메뉴 건너뛰기




Volumn 304, Issue 4, 2003, Pages 831-838

Proteomics in Drosophila melanogaster: First 2D database of larval hemolymph proteins

Author keywords

Drosophila melanogaster; Hemolymph; NanoLC MS; Peptide mass fingerprinting; Protein; Proteomics

Indexed keywords

POLYACRYLAMIDE GEL; PROTEOME;

EID: 0037449203     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00683-1     Document Type: Article
Times cited : (89)

References (37)
  • 2
    • 0030895921 scopus 로고    scopus 로고
    • A comparison of selected mRNA and protein abundances in human liver
    • Anderson L., Seilhamer J. A comparison of selected mRNA and protein abundances in human liver. Electrophoresis. 18:1997;533-537.
    • (1997) Electrophoresis , vol.18 , pp. 533-537
    • Anderson, L.1    Seilhamer, J.2
  • 3
    • 0035977840 scopus 로고    scopus 로고
    • Proteomic profiling from human samples: The body fluid alternative
    • Kennedy S. Proteomic profiling from human samples: the body fluid alternative. Toxicol. Lett. 120:2001;379-384.
    • (2001) Toxicol. Lett. , vol.120 , pp. 379-384
    • Kennedy, S.1
  • 4
    • 0035984343 scopus 로고    scopus 로고
    • Peptide mapping of proteins in human body fluids using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Bergquist J., Palmblad M., Wetterhall M., Hakansson P., Markides K.E. Peptide mapping of proteins in human body fluids using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Mass. Spectrom. Rev. 21:2002;2-15.
    • (2002) Mass. Spectrom. Rev. , vol.21 , pp. 2-15
    • Bergquist, J.1    Palmblad, M.2    Wetterhall, M.3    Hakansson, P.4    Markides, K.E.5
  • 5
    • 0037174927 scopus 로고    scopus 로고
    • Peptidomics of the larval Drosophila melanogaster central nervous system
    • Baggerman G., Cerstiaens A., De Loof A., Schoofs L. Peptidomics of the larval Drosophila melanogaster central nervous system. J. Biol. Chem. 277:2002;40368-40374.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40368-40374
    • Baggerman, G.1    Cerstiaens, A.2    De Loof, A.3    Schoofs, L.4
  • 6
    • 2642615639 scopus 로고    scopus 로고
    • Molecular characterization and phylogenetic relationships of a protein with potential oxygen-binding capabilities in the grasshopper embryo. A hemocyanin in insects?
    • Sanchez D., Ganfornina M.D., Gutierrez G., Bastiani M.J. Molecular characterization and phylogenetic relationships of a protein with potential oxygen-binding capabilities in the grasshopper embryo. A hemocyanin in insects? Mol. Biol. Evol. 15:1998;415-426.
    • (1998) Mol. Biol. Evol. , vol.15 , pp. 415-426
    • Sanchez, D.1    Ganfornina, M.D.2    Gutierrez, G.3    Bastiani, M.J.4
  • 9
    • 0030817280 scopus 로고    scopus 로고
    • Mosquito transferrin, an acute-phase protein that is up-regulated upon infection
    • Yoshiga T., Hernandez V.P., Fallon A.M., Law J.H. Mosquito transferrin, an acute-phase protein that is up-regulated upon infection. Proc. Natl. Acad. Sci. USA. 94:1997;12337-12342.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12337-12342
    • Yoshiga, T.1    Hernandez, V.P.2    Fallon, A.M.3    Law, J.H.4
  • 10
    • 0033388612 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA encoding a transferrin homolog from Bombyx mori
    • Yun E.Y., Kang S.W., Hwang J.S., Goo T.W., Kim S.H., Jin B.R., Kwon O.Y., Kim K.Y. Molecular cloning and characterization of a cDNA encoding a transferrin homolog from Bombyx mori. Biol. Chem. 380:1999;1455-1459.
    • (1999) Biol. Chem. , vol.380 , pp. 1455-1459
    • Yun, E.Y.1    Kang, S.W.2    Hwang, J.S.3    Goo, T.W.4    Kim, S.H.5    Jin, B.R.6    Kwon, O.Y.7    Kim, K.Y.8
  • 11
    • 0033106306 scopus 로고    scopus 로고
    • Drosophila melanogaster transferrin. Cloning, deduced protein sequence, expression during the life cycle, gene localization, and up-regulation on bacterial infection
