메뉴 건너뛰기




Volumn 122, Issue 18, 2009, Pages 3414-3423

The conserved metalloprotease invadolysin localizes to the surface of lipid droplets

Author keywords

Invadolysin; Lipid droplets; Metalloprotease; Phylogeny

Indexed keywords

FAT DROPLET; INVADOLYSIN; METALLOPROTEINASE; TRIACYLGLYCEROL; UNCLASSIFIED DRUG;

EID: 70350418642     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.044610     Document Type: Article
Times cited : (24)

References (62)
  • 2
    • 2942722569 scopus 로고    scopus 로고
    • Prostaglandin E2 inhibits alveolar macrophage phagocytosis through an E-prostanoid 2 receptor-mediated increase in intracellular cyclic AMP
    • Aronoff, D. M., Canetti, C. and Peters-Golden, M. (2004). Prostaglandin E2 inhibits alveolar macrophage phagocytosis through an E-prostanoid 2 receptor-mediated increase in intracellular cyclic AMP. J. Immunol. 173, 559-565.
    • (2004) J. Immunol , vol.173 , pp. 559-565
    • Aronoff, D.M.1    Canetti, C.2    Peters-Golden, M.3
  • 7
    • 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. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0030903768 scopus 로고    scopus 로고
    • Post-translational regulation of perilipin expression: Stabilization by stored intracellular neutral lipids
    • Brasaemle, D. L., Barber, T., Kimmel, A. R. and Londos, C. (1997). Post-translational regulation of perilipin expression: stabilization by stored intracellular neutral lipids. J. Biol. Chem. 272, 9378-9387.
    • (1997) J. Biol. Chem , vol.272 , pp. 9378-9387
    • Brasaemle, D.L.1    Barber, T.2    Kimmel, A.R.3    Londos, C.4
  • 9
    • 33748598240 scopus 로고    scopus 로고
    • The lipid-droplet proteome reveals that droplets are a protein-storage depot
    • Cermelli, S., Guo, Y., Gross, S. P. and Welte, M. A. (2006). The lipid-droplet proteome reveals that droplets are a protein-storage depot. Curr. Biol. 16, 1783-1795.
    • (2006) Curr. Biol , vol.16 , pp. 1783-1795
    • Cermelli, S.1    Guo, Y.2    Gross, S.P.3    Welte, M.A.4
  • 10
    • 48349107532 scopus 로고    scopus 로고
    • Lipid bodies in innate immune response to bacterial and parasite infections
    • D'Avila, H., Maya-Monteiro, C. M. and Bozza, P. T. (2008). Lipid bodies in innate immune response to bacterial and parasite infections. Int. Immunopharmacol. 8, 1308-1315.
    • (2008) Int. Immunopharmacol , vol.8 , pp. 1308-1315
    • D'Avila, H.1    Maya-Monteiro, C.M.2    Bozza, P.T.3
  • 11
    • 0026516594 scopus 로고
    • Identification of a surface metalloproteinase on 13 species of Leishmania isolated from humans, Crithidia fasciculata, and Herpetomonas samuelpessoai
    • Etges, R. (1992). Identification of a surface metalloproteinase on 13 species of Leishmania isolated from humans, Crithidia fasciculata, and Herpetomonas samuelpessoai. Acta Trop. 50, 205-217.
    • (1992) Acta Trop , vol.50 , pp. 205-217
    • Etges, R.1
  • 12
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni, J. V. and Neel, B. G. (1993). Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal. Biochem. 210, 179-187.
    • (1993) Anal. Biochem , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 13
    • 0035809931 scopus 로고    scopus 로고
    • Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell
    • Fujimoto, T., Kogo, H., Ishiguro, K., Tauchi, K. and Nomura, R. (2001). Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell. J. Cell Biol. 152, 1079-1085.
    • (2001) J. Cell Biol , vol.152 , pp. 1079-1085
    • Fujimoto, T.1    Kogo, H.2    Ishiguro, K.3    Tauchi, K.4    Nomura, R.5
  • 14
    • 0033602721 scopus 로고    scopus 로고
    • Architectural dynamics of F-actin in eupodia suggests their role in invasive locomotion in Dictyostelium
    • Fukui, Y., de Hostos, E., Yumura, S., Kitanishi-Yumura, T. and Inou. (1999). Architectural dynamics of F-actin in eupodia suggests their role in invasive locomotion in Dictyostelium. Exp. Cell Res. 249, 33-45.
