메뉴 건너뛰기




Volumn 9, Issue 9, 2009, Pages 2457-2467

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

Author keywords

Acyrthosiphon pisum; Aphid; LC MS; MS; Phloem sap; Saliva

Indexed keywords

CHOLINE; CYSTEINE; DIPEPTIDYL CARBOXYPEPTIDASE; GLUCOSE; METALLOPROTEINASE; METHANOL; OXIDOREDUCTASE; PROTEOME; REGUCALCIN; SERINE; TYROSINE;

EID: 64849087712     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800692     Document Type: Article
Times cited : (213)

References (52)
  • 1
    • 20344387209 scopus 로고    scopus 로고
    • Exploring tick saliva: From biochemistry to 'sialomes' and functional genomics
    • Valenzuela, J. G., Exploring tick saliva: from biochemistry to 'sialomes' and functional genomics. Parasitology 2004, 729, S83-S94.
    • (2004) Parasitology , vol.729
    • Valenzuela, J.G.1
  • 2
    • 39849098637 scopus 로고    scopus 로고
    • Salivating for knowledge: Potential pharmacological agents in tick saliva
    • Hovius, J. W. R., Levi, M., Fikrig, E., Salivating for knowledge: potential pharmacological agents in tick saliva. PLoS Med. 2008, 5, e43.
    • (2008) PLoS Med , vol.5
    • Hovius, J.W.R.1    Levi, M.2    Fikrig, E.3
  • 3
    • 0027621486 scopus 로고
    • The salivary catechol oxidase/peroxidase activities of the mosquito Anopheles albimanus
    • Ribeiro, J. M., Nussenzveig, R. H., The salivary catechol oxidase/peroxidase activities of the mosquito Anopheles albimanus. J. Exp. Biol. 1993, 779, 273-287.
    • (1993) J. Exp. Biol , vol.779 , pp. 273-287
    • Ribeiro, J.M.1    Nussenzveig, R.H.2
  • 4
    • 0037208861 scopus 로고    scopus 로고
    • Role of arthropod saliva in blood feeding: Sialome and post-sialome perspectives
    • Ribeiro, J. M., Francischetti, I. M., Role of arthropod saliva in blood feeding: sialome and post-sialome perspectives. Annu. Rev. Entomol. 2003, 48, 73-88.
    • (2003) Annu. Rev. Entomol , vol.48 , pp. 73-88
    • Ribeiro, J.M.1    Francischetti, I.M.2
  • 5
    • 34848895497 scopus 로고    scopus 로고
    • Aegyptin, a novel mosquito salivary gland protein, specifically binds to collagen and prevents its interaction with platelet glycoprotein VI, integrin {alpha}2beta1, and von Will- ebrand factor
    • Calvo, E., Tokumasu, F., Marinotti, O., Villeval, J.-L. et al., Aegyptin, a novel mosquito salivary gland protein, specifically binds to collagen and prevents its interaction with platelet glycoprotein VI, integrin {alpha}2beta1, and von Will- ebrand factor. J. Biol. Chem. 2007, 282, 26928-26938.
    • (2007) J. Biol. Chem , vol.282 , pp. 26928-26938
    • Calvo, E.1    Tokumasu, F.2    Marinotti, O.3    Villeval, J.-L.4
  • 6
    • 0031401160 scopus 로고    scopus 로고
    • Evidence for chewing insect-specific molecular events distinct from a general wound response in leaves
    • Korth, K. L., Dixon, R. A., Evidence for chewing insect-specific molecular events distinct from a general wound response in leaves. Plant Physiol. 1997, 775, 1299-1305.
    • (1997) Plant Physiol , vol.775 , pp. 1299-1305
    • Korth, K.L.1    Dixon, R.A.2
  • 7
    • 13844296597 scopus 로고    scopus 로고
    • Maize genes induced by her- bivory and volicitin
    • Lawrence, S. D., Novak, N. G., Maize genes induced by her- bivory and volicitin. J. Chem. Ecol. 2004, 30, 2543-2557.