    • Yoshiga T., Georgieva T., Dunkov B.C., Harizanova N., Ralchev K., Law J.H. Drosophila melanogaster transferrin. Cloning, deduced protein sequence, expression during the life cycle, gene localization, and up-regulation on bacterial infection. Eur. J. Biochem. 260:1999;414-420.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 414-420
    • Yoshiga, T.1    Georgieva, T.2    Dunkov, B.C.3    Harizanova, N.4    Ralchev, K.5    Law, J.H.6
  • 12
    • 0028902673 scopus 로고
    • Molecular characterization of an insect transferrin and its selective incorporation into eggs during oogenesis
    • Kurama T., Kurata S., Natori S. Molecular characterization of an insect transferrin and its selective incorporation into eggs during oogenesis. Eur. J. Biochem. 228:1995;229-235.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 229-235
    • Kurama, T.1    Kurata, S.2    Natori, S.3
  • 13
    • 0034185884 scopus 로고    scopus 로고
    • A juvenile hormone-repressible transferrin-like protein from the bean bug, Riptortus clavatus: CDNA sequence analysis and protein identification during diapause and vitellogenesis
    • Hirai M., Watanabe D., Chinzei Y. A juvenile hormone-repressible transferrin-like protein from the bean bug, Riptortus clavatus: cDNA sequence analysis and protein identification during diapause and vitellogenesis. Arch. Insect. Biochem. Physiol. 44:2000;17-26.
    • (2000) Arch. Insect. Biochem. Physiol. , vol.44 , pp. 17-26
    • Hirai, M.1    Watanabe, D.2    Chinzei, Y.3
  • 14
    • 0035940514 scopus 로고    scopus 로고
    • Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays
    • De Gregorio E., Spellman P.T., Rubin G.M., Lemaitre B. Genome-wide analysis of the Drosophila immune response by using oligonucleotide microarrays. Proc. Natl. Acad. Sci. USA. 98:2001;12590-12595.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12590-12595
    • De Gregorio, E.1    Spellman, P.T.2    Rubin, G.M.3    Lemaitre, B.4
  • 15
    • 0035052709 scopus 로고    scopus 로고
    • Antifreeze and ice nucleator proteins in terrestrial arthropods
    • Duman J.G. Antifreeze and ice nucleator proteins in terrestrial arthropods. Annu. Rev. Physiol. 63:2001;327-357.
    • (2001) Annu. Rev. Physiol. , vol.63 , pp. 327-357
    • Duman, J.G.1
  • 16
    • 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. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Schevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68:1996;850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Schevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 18
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity
    • Gharahdaghi F., Weinberg C.R., Meagher D.A., Imai B.S., Mische S.M. Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity. Electrophoresis. 20:1999;601-605.
    • (1999) Electrophoresis , vol.20 , pp. 601-605
    • Gharahdaghi, F.1    Weinberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5
  • 19
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis. 20:1999;3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 20
    • 0034213595 scopus 로고    scopus 로고
    • ProFound - An expert system for protein identification using mass spectrometric peptide mapping information
    • Zhang W., Chait B.T. ProFound - an expert system for protein identification using mass spectrometric peptide mapping information. Anal. Chem. 72:2000;2482-2489.
    • (2000) Anal. Chem. , vol.72 , pp. 2482-2489
    • Zhang, W.1    Chait, B.T.2
  • 21
    • 0036126460 scopus 로고    scopus 로고
    • New insights in Adipokinetic Hormone (AKH) precursor processing in Locusta migratoria obtained by capillary liquid chromatography-tandem mass spectrometry