    • (1999) Exp. Cell Res , vol.249 , pp. 33-45
    • Fukui, Y.1    de Hostos, E.2    Yumura, S.3    Kitanishi-Yumura, T.4    Inou5
  • 15
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Rüth, F. X. (2003). Structural aspects of the metzincin clan of metalloendopeptidases. Mol. Biotechnol. 24, 157-202.
    • (2003) Mol. Biotechnol , vol.24 , pp. 157-202
    • Gomis-Rüth, F.X.1
  • 16
    • 34249984767 scopus 로고    scopus 로고
    • Pollen tube growth: Coping with mechanical obstacles involves the cytoskeleton
    • Gossot, O. and Geitmann, A. (2007). Pollen tube growth: coping with mechanical obstacles involves the cytoskeleton. Planta 226, 405-416.
    • (2007) Planta , vol.226 , pp. 405-416
    • Gossot, O.1    Geitmann, A.2
  • 17
    • 49049119273 scopus 로고    scopus 로고
    • Caveolin-1 in cell polarization and directional migration
    • Grande-Garcia, A. and del Pozo, M. A. (2008). Caveolin-1 in cell polarization and directional migration. Eur. J. Cell Biol. 87, 641-647.
    • (2008) Eur. J. Cell Biol , vol.87 , pp. 641-647
    • Grande-Garcia, A.1    del Pozo, M.A.2
  • 19
    • 0034983018 scopus 로고    scopus 로고
    • Function and assembly of the Leishmania surface coat
    • Ilgoutz, S. C. and McConville, M. J. (2001). Function and assembly of the Leishmania surface coat. Int. J. Parasitol. 31, 899-908.
    • (2001) Int. J. Parasitol , vol.31 , pp. 899-908
    • Ilgoutz, S.C.1    McConville, M.J.2
  • 23
    • 0026523791 scopus 로고
    • Primary structure and expression of a gamete lytic enzyme in Chlamydomonas reinhardtii: Similarity of functional domains to matrix metalloproteases
    • Kinoshita, T., Fukuzawa, H., Shimada, T., Saito, T. and Matsuda, Y. (1992). Primary structure and expression of a gamete lytic enzyme in Chlamydomonas reinhardtii: similarity of functional domains to matrix metalloproteases. Proc. Natl. Acad. Sci. USA 89, 4693-4697.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4693-4697
    • Kinoshita, T.1    Fukuzawa, H.2    Shimada, T.3    Saito, T.4    Matsuda, Y.5
  • 24
    • 0034819564 scopus 로고    scopus 로고
    • Grass group I pollen allergens (beta-expansins) lack proteinase activity and do not cause wall loosening via proteolysis
    • Li, L. C. and Cosgrove, D. J. (2001). Grass group I pollen allergens (beta-expansins) lack proteinase activity and do not cause wall loosening via proteolysis. Eur. J. Biochem. 268, 4217-4226.
    • (2001) Eur. J. Biochem , vol.268 , pp. 4217-4226
    • Li, L.C.1    Cosgrove, D.J.2
  • 25
    • 21044433334 scopus 로고    scopus 로고
    • Podosomes at a glance
    • Linder, S. and Kopp, P. (2005). Podosomes at a glance. J. Cell Sci. 118, 2079-2082.
    • (2005) J. Cell Sci , vol.118 , pp. 2079-2082
    • Linder, S.1    Kopp, P.2
  • 26
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: A new challenge for proteomics
    • López-Otín, C. and Overall, C. M. (2002). Protease degradomics: a new challenge for proteomics. Nat. Rev. Mol. Cell Biol. 3, 509-519.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 509-519
    • López-Otín, C.1    Overall, C.M.2
  • 27
    • 33745619232 scopus 로고    scopus 로고
    • Cell biology: Podosomes and invadopodia help mobile cells step lively
    • Marx, J. (2006). Cell biology: podosomes and invadopodia help mobile cells step lively. Science 312, 1868-1869.
    • (2006) Science , vol.312 , pp. 1868-1869
    • Marx, J.1
  • 28
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • McConville, M. J. and Ferguson, M. A. (1993). The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem. J. 294, 305-324.
