메뉴 건너뛰기




Volumn 290, Issue 5, 2015, Pages 2812-2821

The paired basic amino acid-cleaving enzyme 4 (PACE4) is involved in the maturation of insulin receptor isoform B: An opportunity to reduce the specific insulin receptor-dependent effects of insulin-like growth factor 2 (IGF2)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; MAMMALS;

EID: 84921880502     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.592543     Document Type: Article
Times cited : (21)

References (51)
  • 1
    • 84874727313 scopus 로고    scopus 로고
    • The insulin receptor: Both a prototypical and atypical receptor tyrosine kinase
    • Hubbard, S. R. (2013) The insulin receptor: both a prototypical and atypical receptor tyrosine kinase. Cold Spring Harb. Perspect. Biol. 5, a008946
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5 , pp. a008946
    • Hubbard, S.R.1
  • 2
    • 0020561710 scopus 로고
    • Biosynthesis and glycosylation of the insulin receptor: Evidence for a single polypeptide precursor of the two major subunits
    • Hedo, J. A., Kahn, C. R., Hayashi, M., Yamada, K. M., and Kasuga, M. (1983) Biosynthesis and glycosylation of the insulin receptor: evidence for a single polypeptide precursor of the two major subunits. J. Biol. Chem. 258, 10020-10026
    • (1983) J. Biol. Chem. , vol.258 , pp. 10020-10026
    • Hedo, J.A.1    Kahn, C.R.2    Hayashi, M.3    Yamada, K.M.4    Kasuga, M.5
  • 5
    • 0023881079 scopus 로고
    • Insulin resistance by uncleaved insulin proreceptor: Emergence of binding site by trypsin
    • Kobayashi, M., Sasaoka, T., Takata, Y., Hisatomi, A., and Shigeta, Y. (1988) Insulin resistance by uncleaved insulin proreceptor: emergence of binding site by trypsin. Diabetes 37, 653-656
    • (1988) Diabetes , vol.37 , pp. 653-656
    • Kobayashi, M.1    Sasaoka, T.2    Takata, Y.3    Hisatomi, A.4    Shigeta, Y.5
  • 7
    • 0026342942 scopus 로고
    • Increased hepatic insulin proreceptor-to-receptor ratio in diabetes: A possible processing defect
    • Dardevet, D., Komori, K., Grunfeld, C., Rosenzweig, S. A., and Buse, M. G. (1991) Increased hepatic insulin proreceptor-to-receptor ratio in diabetes: a possible processing defect. Am. J. Physiol. 261, E562-E571
    • (1991) Am. J. Physiol. , vol.261 , pp. E562-E571
    • Dardevet, D.1    Komori, K.2    Grunfeld, C.3    Rosenzweig, S.A.4    Buse, M.G.5
  • 8
    • 84860383419 scopus 로고    scopus 로고
    • The biology and therapeutic targeting of the proprotein convertases
    • Seidah, N. G., and Prat, A. (2012) The biology and therapeutic targeting of the proprotein convertases. Nat. Rev. Drug Discov. 11, 367-383
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 367-383
    • Seidah, N.G.1    Prat, A.2
  • 9
    • 0034710889 scopus 로고    scopus 로고
    • Furin-mediated processing in the early secretory pathway: Sequential cleavage and degradation of misfolded insulin receptors
    • Bass, J., Turck, C., Rouard, M., and Steiner, D. F. (2000) Furin-mediated processing in the early secretory pathway: sequential cleavage and degradation of misfolded insulin receptors. Proc. Natl. Acad. Sci. U.S.A. 97, 11905-11909
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11905-11909
    • Bass, J.1    Turck, C.2    Rouard, M.3    Steiner, D.F.4
  • 10
    • 0027362049 scopus 로고
    • Defective processing of the insulin receptor in an endoprotease-deficient Chinese hamster cell strain is corrected by expression of mouse furin
    • Robertson, B. J., Moehring, J. M., and Moehring, T. J. (1993) Defective processing of the insulin receptor in an endoprotease-deficient Chinese hamster cell strain is corrected by expression of mouse furin. J. Biol. Chem. 268, 24274-24277
