메뉴 건너뛰기




Volumn 75, Issue 2, 2011, Pages 517-531

Mass spectrometrical analysis of cuticular proteins from the wing of Hebemoia glaucippe (Linnaeus, 1758) (Lepidoptera: Pieridae)

Author keywords

Butterfly wings; Cuticular proteins; Hebemoia glaucippe; Mass spectrometry; Posttranslational modifications

Indexed keywords

CHYMOTRYPSIN; CUTICLE PROTEIN CPG31; CUTICULAR PROTEIN B3DBJ; CUTICULAR PROTEIN CPR59A; INSECT PROTEIN; QUINONE DERIVATIVE; TRYPSIN; UNCLASSIFIED DRUG;

EID: 82355169561     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.08.017     Document Type: Article
Times cited : (5)

References (32)
  • 1
    • 77950520962 scopus 로고    scopus 로고
    • Structural cuticular proteins from arthropods: annotation, nomenclature, and sequence characteristics in the genomics era
    • Willis J.H. Structural cuticular proteins from arthropods: annotation, nomenclature, and sequence characteristics in the genomics era. Insect Biochem Mol Biol 2010, 40:189-204.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 189-204
    • Willis, J.H.1
  • 4
    • 0036837102 scopus 로고    scopus 로고
    • A structural model of the chitin-binding domain of cuticle proteins
    • Hamodrakas S.J., Willis J.H., Iconomidou V.A. A structural model of the chitin-binding domain of cuticle proteins. Insect Biochem Mol Biol 2002, 32:1577-1583.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1577-1583
    • Hamodrakas, S.J.1    Willis, J.H.2    Iconomidou, V.A.3
  • 5
    • 17844379783 scopus 로고    scopus 로고
    • Unique features of the structural model of 'hard' cuticle proteins: implications for chitin-protein interactions and cross-linking in cuticle
    • Iconomidou V.A., Willis J.H., Hamodrakas S.J. Unique features of the structural model of 'hard' cuticle proteins: implications for chitin-protein interactions and cross-linking in cuticle. Insect Biochem Mol Biol 2005, 35:553-560.
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 553-560
    • Iconomidou, V.A.1    Willis, J.H.2    Hamodrakas, S.J.3
  • 6
    • 0034804735 scopus 로고    scopus 로고
    • A conserved domain in arthropod cuticular proteins binds chitin
    • Rebers J.E., Willis J.H. A conserved domain in arthropod cuticular proteins binds chitin. Insect Biochem Mol Biol 2001, 31:1083-1093.
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 1083-1093
    • Rebers, J.E.1    Willis, J.H.2
  • 8
    • 51049118330 scopus 로고    scopus 로고
    • Identification of stage-specific larval camouflage associated genes in the swallowtail butterfly, Papilio xuthus
    • Futahashi R., Fujiwara H. Identification of stage-specific larval camouflage associated genes in the swallowtail butterfly, Papilio xuthus. Dev Genes Evol 2008, 218:491-504.
    • (2008) Dev Genes Evol , vol.218 , pp. 491-504
    • Futahashi, R.1    Fujiwara, H.2
  • 9
    • 77950519208 scopus 로고    scopus 로고
    • Identification of the chitin-binding proteins from the larval proteins of silkworm, Bombyx mori
    • Tang L., Liang J., Zhan Z., Xiang Z., He N. Identification of the chitin-binding proteins from the larval proteins of silkworm, Bombyx mori. Insect Biochem Mol Biol 2010, 40:228-234.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 228-234
    • Tang, L.1    Liang, J.2    Zhan, Z.3    Xiang, Z.4    He, N.5
  • 10
    • 70349193687 scopus 로고    scopus 로고
    • Annotation and analysis of low-complexity protein families of Anopheles gambiae that are associated with cuticle
