay. J. Cell Sci. 113: 3141-3150.
PMid:10954413
Thompson JD, Higgins DG and Gibson TJ (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
http://dx.doi.org/10.1093/nar/22.22.4673
PMid:7984417 PMCid:308517
To JP, Haberer G, Ferreira FJ, Deruere J, et al. (2004). Type-A Arabidopsis response regulators are partially redundant negative regulators of cytokinin signaling. Plant Cell 16: 658-671.
http://dx.doi.org/10.1105/tpc.018978
PMid:14973166 PMCid:385279
Ueguchi C, Koizumi H, Suzuki T and Mizuno T (2001). Novel family of sensor histidine kinase genes in Arabidopsis thaliana. Plant Cell Physiol. 42: 231-235.
http://dx.doi.org/10.1093/pcp/pce015
PMid:11230578
Urao T, Yakubov B, Yamaguchi-Shinozaki K and Shinozaki K (1998). Stress-responsive expression of genes for two-component response regulator-like proteins in Arabidopsis thaliana. FEBS Lett. 427: 175-178.
http://dx.doi.org/10.1016/S0014-5793(98)00418-9
West AH and Stock AM (2001). Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 26: 369-376.
http://dx.doi.org/10.1016/S0968-0004(01)01852-7
Yamada S and Shiro Y (2008). Structural basis of the signal transduction in the two-component system. Adv. Exp. Med. Biol. 631: 22-39.
http://dx.doi.org/10.1007/978-0-387-78885-2_3
PMid:18792680
Yang S, Zhang X, Yue JX, Tian D, et al. (2008). Recent duplications dominate NBS-encoding gene expansion in two woody species. Mol. Genet. Genomics 280: 187-198.
http://dx.doi.org/10.1007/s00438-008-0355-0
PMid:18563445
Yonekura-Sakakibara K, Kojima M, Yamaya T and Sakakibara H (2004). Molecular characterization of cytokinin-responsive histidine kinases in maize. Differential ligand preferences and response to cis-zeatin. Plant Physiol. 134: 1654-1661.
http://dx.doi.org/10.1104/pp.103.037176
PMid:15064375 PMCid:419839
“An overview of odorant-binding protein functions in insect peripheral olfactory reception”, vol. 10. pp. 3056-3069, 2011.
, Beale MH, Birkett MA, Bruce TJ, Chamberlain K, et al. (2006). Aphid alarm pheromone produced by transgenic plants affects aphid and parasitoid behavior. Proc. Natl. Acad. Sci. U. S. A. 103: 10509-10513.
http://dx.doi.org/10.1073/pnas.0603998103
PMid:16798877 PMCid:1502488
Benton R, Sachse S, Michnick SW and Vosshall LB (2006). Atypical membrane topology and heteromeric function of Drosophila odorant receptors in vivo. PLoS Biol. 4: e20.
http://dx.doi.org/10.1371/journal.pbio.0040020
PMid:16402857 PMCid:1334387
Benton R, Vannice KS and Vosshall LB (2007). An essential role for a CD36-related receptor in pheromone detection in Drosophila. Nature 450: 289-293.
http://dx.doi.org/10.1038/nature06328
PMid:17943085
Bette S, Breer H and Krieger J (2002). Probing a pheromone binding protein of the silkmoth Antheraea polyphemus by endogenous tryptophan fluorescence. Insect Biochem. Mol. Biol. 32: 241-246.
http://dx.doi.org/10.1016/S0965-1748(01)00171-0
Blomquist GJ and Vogt RG (2003). Insect Pheromone Biochemistry and Molecular Biology. In: The Biosynthesis and Detection of Pheromones and Plant Volatiles (Blomquist GJ and Vogt RG, eds.). Elsevier Academic Press, London, 3-18.
