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Volumn 43, Issue 9, 2004, Pages 2438-2444

Pathway for Polyarginine Entry into Mammalian Cells

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CELL CULTURE; DEGRADATION; LIPIDS; PROTEINS;

EID: 1542327642     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035933x     Document Type: Article
Times cited : (337)

References (61)
  • 2
    • 0038325747 scopus 로고    scopus 로고
    • Protein transduction technology offers novel therapeutic approach for brain ischemia
    • Denicourt, C., and Dowdy, S. F. (2003) Protein transduction technology offers novel therapeutic approach for brain ischemia, Trends Pharmacol. Sci. 24, 216-218.
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 216-218
    • Denicourt, C.1    Dowdy, S.F.2
  • 4
    • 0041698459 scopus 로고    scopus 로고
    • "Translocatory proteins" and "protein transduction domains": A critical analysis of their biological effects and underlying mechanisms
    • Leifert, J. A., and Lindsay Whitton, J. (2003) "Translocatory proteins" and "protein transduction domains": A critical analysis of their biological effects and underlying mechanisms, Mol. Ther. 8, 13-20.
    • (2003) Mol. Ther. , vol.8 , pp. 13-20
    • Leifert, J.A.1    Lindsay Whitton, J.2
  • 7
    • 0001408455 scopus 로고
    • Histones and basic polyamino acids stimulate the uptake of albumin by tumor cells in culture
    • Ryser, H. J., and Hancock, R. (1965) Histones and basic polyamino acids stimulate the uptake of albumin by tumor cells in culture, Science 150, 501-503.
    • (1965) Science , vol.150 , pp. 501-503
    • Ryser, H.J.1    Hancock, R.2
  • 8
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel, A. D., and Pabo, C. O. (1988) Cellular uptake of the tat protein from human immunodeficiency virus, Cell 55, 1189-1193.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 9
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • Green, M., and Loewenstein, P. M. (1988) Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein, Cell 55, 1179-1788.
    • (1988) Cell , vol.55 , pp. 1179-1788
    • Green, M.1    Loewenstein, P.M.2
  • 10
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vives, E., Brodin, P., and Lebleu, B. (1997) A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus, J. Biol. Chem. 272, 16010-16017.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 11
    • 0037169486 scopus 로고    scopus 로고
    • Possible existence of common internalization mechanisms among arginine-rich peptides
    • Suzuki, T., Futaki, S., Niwa, M., Tanaka, S., Ueda, K., and Sugiura, Y. (2002) Possible existence of common internalization mechanisms among arginine-rich peptides, J. Biol. Chem. 277, 2437-2443.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2437-2443
    • Suzuki, T.1    Futaki, S.2    Niwa, M.3    Tanaka, S.4    Ueda, K.5    Sugiura, Y.6
  • 12
    • 0038719684 scopus 로고    scopus 로고
    • The cationic amphipathic α-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeablizes membranes, and efficiently transfects cells
    • Coeytaux, E., Coulaud, D., Le Cam, E., Danos, O., and Kichler, A. (2003) The cationic amphipathic α-helix of HIV-1 viral protein R (Vpr) binds to nucleic acids, permeablizes membranes, and efficiently transfects cells, J. Biol. Chem. 278, 18110-18116.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18110-18116
    • Coeytaux, E.1    Coulaud, D.2    Le Cam, E.3    Danos, O.4    Kichler, A.5
  • 13
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • Mitchell, D. J., Kim, D. T., Steinman, L., Fathman, C. G., and Rothbard, J. B. (2000) Polyarginine enters cells more efficiently than other polycationic homopolymers, J. Pept. Res. 56, 318-325.
    • (2000) J. Pept. Res. , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Steinman, L.3    Fathman, C.G.4    Rothbard, J.B.5
  • 15
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • Schwarze, S. R., Ho, A., Vocero-Akbani, A., and Dowdy, S. F. (1999) In vivo protein transduction: Delivery of a biologically active protein into the mouse, Science 285, 1569-1572.