    • (1993) J. Biol. Chem. , vol.268 , pp. 24274-24277
    • Robertson, B.J.1    Moehring, J.M.2    Moehring, T.J.3
  • 11
    • 0025149102 scopus 로고
    • Effects of amino acid replacements within the tetrabasic cleavage site on the processing of the human insulin receptor precursor expressed in Chinese hamster ovary cells
    • Yoshimasa, Y., Paul, J. I., Whittaker, J., and Steiner, D. F. (1990) Effects of amino acid replacements within the tetrabasic cleavage site on the processing of the human insulin receptor precursor expressed in Chinese hamster ovary cells. J. Biol. Chem. 265, 17230-17237
    • (1990) J. Biol. Chem. , vol.265 , pp. 17230-17237
    • Yoshimasa, Y.1    Paul, J.I.2    Whittaker, J.3    Steiner, D.F.4
  • 12
    • 79953151795 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor 1 is an intracellular inhibitor of furin proprotein convertase
    • Bernot, D., Stalin, J., Stocker, P., Bonardo, B., Scroyen, I., Alessi, M. C., and Peiretti, F. (2011) Plasminogen activator inhibitor 1 is an intracellular inhibitor of furin proprotein convertase. J. Cell Sci. 124, 1224-1230
    • (2011) J. Cell Sci. , vol.124 , pp. 1224-1230
    • Bernot, D.1    Stalin, J.2    Stocker, P.3    Bonardo, B.4    Scroyen, I.5    Alessi, M.C.6    Peiretti, F.7
  • 15
    • 0024539198 scopus 로고
    • Alternative splicing of human insulin receptor messenger RNA
    • Seino, S., and Bell, G. I. (1989) Alternative splicing of human insulin receptor messenger RNA. Biochem. Biophys. Res. Commun. 159, 312-316
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 312-316
    • Seino, S.1    Bell, G.I.2
  • 16
    • 70849120946 scopus 로고    scopus 로고
    • Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease
    • Belfiore, A., Frasca, F., Pandini, G., Sciacca, L., and Vigneri, R. (2009) Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease. Endocr. Rev. 30, 586-623
    • (2009) Endocr. Rev. , vol.30 , pp. 586-623
    • Belfiore, A.1    Frasca, F.2    Pandini, G.3    Sciacca, L.4    Vigneri, R.5
  • 17
    • 34247872895 scopus 로고    scopus 로고
    • Characterization of insulin/IGF hybrid receptors: Contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation
    • Benyoucef, S., Surinya, K. H., Hadaschik, D., and Siddle, K. (2007) Characterization of insulin/IGF hybrid receptors: contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation. Biochem. J. 403, 603-613
    • (2007) Biochem. J. , vol.403 , pp. 603-613
    • Benyoucef, S.1    Surinya, K.H.2    Hadaschik, D.3    Siddle, K.4
  • 18
    • 0032932822 scopus 로고    scopus 로고
    • Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells
    • Frasca, F., Pandini, G., Scalia, P., Sciacca, L., Mineo, R., Costantino, A., Goldfine, I. D., Belfiore, A., and Vigneri, R. (1999) Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells. Mol. Cell Biol. 19, 3278-3288
    • (1999) Mol. Cell Biol. , vol.19 , pp. 3278-3288
    • Frasca, F.1    Pandini, G.2    Scalia, P.3    Sciacca, L.4    Mineo, R.5    Costantino, A.6    Goldfine, I.D.7    Belfiore, A.8    Vigneri, R.9
  • 19
    • 0027537050 scopus 로고
    • Ligand-binding properties of the two isoforms of the human insulin receptor
    • Yamaguchi, Y., Flier, J. S., Benecke, H., Ransil, B. J., and Moller, D. E. (1993) Ligand-binding properties of the two isoforms of the human insulin receptor. Endocrinology 132, 1132-1138
    • (1993) Endocrinology , vol.132 , pp. 1132-1138
