메뉴 건너뛰기




Volumn 1820, Issue 3, 2012, Pages 437-451

Insect transferrins: Multifunctional proteins

Author keywords

Development; Ferritin; Immunity; Insect; Oxidative stress; Transferrin

Indexed keywords

INSECT PROTEIN; IRON; TRANSFERRIN;

EID: 84857358614     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2011.07.011     Document Type: Review
Times cited : (88)

References (129)
  • 1
    • 33645091619 scopus 로고    scopus 로고
    • Insect iron binding proteins: Insights from the genomes
    • B. Dunkov, and T. Georgieva Insect iron binding proteins: insights from the genomes Insect Biochem. Mol. Biol. 36 2006 300 309
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 300-309
    • Dunkov, B.1    Georgieva, T.2
  • 2
    • 33646363763 scopus 로고    scopus 로고
    • Iron-withholding strategy in innate immunity
    • S.T. Ong, J.Z. Ho, B. Ho, and J.L. Ding Iron-withholding strategy in innate immunity Immunobiology 211 2006 295 314
    • (2006) Immunobiology , vol.211 , pp. 295-314
    • Ong, S.T.1    Ho, J.Z.2    Ho, B.3    Ding, J.L.4
  • 4
    • 0001657675 scopus 로고
    • Iron economy in insects: Transport, metabolism, and storage, iron, transport
    • M. Locke, and H. Nichol Iron economy in insects: transport, metabolism, and storage, iron, transport Annu. Rev. Entomol. 37 1992 195 215
    • (1992) Annu. Rev. Entomol. , vol.37 , pp. 195-215
    • Locke, M.1    Nichol, H.2
  • 6
    • 65449120792 scopus 로고    scopus 로고
    • Iron behaving badly: Inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
    • D.B. Kell Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases BMC Med. Genomics 2 2009 2
    • (2009) BMC Med. Genomics , vol.2 , pp. 2
    • Kell, D.B.1
  • 7
    • 47849117134 scopus 로고    scopus 로고
    • Iron withholding: A defense against disease
    • E.D. Weinberg, and J. Miklossy Iron withholding: a defense against disease J. Alzheimers Dis. 13 2008 451 463 (Pubitemid 352039024)
    • (2008) Journal of Alzheimer's Disease , vol.13 , Issue.4 , pp. 451-463
    • Weinberg, E.D.1    Miklossy, J.2
  • 8
    • 64049100955 scopus 로고    scopus 로고
    • Iron in innate immunity: Starve the invaders
    • T. Ganz Iron in innate immunity: starve the invaders Curr. Opin. Immunol. 21 2009 63 67
    • (2009) Curr. Opin. Immunol. , vol.21 , pp. 63-67
    • Ganz, T.1
  • 11
    • 0019493358 scopus 로고
    • Structural characterization of human melanoma-associated antigen p97 with monoclonal antibodies
    • J.P. Brown, K. Nishiyama, I. Hellstrom, and K.E. Hellstrom Structural characterization of human melanoma-associated antigen p97 with monoclonal antibodies J. Immunol. 127 1981 539 546 (Pubitemid 11054661)
    • (1981) Journal of Immunology , vol.127 , Issue.2 , pp. 539-546
    • Brown, J.P.1    Nishiyama, K.2    Hellstrom, I.3    Hellstrom, K.E.4
  • 12
    • 0020029134 scopus 로고
    • Human melanoma-associated antigen p97 is structurally and functionally related to transferrin
    • J.P. Brown, R.M. Hewick, I. Hellstrom, K.E. Hellstrom, R.F. Doolittle, and W.J. Dreyer Human melanoma-associated antigen p97 is structurally and functionally related to transferrin Nature 296 1982 171 173 (Pubitemid 12160920)
    • (1982) Nature , vol.296 , Issue.5853 , pp. 171-173
    • Brown, J.P.1    Hewick, R.M.2    Hellstrom, I.3
  • 15
    • 0031605219 scopus 로고    scopus 로고
    • Transferrin, the transferrin receptor, and the uptake of iron by cells
    • P. Aisen Transferrin, the transferrin receptor, and the uptake of iron by cells Met. Ions Biol. Syst. 35 1998 585 631
    • (1998) Met. Ions Biol. Syst. , vol.35 , pp. 585-631
    • Aisen, P.1
  • 16
    • 77949475176 scopus 로고    scopus 로고
    • Molecular mechanisms of normal iron homeostasis
    • A.S. Zhang, and C.A. Enns Molecular mechanisms of normal iron homeostasis Hematology 2009 207 214
    • (2009) Hematology , pp. 207-214
    • Zhang, A.S.1    Enns, C.A.2
  • 19
    • 13544254492 scopus 로고    scopus 로고
    • Aedes aegypti transferrin. Gene structure, expression pattern, and regulation
    • DOI 10.1111/j.1365-2583.2004.00533.x
    • N. Harizanova, T. Georgieva, B.C. Dunkov, T. Yoshiga, and J.H. Law Aedes aegypti transferrin. Gene structure, expression pattern, and regulation Insect Mol. Biol. 14 2005 79 88 (Pubitemid 40218086)
    • (2005) Insect Molecular Biology , vol.14 , Issue.1 , pp. 79-88
    • Harizanova, N.1    Georgieva, T.2    Dunkov, B.C.3    Yoshiga, T.4    Law, J.H.5
  • 20
    • 33645102838 scopus 로고    scopus 로고
    • Iron metabolism in insect disease vectors: Mining the Anopheles gambiae translated protein database
    • J.J. Winzerling, and D.Q. Pham Iron metabolism in insect disease vectors: mining the Anopheles gambiae translated protein database Insect Biochem. Mol. Biol. 36 2006 310 321
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 310-321
    • Winzerling, J.J.1    Pham, D.Q.2
  • 21
    • 70449379573 scopus 로고    scopus 로고
    • Ironing out the wrinkles in host defense: Interactions between iron homeostasis and innate immunity
    • L. Wang, and B.J. Cherayil Ironing out the wrinkles in host defense: interactions between iron homeostasis and innate immunity J Innate Immun. 1 2009 455 464
    • (2009) J Innate Immun. , vol.1 , pp. 455-464