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 17
    • 0034141430 scopus 로고    scopus 로고
    • In vivo protein transduction: Intracellular delivery of biologically active proteins, compounds and DNA
    • Schwarze, S. R., and Dowdy, S. F. (2000) In vivo protein transduction: Intracellular delivery of biologically active proteins, compounds and DNA, Trends Pharmacol. Sci. 21, 45-48.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 45-48
    • Schwarze, S.R.1    Dowdy, S.F.2
  • 18
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
    • Wender, P. A., Mitchell, D. J., Pattabiraman, K., Pelkey, E. T., Steinman, L., and Rothbard, J. B. (2000) The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters, Proc. Natl. Acad. Sci. U.S.A. 97, 13003-13008.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 21
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi, D., Calvet, S., Trembleau, A., Brunissen, A., Chassaing, G., and Prochiantz, A. (1996) Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent, J. Biol. Chem. 271, 18188-18193.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 22
    • 0037073171 scopus 로고    scopus 로고
    • Oligocarbamate molecular transporters: Design, synthesis, and biological evaluation of a new class of transporters for drug delivery
    • Wender, P. A., Rothbard, J. B., Jessop, T. C., Kreider, E. L., and Wylie, B. L. (2002) Oligocarbamate molecular transporters: Design, synthesis, and biological evaluation of a new class of transporters for drug delivery, J. Am. Chem. Soc. 124, 13382-13383.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 13382-13383
    • Wender, P.A.1    Rothbard, J.B.2    Jessop, T.C.3    Kreider, E.L.4    Wylie, B.L.5
  • 25
    • 0037103242 scopus 로고    scopus 로고
    • Arginine-rich molecular transporters for drug delivery: Role of backbone spacing in cellular uptake
    • Rothbard, J. B., Kreider, E., VanDeusen, C. L., Wright, L., Wylie, B. L., and Wender, P. A. (2002) Arginine-rich molecular transporters for drug delivery: Role of backbone spacing in cellular uptake, J. Med. Chem. 45, 3612-3618.
    • (2002) J. Med. Chem. , vol.45 , pp. 3612-3618
    • Rothbard, J.B.1    Kreider, E.2    VanDeusen, C.L.3    Wright, L.4    Wylie, B.L.5    Wender, P.A.6
  • 26
    • 0037172801 scopus 로고    scopus 로고
    • Translocation of branched-chain arginine peptides through cell membranes: Flexibility in the spatial disposition of positive charges in membrane-permeable peptides
    • Futaki, S., Nakase, I., Suzuki, T., Youjun, Z., and Sugiura, Y. (2002) Translocation of branched-chain arginine peptides through cell membranes: Flexibility in the spatial disposition of positive charges in membrane-permeable peptides, Biochemistry 41, 7925-7930.
    • (2002) Biochemistry , vol.41 , pp. 7925-7930
    • Futaki, S.1    Nakase, I.2    Suzuki, T.3    Youjun, Z.4    Sugiura, Y.5
  • 27
    • 0037119348 scopus 로고    scopus 로고
    • Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate
    • Mai, J. C., Shen, H., Watkins, S. C., Cheng, T., and Robbins, P. D. (2002) Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate, J. Biol. Chem. 277, 30208-30218.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30208-30218
    • Mai, J.C.1    Shen, H.2    Watkins, S.C.3    Cheng, T.4    Robbins, P.D.5
  • 28
    • 0036669511 scopus 로고    scopus 로고
    • Cellular import mediated by nuclear localization signal peptide sequences
    • Ragin, A. D., Morgan, R. A., and Chmielewski, J. (2002) Cellular import mediated by nuclear localization signal peptide sequences, Chem. Biol. 9, 943-948.
    • (2002) Chem. Biol. , vol.9 , pp. 943-948
    • Ragin, A.D.1    Morgan, R.A.2    Chmielewski, J.3
  • 29
    • 0036289650 scopus 로고    scopus 로고
    • Positively charged DNA-binding proteins cause apparent cell membrane translocation
    • Lundberg, M., and Johansson, M. (2002) Positively charged DNA-binding proteins cause apparent cell membrane translocation, Biochem. Biophys. Res. Commun. 291, 367-371.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 367-371
    • Lundberg, M.1    Johansson, M.2
  • 31
    • 0036339597 scopus 로고    scopus 로고
    • Cellular uptake of N-methylpyrrole/N-methylimidazole polyamide-dye conjugates
    • Belitsky, J. M., Leslie, S. J., Arora, P. S., Beerman, T. A., and Dervan, P. B. (2002) Cellular uptake of N-methylpyrrole/N-methylimidazole polyamide-dye conjugates, Bioorg. Med. Chem. 10, 3313-3318.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3313-3318
    • Belitsky, J.M.1    Leslie, S.J.2    Arora, P.S.3    Beerman, T.A.4    Dervan, P.B.5
  • 32
    • 0042199010 scopus 로고    scopus 로고
    • Cell surface adherence and endocytosis of protein transduction domains
    • Lundberg, M., Wikstrom, S., and Johansson, M. (2003) Cell surface adherence and endocytosis of protein transduction domains, Mol. Ther. 8, 143-150.