    • Baggerman G., Huybrechts J., Clynen E., Hens K., Harthoorn L., Vander Horst D., Poulos C., De Loof A., Schoofs L. New insights in Adipokinetic Hormone (AKH) precursor processing in Locusta migratoria obtained by capillary liquid chromatography-tandem mass spectrometry. Peptides. 23:2002;635-644.
    • (2002) Peptides , vol.23 , pp. 635-644
    • Baggerman, G.1    Huybrechts, J.2    Clynen, E.3    Hens, K.4    Harthoorn, L.5    Vander Horst, D.6    Poulos, C.7    De Loof, A.8    Schoofs, L.9
  • 22
    • 0030791329 scopus 로고    scopus 로고
    • Isolation and properties of Drosophila melanogaster ferritin-molecular cloning of a cDNA that encodes one subunit, and localization of the gene on the third chromosome
    • Charlesworth A., Georgieva T., Gospodov I., Law J.H., Dunkov B.C., Ralcheva N., Barillas-Mury C., Ralchev K., Kafatos F.C. Isolation and properties of Drosophila melanogaster ferritin-molecular cloning of a cDNA that encodes one subunit, and localization of the gene on the third chromosome. Eur. J. Biochem. 247:1997;470-475.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 470-475
    • Charlesworth, A.1    Georgieva, T.2    Gospodov, I.3    Law, J.H.4    Dunkov, B.C.5    Ralcheva, N.6    Barillas-Mury, C.7    Ralchev, K.8    Kafatos, F.C.9
  • 23
    • 0033391431 scopus 로고    scopus 로고
    • Organization of the ferritin genes in Drosophila melanogaster
    • Dunkov B.C., Georgieva T. Organization of the ferritin genes in Drosophila melanogaster. DNA Cell Biol. 18:1999;937-944.
    • (1999) DNA Cell Biol. , vol.18 , pp. 937-944
    • Dunkov, B.C.1    Georgieva, T.2
  • 24
    • 0036489168 scopus 로고    scopus 로고
    • Drosophila melanogaster ferritin: CDNA encoding a light chain homologue, temporal, and tissue specific expression of both subunit types
    • Georgieva T., Dunkov B.C., Dimov S., Ralchev K., Law J.H. Drosophila melanogaster ferritin: cDNA encoding a light chain homologue, temporal, and tissue specific expression of both subunit types. Insect. Biochem. Mol. Biol. 32:2002;295-302.
    • (2002) Insect. Biochem. Mol. Biol. , vol.32 , pp. 295-302
    • Georgieva, T.1    Dunkov, B.C.2    Dimov, S.3    Ralchev, K.4    Law, J.H.5
  • 25
    • 0033563153 scopus 로고    scopus 로고
    • Ecdysone-regulation of synthesis and processing of fat body protein 1, the larval serum protein receptor of Drosophila melanogaster
    • Burmester T., Antoniewski C., Lepesant J.A. Ecdysone-regulation of synthesis and processing of fat body protein 1, the larval serum protein receptor of Drosophila melanogaster. Eur. J. Biochem. 262:1999;49-55.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 49-55
    • Burmester, T.1    Antoniewski, C.2    Lepesant, J.A.3
  • 26
    • 0036183723 scopus 로고    scopus 로고
    • Interaction of the anterior fat body protein with the hexamerin receptor in the blowfly Calliphora vicina
    • Hansen I.A., Meyer S.R., Schafer I., Scheller K. Interaction of the anterior fat body protein with the hexamerin receptor in the blowfly Calliphora vicina. Eur. J. Biochem. 269:2002;954-960.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 954-960
    • Hansen, I.A.1    Meyer, S.R.2    Schafer, I.3    Scheller, K.4
  • 27
    • 0036740299 scopus 로고    scopus 로고
    • Genome-wide analysis of the odorant-binding protein gene family in Drosophila melanogaster
    • Hekmat-Scafe D.S., Scafe C.R., McKinney A.J., Tanouye M.A. Genome-wide analysis of the odorant-binding protein gene family in Drosophila melanogaster. Genome Res. 12:2002;1357-1369.
    • (2002) Genome Res. , vol.12 , pp. 1357-1369
    • Hekmat-Scafe, D.S.1    Scafe, C.R.2    McKinney, A.J.3    Tanouye, M.A.4
  • 28
    • 0035679021 scopus 로고    scopus 로고
    • A large family of divergent Drosophila odorant-binding proteins expressed in gustatory and olfactory sensilla