    • Yamaguchi, Y.1    Flier, J.S.2    Benecke, H.3    Ransil, B.J.4    Moller, D.E.5
  • 20
    • 0025773690 scopus 로고
    • The two isotypes of the human insulin receptor (HIR-A and HIR-B) follow different internalization kinetics
    • Vogt, B., Carrascosa, J. M., Ermel, B., Ullrich, A., and Häring, H. U. (1991) The two isotypes of the human insulin receptor (HIR-A and HIR-B) follow different internalization kinetics. Biochem. Biophys. Res. Commun. 177, 1013-1018
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 1013-1018
    • Vogt, B.1    Carrascosa, J.M.2    Ermel, B.3    Ullrich, A.4    Häring, H.U.5
  • 21
    • 0025941580 scopus 로고
    • Functional properties of two naturally occurring isoforms of the human insulin receptor in Chinese hamster ovary cells
    • Yamaguchi, Y., Flier, J. S., Yokota, A., Benecke, H., Backer, J. M., and Moller, D. E. (1991) Functional properties of two naturally occurring isoforms of the human insulin receptor in Chinese hamster ovary cells. Endocrinology 129, 2058-2066
    • (1991) Endocrinology , vol.129 , pp. 2058-2066
    • Yamaguchi, Y.1    Flier, J.S.2    Yokota, A.3    Benecke, H.4    Backer, J.M.5    Moller, D.E.6
  • 22
    • 0035265835 scopus 로고    scopus 로고
    • Selective insulin signaling through A and B insulin receptors regulates transcription of insulin and glucokinase genes in pancreatic beta cells
    • Leibiger, B., Leibiger, I. B., Moede, T., Kemper, S., Kulkarni, R. N., Kahn, C. R., de Vargas, L. M., and Berggren, P. O. (2001) Selective insulin signaling through A and B insulin receptors regulates transcription of insulin and glucokinase genes in pancreatic beta cells. Mol. Cell 7, 559-570
    • (2001) Mol. Cell , vol.7 , pp. 559-570
    • Leibiger, B.1    Leibiger, I.B.2    Moede, T.3    Kemper, S.4    Kulkarni, R.N.5    Kahn, C.R.6    De Vargas, L.M.7    Berggren, P.O.8
  • 23
    • 0347993701 scopus 로고    scopus 로고
    • Isoform-specific insulin receptor signaling involves different plasma membrane domains
    • Uhles, S., Moede, T., Leibiger, B., Berggren, P. O., and Leibiger, I. B. (2003) Isoform-specific insulin receptor signaling involves different plasma membrane domains. J. Cell Biol. 163, 1327-1337
    • (2003) J. Cell Biol. , vol.163 , pp. 1327-1337
    • Uhles, S.1    Moede, T.2    Leibiger, B.3    Berggren, P.O.4    Leibiger, I.B.5
  • 24
    • 34247647980 scopus 로고    scopus 로고
    • Selective gene activation by spatial segregation of insulin receptor B signaling
    • Uhles, S., Moede, T., Leibiger, B., Berggren, P. O., and Leibiger, I. B. (2007) Selective gene activation by spatial segregation of insulin receptor B signaling. FASEB J. 21, 1609-1621
    • (2007) FASEB J. , vol.21 , pp. 1609-1621
    • Uhles, S.1    Moede, T.2    Leibiger, B.3    Berggren, P.O.4    Leibiger, I.B.5
  • 25
    • 0027973010 scopus 로고
    • Accurate and efficient cleavage of the human insulin proreceptor by the human proprotein-processing protease furin. Characterization and kinetic parameters using the purified, secreted soluble protease expressed by a recombinant baculovirus
    • Bravo, D. A., Gleason, J. B., Sanchez, R. I., Roth, R. A., and Fuller, R. S. (1994) Accurate and efficient cleavage of the human insulin proreceptor by the human proprotein-processing protease furin. Characterization and kinetic parameters using the purified, secreted soluble protease expressed by a recombinant baculovirus. J. Biol. Chem. 269, 25830-25837
    • (1994) J. Biol. Chem. , vol.269 , pp. 25830-25837
    • Bravo, D.A.1    Gleason, J.B.2    Sanchez, R.I.3    Roth, R.A.4    Fuller, R.S.5
  • 26