    • (2003) Mol. Ther. , vol.8 , pp. 143-150
    • Lundberg, M.1    Wikstrom, S.2    Johansson, M.3
  • 33
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans
    • Tyagi, M., Rusnati, M., Presta, M., and Giacca, M. (2001) Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans, J. Biol. Chem. 276, 3254-3261.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 34
    • 0037333830 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan as a plasma membrane carrier
    • Belting, M. (2003) Heparan sulfate proteoglycan as a plasma membrane carrier, Trends Biochem. Sci. 28, 145-151.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 145-151
    • Belting, M.1
  • 35
    • 0032382433 scopus 로고    scopus 로고
    • Cellular catabolism of heparan sulfate proteoglycans
    • Yanagishita, M. (1998) Cellular catabolism of heparan sulfate proteoglycans, Trends Glycosci. Glycobiol. 10, 57-63.
    • (1998) Trends Glycosci. Glycobiol. , vol.10 , pp. 57-63
    • Yanagishita, M.1
  • 36
    • 0026577602 scopus 로고
    • A single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesis
    • Lidholt, K., Weinke, J. L., Kiser, C. S., Lugemwa, F. N., Bame, K. J., Cheifetz, S., Massague, J., Lindahl, U., and Esko, J. D. (1992) A single mutation affects both N-acetylglucosaminyltransferase and glucuronosyltransferase activities in a Chinese hamster ovary cell mutant defective in heparan sulfate biosynthesis, Proc. Natl. Acad. Sci. U.S.A. 89, 2267-2271.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2267-2271
    • Lidholt, K.1    Weinke, J.L.2    Kiser, C.S.3    Lugemwa, F.N.4    Bame, K.J.5    Cheifetz, S.6    Massague, J.7    Lindahl, U.8    Esko, J.D.9
  • 37
    • 2142854239 scopus 로고
    • Animal cell mutants defective in glycosaminoglycan biosynthesis
    • Esko, J. D., Stewart, T. E., and Taylor, W. H. (1985) Animal cell mutants defective in glycosaminoglycan biosynthesis, Proc. Natl. Acad. Sci. U.S.A. 82, 3197-3201.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 3197-3201
    • Esko, J.D.1    Stewart, T.E.2    Taylor, W.H.3
  • 38
    • 0036205144 scopus 로고    scopus 로고
    • Transient vesicle leakage initiated by a synthetic apoptotic peptide derived from the death domain of neurotrophin receptor, p75NTR
    • Medina, M. L., Chapman, B. S., Bolender, J. P., and Plesniak, L. A. (2002) Transient vesicle leakage initiated by a synthetic apoptotic peptide derived from the death domain of neurotrophin receptor, p75NTR, J. Pept. Res. 59, 149-158.
    • (2002) J. Pept. Res. , vol.59 , pp. 149-158
    • Medina, M.L.1    Chapman, B.S.2    Bolender, J.P.3    Plesniak, L.A.4
  • 39
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate, and phosphatases
    • Ames, B. N. (1966) Assay of inorganic phosphate, total phosphate, and phosphatases, Methods Enzymol. 8, 115-118.
    • (1966) Methods Enzymol. , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 40
    • 0034802647 scopus 로고    scopus 로고
    • Heparin binding by the HIV-1 tat protein transduction domain
    • Hakansson, S., Jacobs, A., and Caffrey, M. (2001) Heparin binding by the HIV-1 tat protein transduction domain, Protein Sci. 10, 2138-2139.
    • (2001) Protein Sci. , vol.10 , pp. 2138-2139
    • Hakansson, S.1    Jacobs, A.2    Caffrey, M.3
  • 41
    • 0033948268 scopus 로고    scopus 로고
    • Messenger proteins: Homeoproteins, TAT and others
    • Prochiantz, A. (2000) Messenger proteins: Homeoproteins, TAT and others, Curr. Opin. Cell Biol. 12, 400-406.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 400-406
    • Prochiantz, A.1
  • 42
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang, L., Harroun, T. A., Weiss, T. M., Ding, L., and Huang, H. W. (2001) Barrel-stave model or toroidal model? A case study on melittin pores, Biophys. J. 81, 1475-1485.
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 43
    • 0031959657 scopus 로고    scopus 로고
    • Genetic engineering of proteins with cell membrane permeability
    • Rojas, M., Donahue, J. P., Tan, Z., and Lin, Y. Z. (1998) Genetic engineering of proteins with cell membrane permeability, Nat. Biotechnol. 16, 370-375.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 370-375
    • Rojas, M.1    Donahue, J.P.2    Tan, Z.3    Lin, Y.Z.4
  • 44
    • 0033973662 scopus 로고    scopus 로고
    • Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin
    • Fischer, P. M., Zhelev, N. Z., Wang, S., Melville, J. E., Fahraeus, R., and Lane, D. P. (2000) Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin, J. Pept. Res. 55, 163-172.