    • Galindo K., Smith D.P. A large family of divergent Drosophila odorant-binding proteins expressed in gustatory and olfactory sensilla. Genetics. 159:2001;1059-1072.
    • (2001) Genetics , vol.159 , pp. 1059-1072
    • Galindo, K.1    Smith, D.P.2
  • 29
    • 0037167175 scopus 로고    scopus 로고
    • Drosophila acid DNase is a homolog of mammalian DNase II
    • Evans C.J., Merriam J.R., Aguilera R.J. Drosophila acid DNase is a homolog of mammalian DNase II. Gene. 295:2002;61-70.
    • (2002) Gene , vol.295 , pp. 61-70
    • Evans, C.J.1    Merriam, J.R.2    Aguilera, R.J.3
  • 30
    • 0036812208 scopus 로고    scopus 로고
    • Nucleotide polymorphism in the Est6 promoter, which is widespread in derived populations of Drosophila melanogaster, changes the level of Esterase 6 expressed in the male ejaculatory duct
    • Odgers W.A., Aquadro C.F., Coppin C.W., Healy M.J., Oakeshott J.G. Nucleotide polymorphism in the Est6 promoter, which is widespread in derived populations of Drosophila melanogaster, changes the level of Esterase 6 expressed in the male ejaculatory duct. Genetics. 162:2002;785-797.
    • (2002) Genetics , vol.162 , pp. 785-797
    • Odgers, W.A.1    Aquadro, C.F.2    Coppin, C.W.3    Healy, M.J.4    Oakeshott, J.G.5
  • 31
    • 2142857696 scopus 로고    scopus 로고
    • Polypeptides differentially expressed in imaginal discs define the peroxiredoxin family of genes in Drosophila
    • Rodriguez J., Agudo M., Van Damme J., Vandekerckhove J., Santaren J.F. Polypeptides differentially expressed in imaginal discs define the peroxiredoxin family of genes in Drosophila. Eur. J. Biochem. 267:2000;487-497.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 487-497
    • Rodriguez, J.1    Agudo, M.2    Van Damme, J.3    Vandekerckhove, J.4    Santaren, J.F.5
  • 32
    • 0242547005 scopus 로고    scopus 로고
    • Regulation of arginine kinase in imaginal discs
    • Cox C.J., Collier G.E. Regulation of arginine kinase in imaginal discs. A. Dros. Res. Conf. 42:2001;383.
    • (2001) A. Dros. Res. Conf. , vol.42 , pp. 383
    • Cox, C.J.1    Collier, G.E.2
  • 33
    • 0025996530 scopus 로고
    • Structure and expression of the triose phosphate isomerase (Tpi) gene of Drosophila melanogaster
    • Shaw-Lee R., Lissemore J.L., Sullivan D.T. Structure and expression of the triose phosphate isomerase (Tpi) gene of Drosophila melanogaster. Mol. Gen. Genet. 230:1991;225-229.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 225-229
    • Shaw-Lee, R.1    Lissemore, J.L.2    Sullivan, D.T.3
  • 34
  • 35
    • 0022432076 scopus 로고
    • Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae
    • Suzuki T., Natori S. Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae. J. Biol. Chem. 260:1985;5115-5120.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5115-5120
    • Suzuki, T.1    Natori, S.2
  • 36
    • 0020581716 scopus 로고
    • Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner
    • Fyrberg E.A., Mahaffey J.W., Bond B.J., Davidson N. Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner. Cell. 33:1983;115-123.
    • (1983) Cell , vol.33 , pp. 115-123
    • Fyrberg, E.A.1    Mahaffey, J.W.2    Bond, B.J.3    Davidson, N.4
  • 37
    • 0037066770 scopus 로고    scopus 로고
    • Crystal structure of imaginal disc growth factor-2. A member of a new family of growth-promoting glycoproteins from Drosophila melanogaster
    • Varela P.F., Llera A.S., Mariuzza R.A., Tormo J. Crystal structure of imaginal disc growth factor-2. A member of a new family of growth-promoting glycoproteins from Drosophila melanogaster. J. Biol. Chem. 277:2002;13229-13236.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13229-13236
    • Varela, P.F.1    Llera, A.S.2    Mariuzza, R.A.3    Tormo, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.