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Volumn 35, Issue 2, 2005, Pages 141-151

Proteome analysis of abundantly expressed proteins from unfed larvae of the cattle tick, Boophilus microplus

Author keywords

Boophilus microplus; Larvae; Mass spectrometry; Proteome; Two dimensional gel electrophoresis

Indexed keywords

INSECT PROTEIN; PROTEOME;

EID: 12544255329     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2004.10.009     Document Type: Article
Times cited : (37)

References (43)
  • 3
    • 0036275989 scopus 로고    scopus 로고
    • A cement protein of the tick Rhipicephalus appendiculatus, located in the secretpry e cell granules of the type III salivary gland acini, induces strong antibody responses in cattle
    • R. Bishop, B. Lambson, C. Wells, P. Pandit, J. Osaso, C. Nkonge, S. Morzaria, A. Musoke, and V. Nene A cement protein of the tick Rhipicephalus appendiculatus, located in the secretpry e cell granules of the type III salivary gland acini, induces strong antibody responses in cattle Int. J. Parasitol. 32 2002 833 842
    • (2002) Int. J. Parasitol. , vol.32 , pp. 833-842
    • Bishop, R.1    Lambson, B.2    Wells, C.3    Pandit, P.4    Osaso, J.5    Nkonge, C.6    Morzaria, S.7    Musoke, A.8    Nene, V.9
  • 4
    • 0036580517 scopus 로고    scopus 로고
    • Threat of foreign arthropod-borne pathogens to livestock in the United States
    • R.A. Bram, J.E. George, R.E. Reichard, and W.J. Tabachnick Threat of foreign arthropod-borne pathogens to livestock in the United States J. Med. Entomol. 39 2002 405 416
    • (2002) J. Med. Entomol. , vol.39 , pp. 405-416
    • Bram, R.A.1    George, J.E.2    Reichard, R.E.3    Tabachnick, W.J.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0030671264 scopus 로고    scopus 로고
    • A cluster of cuticle protein genes of Drosophila melanogaster at 65A: Sequence, structure, and evolution
    • J.-P. Charles, C. Chihara, S. Nejad, and L.M. Riddiford A cluster of cuticle protein genes of Drosophila melanogaster at 65A sequence, structure, and evolution Genetics 147 1997 1213 1224
    • (1997) Genetics , vol.147 , pp. 1213-1224
    • Charles, J.-P.1    Chihara, C.2    Nejad, S.3    Riddiford, L.M.4
  • 7
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • K.R. Clauser, P.R. Baker, and A.L. Burlingame Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching Anal. Chem. 71 1999 2871 2882
    • (1999) Anal. Chem. , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.R.2    Burlingame, A.L.3
  • 8
    • 0039098475 scopus 로고
    • Ovipositional biology of the cattle tick, Boophilus annulatus (Acari: Ixodidae), in the laboratory
    • R.B. Davey, J. Garza, G.D. Thompson Jr., and R.O. Drummond Ovipositional biology of the cattle tick, Boophilus annulatus (Acari: Ixodidae), in the laboratory J. Med. Entomol. 17 1980 287 289
    • (1980) J. Med. Entomol. , vol.17 , pp. 287-289
    • Davey, R.B.1    Garza, J.2    Thompson Jr., G.D.3    Drummond, R.O.4
  • 9
    • 0037333792 scopus 로고    scopus 로고
    • Cuticular proteins from the horseshoe crab, Limulus polyphemus
    • N. Ditzel, S.O. Andersen, and P. Højrup Cuticular proteins from the horseshoe crab, Limulus polyphemus Comp. Biochem. Physiol. B 134 2003 489 497
    • (2003) Comp. Biochem. Physiol. B , vol.134 , pp. 489-497
    • Ditzel, N.1    Andersen, S.O.2    Højrup, P.3
  • 10
    • 0037048699 scopus 로고    scopus 로고
    • P23 and HSP20/α-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families
    • J.A. Garcia-Ranea, G. Mirey, J. Camonis, and A. Valencia p23 and HSP20/α-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families FEBS Lett. 529 2002 162 167