    • (2004) J. Chem. Ecol , vol.30 , pp. 2543-2557
    • Lawrence, S.D.1    Novak, N.G.2
  • 8
    • 44449179468 scopus 로고    scopus 로고
    • Plant Immunity to Insect Herbivores
    • Howe, G. A., Jander, G., Plant Immunity to Insect Herbivores. Annu. Rev. Plant Biol. 2008, 59, 41-66.
    • (2008) Annu. Rev. Plant Biol , vol.59 , pp. 41-66
    • Howe, G.A.1    Jander, G.2
  • 11
    • 37549023659 scopus 로고    scopus 로고
    • Annotated expressed sequence tags and xenobiotic detoxification in the aphid Myzus persicae (Sulzer)
    • Figueroa, C. C., Prunier-Leterme, N., Rispe, C., Sepulveda, F. et al., Annotated expressed sequence tags and xenobiotic detoxification in the aphid Myzus persicae (Sulzer). Insect Sci. 2007, 74, 29-45.
    • (2007) Insect Sci , vol.74 , pp. 29-45
    • Figueroa, C.C.1    Prunier-Leterme, N.2    Rispe, C.3    Sepulveda, F.4
  • 12
    • 33745056689 scopus 로고    scopus 로고
    • Large-scale gene discovery in the pea aphid Acyrthosiphon pisum (Hemiptera)
    • Sabater-Munozb, B., Legeai, F., Rispe, C., Bonhomme, J. et al., Large-scale gene discovery in the pea aphid Acyrthosiphon pisum (Hemiptera). Genome Biol. 2006, 7:R27.
    • (2006) Genome Biol , vol.7
    • Sabater-Munozb, B.1    Legeai, F.2    Rispe, C.3    Bonhomme, J.4
  • 13
    • 33750585000 scopus 로고    scopus 로고
    • RNAi knockout of a salivary transcript leading to lethality in the pea aphid, Acyrthosiphon pisum
    • [13] Mutti, N. S., Park, Y., Reese, J. C., Reeck, G. R., RNAi knockout of a salivary transcript leading to lethality in the pea aphid, Acyrthosiphon pisum. J. Insect Sci. 2006, 6,38.
    • (2006) J. Insect Sci , vol.6 , pp. 38
    • Mutti, N.S.1    Park, Y.2    Reese, J.C.3    Reeck, G.R.4
  • 14
    • 66249115516 scopus 로고    scopus 로고
    • Identification of aphid salivary proteins: A proteomic investigation of Myzus persicae
    • Harmel, N., Letocart, E., Cherqui, A., Giordanengo, P. etal., Identification of aphid salivary proteins: a proteomic investigation of Myzus persicae. Insect Mol Biol. 2008, 77, 165174.
    • (2008) Insect Mol Biol , vol.77 , pp. 165174
    • Harmel, N.1    Letocart, E.2    Cherqui, A.3    Giordanengo, P.4
  • 15
    • 0031937369 scopus 로고    scopus 로고
    • Mobility of salivary components as a possible reason for differences in response of alfalfa to the spotted alfalfa aphid and pea aphid
    • Madhusudhan, V. V., Miles, P. W., Mobility of salivary components as a possible reason for differences in response of alfalfa to the spotted alfalfa aphid and pea aphid. Entomol. Exp. Appl. 1998, 86, 25-39.
    • (1998) Entomol. Exp. Appl , vol.86 , pp. 25-39
    • Madhusudhan, V.V.1    Miles, P.W.2
  • 16
    • 0033921079 scopus 로고    scopus 로고
    • Salivary proteins of aphids: A pilot study on identification, separation and immunolocali-sation
    • Cherqui, A., Tjallingii, W. F., Salivary proteins of aphids: a pilot study on identification, separation and immunolocali-sation. J. Insect Physiol. 2000, 46, 1177-1186.
    • (2000) J. Insect Physiol , vol.46 , pp. 1177-1186
    • Cherqui, A.1    Tjallingii, W.F.2
  • 17
    • 0035059725 scopus 로고    scopus 로고
    • Effect of different host substrates on hemipteran salivary protein profiles
    • Habibi, J., Backus, E. A., Coudron, T. A., Brandt, S. L., Effect of different host substrates on hemipteran salivary protein profiles Entomol. Exp. Appl. 2001, 98, 369-375.