    • Cornman R.S., Willis J.H. Annotation and analysis of low-complexity protein families of Anopheles gambiae that are associated with cuticle. Insect Mol Biol 2009, 18:607-622.
    • (2009) Insect Mol Biol , vol.18 , pp. 607-622
    • Cornman, R.S.1    Willis, J.H.2
  • 11
    • 31144434367 scopus 로고    scopus 로고
    • Glycine-rich protein genes, which encode a major component of the cuticle, have different developmental profiles from other cuticle protein genes in Bombyx mori
    • Zhong Y.S., Mita K., Shimada T., Kawasaki H. Glycine-rich protein genes, which encode a major component of the cuticle, have different developmental profiles from other cuticle protein genes in Bombyx mori. Insect Biochem Mol Biol 2006, 36:99-110.
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 99-110
    • Zhong, Y.S.1    Mita, K.2    Shimada, T.3    Kawasaki, H.4
  • 12
    • 0000314801 scopus 로고
    • Structural and expression of mRNA for a pupal cuticle protein of the silkworm, Bombyx mori
    • Nakato H., Toriyama M., Izumi S., Tomino S. Structural and expression of mRNA for a pupal cuticle protein of the silkworm, Bombyx mori. Insect Biochem 1990, 20:667-678.
    • (1990) Insect Biochem , vol.20 , pp. 667-678
    • Nakato, H.1    Toriyama, M.2    Izumi, S.3    Tomino, S.4
  • 13
    • 70349188499 scopus 로고    scopus 로고
    • Evidence of multiple pyrethroid resistance mechanisms in the malaria vector Anopheles gambiae sensu stricto from Nigeria
    • Awolola T.S., Oduola O.A., Strode C., Koekemoer L.L., Brooke B., Ranson H. Evidence of multiple pyrethroid resistance mechanisms in the malaria vector Anopheles gambiae sensu stricto from Nigeria. Trans R Soc Trop Med Hyg 2009, 103:1139-1145.
    • (2009) Trans R Soc Trop Med Hyg , vol.103 , pp. 1139-1145
    • Awolola, T.S.1    Oduola, O.A.2    Strode, C.3    Koekemoer, L.L.4    Brooke, B.5    Ranson, H.6
  • 14
    • 34248325168 scopus 로고    scopus 로고
    • Transcriptional analysis of insecticide resistance in Anopheles stephensi using cross-species microarray hybridization
    • Vontas J., David J.P., Nikou D., Hemingway J., Christophides G.K., Louis C., et al. Transcriptional analysis of insecticide resistance in Anopheles stephensi using cross-species microarray hybridization. Insect Mol Biol 2007, 16:315-324.
    • (2007) Insect Mol Biol , vol.16 , pp. 315-324
    • Vontas, J.1    David, J.P.2    Nikou, D.3    Hemingway, J.4    Christophides, G.K.5    Louis, C.6
  • 16
    • 68149117098 scopus 로고    scopus 로고
    • Adaptive differences in gene expression associated with heavy metal tolerance in the soil arthropod Orchesella cincta
    • Roelofs D., Janssens T.K., Timmermans M.J., Nota B., Marien J., Bochdanovits Z., et al. Adaptive differences in gene expression associated with heavy metal tolerance in the soil arthropod Orchesella cincta. Mol Ecol 2009, 18:3227-3239.
    • (2009) Mol Ecol , vol.18 , pp. 3227-3239
    • Roelofs, D.1    Janssens, T.K.2    Timmermans, M.J.3    Nota, B.4    Marien, J.5    Bochdanovits, Z.6
  • 17
    • 34250948597 scopus 로고
    • Die aerodynamische Funktion der Schmetterlingsschuppen
    • Springer, Berlin/Heidelberg
    • Nachtigall W. Die aerodynamische Funktion der Schmetterlingsschuppen. Die Naturwissenschaften 1965, 216-217. Springer, Berlin/Heidelberg.
    • (1965) Die Naturwissenschaften , pp. 216-217
    • Nachtigall, W.1
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 68149165613 scopus 로고    scopus 로고