Buck L and Axel R (1991). A novel multigene family may encode odorant receptors: a molecular basis for odor recognition. Cell 65: 175-187.
http://dx.doi.org/10.1016/0092-8674(91)90418-X
Campanacci V, Krieger J, Bette S, Sturgis JN, et al. (2001). Revisiting the specificity of Mamestra brassicae and Antheraea polyphemus pheromone-binding proteins with a fluorescence binding assay. J. Biol. Chem. 276: 20078-20084.
http://dx.doi.org/10.1074/jbc.M100713200
PMid:11274212
Clyne PJ, Warr CG, Freeman MR, Lessing D, et al. (1999). A novel family of divergent seven-transmembrane proteins: candidate odorant receptors in Drosophila. Neuron 22: 327-338.
http://dx.doi.org/10.1016/S0896-6273(00)81093-4
Damberger F, Nikonova L, Horst R, Peng G, et al. (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.
http://dx.doi.org/10.1110/ps.9.5.1038
PMid:10850815 PMCid:2144629
Damberger FF, Ishida Y, Leal WS and Wuthrich K (2007). Structural basis of ligand binding and release in insect pheromone-binding proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5. J. Mol. Biol. 373: 811-819.
http://dx.doi.org/10.1016/j.jmb.2007.07.078
PMid:17884092
Foret S and Maleszka R (2006). Function and evolution of a gene family encoding odorant binding-like proteins in a social insect, the honey bee (Apis mellifera). Genome Res. 16: 1404-1413.
http://dx.doi.org/10.1101/gr.5075706
PMid:17065610 PMCid:1626642
Francis F, Vandermoten S, Verheggen F, Lognay G, et al. (2005a). Is the (E)-farnesene only volatile terpenoid in aphids? J. Appl. Entomol. 129: 6-11.
http://dx.doi.org/10.1111/j.1439-0418.2005.00925.x
Francis F, Martin T, Lognay G and Haubruge E (2005b). Role of (E)-beta-farnesene in systematic aphid prey location by Episyrphus balteatus larvae (Diptera: Syrphidae). Eur. J. Entomol. 102: 431-436.
Friedrich RW and Korsching SI (1997). Combinatorial and chemotopic odorant coding in the zebrafish olfactory bulb visualized by optical imaging. Neuron 18: 737-752.
http://dx.doi.org/10.1016/S0896-6273(00)80314-1
Gao Q, Yuan B and Chess A (2000). Convergent projections of Drosophila olfactory neurons to specific glomeruli in the antennal lobe. Nat. Neurosci. 3: 780-785.
http://dx.doi.org/10.1038/75753
PMid:10816314
Gong DP, Zhang HJ, Zhao P, Xia QY, et al. (2009). The odorant binding protein gene family from the genome of silkworm, Bombyx mori. BMC Genomics 10: 332.
http://dx.doi.org/10.1186/1471-2164-10-332
PMid:19624863 PMCid:2722677
Ha TS and Smith DP (2006). A pheromone receptor mediates 11-cis-vaccenyl acetate-induced responses in Drosophila. J. Neurosci. 26: 8727-8733.
http://dx.doi.org/10.1523/JNEUROSCI.0876-06.2006
PMid:16928861
Hallem EA, Nicole FA, Zwiebel LJ and Carlson JR (2004). Olfaction: mosquito receptor for human-sweat odorant. Nature 427: 212-213.
http://dx.doi.org/10.1038/427212a
PMid:14724626
Hekmat-Scafe DS, Scafe CR, McKinney AJ and Tanouye MA (2002). Genome-wide analysis of the odorant-binding protein gene family in Drosophila melanogaster. Genome Res. 12: 1357-1369.
http://dx.doi.org/10.1101/gr.239402
PMid:12213773 PMCid:186648
Hildebrand JG and Shepherd GM (1997). Mechanisms of olfactory discrimination: converging evidence for common principles across phyla. Annu. Rev. Neurosci. 20: 595-631.
http://dx.doi.org/10.1146/annurev.neuro.20.1.595
PMid:9056726
Honson N, Johnson MA, Oliver JE, Prestwich GD, et al. (2003). Structure-activity studies with pheromone-binding proteins of the gypsy moth, Lymantria dispar. Chem. Senses 28: 479-489.