    • 77649161633 scopus 로고    scopus 로고
    • A 20 residue motif delineates the furin cleavage site and its physical properties may influence viral fusion
    • Tian, S. (2009) A 20 residue motif delineates the furin cleavage site and its physical properties may influence viral fusion. Biochem. Insights 2, 9-20
    • (2009) Biochem. Insights , vol.2 , pp. 9-20
    • Tian, S.1
  • 28
    • 0030887714 scopus 로고    scopus 로고
    • Cleavage site mutants of the subtype B insulin receptor are uncleaved and fully functional
    • Auzan, C., Debant, A., Rossi, B., and Clauser, E. (1997) Cleavage site mutants of the subtype B insulin receptor are uncleaved and fully functional. Mol. Cell Endocrinol. 128, 129-137
    • (1997) Mol. Cell Endocrinol. , vol.128 , pp. 129-137
    • Auzan, C.1    Debant, A.2    Rossi, B.3    Clauser, E.4
  • 29
    • 0032560449 scopus 로고    scopus 로고
    • α1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: Application as an antipathogenic agent
    • Jean, F., Stella, K., Thomas, L., Liu, G., Xiang, Y., Reason, A. J., and Thomas, G. (1998) α1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: application as an antipathogenic agent. Proc. Natl. Acad. Sci. U.S.A. 95, 7293-7298
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7293-7298
    • Jean, F.1    Stella, K.2    Thomas, L.3    Liu, G.4    Xiang, Y.5    Reason, A.J.6    Thomas, G.7
  • 30
    • 13244260693 scopus 로고    scopus 로고
    • Stability of mutant serpin/furin complexes: Dependence on pH and regulation at the deacylation step
    • Dufour, E. K., Désilets, A., Longpré, J. M., and Leduc, R. (2005) Stability of mutant serpin/furin complexes: dependence on pH and regulation at the deacylation step. Protein Sci. 14, 303-315
    • (2005) Protein Sci. , vol.14 , pp. 303-315
    • Dufour, E.K.1    Désilets, A.2    Longpré, J.M.3    Leduc, R.4
  • 33
    • 77951927648 scopus 로고    scopus 로고
    • Post-endoplasmic reticulum rescue of unstable MHC class I requires proprotein convertase PC7
    • Leonhardt, R. M., Fiegl, D., Rufer, E., Karger, A., Bettin, B., and Knittler, M. R. (2010) Post-endoplasmic reticulum rescue of unstable MHC class I requires proprotein convertase PC7. J. Immunol. 184, 2985-2998
    • (2010) J. Immunol. , vol.184 , pp. 2985-2998
    • Leonhardt, R.M.1    Fiegl, D.2    Rufer, E.3    Karger, A.4    Bettin, B.5    Knittler, M.R.6
  • 34
    • 77949902266 scopus 로고    scopus 로고
    • Down-regulation of tissue inhibitor of metalloproteinase-3 (TIMP-3) expression is necessary for adipocyte differentiation
    • Bernot, D., Barruet, E., Poggi, M., Bonardo, B., Alessi, M. C., and Peiretti, F. (2010) Down-regulation of tissue inhibitor of metalloproteinase-3 (TIMP-3) expression is necessary for adipocyte differentiation. J. Biol. Chem. 285, 6508-6514
    • (2010) J. Biol. Chem. , vol.285 , pp. 6508-6514
    • Bernot, D.1    Barruet, E.2    Poggi, M.3    Bonardo, B.4    Alessi, M.C.5    Peiretti, F.6
  • 35
    • 41649118952 scopus 로고    scopus 로고
    • A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness
    • Coppola, J. M., Bhojani, M. S., Ross, B. D., and Rehemtulla, A. (2008) A small-molecule furin inhibitor inhibits cancer cell motility and invasiveness. Neoplasia 10, 363-370
    • (2008) Neoplasia , vol.10 , pp. 363-370
    • Coppola, J.M.1    Bhojani, M.S.2    Ross, B.D.3    Rehemtulla, A.4
  • 36
    • 84934436733 scopus 로고    scopus 로고
    • High-throughput analysis of the dynamics of recycling cell surface proteins
    • Govers, R., James, D. E., and Coster, A. C. (2008) High-throughput analysis of the dynamics of recycling cell surface proteins. Methods Mol. Biol. 440, 129-146