    • Wang, L.1    Cherayil, B.J.2
  • 22
    • 32644437864 scopus 로고    scopus 로고
    • Iron metabolism in the hemoglobin-deficit mouse: Correlation of diferric transferrin with hepcidin expression
    • DOI 10.1182/blood-2005-07-2614
    • S.J. Wilkins, D.M. Frazer, K.N. Millard, G.D. McLaren, and G.J. Anderson Iron metabolism in the hemoglobin-deficit mouse: correlation of diferric transferrin with hepcidin expression Blood 107 2006 1659 1664 (Pubitemid 43242406)
    • (2006) Blood , vol.107 , Issue.4 , pp. 1659-1664
    • Wilkins, S.J.1    Frazer, D.M.2    Millard, K.N.3    McLaren, G.D.4    Anderson, G.J.5
  • 23
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • J. Wang, and K. Pantopoulos Regulation of cellular iron metabolism Biochem. J. 434 2011 365 381
    • (2011) Biochem. J. , vol.434 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 25
    • 0033081711 scopus 로고    scopus 로고
    • Insect immunity: Molecular cloning, expression, and characterization of cDNAs and genomic DNA encoding three isoforms of insect defensin in Aedes aegypti
    • C.A. Lowenberger, C.T. Smartt, P. Bulet, M.T. Ferdig, D.W. Severson, J.A. Hoffmann, and B.M. Christensen Insect immunity: molecular cloning, expression, and characterization of cDNAs and genomic DNA encoding three isoforms of insect defensin in Aedes aegypti Insect Mol. Biol. 8 1999 107 118 (Pubitemid 29032136)
    • (1999) Insect Molecular Biology , vol.8 , Issue.1 , pp. 107-118
    • Lowenberger, C.A.1    Smartt, C.T.2    Bulet, P.3    Ferdig, M.T.4    Severson, D.W.5    Hoffmann, J.A.6    Christensen, B.M.7
  • 26
    • 0036747342 scopus 로고    scopus 로고
    • Reverse genetics in the mosquito Anopheles gambiae: Targeted disruption of the Defensin gene
    • DOI 10.1093/embo-reports/kvf180
    • S. Blandin, L.F. Moita, T. Kocher, M. Wilm, F.C. Kafatos, and E.A. Levashina Reverse genetics in the mosquito Anopheles gambiae: targeted disruption of the Defensin gene EMBO Rep. 3 2002 852 856 (Pubitemid 35154110)
    • (2002) EMBO Reports , vol.3 , Issue.9 , pp. 852-856
    • Blandin, S.1    Moita, L.F.2    Kocher, T.3    Wilm, M.4    Kafatos, F.C.5    Levashina, E.A.6
  • 27
    • 55049121378 scopus 로고    scopus 로고
    • Expression of defensin, cecropin, and transferrin in Aedes aegypti (Diptera: Culicidae) infected with Wuchereria bancrofti (Spirurida: Onchocercidae), and the abnormal development of nematodes in the mosquito
    • T. Magalhaes, I.F. Oliveira, M.A. Melo-Santos, C.M. Oliveira, C.A. Lima, and C.F. Ayres Expression of defensin, cecropin, and transferrin in Aedes aegypti (Diptera: Culicidae) infected with Wuchereria bancrofti (Spirurida: Onchocercidae), and the abnormal development of nematodes in the mosquito Exp. Parasitol. 120 2008 364 371
    • (2008) Exp. Parasitol. , vol.120 , pp. 364-371
    • Magalhaes, T.1    Oliveira, I.F.2    Melo-Santos, M.A.3    Oliveira, C.M.4    Lima, C.A.5    Ayres, C.F.6
  • 28
    • 0025695557 scopus 로고
    • Isolation and molecular cloning of transferrin from the tobacco hornworm Manduca sexta
    • N.S. Bartfeld, and J.H. Law Isolation and molecular cloning of transferrin from the tobacco hornworm Manduca sexta J. Biol. Chem. 265 1990 21684 21691
    • (1990) J. Biol. Chem. , vol.265 , pp. 21684-21691
    • Bartfeld, N.S.1    Law, J.H.2
  • 30
    • 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
    • DOI 10.1046/j.1432-1327.1999.00173.x
    • T. Yoshiga, T. Georgieva, B.C. Dunkov, N. Harizanova, K. Ralchev, and J.H. Law 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 (Pubitemid 29122537)
    • (1999) European Journal of Biochemistry , vol.260 , Issue.2 , pp. 414-420
    • Yoshiga, T.1    Georgieva, T.2    Dunkov, B.C.3    Harizanova, N.4    Ralchev, K.5    Law, J.H.6
  • 31
    • 0037321923 scopus 로고    scopus 로고
    • Isolation and characterization of a termite transferrin gene up-regulated on infection
    • DOI 10.1046/j.1365-2583.2003.00381.x
    • G.J. Thompson, Y.C. Crozier, and R.H. Crozier Isolation and characterization of a termite transferrin gene up-regulated on infection Insect Mol. Biol. 12 2003 1 7 (Pubitemid 36224815)
    • (2003) Insect Molecular Biology , vol.12 , Issue.1 , pp. 1-7
    • Thompson, G.J.1    Crozier, Y.C.2    Crozier, R.H.3
  • 35
    • 44449155195 scopus 로고    scopus 로고
    • Physical stress primes the immune response of Galleria mellonella larvae to infection by Candida albicans
    • P. Mowlds, A. Barron, and K. Kavanagh Physical stress primes the immune response of Galleria mellonella larvae to infection by Candida albicans Microbes Infect. 10 2008 628 634
    • (2008) Microbes Infect. , vol.10 , pp. 628-634
    • Mowlds, P.1    Barron, A.2    Kavanagh, K.3
  • 36
    • 67650367215 scopus 로고    scopus 로고
    • Gene expression responses in larvae of the fleshfly Sarcophaga bullata after immune stimulation
    • A. Masova, R. Sindelka, M. Kubista, J. Kindl, and J. Jiracek Gene expression responses in larvae of the fleshfly Sarcophaga bullata after immune stimulation Folia Biol. (Praha) 55 2009 98 106
    • (2009) Folia Biol. (Praha) , vol.55 , pp. 98-106
    • Masova, A.1    Sindelka, R.2    Kubista, M.3    Kindl, J.4    Jiracek, J.5
  • 38