    • (2001) Entomol. Exp. Appl , vol.98 , pp. 369-375
    • Habibi, J.1    Backus, E.A.2    Coudron, T.A.3    Brandt, S.L.4
  • 18
    • 0000791348 scopus 로고
    • Protein toxicity to aphids-an in vitro test on Acyrthosiphon pisum
    • Rahbe, Y., Febvay, G., Protein toxicity to aphids-an in vitro test on Acyrthosiphon pisum. Entomol. Exp. Appl. 1993, 67, 149-160.
    • (1993) Entomol. Exp. Appl , vol.67 , pp. 149-160
    • Rahbe, Y.1    Febvay, G.2
  • 19
    • 33646742463 scopus 로고    scopus 로고
    • Sweet problems: Insect traits defining the limits to dietary sugar utilisation by the pea aphid, Acyrthosiphon pisum
    • Douglas, A. E., Price, D. R. G., Minto, L. B., Jones, E. etal., Sweet problems: insect traits defining the limits to dietary sugar utilisation by the pea aphid, Acyrthosiphon pisum. J. Exp. Biol. 2006, 209, 1395-1403.
    • (2006) J. Exp. Biol , vol.209 , pp. 1395-1403
    • Douglas, A.E.1    Price, D.R.G.2    Minto, L.B.3    Jones, E.4
  • 20
    • 85153993276 scopus 로고    scopus 로고
    • Yan, J. X., Wait, R., Berkelman, T., Harry, R. A, Westbrook, J. A. et al., A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrom- etry. Electrophoresis 2000, 77, 3666-3672.
    • Yan, J. X., Wait, R., Berkelman, T., Harry, R. A, Westbrook, J. A. et al., A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrom- etry. Electrophoresis 2000, 77, 3666-3672.
  • 21
    • 0000857494 scopus 로고
    • An approach to correlate MS/MS data to amino acid sequences in protein database
    • Eng, J. K., McCormack, A. L., Yates, J. R. III, An approach to correlate MS/MS data to amino acid sequences in protein database. J. Am. Soc. Mass Spectrom. 1994, 5, 976-989.
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 22
    • 0032849859 scopus 로고    scopus 로고
    • CAP3: A DNA sequence assembly program
    • Huang, X., Madan, A., CAP3: A DNA sequence assembly program. Genome Res. 1999, 9, 868-877.
    • (1999) Genome Res , vol.9 , pp. 868-877
    • Huang, X.1    Madan, A.2
  • 24
    • 25844453957 scopus 로고    scopus 로고
    • A proteomic analysis of salivary glands of female Anopheles gambiae mosquito
    • Kalume, D. E., Okulate, M., Zhong, J., Reddy, R. et al., A proteomic analysis of salivary glands of female Anopheles gambiae mosquito. Proteomics 2005, 5, 3765-3777.
    • (2005) Proteomics , vol.5 , pp. 3765-3777
    • Kalume, D.E.1    Okulate, M.2    Zhong, J.3    Reddy, R.4
  • 25
    • 0001205869 scopus 로고
    • Identification of electrically recorded curve patterns associated with aphid salivation and ingestion
    • McLean, D. L., Kinsey, M. G., Identification of electrically recorded curve patterns associated with aphid salivation and ingestion. Nature 1965, 205, 1130-1131.
    • (1965) Nature , vol.205 , pp. 1130-1131
    • McLean, D.L.1    Kinsey, M.G.2
  • 26
    • 33644929267 scopus 로고    scopus 로고
    • Salivary secretions by aphids interacting with proteins of phloem wound responses
    • Tjallingii, W. F., Salivary secretions by aphids interacting with proteins of phloem wound responses. J. Exp. Bot. 2006, 57, 739-745.
    • (2006) J. Exp. Bot , vol.57 , pp. 739-745
    • Tjallingii, W.F.1
  • 27
    • 33644890500 scopus 로고    scopus 로고
    • Physical and chemical interactions between aphids and plants
    • Will, T., van Bel, A. J. E., Physical and chemical interactions between aphids and plants. J. Exp. Bot. 2006, 57, 729-737.