    • (2008) Methods Mol. Biol. , vol.440 , pp. 129-146
    • Govers, R.1    James, D.E.2    Coster, A.C.3
  • 37
    • 84868214947 scopus 로고    scopus 로고
    • A nonradioisotope chemiluminescent assay for evaluation of 2-deoxyglucose uptake in 3T3-L1 adipocytes. Effect of various carbonyls species on insulin action
    • Vidal, N., Cavaillé, J. P., Poggi, M., Peiretti, F., and Stocker, P. (2012) A nonradioisotope chemiluminescent assay for evaluation of 2-deoxyglucose uptake in 3T3-L1 adipocytes. Effect of various carbonyls species on insulin action. Biochimie 94, 2569-2576
    • (2012) Biochimie , vol.94 , pp. 2569-2576
    • Vidal, N.1    Cavaillé, J.P.2    Poggi, M.3    Peiretti, F.4    Stocker, P.5
  • 38
    • 84859735363 scopus 로고    scopus 로고
    • Computational prediction of furin cleavage sites by a hybrid method and understanding mechanism underlying diseases
    • Tian, S., Huajun, W., and Wu, J. (2012) Computational prediction of furin cleavage sites by a hybrid method and understanding mechanism underlying diseases. Sci. Rep. 2, 261
    • (2012) Sci. Rep. , vol.2 , pp. 261
    • Tian, S.1    Huajun, W.2    Wu, J.3
  • 40
    • 0037474206 scopus 로고    scopus 로고
    • Secretory proprotein convertases PACE4 and PC6A are heparin-binding proteins which are localized in the extracellular matrix. Potential role of PACE4 in the activation of proproteins in the extracellular matrix
    • Tsuji, A., Sakurai, K., Kiyokage, E., Yamazaki, T., Koide, S., Toida, K., Ishimura, K., and Matsuda, Y. (2003) Secretory proprotein convertases PACE4 and PC6A are heparin-binding proteins which are localized in the extracellular matrix. Potential role of PACE4 in the activation of proproteins in the extracellular matrix. Biochim. Biophys. Acta 1645, 95-104
    • (2003) Biochim. Biophys. Acta , vol.1645 , pp. 95-104
    • Tsuji, A.1    Sakurai, K.2    Kiyokage, E.3    Yamazaki, T.4    Koide, S.5    Toida, K.6    Ishimura, K.7    Matsuda, Y.8
  • 41
    • 79960914019 scopus 로고    scopus 로고
    • New substrate analogue furin inhibitors derived from 4-amidinobenzylamide
    • Becker, G. L., Hardes, K., and Steinmetzer, T. (2011) New substrate analogue furin inhibitors derived from 4-amidinobenzylamide. Bioorg Med. Chem. Lett. 21, 4695-4697
    • (2011) Bioorg Med. Chem. Lett. , vol.21 , pp. 4695-4697
    • Becker, G.L.1    Hardes, K.2    Steinmetzer, T.3
  • 42
    • 27644458702 scopus 로고    scopus 로고
    • The cysteine-rich domain of the secreted proprotein convertases PC5A and PACE4 functions as a cell surface anchor and interacts with tissue inhibitors of metalloproteinases
    • Nour, N., Mayer, G., Mort, J. S., Salvas, A., Mbikay, M., Morrison, C. J., Overall, C. M., and Seidah, N. G. (2005) The cysteine-rich domain of the secreted proprotein convertases PC5A and PACE4 functions as a cell surface anchor and interacts with tissue inhibitors of metalloproteinases. Mol. Biol. Cell 16, 5215-5226
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5215-5226
    • Nour, N.1    Mayer, G.2    Mort, J.S.3    Salvas, A.4    Mbikay, M.5    Morrison, C.J.6    Overall, C.M.7    Seidah, N.G.8
  • 44
    • 0027965348 scopus 로고
    • The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functions
    • Seidah, N. G., Chrétien, M., and Day, R. (1994) The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions. Biochimie 76, 197-209
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chrétien, M.2    Day, R.3
  • 45
    • 38349112617 scopus 로고    scopus 로고