    • (2002) FEBS Lett. , vol.529 , pp. 162-167
    • Garcia-Ranea, J.A.1    Mirey, G.2    Camonis, J.3    Valencia, A.4
  • 12
    • 0017779755 scopus 로고
    • Eradication programs for the arthropod parasites of livestock
    • O.H. Graham, and J.L. Hourrigan Eradication programs for the arthropod parasites of livestock J. Med. Entomol. 13 1977 629 658
    • (1977) J. Med. Entomol. , vol.13 , pp. 629-658
    • Graham, O.H.1    Hourrigan, J.L.2
  • 13
    • 0016172947 scopus 로고
    • The soluble cuticular proteins from the arthropod species: Scylla serrata (Decapoda: Portunidae), Boophilus microplus (Acarina: Ixodidae), and Agrianome spinicollis (Coleoptera: Cerambycidae)
    • R.H. Hackman The soluble cuticular proteins from the arthropod species scylla serrata (Decapoda: Portunidae), Boophilus microplus (Acarina: Ixodidae), and Agrianome spinicollis (Coleoptera: Cerambycidae) Comp. Biochem. Physiol. B 49 1974 457 464
    • (1974) Comp. Biochem. Physiol. B , vol.49 , pp. 457-464
    • Hackman, R.H.1
  • 14
    • 0016550511 scopus 로고
    • Expanding abdominal cuticle in the bug Rhodnius and the tick Boophilus
    • R.H. Hackman Expanding abdominal cuticle in the bug Rhodnius and the tick Boophilus J. Insect Physiol. 21 1975 1613 1623
    • (1975) J. Insect Physiol. , vol.21 , pp. 1613-1623
    • Hackman, R.H.1
  • 16
    • 0036837495 scopus 로고    scopus 로고
    • The major protein in the midgut of teneral Glossina morsitans morsitans is a molecular chaperone from the endosymbiotic bacterium Wigglesworthia glossinidia
    • L.R. Haines, J.D. Haddow, S. Aksoy, R.H. Gooding, and T.W. Pearson The major protein in the midgut of teneral Glossina morsitans morsitans is a molecular chaperone from the endosymbiotic bacterium Wigglesworthia glossinidia Insect Biochem. Molec. Biol. 32 2002 1429 1438
    • (2002) Insect Biochem. Molec. Biol. , vol.32 , pp. 1429-1438
    • Haines, L.R.1    Haddow, J.D.2    Aksoy, S.3    Gooding, R.H.4    Pearson, T.W.5
  • 17
    • 0024564370 scopus 로고
    • Expression and hormonal control of a new larval cuticular multigene family at the onset of metamorphosis of the tobacco hornworm
    • F.M. Horodyski, and L.M. Riddiford Expression and hormonal control of a new larval cuticular multigene family at the onset of metamorphosis of the tobacco hornworm Dev. Biol. 132 1989 292 303
    • (1989) Dev. Biol. , vol.132 , pp. 292-303
    • Horodyski, F.M.1    Riddiford, L.M.2
  • 18
    • 0001510436 scopus 로고
    • Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis
    • W.J. Hurkman, and C.K. Tanaka Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis Plant Physiol. 81 1986 802 806
    • (1986) Plant Physiol. , vol.81 , pp. 802-806
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 19
    • 0001897462 scopus 로고
    • Tick attachment and feeding: Role of the mouthparts, feeding apparatus, salivary gland secretions, and the host response
    • F.D. Obenchain R. Galun Pergamon Press New York
    • D.H. Kemp, B.F. Stone, and K.C. Binnington Tick attachment and feeding role of the mouthparts, feeding apparatus, salivary gland secretions, and the host response F.D. Obenchain R. Galun Physiology of Ticks 1982 Pergamon Press New York 119 168
    • (1982) Physiology of Ticks , pp. 119-168
    • Kemp, D.H.1    Stone, B.F.2    Binnington, K.C.3
  • 20
    • 0038245262 scopus 로고    scopus 로고
    • Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase
    • R. Kern, A. Malki, A. Holmgren, and G. Richarme Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase Biochem. J. 371 2003 965 972