    • (2006) J. Exp. Bot , vol.57 , pp. 729-737
    • Will, T.1    van Bel, A.J.E.2
  • 28
    • 0029041265 scopus 로고
    • Peptidyl dipeptidase A: Angiotensin I-converting enzyme
    • Corvol, P., Williams, T. A., Soubrier, F., Peptidyl dipeptidase A: angiotensin I-converting enzyme. Methods Enzymol. 1995, 24S, 283-305.
    • (1995) Methods Enzymol , vol.24 S , pp. 283-305
    • Corvol, P.1    Williams, T.A.2    Soubrier, F.3
  • 29
    • 0035186775 scopus 로고    scopus 로고
    • Isolation and expression of the ecdysteroid-inducible angiotensin- converting enzyme-related gene in wing discs of Bombyx mori
    • Quan, G. X., Mita, K., Okano, K., Shimada, T. etal., Isolation and expression of the ecdysteroid-inducible angiotensin- converting enzyme-related gene in wing discs of Bombyx mori. Insect Biochem. Mol. Biol. 2001, 31, 97-103.
    • (2001) Insect Biochem. Mol. Biol , vol.31 , pp. 97-103
    • Quan, G.X.1    Mita, K.2    Okano, K.3    Shimada, T.4
  • 30
    • 0036799146 scopus 로고    scopus 로고
    • Ance, a Drosophila angiotensin-converting enzyme homo- logue, is expressed in imaginal cells during metamorphosis and is regulated by the steroid, 20-hydroxyecdysone
    • Siviter, R. J., Taylor, C. A. M., Cotta, D. M., Denton, A. et al., Ance, a Drosophila angiotensin-converting enzyme homo- logue, is expressed in imaginal cells during metamorphosis and is regulated by the steroid, 20-hydroxyecdysone. Bio- chem. J. 2002, 367, 187-193.
    • (2002) Bio- chem. J , vol.367 , pp. 187-193
    • Siviter, R.J.1    Taylor, C.A.M.2    Cotta, D.M.3    Denton, A.4
  • 31
    • 0032520023 scopus 로고    scopus 로고
    • Anovel activity of insect peptidyl-dipeptidase A (angiotensin I-converting enzyme): The hydrolysis of lysyl-arginine and arginyl-arginine from the C-terminus of an insect pro- hormone peptide
    • Isaac, R., Schoofs, L., Williams, T. A., Veelaert, D. et al., Anovel activity of insect peptidyl-dipeptidase A (angiotensin I-converting enzyme): the hydrolysis of lysyl-arginine and arginyl-arginine from the C-terminus of an insect pro- hormone peptide. Biochem. J. 1998, 330, 61-65.
    • (1998) Biochem. J , vol.330 , pp. 61-65
    • Isaac, R.1    Schoofs, L.2    Williams, T.A.3    Veelaert, D.4
  • 32
    • 0030895982 scopus 로고    scopus 로고
    • Hydrolysis of insect neuropeptides by an angiotensin- converting enzyme from the housefly, Musca domestica
    • Lamango, N. S., Nachman, R. J., Hayes,T. K., Strey, A., Isaac, R. E., Hydrolysis of insect neuropeptides by an angiotensin- converting enzyme from the housefly, Musca domestica. Peptides 1997, 18, 47-52.
    • (1997) Peptides , vol.18 , pp. 47-52
    • Lamango, N.S.1    Nachman, R.J.2    Hayes, T.K.3    Strey, A.4    Isaac, R.E.5
  • 33
    • 38149020613 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme in Spo- doptera littoralis: Molecular characterization, expression and activity profile during development
    • Lemeire, E., Vanholme, B., Van Leeuwen, T., Van Camp, J., Smagghe, G., Angiotensin-converting enzyme in Spo- doptera littoralis: molecular characterization, expression and activity profile during development. Insect Biochem. Mol. Biol. 2008, 38,166-175.
    • (2008) Insect Biochem. Mol. Biol , vol.38 , pp. 166-175
    • Lemeire, E.1    Vanholme, B.2    Van Leeuwen, T.3    Van Camp, J.4    Smagghe, G.5
  • 34
    • 0037434846 scopus 로고    scopus 로고
    • Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril
    • Kim, H. M., Shin, D. R., Yoo, O. J., Lee, H., Lee, J. O., Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril. FEBS Lett. 2003, 538,65-70.