    • The regulated cell surface zymogen activation of the proprotein convertase PC5A directs the processing of its secretory substrates
    • Mayer, G., Hamelin, J., Asselin, M. C., Pasquato, A., Marcinkiewicz, E., Tang, M., Tabibzadeh, S., and Seidah, N. G. (2008) The regulated cell surface zymogen activation of the proprotein convertase PC5A directs the processing of its secretory substrates. J. Biol. Chem. 283, 2373-2384
    • (2008) J. Biol. Chem. , vol.283 , pp. 2373-2384
    • Mayer, G.1    Hamelin, J.2    Asselin, M.C.3    Pasquato, A.4    Marcinkiewicz, E.5    Tang, M.6    Tabibzadeh, S.7    Seidah, N.G.8
  • 46
    • 0028559222 scopus 로고
    • Exon 11 enhances insulin binding affinity and tyrosine kinase activity of the human insulin proreceptor
    • Pashmforoush, M., Yoshimasa, Y., and Steiner, D. F. (1994) Exon 11 enhances insulin binding affinity and tyrosine kinase activity of the human insulin proreceptor. J. Biol. Chem. 269, 32639-32648
    • (1994) J. Biol. Chem. , vol.269 , pp. 32639-32648
    • Pashmforoush, M.1    Yoshimasa, Y.2    Steiner, D.F.3
  • 47
    • 0021735901 scopus 로고
    • Biogenesis, transit, and functional properties of the insulin proreceptor and modified insulin receptors in 3T3-L1 adipocytes. Use of monensin to probe proreceptor cleavage and generate altered receptor subunits
    • Salzman, A., Wan, C. F., and Rubin, C. S. (1984) Biogenesis, transit, and functional properties of the insulin proreceptor and modified insulin receptors in 3T3-L1 adipocytes. Use of monensin to probe proreceptor cleavage and generate altered receptor subunits. Biochemistry 23, 6555-6565
    • (1984) Biochemistry , vol.23 , pp. 6555-6565
    • Salzman, A.1    Wan, C.F.2    Rubin, C.S.3
  • 48
    • 0024349263 scopus 로고
    • Binding specificity and intramolecular signal transmission of uncleaved insulin proreceptor in transformed lymphocytes from a patient with extreme insulin resistance
    • Sasaoka, T., Shigeta, Y., Takata, Y., Sugibayashi, M., Hisatomi, A., and Kobayashi, M. (1989) Binding specificity and intramolecular signal transmission of uncleaved insulin proreceptor in transformed lymphocytes from a patient with extreme insulin resistance. Diabetologia 32, 371-377
    • (1989) Diabetologia , vol.32 , pp. 371-377
    • Sasaoka, T.1    Shigeta, Y.2    Takata, Y.3    Sugibayashi, M.4    Hisatomi, A.5    Kobayashi, M.6
  • 49
    • 77955623211 scopus 로고    scopus 로고
    • Blockade of furin activity and furin-induced tumor cells malignant phenotypes by the chemically synthesized human furin prodomain
    • Basak, A., Chen, A., Scamuffa, N., Mohottalage, D., Basak, S., and Khatib, A. M. (2010) Blockade of furin activity and furin-induced tumor cells malignant phenotypes by the chemically synthesized human furin prodomain. Curr. Med. Chem. 17, 2214-2221
    • (2010) Curr. Med. Chem. , vol.17 , pp. 2214-2221
    • Basak, A.1    Chen, A.2    Scamuffa, N.3    Mohottalage, D.4    Basak, S.5    Khatib, A.M.6
  • 51
    • 84877993047 scopus 로고    scopus 로고
    • Inhibition of tumor cells proliferation and migration by the flavonoid furin inhibitor isolated from Oroxylum indicum
    • Lalou, C., Basak, A., Mishra, P., Mohanta, B. C., Banik, R., Dinda, B., and Khatib, A. M. (2013) Inhibition of tumor cells proliferation and migration by the flavonoid furin inhibitor isolated from Oroxylum indicum. Curr. Med. Chem. 20, 583-591
    • (2013) Curr. Med. Chem. , vol.20 , pp. 583-591
    • Lalou, C.1    Basak, A.2    Mishra, P.3    Mohanta, B.C.4    Banik, R.5    Dinda, B.6    Khatib, A.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.