메뉴 건너뛰기




Volumn 110, Issue 51, 2013, Pages 20461-20466

Cytokine Spätzle binds to the Drosophila immunoreceptor Toll with a neurotrophin-like specificity and couples receptor activation

Author keywords

Crystallography; Isothermal titration calorimetry; Mass spectrometry; Spz ligand; Toll receptor

Indexed keywords

CYSTINE; CYTOKINE; GLYCAN; LEUCINE; MEMBRANE PROTEIN; NERVE GROWTH FACTOR; NEUROTROPHIN; NEUROTROPHIN RECEPTOR; NEUROTROPHIN RECEPTOR P75; SPZ PROTEIN; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG; DROSOPHILA PROTEIN; ENDOTOXIN; NERVE GROWTH FACTOR RECEPTOR; PROTEIN BINDING; SPATZLE PROTEIN, DROSOPHILA; TL PROTEIN, DROSOPHILA;

EID: 84890847576     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1317002110     Document Type: Article
Times cited : (32)

References (52)
  • 1
    • 0022189558 scopus 로고
    • Establishment of dorsal-Ventral polarity in the Drosophila embryo: The induction of polarity by the Toll gene product
    • Anderson KV, Bokla L, Nüsslein-Volhard C (1985) Establishment of dorsal-Ventral polarity in the Drosophila embryo: The induction of polarity by the Toll gene product. Cell 42(3):791-798.
    • (1985) Cell , vol.42 , Issue.3 , pp. 791-798
    • Anderson, K.V.1    Bokla, L.2    Nüsslein-Volhard, C.3
  • 2
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA (1996) The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86(6):973-983.
    • (1996) Cell , vol.86 , Issue.6 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 3
    • 0028922245 scopus 로고
    • Signals from the IL-1 receptor homolog, Toll, can activate an immune response in a Drosophila hemocyte cell line
    • Rosetto M, Engström Y, Baldari CT, Telford JL, Hultmark D (1995) Signals from the IL-1 receptor homolog, Toll, can activate an immune response in a Drosophila hemocyte cell line. Biochem Biophys Res Commun 209(1):111-116.
    • (1995) Biochem Biophys Res Commun , vol.209 , Issue.1 , pp. 111-116
    • Rosetto, M.1    Engström, Y.2    Baldari, C.T.3    Telford, J.L.4    Hultmark, D.5
  • 4
    • 71449095250 scopus 로고    scopus 로고
    • Toll-Dependent antimicrobial responses in Drosophila larval fat body require Spätzle secreted by haemocytes
    • Shia AK, et al. (2009) Toll-Dependent antimicrobial responses in Drosophila larval fat body require Spätzle secreted by haemocytes. J Cell Sci 122(Pt 24):4505-4515.
    • (2009) J Cell Sci , vol.122 , Issue.PART 24 , pp. 4505-4515
    • Shia, A.K.1
  • 5
    • 2442456719 scopus 로고    scopus 로고
    • Monomeric and polymeric gram-Negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway
    • Kaneko T, et al. (2004) Monomeric and polymeric gram-Negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway. Immunity 20(5):637-649.
    • (2004) Immunity , vol.20 , Issue.5 , pp. 637-649
    • Kaneko, T.1
  • 7
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R, Preston-Hurlburt P, Janeway CA, Jr. (1997) A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 388(6640): 394-397.
    • (1997) Nature , vol.388 , Issue.6640 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 8
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene
    • Poltorak A, et al. (1998) Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene. Science 282(5396):2085-2088.
    • (1998) Science , vol.282 , Issue.5396 , pp. 2085-2088
    • Poltorak, A.1
  • 10
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S, Uematsu S, Takeuchi O (2006) Pathogen recognition and innate immunity. Cell 124(4):783-801.
    • (2006) Cell , vol.124 , Issue.4 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 11
    • 42349090335 scopus 로고    scopus 로고
    • Structural basis of toll-Like receptor 3 signaling with doublestranded RNA
    • Liu L, et al. (2008) Structural basis of toll-Like receptor 3 signaling with doublestranded RNA. Science 320(5874):379-381.
    • (2008) Science , vol.320 , Issue.5874 , pp. 379-381
    • Liu, L.1
  • 12
    • 79959447465 scopus 로고    scopus 로고
    • Structural biology of the Toll-Like receptor family
    • Kang JY, Lee JO (2011) Structural biology of the Toll-Like receptor family. Annu Rev Biochem 80:917-941.