    • 77954324667 scopus 로고    scopus 로고
    • A viral histone H4 suppresses expression of a transferrin that plays a role in the immune response of the diamondback moth, Plutella xylostella
    • J. Kim, and Y. Kim A viral histone H4 suppresses expression of a transferrin that plays a role in the immune response of the diamondback moth, Plutella xylostella Insect Mol. Biol. 19 2010 567 574
    • (2010) Insect Mol. Biol. , vol.19 , pp. 567-574
    • Kim, J.1    Kim, Y.2
  • 39
    • 0036968089 scopus 로고    scopus 로고
    • Transferrin regulates transcription of the MBP gene and its action synergizes with IGF-1 to enhance myelinogenesis in the md rat
    • DOI 10.1159/000065698
    • A. Espinosa-Jeffrey, S. Kumar, P.M. Zhao, O. Awosika, C. Agbo, A. Huang, R. Chang, and J. De Vellis Transferrin regulates transcription of the MBP gene and its action synergizes with IGF-1 to enhance myelinogenesis in the md rat Dev. Neurosci. 24 2002 227 241 (Pubitemid 36151454)
    • (2002) Developmental Neuroscience , vol.24 , Issue.2-3 , pp. 227-241
    • Espinosa-Jeffrey, A.1    Kumar, S.2    Zhao, P.M.3    Awosika, O.4    Agbo, C.5    Huang, A.6    Chang, R.7    De Vellis, J.8
  • 40
    • 0025786711 scopus 로고
    • Transferrin receptor expression and iron uptake in the injured and regenerating rat sciatic nerve
    • G. Raivich, M.B. Graeber, J. Gehrmann, and G.W. Kreutzberg Transferrin receptor expression and iron uptake in the injured and regenerating rat sciatic nerve Eur. J. Neurosci. 3 1991 919 927
    • (1991) Eur. J. Neurosci. , vol.3 , pp. 919-927
    • Raivich, G.1    Graeber, M.B.2    Gehrmann, J.3    Kreutzberg, G.W.4
  • 42
    • 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
    • M. Hirai, D. Watanabe, and Y. Chinzei 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
  • 44
    • 0141918811 scopus 로고    scopus 로고
    • Lactoferrin - A multifunctional protein with antimicrobial properties
    • DOI 10.1016/S0161-5890(03)00152-4
    • S. Farnaud, and R.W. Evans Lactoferrin-a multifunctional protein with antimicrobial properties Mol. Immunol. 40 2003 395 405 (Pubitemid 37244032)
    • (2003) Molecular Immunology , vol.40 , Issue.7 , pp. 395-405
    • Farnaud, S.1    Evans, R.W.2
  • 45
    • 0028902673 scopus 로고
    • Molecular characterization of an insect transferrin and its selective incorporation into eggs during oogenesis
    • T. Kurama, S. Kurata, and S. Natori 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
  • 46
    • 1942470608 scopus 로고    scopus 로고
    • Honey bee (Apis mellifera) transferrin-gene structure and the role of ecdysteroids in the developmental regulation of its expression
    • DOI 10.1016/j.ibmb.2003.12.003, PII S0965174803002327
    • A.M. do Nascimento, V. Cuvillier-Hot, A.R. Barchuk, Z.L. Simoes, and K. Hartfelder Honey bee (Apis mellifera) transferrin-gene structure and the role of ecdysteroids in the developmental regulation of its expression Insect Biochem. Mol. Biol. 34 2004 415 424 (Pubitemid 38527137)
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , Issue.5 , pp. 415-424
    • Do Nascimento, A.M.1    Cuvillier-Hot, V.2    Barchuk, A.R.3    Simoes, Z.L.P.4    Hartfelder, K.5
  • 47
    • 38149024831 scopus 로고    scopus 로고
    • Identity and transfer of male reproductive gland proteins of the dengue vector mosquito, Aedes aegypti: Potential tools for control of female feeding and reproduction
    • L.K. Sirot, R.L. Poulson, M.C. McKenna, H. Girnary, M.F. Wolfner, and L.C. Harrington Identity and transfer of male reproductive gland proteins of the dengue vector mosquito, Aedes aegypti: potential tools for control of female feeding and reproduction Insect Biochem. Mol. Biol. 38 2008 176 189
    • (2008) Insect Biochem. Mol. Biol. , vol.38 , pp. 176-189
    • Sirot, L.K.1    Poulson, R.L.2    McKenna, M.C.3    Girnary, H.4    Wolfner, M.F.5    Harrington, L.C.6
  • 48
    • 60449097146 scopus 로고    scopus 로고
    • Expression of vitellogenin and transferrin in activated ovaries of worker honey bees, Apis mellifera
    • P. Koywiwattrakul, and S. Sittipraneed Expression of vitellogenin and transferrin in activated ovaries of worker honey bees, Apis mellifera Biochem. Genet. 47 2009 19 26
    • (2009) Biochem. Genet. , vol.47 , pp. 19-26
    • Koywiwattrakul, P.1    Sittipraneed, S.2
  • 49
    • 68749113723 scopus 로고    scopus 로고
    • A transferrin-like homolog in amphioxus Branchiostoma belcheri: Identification, expression and functional characterization
    • J. Liu, S. Zhang, and L. Li A transferrin-like homolog in amphioxus Branchiostoma belcheri: identification, expression and functional characterization Mol. Immunol. 46 2009 3117 3124
    • (2009) Mol. Immunol. , vol.46 , pp. 3117-3124
    • Liu, J.1    Zhang, S.2    Li, L.3
  • 50
    • 77951210562 scopus 로고    scopus 로고
    • Transcriptome analysis of reproductive tissue and intrauterine developmental stages of the tsetse fly (Glossina morsitans morsitans)
    • G.M. Attardo, J.M. Ribeiro, Y. Wu, M. Berriman, and S. Aksoy Transcriptome analysis of reproductive tissue and intrauterine developmental stages of the tsetse fly (Glossina morsitans morsitans) BMC Genomics 11 2010 160
    • (2010) BMC Genomics , vol.11 , pp. 160