http://dx.doi.org/10.1093/chemse/28.6.479
PMid:12907585
Hooper AM, Dufour S, He X, Muck A, et al. (2009). High-throughput ESI-MS analysis of binding between the Bombyx mori pheromone-binding protein BmorPBP1, its pheromone components and some analogues. Chem. Commun. 5725-5727.
http://dx.doi.org/10.1039/b914294k
PMid:19774249
Horst R, Damberger F, Luginbühl P, Güntert P, et al. (2001). NMR structure reveals intramolecular regulation mechanism for pheromone binding and release. Proc. Natl. Acad. Sci. U. S. A. 98: 14374-14379.
http://dx.doi.org/10.1073/pnas.251532998
PMid:11724947 PMCid:64689
Jacobs SP, Liggins AP, Zhou JJ, Pickett JA, et al. (2005). OS-D-like genes and their expression in aphids (Hemiptera: Aphididae). Insect Mol. Biol. 14: 423-432.
http://dx.doi.org/10.1111/j.1365-2583.2005.00573.x
PMid:16033435
Jin X, Ha TS and Smith DP (2008). SNMP is a signaling component required for pheromone sensitivity in Drosophila. Proc. Natl. Acad. Sci. U. S. A.105: 10996-11001.
http://dx.doi.org/10.1073/pnas.0803309105
PMid:18653762 PMCid:2504837
Kaissling KE (1972). Kinetic Studies of Transduction in Olfactory Receptors of Bombyx Mori. In: Int. Symp. Olfaction and Taste IV (Schneider D, ed.). Wissenschaftl Verlagsges, Stuttgart, 207-213.
Kaissling KE (1998a). Flux detectors versus concentration detectors: two types of chemoreceptors. Chem. Senses 23: 99-111.
http://dx.doi.org/10.1093/chemse/23.1.99
PMid:9530975
Kaissling KE (1998b). Pheromone deactivation catalyzed by receptor molecules: a quantitative kinetic model. Chem. Senses 23: 385-395.
http://dx.doi.org/10.1093/chemse/23.4.385
PMid:9759524
Kaissling KE (2001). Olfactory perireceptor and receptor events in moths: a kinetic model. Chem. Senses 26: 125-150.
http://dx.doi.org/10.1093/chemse/26.2.125
PMid:11238244
Kaissling KE (2009). Olfactory perireceptor and receptor events in moths: a kinetic model revised. J. Comp Physiol. A Neuroethol. Sens. Neural Behav. Physiol. 195: 895-922.
http://dx.doi.org/10.1007/s00359-009-0461-4
PMid:19697043 PMCid:2749182
Kaissling KE and Thorson J (1980). Insect Olfactory Sensilla: Structure, Chemical and Electrical Aspects of the Functional Organization. In: Receptors for Transmitters, Hormones and Pheromones in Insects (Sattelle DB, Hall LM and Hildebrand JG, eds.). Elsevier, Amsterdam, 261-282.
Kasang G, von Proff L and Nicholls M (1988). Enzymatic conversion and degradation of sex pheromones in antennae of the male silkworm moth Antheraea polyphemus. Z. Naturforsch. C Biosci. 43c: 275-284.
Keller A and Vosshall LB (2007). Influence of odorant receptor repertoire on odor perception in humans and fruit flies. Proc. Natl. Acad. Sci. U. S. A. 104: 5614-5619.
http://dx.doi.org/10.1073/pnas.0605321104
PMid:17372215 PMCid:1838502
Kim MS, Repp A and Smith DP (1998). LUSH odorant-binding protein mediates chemosensory responses to alcohols in Drosophila melanogaster. Genetics 150: 711-721.