    • (2011) Annu Rev Biochem , vol.80 , pp. 917-941
    • Kang, J.Y.1    Lee, J.O.2
  • 13
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park BS, et al. (2009) The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 458(7242):1191-1195.
    • (2009) Nature , vol.458 , Issue.7242 , pp. 1191-1195
    • Park, B.S.1
  • 14
    • 0035140845 scopus 로고    scopus 로고
    • Multiple isoforms of the Drosophila Spätzle protein are encoded by alternatively spliced maternal mRNAs in the precellular blastoderm embryo
    • DeLotto Y, Smith C, DeLotto R (2001) Multiple isoforms of the Drosophila Spätzle protein are encoded by alternatively spliced maternal mRNAs in the precellular blastoderm embryo. Mol Gen Genet 264(5):643-652.
    • (2001) Mol Gen Genet , vol.264 , Issue.5 , pp. 643-652
    • Delotto, Y.1    Smith, C.2    Delotto, R.3
  • 15
    • 0028167111 scopus 로고
    • The spätzle gene encodes a component of the extracellular signaling pathway establishing the dorsal-Ventral pattern of the Drosophila embryo
    • Morisato D, Anderson KV (1994) The spätzle gene encodes a component of the extracellular signaling pathway establishing the dorsal-Ventral pattern of the Drosophila embryo. Cell 76(4):677-688.
    • (1994) Cell , vol.76 , Issue.4 , pp. 677-688
    • Morisato, D.1    Anderson, K.V.2
  • 16
    • 0028182623 scopus 로고
    • A processed form of the Spätzle protein defines dorsal-Ventral polarity in the Drosophila embryo
    • Schneider DS, Jin Y, Morisato D, Anderson KV (1994) A processed form of the Spätzle protein defines dorsal-Ventral polarity in the Drosophila embryo. Development 120(5): 1243-1250.
    • (1994) Development , vol.120 , Issue.5 , pp. 1243-1250
    • Schneider, D.S.1    Jin, Y.2    Morisato, D.3    Anderson, K.V.4
  • 17
    • 0032033030 scopus 로고    scopus 로고
    • Proteolytic processing of the Drosophila Spätzle protein by easter generates a dimeric NGF-Like molecule with ventralising activity
    • DeLotto Y, DeLotto R (1998) Proteolytic processing of the Drosophila Spätzle protein by easter generates a dimeric NGF-Like molecule with ventralising activity. Mech Dev 72(1-2):141-148.
    • (1998) Mech Dev , vol.72 , Issue.1-2 , pp. 141-148
    • Delotto, Y.1    Delotto, R.2
  • 18
    • 0032126433 scopus 로고    scopus 로고
    • Getting knotted: A model for the structure and activation of Spätzle
    • Mizuguchi K, Parker JS, Blundell TL, Gay NJ (1998) Getting knotted: A model for the structure and activation of Spätzle. Trends Biochem Sci 23(7):239-242.
    • (1998) Trends Biochem Sci , vol.23 , Issue.7 , pp. 239-242
    • Mizuguchi, K.1    Parker, J.S.2    Blundell, T.L.3    Gay, N.J.4
  • 19
    • 57749102799 scopus 로고    scopus 로고
    • Biophysical characterization of refolded Drosophila Spätzle, a cystine knot protein, reveals distinct properties of three isoforms
    • Hoffmann A, et al. (2008) Biophysical characterization of refolded Drosophila Spätzle, a cystine knot protein, reveals distinct properties of three isoforms. J Biol Chem 283(47):32598-32609.
    • (2008) J Biol Chem , vol.283 , Issue.47 , pp. 32598-32609
    • Hoffmann, A.1
  • 20
    • 77953493188 scopus 로고    scopus 로고
    • Molecular mechanism that induces activation of Spätzle, the ligand for the Drosophila Toll receptor
    • Arnot CJ, Gay NJ, Gangloff M (2010) Molecular mechanism that induces activation of Spätzle, the ligand for the Drosophila Toll receptor. J Biol Chem 285(25):19502-19509.
    • (2010) J Biol Chem , vol.285 , Issue.25 , pp. 19502-19509
    • Arnot, C.J.1    Gay, N.J.2    Gangloff, M.3
  • 21
    • 34250314533 scopus 로고    scopus 로고
    • Role of the Spatzle Pro-Domain in the generation of an active toll receptor ligand
    • Weber AN, et al. (2007) Role of the Spatzle Pro-Domain in the generation of an active toll receptor ligand. J Biol Chem 282(18):13522-13531.