    • Attardo, G.M.1    Ribeiro, J.M.2    Wu, Y.3    Berriman, M.4    Aksoy, S.5
  • 51
  • 52
    • 0020961467 scopus 로고
    • Transferrin receptor induction in mitogen-stimulated human T lymphocytes is required for DNA synthesis and cell division and is regulated by interleukin 2
    • L.M. Neckers, and J. Cossman Transferrin receptor induction in mitogen-stimulated human T lymphocytes is required for DNA synthesis and cell division and is regulated by interleukin 2 Proc. Natl Acad. Sci. USA 80 1983 3494 3498 (Pubitemid 13060190)
    • (1983) Proceedings of the National Academy of Sciences of the United States of America , vol.80 , Issue.11 , pp. 3494-3498
    • Neckers, L.M.1    Cossman, J.2
  • 53
    • 0027312095 scopus 로고
    • Glycosyl phosphatidylinositol membrane anchoring of melanotransferrin (p97): Apical compartmentalization in intestinal epithelial cells
    • R. Alemany, M.R. Vila, C. Franci, G. Egea, F.X. Real, and T.M. Thomson Glycosyl phosphatidylinositol membrane anchoring of melanotransferrin (p97): apical compartmentalization in intestinal epithelial cells J. Cell Sci. 104 Pt 4 1993 1155 1162 (Pubitemid 23154323)
    • (1993) Journal of Cell Science , vol.104 , Issue.4 , pp. 1155-1162
    • Alemany, R.1    Vila, M.R.2    Franci, C.3    Egea, G.4    Real, F.X.5    Thomson, T.M.6
  • 54
    • 0028111120 scopus 로고
    • Transport and expression in human melanomas of a transferrin-like glycosylphosphatidylinositol-anchored protein
    • M.R. Food, S. Rothenberger, R. Gabathuler, I.D. Haidl, G. Reid, and W.A. Jefferies Transport and expression in human melanomas of a transferrin-like glycosylphosphatidylinositol-anchored protein J. Biol. Chem. 269 1994 3034 3040 (Pubitemid 24235812)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.4 , pp. 3034-3040
    • Food, M.R.1    Rothenberger, S.2    Gabathuler, R.3    Haidl, I.D.4    Reid, G.5    Jefferies, W.A.6
  • 55
    • 0036381706 scopus 로고    scopus 로고
    • The soluble form of the membrane-bound transferrin homologue, melanotransferrin, inefficiently donates iron to cells via nonspecific internalization and degradation of the protein
    • M.R. Food, E.O. Sekyere, and D.R. Richardson The soluble form of the membrane-bound transferrin homologue, melanotransferrin, inefficiently donates iron to cells via nonspecific internalization and degradation of the protein Eur. J. Biochem. 269 2002 4435 4445
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4435-4445
    • Food, M.R.1    Sekyere, E.O.2    Richardson, D.R.3
  • 56
    • 0029955035 scopus 로고    scopus 로고
    • Serum levels of the iron binding protein p97 are elevated in Alzheimer's disease
    • DOI 10.1038/nm1196-1230
    • M.L. Kennard, H. Feldman, T. Yamada, and W.A. Jefferies Serum levels of the iron binding protein p97 are elevated in Alzheimer's disease Nat. Med. 2 1996 1230 1235 (Pubitemid 26375407)
    • (1996) Nature Medicine , vol.2 , Issue.11 , pp. 1230-1235
    • Kennard, M.L.1    Feldman, H.2    Yamada, T.3    Jefferies, W.A.4
  • 58
    • 0026081935 scopus 로고
    • The release of iron and transferrin from the human melanoma cell
    • D.R. Richardson, and E. Baker The release of iron and transferrin from the human melanoma cell Biochim. Biophys. Acta 1091 1991 294 302
    • (1991) Biochim. Biophys. Acta , vol.1091 , pp. 294-302
    • Richardson, D.R.1    Baker, E.2
  • 60
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • DOI 10.1016/S0304-4157(96)00014-7, PII S0304415796000147
    • D.R. Richardson, and P. Ponka The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells Biochim. Biophys. Acta 1331 1997 1 40 (Pubitemid 27168147)
    • (1997) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1331 , Issue.1 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 61
    • 0034010481 scopus 로고    scopus 로고
    • Role of melanotransferrin (p97) in non-transferrin iron uptake by HeLa and K562 cells
    • K. Kriegerbeckova, and J. Kovar Role of melanotransferrin (p97) in non-transferrin iron uptake by HeLa and K562 cells Folia Biol. 46 2000 77 81 (Pubitemid 30235019)
    • (2000) Folia Biologica , vol.46 , Issue.2 , pp. 77-81
    • Kriegerbeckova, K.1    Kovar, J.2
  • 62
    • 33645528381 scopus 로고    scopus 로고
    • Role of melanotransferrin in iron metabolism: Studies using targeted gene disruption in vivo
    • E.O. Sekyere, L.L. Dunn, Y.S. Rahmanto, and D.R. Richardson Role of melanotransferrin in iron metabolism: studies using targeted gene disruption in vivo Blood 107 2006 2599 2601
    • (2006) Blood , vol.107 , pp. 2599-2601
    • Sekyere, E.O.1    Dunn, L.L.2    Rahmanto, Y.S.3    Richardson, D.R.4
  • 63
    • 0024539607 scopus 로고
    • In situ localization of melanotransferrin (melanoma-associated antigen P97) in human liver. A light- and electronmicroscopic immunohistochemical study
    • R. Sciot, R. de Vos, P. van Eyken, K. van der Steen, P. Moerman, and V.J. Desmet In situ localization of melanotransferrin (melanoma-associated antigen P97) in human liver. A light- and electronmicroscopic immunohistochemical study Liver 9 1989 110 119 (Pubitemid 19099729)
    • (1989) Liver , vol.9 , Issue.2 , pp. 110-119