    • (2003) Biochem. J. , vol.371 , pp. 965-972
    • Kern, R.1    Malki, A.2    Holmgren, A.3    Richarme, G.4
  • 21
    • 0033829202 scopus 로고    scopus 로고
    • Expression of arginine kinase enzymatic activity and mRNA in gills of the euryhaline crabs Carcinus maenas and Callinectes sapidus
    • S. Kotlyar, D. Weihrauch, R.S. Paulsen, and D.W. Towle Expression of arginine kinase enzymatic activity and mRNA in gills of the euryhaline crabs Carcinus maenas and Callinectes sapidus J. Exp. Biol. 203 2000 2395 2404
    • (2000) J. Exp. Biol. , vol.203 , pp. 2395-2404
    • Kotlyar, S.1    Weihrauch, D.2    Paulsen, R.S.3    Towle, D.W.4
  • 22
    • 0018969725 scopus 로고
    • Localization of arginine kinase in muscle fibres of Drosophila melanogaster
    • A.B. Lang, C. Wyss, and H.M. Eppenberger Localization of arginine kinase in muscle fibres of Drosophila melanogaster J. Muscle Res. Cell Mot. 1 1980 147 161
    • (1980) J. Muscle Res. Cell Mot. , vol.1 , pp. 147-161
    • Lang, A.B.1    Wyss, C.2    Eppenberger, H.M.3
  • 23
    • 0027287821 scopus 로고
    • Ancestry and diversity of the HMG box superfamily
    • V. Laudet, D. Stehelin, and H. Clevers Ancestry and diversity of the HMG box superfamily Nucleic Acids Res. 21 1993 2493 2501
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2493-2501
    • Laudet, V.1    Stehelin, D.2    Clevers, H.3
  • 25
    • 1642331278 scopus 로고    scopus 로고
    • Resistance to coumaphos and diazinon in Boophilus microplus (Acari: Ixodidae) and evidence for the involvement of an oxidative detoxification mechanism
    • A. Li, R.B. Davey, R.J. Miller, and J.E. George Resistance to coumaphos and diazinon in Boophilus microplus (Acari: Ixodidae) and evidence for the involvement of an oxidative detoxification mechanism J. Med. Entomol. 40 2003 482 490
    • (2003) J. Med. Entomol. , vol.40 , pp. 482-490
    • Li, A.1    Davey, R.B.2    Miller, R.J.3    George, J.E.4
  • 27
    • 0036798777 scopus 로고    scopus 로고
    • Stress-mediated signaling in PC12 cells-The role of the small heat shock protein, Hsp27, and Akt in protecting cells from heat stress and nerve growth factor withdrawal
    • K.M. Mearow, M.E. Dodge, M. Rahimtula, and C. Yegappan Stress-mediated signaling in PC12 cells-The role of the small heat shock protein, Hsp27, and Akt in protecting cells from heat stress and nerve growth factor withdrawal J. Neurochem. 83 2002 452 462
    • (2002) J. Neurochem. , vol.83 , pp. 452-462
    • Mearow, K.M.1    Dodge, M.E.2    Rahimtula, M.3    Yegappan, C.4
  • 28
    • 0032506695 scopus 로고    scopus 로고
    • Role of heat shock protein Hsp25 in the response of the orofacial nuclei motor system to physiological stress
    • A.K. Murashov, S. Talebian, and D.J. Wolgemuth Role of heat shock protein Hsp25 in the response of the orofacial nuclei motor system to physiological stress Brain Res. Molec. Brain Res. 63 1998 14 24
    • (1998) Brain Res. Molec. Brain Res. , vol.63 , pp. 14-24
    • Murashov, A.K.1    Talebian, S.2    Wolgemuth, D.J.3
  • 29
    • 0036830252 scopus 로고    scopus 로고
    • AvGI, an index of genes transcribed in the salivary glands of the ixodid tick, Amblyomma variegatum
    • V. Nene, D. Lee, J. Quackenbush, R. Skilton, S. Mwaura, M.J. Gardner, and R. Bishop AvGI, an index of genes transcribed in the salivary glands of the ixodid tick, Amblyomma variegatum Int. J. Parasitol. 32 2002 1447 1456
    • (2002) Int. J. Parasitol. , vol.32 , pp. 1447-1456
    • Nene, V.1    Lee, D.2    Quackenbush, J.3    Skilton, R.4    Mwaura, S.5    Gardner, M.J.6    Bishop, R.7
  • 31