    • (2003) FEBS Lett , vol.538 , pp. 65-70
    • Kim, H.M.1    Shin, D.R.2    Yoo, O.J.3    Lee, H.4    Lee, J.O.5
  • 35
    • 0032473594 scopus 로고    scopus 로고
    • Immunocytochemical distribution of angiotensin I-con- verting enzyme like immunoreactivity in the brain and testis of insects
    • Schoofs, L., Veelaert, D., De Loof, A., Huybrechts, R., Isaac, E., Immunocytochemical distribution of angiotensin I-con- verting enzyme like immunoreactivity in the brain and testis of insects. Brain Res. 1998, 785, 215-227.
    • (1998) Brain Res , vol.785 , pp. 215-227
    • Schoofs, L.1    Veelaert, D.2    De Loof, A.3    Huybrechts, R.4    Isaac, E.5
  • 36
    • 2442530754 scopus 로고    scopus 로고
    • Zinc-metalloproteases in insects: ACE and ECE
    • Macours, N., Hens, K., Zinc-metalloproteases in insects: ACE and ECE. Insect Biochem. Mol. Biol. 2004, 34, 501-510.
    • (2004) Insect Biochem. Mol. Biol , vol.34 , pp. 501-510
    • Macours, N.1    Hens, K.2
  • 37
    • 8444241618 scopus 로고    scopus 로고
    • Identification of the most abundant secreted proteins from the salivary glands of the sand fly Lutzomyia longipalpis, vector of Leishmania chagasi
    • Valenzuela, J. G., Garfield, M., Rowton, E. D., Pham, V. M., Identification of the most abundant secreted proteins from the salivary glands of the sand fly Lutzomyia longipalpis, vector of Leishmania chagasi. J. Exp. Biol. 2004, 207, 3717-3729.
    • (2004) J. Exp. Biol , vol.207 , pp. 3717-3729
    • Valenzuela, J.G.1    Garfield, M.2    Rowton, E.D.3    Pham, V.M.4
  • 38
    • 27744513868 scopus 로고    scopus 로고
    • An updated catalogue of salivary gland transcripts in the adult female mosquito, Anopheles gambiae
    • Arca, B., Lombardo, F., Valenzuela, J. G., Francischetti, I. M. et al., An updated catalogue of salivary gland transcripts in the adult female mosquito, Anopheles gambiae. J. Exp. Biol. 2005, 208,3971-3986.
    • (2005) J. Exp. Biol , vol.208 , pp. 3971-3986
    • Arca, B.1    Lombardo, F.2    Valenzuela, J.G.3    Francischetti, I.M.4
  • 39
    • 40749097363 scopus 로고    scopus 로고
    • A family of putative metalloproteases in the salivary glands of the tick Ixodes ricinus
    • Decrem, Y., Beaufays, J., Blasioli, V., Lahaye, K. et al.,A family of putative metalloproteases in the salivary glands of the tick Ixodes ricinus. FEBS J. 2008, 275, 1485-1499.
    • (2008) FEBS J , vol.275 , pp. 1485-1499
    • Decrem, Y.1    Beaufays, J.2    Blasioli, V.3    Lahaye, K.4
  • 40
    • 0037904919 scopus 로고    scopus 로고
    • Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin(ogin)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis. Biochem. Bio- phys
    • Francischetti, I. M., Mather, T. N., Ribeiro, J. M., Cloning of a salivary gland metalloprotease and characterization of gelatinase and fibrin(ogin)lytic activities in the saliva of the Lyme disease tick vector Ixodes scapularis. Biochem. Bio- phys. Res. Commun. 2003, 305, 869-875.
    • (2003) Res. Commun , vol.305 , pp. 869-875
    • Francischetti, I.M.1    Mather, T.N.2    Ribeiro, J.M.3
  • 41
    • 33644926728 scopus 로고    scopus 로고
    • Phloem sap proteins: Their identities and potential roles in the interactions between plants and phloem-feeding insects
    • Kehr, J., Phloem sap proteins: their identities and potential roles in the interactions between plants and phloem-feeding insects. J. Exp. Bot. 2006, 57, 767-774.