PMid:9755202 PMCid:1460366
Klein U (1987). Sensillum-lymph proteins from antennal olfactory hairs of the moth Antheraea polyphemus (Saturniidae). Insect Biochem. 17: 1193-1204.
http://dx.doi.org/10.1016/0020-1790(87)90093-X
Kruse SW, Zhao R, Smith DP and 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.
http://dx.doi.org/10.1038/nsb960
PMid:12881720
Kurtovic A, Widmer A and Dickson BJ (2007). A single class of olfactory neurons mediates behavioural responses to a Drosophila sex pheromone. Nature 446: 542-546.
http://dx.doi.org/10.1038/nature05672
PMid:17392786
Laissue PP and Vosshall LB (2008). The olfactory sensory map in Drosophila. Adv. Exp. Med. Biol. 628: 102-114.
http://dx.doi.org/10.1007/978-0-387-78261-4_7
PMid:18683641
Lartigue A, Gruez A, Spinelli S, Riviere S, et al. (2003). The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism. J. Biol. Chem. 278: 30213-30218.
http://dx.doi.org/10.1074/jbc.M304688200
PMid:12766173
Laughlin JD, Ha TS, Jones DN and Smith DP (2008). Activation of pheromone-sensitive neurons is mediated by conformational activation of pheromone-binding protein. Cell 133: 1255-1265.
http://dx.doi.org/10.1016/j.cell.2008.04.046
PMid:18585358
Lautenschlager C, Leal WS and Clardy J (2005). Coil-to-helix transition and ligand release of Bombyx mori pheromone-binding protein. Biochem. Biophys. Res. Commun. 335: 1044-1050.
http://dx.doi.org/10.1016/j.bbrc.2005.07.176
PMid:16111659
Lautenschlager C, Leal WS and Clardy J (2007). Bombyx mori pheromone-binding protein binding nonpheromone ligands: implications for pheromone recognition. Structure 15: 1148-1154.
http://dx.doi.org/10.1016/j.str.2007.07.013
PMid:17850754 PMCid:2072049
Lazar J, Greenwood DR, Rasmussen LE and Prestwich GD (2002). Molecular and functional characterization of an odorant binding protein of the Asian elephant, Elephas maximus: implications for the role of lipocalins in mammalian olfaction. Biochemistry 41: 11786-11794.
http://dx.doi.org/10.1021/bi0256734
PMid:12269821
Leal WS, Chen AM, Ishida Y, Chiang VP, et al. (2005). Kinetics and molecular properties of pheromone binding and release. Proc. Natl. Acad. Sci. U. S. A. 102: 5386-5391.
http://dx.doi.org/10.1073/pnas.0501447102
PMid:15784736 PMCid:555038
Leal WS, Barbosa RM, Xu W, Ishida Y, et al. (2008). Reverse and conventional chemical ecology approaches for the development of oviposition attractants for Culex mosquitoes. PLoS One 3: e3045.
http://dx.doi.org/10.1371/journal.pone.0003045
PMid:18725946 PMCid:2516325
Lee D, Damberger FF, Peng G, Horst R, et al. (2002). NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH. FEBS Lett. 531: 314-318.
http://dx.doi.org/10.1016/S0014-5793(02)03548-2
Leite NR, Krogh R, Xu W, Ishida Y, et al. (2009). Structure of an odorant-binding protein from the mosquito Aedes aegypti suggests a binding pocket covered by a pH-sensitive “Lid”. PLoS One 4: e8006.
http://dx.doi.org/10.1371/journal.pone.0008006
PMid:19956631 PMCid:2778553
Lescop E, Briand L, Pernollet JC, Van Heijenoort C, et al. (2001). Letter to the Editor: 1H, 13C and 15N chemical shift assignment of the honeybee odorant-binding protein ASP2. J. Biomol. NMR 21: 181-182.
Mao Y, Xu X, Xu W, Ishida Y, et al. (2010). Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone. Proc. Natl. Acad. Sci. U. S. A. 107: 19102-19107.
http://dx.doi.org/10.1073/pnas.1012274107
PMid:20956299 PMCid:2973904
Matsuo T, Sugaya S, Yasukawa J, Aigaki T, et al. (2007). Odorant-binding proteins OBP57d and OBP57e affect taste perception and host-plant preference in Drosophila sechellia. PLoS Biol. 5: e118.
http://dx.doi.org/10.1371/journal.pbio.0050118
PMid:17456006 PMCid:1854911
Mohanty S, Zubkov S and Gronenborn AM (2004). The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins. J. Mol. Biol. 337: 443-451.