    • Sciot, R.1    De Vos, R.2    Van Eyken, P.3    Van Der Steen, K.4    Moerman, P.5    Desmet, V.J.6
  • 64
    • 0026690909 scopus 로고
    • Two mechanisms of iron uptake from transferrin by melanoma cells
    • D. Richardson, and E. Baker Two mechanisms of iron uptake from transferrin by melanoma cells J. Biol. Chem. 267 1992 13972 13979
    • (1992) J. Biol. Chem. , vol.267 , pp. 13972-13979
    • Richardson, D.1    Baker, E.2
  • 65
    • 0034054183 scopus 로고    scopus 로고
    • The role of the membrane-bound tumour antigen, melanotransferrin (p97), in iron uptake by the human malignant melanoma cell
    • DOI 10.1046/j.1432-1327.2000.01079.x
    • D.R. Richardson The role of the membrane-bound tumour antigen, melanotransferrin (p97), in iron uptake by the human malignant melanoma cell Eur. J. Biochem. 267 2000 1290 1298 (Pubitemid 30143266)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.5 , pp. 1290-1298
    • Richardson, D.R.1
  • 66
    • 14544273227 scopus 로고    scopus 로고
    • Examination of the distribution of the transferrin homologue, melanotransferrin (tumour antigen p97), in mouse and human
    • DOI 10.1016/j.bbagen.2004.12.002
    • E.O. Sekyere, L.L. Dunn, and D.R. Richardson Examination of the distribution of the transferrin homologue, melanotransferrin (tumour antigen p97), in mouse and human Biochim. Biophys. Acta 1722 2005 131 142 (Pubitemid 40299003)
    • (2005) Biochimica et Biophysica Acta - General Subjects , vol.1722 , Issue.2 , pp. 131-142
    • Sekyere, E.O.1    Dunn, L.L.2    Richardson, D.R.3
  • 67
    • 33750429650 scopus 로고    scopus 로고
    • The function of melanotransferrin: A role in melanoma cell proliferation and tumorigenesis
    • DOI 10.1093/carcin/bgl045
    • L.L. Dunn, E.O. Sekyere, Y.S. Rahmanto, and D.R. Richardson The function of melanotransferrin: a role in melanoma cell proliferation and tumorigenesis Carcinogenesis 27 2006 2157 2169 (Pubitemid 44644804)
    • (2006) Carcinogenesis , vol.27 , Issue.11 , pp. 2157-2169
    • Dunn, L.L.1    Sekyer, E.O.2    Suryo Rahmanto, Y.3    Richardson, D.R.4
  • 68
    • 0034644835 scopus 로고    scopus 로고
    • The membrane-bound transferrin homologue melanotransferrin: Roles other than iron transport?
    • E. Sekyere, and D.R. Richardson The membrane-bound transferrin homologue melanotransferrin: roles other than iron transport? FEBS Lett. 483 2000 11 16
    • (2000) FEBS Lett. , vol.483 , pp. 11-16
    • Sekyere, E.1    Richardson, D.R.2
  • 69
    • 48149092101 scopus 로고    scopus 로고
    • Isolation and characterization of the iron-binding properties of a primitive monolobal transferrin from Ciona intestinalis
    • R. Uppal, K.V. Lakshmi, and A.M. Valentine Isolation and characterization of the iron-binding properties of a primitive monolobal transferrin from Ciona intestinalis J. Biol. Inorg. Chem. 13 2008 873 885
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 873-885
    • Uppal, R.1    Lakshmi, K.V.2    Valentine, A.M.3
  • 72
    • 35348897832 scopus 로고    scopus 로고
    • Analysis of the immune-inducible genes of Plutella xylostella using expressed sequence tags and cDNA microarray
    • DOI 10.1016/j.dci.2007.02.002, PII S0145305X07000195
    • J. Eum, S. Han, and S. Kang Analysis of the immune-inducible genes of Plutella xylostella using expressed sequence tags and cDNA microarray Dev. Comp. Immunol. 31 2007 1107 1120 (Pubitemid 47588406)
    • (2007) Developmental and Comparative Immunology , vol.31 , Issue.11 , pp. 1107-1120
    • Eum, J.H.1    Seo, Y.R.2    Yoe, S.M.3    Kang, S.W.4    Han, S.S.5
  • 73
    • 34250795838 scopus 로고    scopus 로고
    • Transferrin in the mosquito, Culex quinquefasciatus Say (Diptera: Culicidae), up-regulated upon infection and development of the filarial parasite, Wuchereria bancrofti (Cobbold) (Spirurida: Onchocercidae)
    • DOI 10.1007/s00436-007-0474-2
    • K.P. Paily, B.A. Kumar, and K. Balaraman Transferrin in the mosquito, Culex quinquefasciatus Say (Diptera: Culicidae), up-regulated upon infection and development of the filarial parasite, Wuchereria bancrofti (Cobbold) (Spirurida: Onchocercidae) Parasitol. Res. 101 2007 325 330 (Pubitemid 46980522)
    • (2007) Parasitology Research , vol.101 , Issue.2 , pp. 325-330
    • Paily, K.P.1    Kumar, B.A.2    Balaraman, K.3
  • 74
    • 33845978763 scopus 로고    scopus 로고
    • Molecular characterization of iron binding proteins from Glossina morsitans morsitans (Diptera: Glossinidae)
    • DOI 10.1016/j.ibmb.2006.09.003, PII S0965174806001731
    • P.M. Strickler-Dinglasan, N. Guz, G. Attardo, and S. Aksoy Molecular characterization of iron binding proteins from Glossina morsitans morsitans (Diptera: Glossinidae) Insect Biochem. Mol. Biol. 36 2006 921 933 (Pubitemid 46053795)
    • (2006) Insect Biochemistry and Molecular Biology , vol.36 , Issue.12 , pp. 921-933
    • Strickler-Dinglasan, P.M.1    Guz, N.2    Attardo, G.3    Aksoy, S.4
  • 75
    • 34447509457 scopus 로고    scopus 로고
    • Molecular aspects of transferrin expression in the tsetse fly (Glossina morsitans morsitans)
    • DOI 10.1016/j.jinsphys.2007.03.013, PII S0022191007000844
    • N. Guz, G.M. Attardo, Y. Wu, and S. Aksoy Molecular aspects of transferrin expression in the tsetse fly (Glossina morsitans morsitans) J. Insect Physiol. 53 2007 715 723 (Pubitemid 47069368)