    • (1993) Biochem. J , vol.294 , pp. 305-324
    • McConville, M.J.1    Ferguson, M.A.2
  • 29
    • 9444240314 scopus 로고    scopus 로고
    • Invadolysin: A novel, conserved metalloprotease links mitotic structural rearrangements with cell migration
    • McHugh, B., Krause, S. A., Yu, B., Deans, A. M., Heasman, S., McLaughlin, P. and Heck, M. M. (2004). Invadolysin: a novel, conserved metalloprotease links mitotic structural rearrangements with cell migration. J. Cell Biol. 167, 673-686.
    • (2004) J. Cell Biol , vol.167 , pp. 673-686
    • McHugh, B.1    Krause, S.A.2    Yu, B.3    Deans, A.M.4    Heasman, S.5    McLaughlin, P.6    Heck, M.M.7
  • 31
    • 0034903123 scopus 로고    scopus 로고
    • The biogenesis and functions of lipid bodies in animals, plants and microorganisms
    • Murphy, D. J. (2001). The biogenesis and functions of lipid bodies in animals, plants and microorganisms. Prog. Lipid Res. 40, 325-438.
    • (2001) Prog. Lipid Res , vol.40 , pp. 325-438
    • Murphy, D.J.1
  • 32
    • 38849166022 scopus 로고    scopus 로고
    • 2 and the sulfonylurea drug, glimepiride, in rat adipocytes
    • 2 and the sulfonylurea drug, glimepiride, in rat adipocytes. Biochemistry 47, 1274-1287.
    • (2008) Biochemistry , vol.47 , pp. 1274-1287
    • Müller, G.1    Over, S.2    Wied, S.3    Frick, W.4
  • 34
    • 0005292810 scopus 로고
    • Role of proteolytic enzymes in biological regulation (a review)
    • Neurath, H. and Walsh, K. A. (1976). Role of proteolytic enzymes in biological regulation (a review). Proc. Natl. Acad. Sci. USA 73, 3825-3832.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3825-3832
    • Neurath, H.1    Walsh, K.A.2
  • 35
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G. and Heringa, J. (2000). T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217.
    • (2000) J. Mol. Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 36
    • 27544441823 scopus 로고    scopus 로고
    • Fixation and permeabilization protocol is critical for the immunolabeling of lipid droplet proteins
    • Ohsaki, Y., Maeda, T. and Fujimoto, T. (2005). Fixation and permeabilization protocol is critical for the immunolabeling of lipid droplet proteins. Histochem. Cell Biol. 124, 445-452.
    • (2005) Histochem. Cell Biol , vol.124 , pp. 445-452
    • Ohsaki, Y.1    Maeda, T.2    Fujimoto, T.3
  • 37
    • 33744755382 scopus 로고    scopus 로고
    • Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B
    • Ohsaki, Y., Cheng, J., Fujita, A., Tokumoto, T. and Fujimoto, T. (2006). Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B. Mol. Biol. Cell 17, 2674-2683.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2674-2683
    • Ohsaki, Y.1    Cheng, J.2    Fujita, A.3    Tokumoto, T.4    Fujimoto, T.5
  • 38
    • 0031750101 scopus 로고    scopus 로고
    • Filipin-dependent inhibition of cholera toxin: Evidence for toxin internalization and activation through caveolae-like domains
    • Orlandi, P. A. and Fishman, P. H. (1998). Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains. J. Cell Biol. 141, 905-915.
    • (1998) J. Cell Biol , vol.141 , pp. 905-915
    • Orlandi, P.A.1    Fishman, P.H.2
  • 39
    • 0035809923 scopus 로고    scopus 로고
    • Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets
    • Ostermeyer, A. G., Paci, J. M., Zeng, Y., Lublin, D. M., Munro, S. and Brown, D. A. (2001). Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets. J. Cell Biol. 152, 1071-1078.
    • (2001) J. Cell Biol , vol.152 , pp. 1071-1078
    • Ostermeyer, A.G.1    Paci, J.M.2    Zeng, Y.3    Lublin, D.M.4    Munro, S.5    Brown, D.A.6
  • 40
    • 0346099345 scopus 로고    scopus 로고
    • Dynamic and regulated association of caveolin with lipid bodies: Modulation of lipid body motility and function by a dominant negative mutant
    • Pol, A., Martin, S., Fernandez, M. A., Ferguson, C., Carozzi, A., Luetterforst, R., Enrich, C. and Parton, R. G. (2004). Dynamic and regulated association of caveolin with lipid bodies: modulation of lipid body motility and function by a dominant negative mutant. Mol. Biol. Cell 15, 99-110.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 99-110
    • Pol, A.1    Martin, S.2    Fernandez, M.A.3    Ferguson, C.4    Carozzi, A.5    Luetterforst, R.6    Enrich, C.7    Parton, R.G.8
  • 41
    • 0037350449 scopus 로고    scopus 로고
    • Real-time analysis of clathrin-mediated endocytosis during cell migration
    • Rappoport, J. Z. and Simon, S. M. (2003). Real-time analysis of clathrin-mediated endocytosis during cell migration. J. Cell Sci. 116, 847-855.