http://dx.doi.org/10.1016/j.jmb.2004.01.009
PMid:15003458
Mohl C, Breer H and Krieger J (2002). Species-specific pheromonal compounds induce distinct conformational changes of pheromone binding protein subtypes from Antheraea polyphemus. Invert. Neurosci. 4: 165-174.
http://dx.doi.org/10.1007/s10158-002-0018-5
PMid:12488967
Mori K, Nagao H and Yoshihara Y (1999). The olfactory bulb: coding and processing of odor molecule information. Science 286: 711-715.
http://dx.doi.org/10.1126/science.286.5440.711
PMid:10531048
Neuhaus EM, Gisselmann G, Zhang W, Dooley R, et al. (2005). Odorant receptor heterodimerization in the olfactory system of Drosophila melanogaster. Nat. Neurosci. 8: 15-17.
http://dx.doi.org/10.1038/nn1371
PMid:15592462
Novotny V, Basset Y, Miller SE, Weiblen GD, et al. (2002). Low host specificity of herbivorous insects in a tropical forest. Nature 416: 841-844.
http://dx.doi.org/10.1038/416841a
PMid:11976681
Pelletier J and Leal WS (2009). Genome analysis and expression patterns of odorant-binding proteins from the Southern House mosquito Culex pipiens quinquefasciatus. PLoS One 4: e6237.
http://dx.doi.org/10.1371/journal.pone.0006237
PMid:19606229 PMCid:2707629
Pelosi P, Pisanelli AM, Baldaccini NE and Gagliardo A (1981). Binding of [3H]-2-isobutyl-3-methoxypyrazine to cow olfactory mucosa. Chem. Senses 6: 77-85.
http://dx.doi.org/10.1093/chemse/6.2.77
Pelosi P, Baldaccini NE and Pisanelli AM (1982). Identification of a specific olfactory receptor for 2-isobutyl-3- methoxypyrazine. Biochem. J. 201: 245-248.
PMid:7082286 PMCid:1163633
Pelosi P, Zhou JJ, Ban L and Calvello M (2006). Soluble proteins in insect chemical communication. Cell. Mol. Life Sci. 63: 1658-1676.
http://dx.doi.org/10.1007/s00018-005-5607-0
PMid:16786224
Pesenti ME, Spinelli S, Bezirard V, Briand L, et al. (2008). Structural basis of the honey bee PBP pheromone and pH-induced conformational change. J. Mol. Biol. 380: 158-169.
http://dx.doi.org/10.1016/j.jmb.2008.04.048
PMid:18508083
Pesenti ME, Spinelli S, Bezirard V, Briand L, et al. (2009). Queen bee pheromone binding protein pH-induced domain swapping favors pheromone release. J. Mol. Biol. 390: 981-990.
http://dx.doi.org/10.1016/j.jmb.2009.05.067
PMid:19481550
Pophof B (2002). Moth pheromone binding proteins contribute to the excitation of olfactory receptor cells. Naturwissenschaften 89: 515-518.
http://dx.doi.org/10.1007/s00114-002-0364-5
PMid:12451455
Pophof B (2004). Pheromone-binding proteins contribute to the activation of olfactory receptor neurons in the silkmoths Antheraea polyphemus and Bombyx mori. Chem. Senses 29: 117-125.
http://dx.doi.org/10.1093/chemse/bjh012
PMid:14977808
Qiao H, Tuccori E, He X, Gazzano A, et al. (2009). Discrimination of alarm pheromone (E)-beta-farnesene by aphid odorant-binding proteins. Insect Biochem. Mol. Biol. 39: 414-419.
http://dx.doi.org/10.1016/j.ibmb.2009.03.004
PMid:19328854
Sandler BH, Nikonova L, Leal WS and Clardy J (2000). Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex. Chem. Biol. 7: 143-151.
http://dx.doi.org/10.1016/S1074-5521(00)00078-8
Sato K, Pellegrino M, Nakagawa T, Nakagawa T, et al. (2008). Insect olfactory receptors are heteromeric ligand-gated ion channels. Nature 452: 1002-1006.