    • (2007) J Biol Chem , vol.282 , Issue.18 , pp. 13522-13531
    • Weber, A.N.1
  • 22
    • 0041989575 scopus 로고    scopus 로고
    • Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling
    • Weber AN, et al. (2003) Binding of the Drosophila cytokine Spätzle to Toll is direct and establishes signaling. Nat Immunol 4(8):794-800.
    • (2003) Nat Immunol , vol.4 , Issue.8 , pp. 794-800
    • Weber, A.N.1
  • 23
    • 0842307067 scopus 로고    scopus 로고
    • Regulated assembly of the Toll signaling complex drives Drosophila dorsoventral patterning
    • Sun H, Towb P, Chiem DN, Foster BA, Wasserman SA (2004) Regulated assembly of the Toll signaling complex drives Drosophila dorsoventral patterning. EMBO J 23(1): 100-110.
    • (2004) EMBO J , vol.23 , Issue.1 , pp. 100-110
    • Sun, H.1    Towb, P.2    Chiem, D.N.3    Foster, B.A.4    Wasserman, S.A.5
  • 24
    • 0029002270 scopus 로고
    • Ventralization of the Drosophila embryo by deletion of extracellular leucine-Rich repeats in the Toll protein
    • Winans KA, Hashimoto C (1995) Ventralization of the Drosophila embryo by deletion of extracellular leucine-Rich repeats in the Toll protein. Mol Biol Cell 6(5):587-596.
    • (1995) Mol Biol Cell , vol.6 , Issue.5 , pp. 587-596
    • Winans, K.A.1    Hashimoto, C.2
  • 25
    • 79959536183 scopus 로고    scopus 로고
    • The ectodomain of the Toll-Like receptor 4 prevents constitutive receptor activation
    • Panter G, Jerala R (2011) The ectodomain of the Toll-Like receptor 4 prevents constitutive receptor activation. J Biol Chem 286(26):23334-23344.
    • (2011) J Biol Chem , vol.286 , Issue.26 , pp. 23334-23344
    • Panter, G.1    Jerala, R.2
  • 26
    • 0025804653 scopus 로고
    • Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal-Ventral polarity in the Drosophila embryo
    • Schneider DS, Hudson KL, Lin TY, Anderson KV (1991) Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal-Ventral polarity in the Drosophila embryo. Genes Dev 5(5):797-807.
    • (1991) Genes Dev , vol.5 , Issue.5 , pp. 797-807
    • Schneider, D.S.1    Hudson, K.L.2    Lin, T.Y.3    Anderson, K.V.4
  • 27
    • 3042645409 scopus 로고    scopus 로고
    • Multimerization and interaction of Toll and Spätzle in Drosophila
    • Hu X, Yagi Y, Tanji T, Zhou S, Ip YT (2004) Multimerization and interaction of Toll and Spätzle in Drosophila. Proc Natl Acad Sci USA 101(25):9369-9374.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.25 , pp. 9369-9374
    • Hu, X.1    Yagi, Y.2    Tanji, T.3    Zhou, S.4    Ip, Y.T.5
  • 28
    • 33748090945 scopus 로고    scopus 로고
    • Toll-Like receptors as molecular switches
    • Gay NJ, Gangloff M, Weber AN (2006) Toll-Like receptors as molecular switches. Nat Rev Immunol 6(9):693-698.
    • (2006) Nat Rev Immunol , vol.6 , Issue.9 , pp. 693-698
    • Gay, N.J.1    Gangloff, M.2    Weber, A.N.3
  • 29
    • 23044488902 scopus 로고    scopus 로고
    • The yin and yang of neurotrophin action
    • Lu B, Pang PT, Woo NH (2005) The yin and yang of neurotrophin action. Nat Rev Neurosci 6(8):603-614.
    • (2005) Nat Rev Neurosci , vol.6 , Issue.8 , pp. 603-614
    • Lu, B.1    Pang, P.T.2    Woo, N.H.3
  • 30
    • 79957576736 scopus 로고    scopus 로고
    • Regulation of neural process growth, elaboration and structural plasticity by NF-ÊB
    • Gutierrez H, Davies AM (2011) Regulation of neural process growth, elaboration and structural plasticity by NF-ÊB. Trends Neurosci 34(6):316-325.
    • (2011) Trends Neurosci , vol.34 , Issue.6 , pp. 316-325
    • Gutierrez, H.1    Davies, A.M.2
  • 31
    • 0034667635 scopus 로고    scopus 로고
    • NF-Kappa B signaling promotes both cell survival and neurite process formation in nerve growth factor-Stimulated PC12 cells
    • Foehr ED, et al. (2000) NF-Kappa B signaling promotes both cell survival and neurite process formation in nerve growth factor-Stimulated PC12 cells. J Neurosci 20(20): 7556-7563.