    • (2006) J. Exp. Bot , vol.57 , pp. 767-774
    • Kehr, J.1
  • 42
    • 0026544690 scopus 로고
    • A newly defined family of homologous proteins with diverse catalytic activities
    • Cavener, D. R., GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities. J. Mol. Biol. 1992, 223, 811-814.
    • (1992) J. Mol. Biol , vol.223 , pp. 811-814
    • Cavener, D.1    GMC oxidoreductases, R.2
  • 45
    • 51249167470 scopus 로고
    • The significance of antioxidants in the aphid-plant interaction: The redox hypothesis
    • Miles, P. W., Oertli, J. J., The significance of antioxidants in the aphid-plant interaction: the redox hypothesis. Entomol. Exp. Appl. 1993, 67, 285-273.
    • (1993) Entomol. Exp. Appl , vol.67 , pp. 285-273
    • Miles, P.W.1    Oertli, J.J.2
  • 46
    • 0002931974 scopus 로고
    • Enhancement of phloem exudation from cut petioles by chelating-agents
    • King, R. W., Zeevaart, J. A., Enhancement of phloem exudation from cut petioles by chelating-agents. Plant Physiol. 1974, 53, 96-103.
    • (1974) Plant Physiol , vol.53 , pp. 96-103
    • King, R.W.1    Zeevaart, J.A.2
  • 48
    • 0035018617 scopus 로고    scopus 로고
    • Reversible calcium-regulated stopcocks in legume sieve tubes
    • Knoblauch, M., Peters, S. W., Ehlers, K., van Bel, A. J. E., Reversible calcium-regulated stopcocks in legume sieve tubes. The Plant Cell2001, 13, 1221-1230.
    • (2001) The Plant Cell , vol.13 , pp. 1221-1230
    • Knoblauch, M.1    Peters, S.W.2    Ehlers, K.3    van Bel, A.J.E.4
  • 49
    • 0141886923 scopus 로고    scopus 로고
    • ATP- independent contractile proteins from plants
    • Knoblauch, M., Noll, G. A., Mueller, T., Pruefer, D. etal., ATP- independent contractile proteins from plants. Nat. Mats. 2003, 2, 600-603.
    • (2003) Nat. Mats , vol.2 , pp. 600-603
    • Knoblauch, M.1    Noll, G.A.2    Mueller, T.3    Pruefer, D.4
  • 50
    • 0034089719 scopus 로고    scopus 로고
    • Expression of Drosophila homologue of senescence marker protein-30 during cold acclimation
    • Goto, S. G., Expression of Drosophila homologue of senescence marker protein-30 during cold acclimation. J. Insect Physiol. 2000, 46, 1111-1120.
    • (2000) J. Insect Physiol , vol.46 , pp. 1111-1120
    • Goto, S.G.1
  • 51
    • 19644384999 scopus 로고    scopus 로고
    • Role of regucalcin in maintaining cell homeostasis and function
    • Yamaguchi, M., Role of regucalcin in maintaining cell homeostasis and function. Int. J. Mol. Med. 2005, 15, 371389.
    • (2005) Int. J. Mol. Med , vol.15 , pp. 371389
    • Yamaguchi, M.1
  • 52
    • 41549095761 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of regucalcin in disk abalone (Haliotis discus discus): Intramuscular calcium administration stimulates the regucalcin mRNA expression
    • Nikapitiya, C., De Zoysa, M., Kang, H. S., Oh, C., Whang, I., Lee, J., Molecular characterization and expression analysis of regucalcin in disk abalone (Haliotis discus discus): Intramuscular calcium administration stimulates the regucalcin mRNA expression. Comp. Biochem. Physiol. B Biochem Mol. Biol. 2008, 150, 117-124.
    • (2008) Comp. Biochem. Physiol. B Biochem Mol. Biol , vol.150 , pp. 117-124
    • Nikapitiya, C.1    De Zoysa, M.2    Kang, H.S.3    Oh, C.4    Whang, I.5    Lee, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.