    • Gel-based mass spectrometric analysis of a strongly hydrophobic GABAA-receptor subunit containing four transmembrane domains
    • Kang S.U., Fuchs K., Sieghart W., Pollak A., Csaszar E., Lubec G. Gel-based mass spectrometric analysis of a strongly hydrophobic GABAA-receptor subunit containing four transmembrane domains. Nat Protoc 2009, 4:1093-1102.
    • (2009) Nat Protoc , vol.4 , pp. 1093-1102
    • Kang, S.U.1    Fuchs, K.2    Sieghart, W.3    Pollak, A.4    Csaszar, E.5    Lubec, G.6
  • 21
    • 3042735127 scopus 로고    scopus 로고
    • The need for guidelines in publication of peptide and protein identification data: Working Group on Publication Guidelines for Peptide and Protein Identification Data
    • Carr S., Aebersold R., Baldwin M., Burlingame A., Clauser K., Nesvizhskii A. The need for guidelines in publication of peptide and protein identification data: Working Group on Publication Guidelines for Peptide and Protein Identification Data. Mol Cell Proteomics 2004, 3:531-533.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3    Burlingame, A.4    Clauser, K.5    Nesvizhskii, A.6
  • 22
    • 77954565511 scopus 로고    scopus 로고
    • Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells
    • Zhou W., Capello M., Fredolini C., Piemonti L., Liotta L.A., Novelli F., et al. Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells. J Proteome Res 2010, 9:2929-2936.
    • (2010) J Proteome Res , vol.9 , pp. 2929-2936
    • Zhou, W.1    Capello, M.2    Fredolini, C.3    Piemonti, L.4    Liotta, L.A.5    Novelli, F.6
  • 23
    • 33747797328 scopus 로고    scopus 로고
    • Real and imaginary artefacts in proteome analysis via two-dimensional maps
    • Righetti P.G. Real and imaginary artefacts in proteome analysis via two-dimensional maps. J Chromatogr B Analyt Technol Biomed Life Sci 2006, 841:14-22.
    • (2006) J Chromatogr B Analyt Technol Biomed Life Sci , vol.841 , pp. 14-22
    • Righetti, P.G.1
  • 24
    • 0033920377 scopus 로고    scopus 로고
    • Deamidation as a widespread phenomenon in two-dimensional polyacrylamide gel electrophoresis of human blood plasma proteins
    • Sarioglu H., Lottspeich F., Walk T., Jung G., Eckerskorn C. Deamidation as a widespread phenomenon in two-dimensional polyacrylamide gel electrophoresis of human blood plasma proteins. Electrophoresis 2000, 21:2209-2218.
    • (2000) Electrophoresis , vol.21 , pp. 2209-2218
    • Sarioglu, H.1    Lottspeich, F.2    Walk, T.3    Jung, G.4    Eckerskorn, C.5
  • 25
    • 79952246176 scopus 로고    scopus 로고
    • Small peptides released from muscle glycolytic enzymes during dry-cured ham processing
    • Mora L., Valero M.L., Sanchez Del Pino M.M., Sentandreu M.A., Toldra F. Small peptides released from muscle glycolytic enzymes during dry-cured ham processing. J Proteomics 2011, 74:442-450.
    • (2011) J Proteomics , vol.74 , pp. 442-450
    • Mora, L.1    Valero, M.L.2    Sanchez Del Pino, M.M.3    Sentandreu, M.A.4    Toldra, F.5
  • 26
    • 0034680365 scopus 로고    scopus 로고
    • Controlling beta-sheet assembly in genetically engineered silk by enzymatic phosphorylation/dephosphorylation
    • Winkler S., Wilson D., Kaplan D.L. Controlling beta-sheet assembly in genetically engineered silk by enzymatic phosphorylation/dephosphorylation. Biochemistry 2000, 39:12739-12746.
    • (2000) Biochemistry , vol.39 , pp. 12739-12746
    • Winkler, S.1    Wilson, D.2    Kaplan, D.L.3
  • 27
    • 0037676201 scopus 로고    scopus 로고