    • (2007) Journal of Insect Physiology , vol.53 , Issue.7 , pp. 715-723
    • Guz, N.1    Attardo, G.M.2    Wu, Y.3    Aksoy, S.4
  • 76
    • 33748926247 scopus 로고    scopus 로고
    • Rhodnius prolixus: Identification of immune-related genes up-regulated in response to pathogens and parasites using suppressive subtractive hybridization
    • DOI 10.1016/j.dci.2006.05.008, PII S0145305X06000851
    • R.J. Ursic-Bedoya, and C.A. Lowenberger Rhodnius prolixus: identification of immune-related genes up-regulated in response to pathogens and parasites using suppressive subtractive hybridization Dev. Comp. Immunol. 31 2007 109 120 (Pubitemid 44436571)
    • (2007) Developmental and Comparative Immunology , vol.31 , Issue.2 , pp. 109-120
    • Ursic-Bedoya, R.J.1    Lowenberger, C.A.2
  • 79
    • 77951223590 scopus 로고    scopus 로고
    • Molecular characterization of two novel milk proteins in the tsetse fly (Glossina morsitans morsitans)
    • G. Yang, G.M. Attardo, C. Lohs, and S. Aksoy Molecular characterization of two novel milk proteins in the tsetse fly (Glossina morsitans morsitans) Insect Mol. Biol. 19 2010 253 262
    • (2010) Insect Mol. Biol. , vol.19 , pp. 253-262
    • Yang, G.1    Attardo, G.M.2    Lohs, C.3    Aksoy, S.4
  • 80
    • 1842800034 scopus 로고    scopus 로고
    • Proteomic analysis of the systemic immune response of Drosophila
    • DOI 10.1074/mcp.M300114-MCP200
    • F. Levy, P. Bulet, and L. Ehret-Sabatier Proteomic analysis of the systemic immune response of Drosophila Mol.Cell. Proteomics 3 2004 156 166 (Pubitemid 38714273)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.2 , pp. 156-166
    • Levy, F.1    Bulet, P.2    Ehret-Sabatier, L.3
  • 81
    • 1942470573 scopus 로고    scopus 로고
    • Cloning and expression of a putative transferrin cDNA of the spruce budworm, Choristoneura fumiferana
    • DOI 10.1016/j.ibmb.2004.03.002, PII S0965174804000359
    • D.R. Ampasala, S.C. Zheng, A. Retnakaran, P.J. Krell, B.M. Arif, and Q.L. Feng Cloning and expression of a putative transferrin cDNA of the spruce budworm, Choristoneura fumiferana Insect Biochem. Mol. Biol. 34 2004 493 500 (Pubitemid 38527146)
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , Issue.5 , pp. 493-500
    • Ampasala, D.R.1    Zheng, S.-C.2    Retnakaran, A.3    Krell, P.J.4    Arif, B.M.5    Feng, Q.-L.6
  • 82
    • 8344276855 scopus 로고    scopus 로고
    • Molecular cloning, nucleotide sequence and gene expression of a transferrin gene from the rice stem borer, Chilo suppressalis Walker (Lepidoptera: Crambidae)
    • DOI 10.1303/aez.2004.463
    • S. Sonoda, T. Maruyama, Y. Izumi, H. Yoshida, and H. Tsumuki Molecular cloning, nucleotide sequence and gene expression of a transferrin gene from the rice stem borer, Chilo suppressalis Walker (Lepidoptera: Crambidae) Appl. Entomol. Zool. (Jpn.) 39 2004 463 468 (Pubitemid 39474490)
    • (2004) Applied Entomology and Zoology , vol.39 , Issue.3 , pp. 463-468
    • Sonoda, S.1    Maruyama, T.2    Izumi, Y.3    Yoshida, H.4    Tsumuki, H.5
  • 84
    • 1942429543 scopus 로고    scopus 로고
    • Transcriptional profiling reveals multifunctional roles for transferrin in the honeybee, Apis mellifera
    • R. Kucharski, and R. Maleszka Transcriptional profiling reveals multifunctional roles for transferrin in the honeybee, Apis mellifera J.Insect Sci. 3 2003 27
    • (2003) J.Insect Sci. , vol.3 , pp. 27
    • Kucharski, R.1    Maleszka, R.2
  • 85
    • 33750460281 scopus 로고    scopus 로고
    • Insights into social insects from the genome of the honeybee Apis mellifera
    • H.G.S. Consortium Insights into social insects from the genome of the honeybee Apis mellifera Nature 443 2006 931 949
    • (2006) Nature , vol.443 , pp. 931-949
    • Consortium, H.G.S.1
  • 87
    • 24944515848 scopus 로고    scopus 로고
    • Solenopsis invicta transferrin: cDNA cloning, gene architecture, and up-regulation in response to Beauveria bassiana infection
    • DOI 10.1016/j.gene.2005.05.017, PII S0378111905002738
    • S.M. Valles, and R.M. Pereira Solenopsis invicta transferrin: cDNA cloning, gene architecture, and up-regulation in response to Beauveria bassiana infection Gene 358 2005 60 66 (Pubitemid 41306048)
    • (2005) Gene , vol.358 , Issue.1-2 , pp. 60-66
    • Valles, S.M.1    Pereira, R.M.2
  • 88
    • 43049163230 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a transferrin cDNA from the white-spotted flower chafer, Protaetia brevitarsis
    • DOI 10.1080/10425170701461854, PII 780443958
    • B.Y. Kim, K.S. Lee, Y.M. Choo, I. Kim, J.S. Hwang, H.D. Sohn, and B.R. Jin Molecular cloning and characterization of a transferrin cDNA from the white-spotted flower chafer, Protaetia brevitarsis DNA Seq. 19 2008 146 150 (Pubitemid 351640179)
    • (2008) DNA Sequence - Journal of DNA Sequencing and Mapping , vol.19 , Issue.2 , pp. 146-150
    • Kim, B.Y.1    Lee, K.S.2    Choo, Y.M.3    Kim, I.4    Hwang, J.S.5    Sohn, H.D.6    Jin, B.R.7
  • 90
    • 35348854423 scopus 로고    scopus 로고
    • Differentially-expressed glycoproteins in Locusta migratoria hemolymph infected with Metarhizium anisopliae