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear backgrounds at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • V. Neuhoff, N. Arold, D. Taube, and W. Ehrhardt Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear backgrounds at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250 Electrophoresis 9 1988 255 262
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 33
    • 0346651484 scopus 로고    scopus 로고
    • Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism
    • S. Rahlfs, C. Nickel, M. Deponte, R.H. Schirmer, and K. Becker Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism Redox Rep. 8 2003 246 250
    • (2003) Redox Rep. , vol.8 , pp. 246-250
    • Rahlfs, S.1    Nickel, C.2    Deponte, M.3    Schirmer, R.H.4    Becker, K.5
  • 34
    • 0034804735 scopus 로고    scopus 로고
    • A conserved domain in arthropod cuticular proteins binds chitin
    • J.E. Rebers, and J.H. Willis A conserved domain in arthropod cuticular proteins binds chitin Insect Biochem. Molec. Biol. 31 2001 1083 1093
    • (2001) Insect Biochem. Molec. Biol. , vol.31 , pp. 1083-1093
    • Rebers, J.E.1    Willis, J.H.2
  • 36
    • 0032104132 scopus 로고    scopus 로고
    • Structure, organization and expression of two clustered cuticle protein genes during the metamorphosis of an insect, Tenebrio molitor
    • I. Rondot, B. Quennedey, and J. Delachambre Structure, organization and expression of two clustered cuticle protein genes during the metamorphosis of an insect, Tenebrio molitor Eur. J. Biochem. 254 1998 304 312
    • (1998) Eur. J. Biochem. , vol.254 , pp. 304-312
    • Rondot, I.1    Quennedey, B.2    Delachambre, J.3
  • 37
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • V. Santoni, M. Molloy, and T. Rabilloud Membrane proteins and proteomics un amour impossible? Electrophoresis 21 2000 1054 1070
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 38
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequences genomes by MALDI-Quadrupole Time-of-Flight mass spectrometry and BLAST homology searching
    • A. Shevchenko, S. Sunyaev, A. Loboda, A. Shevchenko, P. Bork, W. Ens, and K. Standing Charting the proteomes of organisms with unsequences genomes by MALDI-Quadrupole Time-of-Flight mass spectrometry and BLAST homology searching Anal. Chem. 73 2001 1917 1926
    • (2001) Anal. Chem. , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4    Bork, P.5    Ens, W.6    Standing, K.7
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignments through sequence weighting, position-specific gap penalties, and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W improving the sensitivity of progressive multiple sequence alignments through sequence weighting, position-specific gap penalties, and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 0037019903 scopus 로고    scopus 로고
    • Dual action ectoparasite vaccine targeting 'exposed' and 'concealed' antigens
    • A.R. Trimnell, R.S. Hails, and P.A. Nuttall Dual action ectoparasite vaccine targeting 'exposed' and 'concealed' antigens Vaccine 20 2002 3560 3568
    • (2002) Vaccine , vol.20 , pp. 3560-3568
    • Trimnell, A.R.1    Hails, R.S.2    Nuttall, P.A.3
  • 43
    • 0141569383 scopus 로고    scopus 로고
    • In vitro detection of acaricide resistance in Boophilus microplus (Acari: Ixodidae)
    • M.A. Villarino, G.G. Wagner, and J.E. George In vitro detection of acaricide resistance in Boophilus microplus (Acari: Ixodidae) Exp. Appl. Acarol. 28 2002 265 271
    • (2002) Exp. Appl. Acarol. , vol.28 , pp. 265-271
    • Villarino, M.A.1    Wagner, G.G.2    George, J.E.3


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