http://dx.doi.org/10.1038/nature06850
PMid:18408712
Silbering AF and Benton R (2010). Ionotropic and metabotropic mechanisms in chemoreception: “chance or design”? EMBO Rep. 11: 173-179.
http://dx.doi.org/10.1038/embor.2010.8
PMid:20111052 PMCid:2838705
Strausfeld NJ and Hildebrand JG (1999). Olfactory systems: common design, uncommon origins? Curr. Opin. Neurobiol. 9: 634-639.
http://dx.doi.org/10.1016/S0959-4388(99)00019-7
Tegoni M, Campanacci V and Cambillau C (2004). Structural aspects of sexual attraction and chemical communication in insects. Trends Biochem. Sci. 29: 257-264.
http://dx.doi.org/10.1016/j.tibs.2004.03.003
PMid:15130562
Thode AB, Kruse SW, Nix JC and Jones DN (2008). The role of multiple hydrogen-bonding groups in specific alcohol binding sites in proteins: insights from structural studies of LUSH. J. Mol. Biol. 376: 1360-1376.
http://dx.doi.org/10.1016/j.jmb.2007.12.063
PMid:18234222 PMCid:2293277
Uchida N, Takahashi YK, Tanifuji M and Mori K (2000). Odor maps in the mammalian olfactory bulb: domain organization and odorant structural features. Nat. Neurosci. 3: 1035-1043.
http://dx.doi.org/10.1038/79857
PMid:11017177
Van den Berg MJ and Ziegelberger G (1991). On the function of the pheromone binding protein in the olfactory hairs of Antheraea polyphemus. J. Insect Physiol. 37: 79-85.
http://dx.doi.org/10.1016/0022-1910(91)90022-R
Vogt RG (2005). Molecular Basis of Pheromone Detection in Insects. In: Comprehensive Insect Physiology, Biochemistry, Pharmacology and Molecular Biology (Gilbert L, Latro G and Gill S, eds.). Elsevier, London, 753-804.
Vogt RG and Riddiford LM (1981). Pheromone binding and inactivation by moth antennae. Nature 293: 161-163.
http://dx.doi.org/10.1038/293161a0
PMid:18074618
Vogt RG and Riddiford LM (1986). Pheromone Reception: A Kinetic Equilibrium. In: Mechanisms in Insect Olfaction (Payne T, Birch M and Kennedy C, eds.). Clarendon Press, Oxford, 201-208.
Vosshall LB, Amrein H, Morozov PS, Rzhetsky A, et al. (1999). A spatial map of olfactory receptor expression in the Drosophila antenna. Cell 96: 725-736.
http://dx.doi.org/10.1016/S0092-8674(00)80582-6
Vosshall LB, Wong AM and Axel R (2000). An olfactory sensory map in the fly brain. Cell 102: 147-159.
http://dx.doi.org/10.1016/S0092-8674(00)00021-0
Wang P, Lyman RF, Shabalina SA, Mackay TFC, et al. (2007). Association of polymorphisms in odorant-binding protein genes with variation in olfactory response to benzaldehyde in Drosophila. Genetics 177: 1655-1665.
http://dx.doi.org/10.1534/genetics.107.079731
PMid:17720903 PMCid:2147940
Wang P, Lyman RF, Mackay TF and Anholt RR (2010). Natural variation in odorant recognition among odorant-binding proteins in Drosophila melanogaster. Genetics 184: 759-767.
http://dx.doi.org/10.1534/genetics.109.113340
PMid:20026676 PMCid:2845343
Wetzel CH, Behrendt HJ, Gisselmann G, Stortkuhl KF, et al. (2001). Functional expression and characterization of a Drosophila odorant receptor in a heterologous cell system. Proc. Natl. Acad. Sci. U. S. A. 98: 9377-9380.
http://dx.doi.org/10.1073/pnas.151103998
PMid:11481494 PMCid:55428
Wicher D, Schafer R, Bauernfeind R, Stensmyr MC, et al. (2008). Drosophila odorant receptors are both ligand-gated and cyclic-nucleotide-activated cation channels. Nature 452: 1007-1011.