    • (2003) J. Cell Sci , vol.116 , pp. 847-855
    • Rappoport, J.Z.1    Simon, S.M.2
  • 43
    • 2942699852 scopus 로고    scopus 로고
    • Yeast genetics targets lipids in Parkinson's disease
    • Scherzer, C. R. and Feany, M. B. (2004). Yeast genetics targets lipids in Parkinson's disease. Trends Genet. 20, 273-277.
    • (2004) Trends Genet , vol.20 , pp. 273-277
    • Scherzer, C.R.1    Feany, M.B.2
  • 44
    • 0032529002 scopus 로고    scopus 로고
    • The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63)
    • Schlagenhauf, E., Etges, R. and Metcalf, P. (1998). The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63). Structure 6, 1035-1046.
    • (1998) Structure , vol.6 , pp. 1035-1046
    • Schlagenhauf, E.1    Etges, R.2    Metcalf, P.3
  • 45
    • 37348999201 scopus 로고    scopus 로고
    • Lessons from "lower" organisms: What worms, flies, and zebrafish can teach us about human energy metabolism
    • Schlegel, A. and Stainier, D. Y. (2007). Lessons from "lower" organisms: what worms, flies, and zebrafish can teach us about human energy metabolism. PLoS Genet. 3, e199.
    • (2007) PLoS Genet , vol.3
    • Schlegel, A.1    Stainier, D.Y.2
  • 46
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: Maximum likelihood phylogenetic analysis using quartets and parallel computing
    • Schmidt, H. A., Strimmer, K., Vingron, M. and von Haeseler, A. (2002). TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing. Bioinformatics 18, 502-504.
    • (2002) Bioinformatics , vol.18 , pp. 502-504
    • Schmidt, H.A.1    Strimmer, K.2    Vingron, M.3    von Haeseler, A.4
  • 48
    • 33646144117 scopus 로고    scopus 로고
    • ATGL has a key role in lipid droplet/ adiposome degradation in mammalian cells
    • Smirnova, E., Goldberg, E. B., Makarova, K. S., Lin, L., Brown, W. J. and Jackson, C. L. (2006). ATGL has a key role in lipid droplet/ adiposome degradation in mammalian cells. EMBO Rep. 7, 106-113.
    • (2006) EMBO Rep , vol.7 , pp. 106-113
    • Smirnova, E.1    Goldberg, E.B.2    Makarova, K.S.3    Lin, L.4    Brown, W.J.5    Jackson, C.L.6
  • 49
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding, J., Biegert, A. and Lupas, A. N. (2005). The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244-W248.
    • (2005) Nucleic Acids Res , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 51
    • 0037903214 scopus 로고    scopus 로고
    • Live cell analysis and targeting of the lipid droplet-binding adipocyte differentiation-related protein
    • Targett-Adams, P., Chambers, D., Gledhill, S., Hope, R. G., Coy, J. F., Girod, A. and McLauchlan, J. (2003). Live cell analysis and targeting of the lipid droplet-binding adipocyte differentiation-related protein. J. Biol. Chem. 278, 15998-16007.
    • (2003) J. Biol. Chem , vol.278 , pp. 15998-16007
    • Targett-Adams, P.1    Chambers, D.2    Gledhill, S.3    Hope, R.G.4    Coy, J.F.5    Girod, A.6    McLauchlan, J.7
  • 52
    • 0141672132 scopus 로고    scopus 로고
    • Drosophila Perilipin/ADRP homologue Lsd2 regulates lipid metabolism
    • Teixeira, L., Rabouille, C., Rorth, P., Ephrussi, A. and Vanzo, N. F. (2003). Drosophila Perilipin/ADRP homologue Lsd2 regulates lipid metabolism. Mech. Dev. 120, 1071-1081.