    • DOI 10.1016/j.jip.2007.05.012, PII S0022201107001139
    • C. Wang, Y. Cao, Z. Wang, Y. Yin, G. Peng, Z. Li, H. Zhao, and Y. Xia Differentially-expressed glycoproteins in Locusta migratoria hemolymph infected with Metarhizium anisopliae J. Invertebr. Pathol. 96 2007 230 236 (Pubitemid 47588289)
    • (2007) Journal of Invertebrate Pathology , vol.96 , Issue.3 , pp. 230-236
    • Wang, C.1    Cao, Y.2    Wang, Z.3    Yin, Y.4    Peng, G.5    Li, Z.6    Zhao, H.7    Xia, Y.8
  • 92
    • 77649141259 scopus 로고    scopus 로고
    • Genome sequence of the pea aphid Acyrthosiphon pisum
    • I.A.G. Consortium Genome sequence of the pea aphid Acyrthosiphon pisum PLoS Biol. 8 2010 e1000313
    • (2010) PLoS Biol. , vol.8 , pp. 1000313
    • Consortium, I.A.G.1
  • 93
    • 33745684283 scopus 로고    scopus 로고
    • Anopheles gambiae immune responses to human and rodent Plasmodium parasite species
    • Y. Dong, R. Aguilar, Z. Xi, E. Warr, E. Mongin, and G. Dimopoulos Anopheles gambiae immune responses to human and rodent Plasmodium parasite species PLoS Pathog. 2 2006 e52
    • (2006) PLoS Pathog. , vol.2 , pp. 52
    • Dong, Y.1    Aguilar, R.2    Xi, Z.3    Warr, E.4    Mongin, E.5    Dimopoulos, G.6
  • 96
    • 0025273929 scopus 로고
    • Secretory glycoproteins of the rat subcommissural organ are N-linked complex-type glycoproteins. Demonstration by combined use of lectins and specific glycosidases, and by the administration of Tunicamycin
    • H. Herrera, and E.M. Rodriguez Secretory glycoproteins of the rat subcommissural organ are N-linked complex-type glycoproteins. Demonstration by combined use of lectins and specific glycosidases, and by the administration of Tunicamycin Histochemistry 93 1990 607 615 (Pubitemid 20111561)
    • (1990) Histochemistry , vol.93 , Issue.6 , pp. 607-615
    • Herrera, H.1    Rodriguez, E.M.2
  • 97
    • 0026000557 scopus 로고
    • Isoprenoids and astroglial cell cycling: Diminished mevalonate availability and inhibition of dolichol-linked glycoprotein synthesis arrest cycling through distinct mechanisms
    • T.J. Langan, and M.C. Slater Isoprenoids and astroglial cell cycling: diminished mevalonate availability and inhibition of dolichol-linked glycoprotein synthesis arrest cycling through distinct mechanisms J. Cell. Physiol. 149 1991 284 292 (Pubitemid 21910191)
    • (1991) Journal of Cellular Physiology , vol.149 , Issue.2 , pp. 284-292
    • Langan, T.J.1    Slater, M.C.2
  • 98
    • 0026785696 scopus 로고
    • Evidence that the hamster tunicamycin resistance gene encodes UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase
    • X. Zhu, Y. Zeng, and M.A. Lehrman Evidence that the hamster tunicamycin resistance gene encodes UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1- phosphate transferase J. Biol. Chem. 267 1992 8895 8902
    • (1992) J. Biol. Chem. , vol.267 , pp. 8895-8902
    • Zhu, X.1    Zeng, Y.2    Lehrman, M.A.3
  • 99
    • 0030561519 scopus 로고    scopus 로고
    • Cockroach transferrin closely resembles vertebrate transferrins in its metal ion-binding properties: A spectroscopic study
    • DOI 10.1016/S0162-0134(96)00052-9, PII S0162013496000529
    • J.R. Gasdaska, J.H. Law, C.J. Bender, and P. Aisen Cockroach transferrin closely resembles vertebrate transferrins in its metal ion-binding properties: a spectroscopic study J. Inorg. Biochem. 64 1996 247 258 (Pubitemid 26374516)
    • (1996) Journal of Inorganic Biochemistry , vol.64 , Issue.4 , pp. 247-258
    • Gasdaska, J.R.1    Law, J.H.2    Bender, C.J.3    Aisen, P.4
  • 103
    • 0000691686 scopus 로고
    • Vacuolar apoferritin synthesis by the fat body of an insect (Calpodes ethlius)
    • M. Locke, C. Ketola-Pirie, H. Leung, and H. Nichol Vacuolar apoferritin synthesis by the fat body of an insect (Calpodes ethlius) J. Insect Physiol. 37 1991 297 309
    • (1991) J. Insect Physiol. , vol.37 , pp. 297-309
    • Locke, M.1    Ketola-Pirie, C.2    Leung, H.3    Nichol, H.4
  • 104
    • 0033230271 scopus 로고    scopus 로고
    • Secreted ferritin subunits are of two kinds in insects molecular cloning of cDNAs encoding two major subunits of secreted ferritin from Calpodes ethlius
    • DOI 10.1016/S0965-1748(99)00076-4, PII S0965174899000764
    • H. Nichol, and M. Locke Secreted ferritin subunits are of two kinds in insects molecular cloning of cDNAs encoding two major subunits of secreted ferritin from Calpodes ethlius Insect Biochem. Mol. Biol. 29 1999 999 1013 (Pubitemid 29510667)
    • (1999) Insect Biochemistry and Molecular Biology , vol.29 , Issue.11 , pp. 999-1013
    • Nichol, H.1    Locke, M.2
  • 106
    • 19444383537 scopus 로고    scopus 로고
    • Crystal structure of a secreted insect ferritin reveals a symmetrical arrangement of heavy and light chains
    • DOI 10.1016/j.jmb.2005.03.074, PII S002228360500375X
    • A.E. Hamburger, A.P.J. West, Z.A. Hamburger, P. Hamburger, and P.J. Bjorkman Crystal structure of a secreted insect ferritin reveals a symmetrical arrangement of heavy and light chains J. Mol. Biol. 349 2005 558 569 (Pubitemid 40724566)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.3 , pp. 558-569
    • Hamburger, A.E.1    West Jr., A.P.2    Hamburger, Z.A.3    Hamburger, P.4    Bjorkman, P.J.5