    • (2000) J Neurosci , vol.20 , Issue.20 , pp. 7556-7563
    • Foehr, E.D.1
  • 32
    • 0029869593 scopus 로고    scopus 로고
    • Selective activation of NF-Kappa B by nerve growth factor through the neurotrophin receptor p75
    • Carter BD, et al. (1996) Selective activation of NF-Kappa B by nerve growth factor through the neurotrophin receptor p75. Science 272(5261):542-545.
    • (1996) Science , vol.272 , Issue.5261 , pp. 542-545
    • Carter, B.D.1
  • 33
    • 49649094883 scopus 로고    scopus 로고
    • Crystal structure of the neurotrophin-3 and p75NTR symmetrical complex
    • Gong Y, Cao P, Yu HJ, Jiang T (2008) Crystal structure of the neurotrophin-3 and p75NTR symmetrical complex. Nature 454(7205):789-793.
    • (2008) Nature , vol.454 , Issue.7205 , pp. 789-793
    • Gong, Y.1    Cao, P.2    Yu, H.J.3    Jiang, T.4
  • 34
    • 33845695804 scopus 로고    scopus 로고
    • Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors
    • Wehrman T, et al. (2007) Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors. Neuron 53(1):25-38.
    • (2007) Neuron , vol.53 , Issue.1 , pp. 25-38
    • Wehrman, T.1
  • 35
    • 0033539065 scopus 로고    scopus 로고
    • Crystal structure of nerve growth factor in complex with the ligand-Binding domain of the TrkA receptor
    • Wiesmann C, Ultsch MH, Bass SH, de Vos AM (1999) Crystal structure of nerve growth factor in complex with the ligand-Binding domain of the TrkA receptor. Nature 401(6749):184-188.
    • (1999) Nature , vol.401 , Issue.6749 , pp. 184-188
    • Wiesmann, C.1    Ultsch, M.H.2    Bass, S.H.3    De Vos, A.M.4
  • 36
    • 2442434770 scopus 로고    scopus 로고
    • Structure of nerve growth factor complexed with the shared neurotrophin receptor p75
    • He XL, Garcia KC (2004) Structure of nerve growth factor complexed with the shared neurotrophin receptor p75. Science 304(5672):870-875.
    • (2004) Science , vol.304 , Issue.5672 , pp. 870-875
    • He, X.L.1    Garcia, K.C.2
  • 37
    • 84883449263 scopus 로고    scopus 로고
    • Toll-6 and Toll-7 function as neurotrophin receptors in the Drosophila melanogaster CNS
    • McIlroy G, et al. (2013) Toll-6 and Toll-7 function as neurotrophin receptors in the Drosophila melanogaster CNS. Nat Neurosci 16(9):1248-1256.
    • (2013) Nat Neurosci , vol.16 , Issue.9 , pp. 1248-1256
    • McIlroy, G.1
  • 38
    • 84859991798 scopus 로고    scopus 로고
    • Virus recognition by Toll-7 activates antiviral autophagy in Drosophila
    • Nakamoto M, et al. (2012) Virus recognition by Toll-7 activates antiviral autophagy in Drosophila. Immunity 36(4):658-667.
    • (2012) Immunity , vol.36 , Issue.4 , pp. 658-667
    • Nakamoto, M.1
  • 39
    • 84872153469 scopus 로고    scopus 로고
    • Functional insights from the crystal structure of the N-Terminal domain of the prototypical toll receptor
    • Gangloff M, Arnot CJ, Lewis M, Gay NJ (2013) Functional insights from the crystal structure of the N-Terminal domain of the prototypical toll receptor. Structure 21(1): 143-153.
    • (2013) Structure , vol.21 , Issue.1 , pp. 143-153
    • Gangloff, M.1    Arnot, C.J.2    Lewis, M.3    Gay, N.J.4
  • 40
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-Based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-Based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1
  • 41
    • 0035942252 scopus 로고    scopus 로고
    • Activation of a protease cascade involved in patterning the Drosophila embryo
    • LeMosy EK, Tan YQ, Hashimoto C (2001) Activation of a protease cascade involved in patterning the Drosophila embryo. Proc Natl Acad Sci USA 98(9):5055-5060.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.9 , pp. 5055-5060
    • Lemosy, E.K.1    Tan, Y.Q.2    Hashimoto, C.3
  • 42
    • 84860832650 scopus 로고    scopus 로고
    • Structural basis of species-Specific endotoxin sensing by innate immune receptor TLR4/MD-2
    • Ohto U, Fukase K, Miyake K, Shimizu T (2012) Structural basis of species-Specific endotoxin sensing by innate immune receptor TLR4/MD-2. Proc Natl Acad Sci USA 109(19):7421-7426.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.19 , pp. 7421-7426
    • Ohto, U.1    Fukase, K.2    Miyake, K.3    Shimizu, T.4
  • 43
    • 84857335818 scopus 로고    scopus 로고
    • Structural basis of TLR5-Flagellin recognition and signaling
    • Yoon SI, et al. (2012) Structural basis of TLR5-Flagellin recognition and signaling. Science 335(6070):859-864.