http://dx.doi.org/10.1038/nature06861
PMid:18408711
Wogulis M, Morgan T, Ishida Y, Leal WS, et al. (2006). The crystal structure of an odorant binding protein from Anopheles gambiae: evidence for a common ligand release mechanism. Biochem. Biophys. Res. Commun. 339: 157-164.
http://dx.doi.org/10.1016/j.bbrc.2005.10.191
PMid:16300742
Wojtasek H and Leal WS (1999). Conformational change in the pheromone-binding protein from Bombyx mori induced by pH and by interaction with membranes. J. Biol. Chem. 274: 30950-30956.
http://dx.doi.org/10.1074/jbc.274.43.30950
PMid:10521490
Xu P, Atkinson R, Jones DN and Smith DP (2005). Drosophila OBP LUSH is required for activity of pheromone-sensitive neurons. Neuron 45: 193-200.
http://dx.doi.org/10.1016/j.neuron.2004.12.031
PMid:15664171
Xu PX, Zwiebel LJ and Smith DP (2003). Identification of a distinct family of genes encoding atypical odorant-binding proteins in the malaria vector mosquito, Anopheles gambiae. Insect Mol. Biol. 12: 549-560.
http://dx.doi.org/10.1046/j.1365-2583.2003.00440.x
PMid:14986916
Xu W and Leal WS (2008). Molecular switches for pheromone release from a moth pheromone-binding protein. Biochem. Biophys. Res. Commun. 372: 559-564.
http://dx.doi.org/10.1016/j.bbrc.2008.05.087
PMid:18503757
Xu X, Xu W, Rayo J, Ishida Y, et al. (2010). NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection. Biochemistry 49: 1469-1476.
http://dx.doi.org/10.1021/bi9020132
PMid:20088570 PMCid:2822879
Zhou JJ, Huang W, Zhang GA, Pickett JA, et al. (2004a). “Plus-C” odorant-binding protein genes in two Drosophila species and the malaria mosquito Anopheles gambiae. Gene 327: 117-129.
http://dx.doi.org/10.1016/j.gene.2003.11.007
PMid:14960367
Zhou JJ, Zhang GA, Huang W, Birkett MA, et al. (2004b). Revisiting the odorant-binding protein LUSH of Drosophila melanogaster: evidence for odour recognition and discrimination. FEBS Lett. 558: 23-26.
http://dx.doi.org/10.1016/S0014-5793(03)01521-7
Zhou JJ, He XL, Pickett JA and Field LM (2008). Identification of odorant-binding proteins of the yellow fever mosquito Aedes aegypti: genome annotation and comparative analyses. Insect Mol. Biol. 17: 147-163.
http://dx.doi.org/10.1111/j.1365-2583.2007.00789.x
PMid:18353104
Zhou JJ, Robertson G, He X, Dufour S, et al. (2009). Characterisation of Bombyx mori Odorant-binding proteins reveals that a general odorant-binding protein discriminates between sex pheromone components. J. Mol. Biol. 389: 529-545.
http://dx.doi.org/10.1016/j.jmb.2009.04.015
PMid:19371749
Zhou JJ, Field LM and He XL (2010a). Insect odorant-binding proteins: do they offer an alternative pest control strategy? Outlooks Pest Manag. 21: 31-34.
http://dx.doi.org/10.1564/21feb08
Zhou JJ, Vieira FG, He XL, Smadja C, et al. (2010b). Genome annotation and comparative analyses of the odorant-binding proteins and chemosensory proteins in the pea aphid Acyrthosiphon pisum. Insect Mol. Biol. 19 (Suppl 2): 113-122.
http://dx.doi.org/10.1111/j.1365-2583.2009.00919.x
PMid:20482644
Zubkov S, Gronenborn AM, Byeon IJ and Mohanty S (2005). Structural consequences of the pH-induced conformational switch in A. polyphemus pheromone-binding protein: mechanisms of ligand release. J. Mol. Biol. 354: 1081-1090.
http://dx.doi.org/10.1016/j.jmb.2005.10.015
PMid:16289114