    • (2003) Mech. Dev , vol.120 , pp. 1071-1081
    • Teixeira, L.1    Rabouille, C.2    Rorth, P.3    Ephrussi, A.4    Vanzo, N.F.5
  • 53
    • 47149111389 scopus 로고    scopus 로고
    • Cell biology of lipid droplets
    • Thiele, C. and Spandl, J. (2008). Cell biology of lipid droplets. Curr. Opin. Cell Biol. 20, 378-385.
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 378-385
    • Thiele, C.1    Spandl, J.2
  • 54
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 55
    • 22544449852 scopus 로고    scopus 로고
    • Single-cell Raman and fluorescence microscopy reveal the association of lipid bodies with phagosomes in leukocytes
    • van Manen, H. J., Kraan, Y. M., Roos, D. and Otto, C. (2005). Single-cell Raman and fluorescence microscopy reveal the association of lipid bodies with phagosomes in leukocytes. Proc. Natl. Acad. Sci. USA 102, 10159-10164.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10159-10164
    • van Manen, H.J.1    Kraan, Y.M.2    Roos, D.3    Otto, C.4
  • 56
    • 18944391677 scopus 로고    scopus 로고
    • Neutral lipid bodies in prokaryotes: Recent insights into structure, formation, and relationship to eukaryotic lipid depots
    • Waltermann, M. and Steinbuchel, A. (2005). Neutral lipid bodies in prokaryotes: recent insights into structure, formation, and relationship to eukaryotic lipid depots. J. Bacteriol. 187, 3607-3619.
    • (2005) J. Bacteriol , vol.187 , pp. 3607-3619
    • Waltermann, M.1    Steinbuchel, A.2
  • 57
    • 34548514866 scopus 로고    scopus 로고
    • Proteins under new management: Lipid droplets deliver
    • Welte, M. A. (2007). Proteins under new management: lipid droplets deliver. Trends Cell Biol. 17, 363-369.
    • (2007) Trends Cell Biol , vol.17 , pp. 363-369
    • Welte, M.A.1
  • 58
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan, S. and Goldman, N. (2001). A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 18, 691-699.
    • (2001) Mol. Biol. Evol , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 59
    • 33749058310 scopus 로고    scopus 로고
    • A proposed model of fat packaging by exchangeable lipid droplet proteins
    • Wolins, N. E., Brasaemle, D. L. and Bickel, P. E. (2006). A proposed model of fat packaging by exchangeable lipid droplet proteins. FEBS Lett. 580, 5484-5491.
    • (2006) FEBS Lett , vol.580 , pp. 5484-5491
    • Wolins, N.E.1    Brasaemle, D.L.2    Bickel, P.E.3
  • 60
    • 0141888314 scopus 로고    scopus 로고
    • The major surface protease (MSP or GP63) of Leishmania sp. Biosynthesis, regulation of expression, and function
    • Yao, C., Donelson, J. E. and Wilson, M. E. (2003). The major surface protease (MSP or GP63) of Leishmania sp. Biosynthesis, regulation of expression, and function. Mol. Biochem. Parasitol. 132, 1-16.
    • (2003) Mol. Biochem. Parasitol , vol.132 , pp. 1-16
    • Yao, C.1    Donelson, J.E.2    Wilson, M.E.3
  • 61
    • 33846289955 scopus 로고    scopus 로고
    • Expression of adipose differentiation-related protein: A predictor of cancer-specific survival in clear cell renal carcinoma
    • Yao, M., Huang, Y., Shioi, K., Hattori, K., Murakami, T., Nakaigawa, N., Kishida, T., Nagashima, Y. and Kubota, Y. (2007). Expression of adipose differentiation-related protein: a predictor of cancer-specific survival in clear cell renal carcinoma. Clin. Cancer Res. 13, 152-160.
    • (2007) Clin. Cancer Res , vol.13 , pp. 152-160
    • Yao, M.1    Huang, Y.2    Shioi, K.3    Hattori, K.4    Murakami, T.5    Nakaigawa, N.6    Kishida, T.7    Nagashima, Y.8    Kubota, Y.9
  • 62
    • 0030595327 scopus 로고    scopus 로고
    • Signal sequences: The same yet different
    • Zheng, N. and Gierasch, L. M. (1996). Signal sequences: the same yet different. Cell 86, 849-852.
    • (1996) Cell , vol.86 , pp. 849-852
    • Zheng, N.1    Gierasch, L.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.