    • (2012) Science , vol.335 , Issue.6070 , pp. 859-864
    • Yoon, S.I.1
  • 44
    • 77950346220 scopus 로고    scopus 로고
    • Molecular and structural insight into proNGF engagement of p75NTR and sortilin
    • Feng D, et al. (2010) Molecular and structural insight into proNGF engagement of p75NTR and sortilin. J Mol Biol 396(4):967-984.
    • (2010) J Mol Biol , vol.396 , Issue.4 , pp. 967-984
    • Feng, D.1
  • 45
    • 34548222514 scopus 로고    scopus 로고
    • Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran
    • Kim HM, et al. (2007) Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell 130(5):906-917.
    • (2007) Cell , vol.130 , Issue.5 , pp. 906-917
    • Kim, H.M.1
  • 46
    • 20744451399 scopus 로고    scopus 로고
    • Ligand-Receptor and receptor-Receptor interactions act in concert to activate signaling in the Drosophila toll pathway
    • Weber AN, Moncrieffe MC, Gangloff M, Imler JL, Gay NJ (2005) Ligand-Receptor and receptor-Receptor interactions act in concert to activate signaling in the Drosophila toll pathway. J Biol Chem 280(24):22793-22799.
    • (2005) J Biol Chem , vol.280 , Issue.24 , pp. 22793-22799
    • Weber, A.N.1    Moncrieffe, M.C.2    Gangloff, M.3    Imler, J.L.4    Gay, N.J.5
  • 47
    • 47249114405 scopus 로고    scopus 로고
    • Structural insight into the mechanism of activation of the Toll receptor by the dimeric ligand Spätzle
    • Gangloff M, et al. (2008) Structural insight into the mechanism of activation of the Toll receptor by the dimeric ligand Spätzle. J Biol Chem 283(21):14629-14635.
    • (2008) J Biol Chem , vol.283 , Issue.21 , pp. 14629-14635
    • Gangloff, M.1
  • 48
    • 25844526398 scopus 로고    scopus 로고
    • Characterization of symmetric complexes of nerve growth factor and the ectodomain of the pan-Neurotrophin receptor, p75NTR
    • Aurikko JP, et al. (2005) Characterization of symmetric complexes of nerve growth factor and the ectodomain of the pan-Neurotrophin receptor, p75NTR. J Biol Chem 280(39):33453-33460.
    • (2005) J Biol Chem , vol.280 , Issue.39 , pp. 33453-33460
    • Aurikko, J.P.1
  • 49
    • 0025986121 scopus 로고
    • New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor
    • McDonald NQ, et al. (1991) New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor. Nature 354(6352):411-414.
    • (1991) Nature , vol.354 , Issue.6352 , pp. 411-414
    • McDonald, N.Q.1
  • 50
    • 56849126862 scopus 로고    scopus 로고
    • Drosophila neurotrophins reveal a common mechanism for nervous system formation
    • Zhu B, et al. (2008) Drosophila neurotrophins reveal a common mechanism for nervous system formation. PLoS Biol 6(11):e284.
    • (2008) PLoS Biol , vol.6 , Issue.11
    • Zhu, B.1
  • 51
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-Type catalytic proficiency
    • Kapust RB, et al. (2001) Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-Type catalytic proficiency. Protein Eng 14(12):993-1000.
    • (2001) Protein Eng , vol.14 , Issue.12 , pp. 993-1000
    • Kapust, R.B.1
  • 52
    • 0028789632 scopus 로고
    • Biochemical analysis of the N-Glycosylation pathway in baculovirus-Infected lepidopteran insect cells
    • Jarvis DL, Finn EE (1995) Biochemical analysis of the N-Glycosylation pathway in baculovirus-Infected lepidopteran insect cells. Virology 212(2):500-511.
    • (1995) Virology , vol.212 , Issue.2 , pp. 500-511
    • Jarvis, D.L.1    Finn, E.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.