    • Sequence determination of three cuticular proteins and isoforms from the migratory locust, Locusta migratoria, using a combination of Edman degradation and mass spectrometric techniques
    • Kalume D.E., Kieffer S., Rafn K., Skou L., Andersen S.O., Roepstorff P. Sequence determination of three cuticular proteins and isoforms from the migratory locust, Locusta migratoria, using a combination of Edman degradation and mass spectrometric techniques. Biochim Biophys Acta 2003, 1645:152-163.
    • (2003) Biochim Biophys Acta , vol.1645 , pp. 152-163
    • Kalume, D.E.1    Kieffer, S.2    Rafn, K.3    Skou, L.4    Andersen, S.O.5    Roepstorff, P.6
  • 28
    • 38249036082 scopus 로고
    • Post-translational modifications of the cuticular proteins of Hyalophora cecropia from different anatomical regions and metamorphic stages
    • Cox D.L., Willis J.H. Post-translational modifications of the cuticular proteins of Hyalophora cecropia from different anatomical regions and metamorphic stages. Insect Biochem 1987, 17:469-484.
    • (1987) Insect Biochem , vol.17 , pp. 469-484
    • Cox, D.L.1    Willis, J.H.2
  • 29
    • 36949024466 scopus 로고    scopus 로고
    • Inhibition kinetics of cabbage butterfly (Pieris rapae L.) larvae phenoloxidase activity by 3-hydroxy-4-methoxybenzaldehyde thiosemicarbazone
    • Xue C.B., Luo W.C., Jiang L., Xie X.Y., Xiao T., Yan L. Inhibition kinetics of cabbage butterfly (Pieris rapae L.) larvae phenoloxidase activity by 3-hydroxy-4-methoxybenzaldehyde thiosemicarbazone. Appl Biochem Biotechnol 2007, 143:101-114.
    • (2007) Appl Biochem Biotechnol , vol.143 , pp. 101-114
    • Xue, C.B.1    Luo, W.C.2    Jiang, L.3    Xie, X.Y.4    Xiao, T.5    Yan, L.6
  • 30
    • 34548186744 scopus 로고    scopus 로고
    • An enzymatic deglycosylation scheme enabling identification of core fucosylated N-glycans and O-glycosylation site mapping of human plasma proteins
    • Hagglund P., Matthiesen R., Elortza F., Hojrup P., Roepstorff P., Jensen O.N., et al. An enzymatic deglycosylation scheme enabling identification of core fucosylated N-glycans and O-glycosylation site mapping of human plasma proteins. J Proteome Res 2007, 6:3021-3031.
    • (2007) J Proteome Res , vol.6 , pp. 3021-3031
    • Hagglund, P.1    Matthiesen, R.2    Elortza, F.3    Hojrup, P.4    Roepstorff, P.5    Jensen, O.N.6
  • 31
    • 77952404793 scopus 로고    scopus 로고
    • Cooperation between subunits is essential for high-affinity binding of N-acetyl-d-hexosamines to dimeric soluble and dimeric cellular forms of human CD69
    • Kavan D., Kubickova M., Bily J., Vanek O., Hofbauerova K., Mrazek H., et al. Cooperation between subunits is essential for high-affinity binding of N-acetyl-d-hexosamines to dimeric soluble and dimeric cellular forms of human CD69. Biochemistry 2010, 49:4060-4067.
    • (2010) Biochemistry , vol.49 , pp. 4060-4067
    • Kavan, D.1    Kubickova, M.2    Bily, J.3    Vanek, O.4    Hofbauerova, K.5    Mrazek, H.6
  • 32
    • 58149091978 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine is present on the extracellular domain of notch receptors
    • Matsuura A., Ito M., Sakaidani Y., Kondo T., Murakami K., Furukawa K., et al. O-linked N-acetylglucosamine is present on the extracellular domain of notch receptors. J Biol Chem 2008, 283:35486-35495.
    • (2008) J Biol Chem , vol.283 , pp. 35486-35495
    • Matsuura, A.1    Ito, M.2    Sakaidani, Y.3    Kondo, T.4    Murakami, K.5    Furukawa, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.