  • 107
    • 61749102565 scopus 로고    scopus 로고
    • Receptor-mediated uptake of ferritin-bound iron by human intestinal Caco-2 cells
    • S. Kalgaonkar, and B. Lonnerdal Receptor-mediated uptake of ferritin-bound iron by human intestinal Caco-2 cells J. Nutr. Biochem. 20 2009 304 311
    • (2009) J. Nutr. Biochem. , vol.20 , pp. 304-311
    • Kalgaonkar, S.1    Lonnerdal, B.2
  • 108
    • 64849087354 scopus 로고    scopus 로고
    • Expression profile of the iron-binding proteins transferrin and ferritin heavy chain subunit in the bumblebee Bombus ignitus
    • B.Y. Kim, K.S. Lee, H.J. Yoon, I. Kim, J. Li, H.D. Sohn, and B.R. Jin Expression profile of the iron-binding proteins transferrin and ferritin heavy chain subunit in the bumblebee Bombus ignitus Comp. Biochem. Physiol. B Biochem. Mol Biol. 153 2009 165 170
    • (2009) Comp. Biochem. Physiol. B Biochem. Mol Biol. , vol.153 , pp. 165-170
    • Kim, B.Y.1    Lee, K.S.2    Yoon, H.J.3    Kim, I.4    Li, J.5    Sohn, H.D.6    Jin, B.R.7
  • 109
    • 8844231742 scopus 로고    scopus 로고
    • Peptidomic and proteomic analyses of the systemic immune response of Drosophila
    • DOI 10.1016/j.biochi.2004.07.007, PII S0300908404001142
    • F. Levy, D. Rabel, M. Charlet, P. Bulet, J.A. Hoffmann, and L. Ehret-Sabatier Peptidomic and proteomic analyses of the systemic immune response of Drosophila Biochimie 86 2004 607 616 (Pubitemid 39535632)
    • (2004) Biochimie , vol.86 , Issue.9-10 , pp. 607-616
    • Levy, F.1    Rabel, D.2    Charlet, M.3    Bulet, P.4    Hoffmann, J.A.5    Ehret-Sabatier, L.6
  • 110
    • 0028854932 scopus 로고
    • Regional differences in late-onset iron deposition, ferritin, transferrin, astrocyte proliferation, and microglial activation after transient forebrain ischemia in rat brain
    • Y. Kondo, N. Ogawa, M. Asanuma, Z. Ota, and A. Mori Regional differences in late-onset iron deposition, ferritin, transferrin, astrocyte proliferation, and microglial activation after transient forebrain ischemia in rat brain J. Cereb. Blood Flow Metab. 15 1995 216 226
    • (1995) J. Cereb. Blood Flow Metab. , vol.15 , pp. 216-226
    • Kondo, Y.1    Ogawa, N.2    Asanuma, M.3    Ota, Z.4    Mori, A.5
  • 112
    • 40849086137 scopus 로고    scopus 로고
    • Identification and characterization of two novel lysozymes from Rhodnius prolixus, a vector of Chagas disease
    • R.J. Ursic-Bedoya, H. Nazzari, D. Cooper, O. Triana, M. Wolff, and C. Lowenberger Identification and characterization of two novel lysozymes from Rhodnius prolixus, a vector of Chagas disease J. Insect Physiol. 54 2008 593 603
    • (2008) J. Insect Physiol. , vol.54 , pp. 593-603
    • Ursic-Bedoya, R.J.1    Nazzari, H.2    Cooper, D.3    Triana, O.4    Wolff, M.5    Lowenberger, C.6
  • 113
    • 34047268684 scopus 로고    scopus 로고
    • The host defense of Drosophila melanogaster
    • DOI 10.1146/annurev.immunol.25.022106.141615
    • B. Lemaitre, and J. Hoffmann The host defense of Drosophila melanogaster Annu. Rev. Immunol. 25 2007 697 743 (Pubitemid 46697922)
    • (2007) Annual Review of Immunology , vol.25 , pp. 697-743
    • Lemaitre, B.1    Hoffmann, J.2
  • 116
    • 58549099123 scopus 로고    scopus 로고
    • Prolonged gene knockdown in the tsetse fly Glossina by feeding double stranded RNA
    • D.P. Walshe, S.M. Lehane, M.J. Lehane, and L.R. Haines Prolonged gene knockdown in the tsetse fly Glossina by feeding double stranded RNA Insect Mol. Biol. 18 2009 11 19
    • (2009) Insect Mol. Biol. , vol.18 , pp. 11-19
    • Walshe, D.P.1    Lehane, S.M.2    Lehane, M.J.3    Haines, L.R.4
  • 117
    • 77952794601 scopus 로고    scopus 로고
    • Molecular Cloning and Characterization of Transferrin from Wax Moth, Galleria mellonella
    • J. Han, K.-P. Nam, S. Seo, and C.-Y. Yun Molecular Cloning and Characterization of Transferrin from Wax Moth, Galleria mellonella Entomol. Res. 34 2004 139 145
    • (2004) Entomol. Res. , vol.34 , pp. 139-145
    • Han, J.1    Nam, K.-P.2    Seo, S.3    Yun, C.-Y.4
  • 121
    • 2442713832 scopus 로고    scopus 로고
    • GeneWise and Genomewise
    • DOI 10.1101/gr.1865504
    • E. Birney, M. Clamp, and R. Durbin GeneWise and Genomewise Genome Res. 14 2004 988 995 (Pubitemid 38660520)
    • (2004) Genome Research , vol.14 , Issue.5 , pp. 988-995
    • Birney, E.1    Clamp, M.2    Durbin, R.3
  • 123
    • 0037460964 scopus 로고    scopus 로고
    • Prediction of human protein function according to Gene Ontology categories
    • DOI 10.1093/bioinformatics/btg036
    • L.J. Jensen, R. Gupta, H.H. Staerfeldt, and S. Brunak Prediction of human protein function according to Gene Ontology categories Bioinformatics 19 2003 635 642 (Pubitemid 36417058)
    • (2003) Bioinformatics , vol.19 , Issue.5 , pp. 635-642
    • Jensen, L.J.1    Gupta, R.2    Staerfeldt, H.-H.3    Brunak, S.4
  • 125
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signalling interactions using short sequence motifs
    • DOI 10.1093/nar/gkg584
    • J.C. Obenauer, L.C. Cantley, and M.B. Yaffe Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs Nucleic Acids Res. 31 2003 3635 3641 (Pubitemid 37442212)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.