    • (2000) J. Pept. Res. , vol.55 , pp. 163-172
    • Fischer, P.M.1    Zhelev, N.Z.2    Wang, S.3    Melville, J.E.4    Fahraeus, R.5    Lane, D.P.6
  • 45
    • 0034613057 scopus 로고    scopus 로고
    • The Antennapedia peptide penetratin translocates across lipid bilayers-the first direct observation
    • Thoren, P. E., Persson, D., Karlsson, M., and Norden, B. (2000) The Antennapedia peptide penetratin translocates across lipid bilayers-the first direct observation, FEBS Lett. 482, 265-268.
    • (2000) FEBS Lett. , vol.482 , pp. 265-268
    • Thoren, P.E.1    Persson, D.2    Karlsson, M.3    Norden, B.4
  • 46
    • 0036159271 scopus 로고    scopus 로고
    • Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat
    • Silhol, M., Tyagi, M., Giacca, M., Lebleu, B., and Vives, E. (2002) Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat, Eur. J. Biochem. 269, 494-501.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 494-501
    • Silhol, M.1    Tyagi, M.2    Giacca, M.3    Lebleu, B.4    Vives, E.5
  • 47
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines, R. T. (1998) Ribonuclease A, Chem. Rev. 98, 1045-1065.
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1065
    • Raines, R.T.1
  • 48
    • 0036594060 scopus 로고    scopus 로고
    • Effect of replacing the aspartic acid/glutamic acid residues of bullfrog sialic acid binding lectin with asparagine/glutamine and arginine on the inhibition of cell proliferation in murine leukemia P388 cells
    • Ogawa, Y., Iwama, M., Ohgi, K., Tsuji, T., Irie, M., Itagaki, T., Kobayashi, H., and Inokuchi, N. (2002) Effect of replacing the aspartic acid/glutamic acid residues of bullfrog sialic acid binding lectin with asparagine/glutamine and arginine on the inhibition of cell proliferation in murine leukemia P388 cells, Biol. Pharm. Bull. 25, 722-727.
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 722-727
    • Ogawa, Y.1    Iwama, M.2    Ohgi, K.3    Tsuji, T.4    Irie, M.5    Itagaki, T.6    Kobayashi, H.7    Inokuchi, N.8
  • 50
    • 0034959158 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans: Intricate molecules with intriguing functions
    • Renato, V. (2001) Heparan sulfate proteoglycans: Intricate molecules with intriguing functions, J. Clin. Invest. 108, 165-167.
    • (2001) J. Clin. Invest. , vol.108 , pp. 165-167
    • Renato, V.1
  • 52
    • 0041409724 scopus 로고    scopus 로고
    • The sweet science of glycobiology
    • Sasisekharan, R., and Myette, J. R. (2003) The sweet science of glycobiology, Am. Sci. 91, 432-441.
    • (2003) Am. Sci. , vol.91 , pp. 432-441
    • Sasisekharan, R.1    Myette, J.R.2
  • 53
    • 0021242622 scopus 로고
    • Metabolism of proteoglycans in rat ovarian granulosa cell culture
    • Yanagishitia, M., and Hascall, V. C. (1984) Metabolism of proteoglycans in rat ovarian granulosa cell culture, J. Biol. Chem. 259, 10207-10283.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10207-10283
    • Yanagishitia, M.1    Hascall, V.C.2
  • 54
    • 0030957937 scopus 로고    scopus 로고
    • A novel role of follistatin, an activin-binding protein, in the inhibition of activin action in rat pituitary cells. Endocytotic degradation of activin and its acceleration by follistatin associated with cell-surface heparan sulfate
    • Hashimoto, O., Nakamura, T., Shoji, H., Shimasaki, S., Hayashi, Y., and Sugino, H. (1997) A novel role of follistatin, an activin-binding protein, in the inhibition of activin action in rat pituitary cells. Endocytotic degradation of activin and its acceleration by follistatin associated with cell-surface heparan sulfate, J. Biol. Chem. 272, 13835-13842.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13835-13842
    • Hashimoto, O.1    Nakamura, T.2    Shoji, H.3    Shimasaki, S.4    Hayashi, Y.5    Sugino, H.6
  • 55
    • 0033635310 scopus 로고    scopus 로고
    • Heparin and heparan sulfate: Biosynthesis, structure and function
    • Sasisekharan, R., and Venkataraman, G. (2000) Heparin and heparan sulfate: Biosynthesis, structure and function, Curr. Opin. Chem. Biol. 4, 626-631.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 626-631
    • Sasisekharan, R.1    Venkataraman, G.2
  • 56
    • 0025258894 scopus 로고
    • Identification and characterization of heparan sulfate-binding proteins from human lung carcinoma cells
    • Bilozur, M. E., and Biswas, C. (1990) Identification and characterization of heparan sulfate-binding proteins from human lung carcinoma cells, J. Biol. Chem. 265, 19697-19703.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19697-19703
    • Bilozur, M.E.1    Biswas, C.2
  • 57
    • 0028321612 scopus 로고
    • Mapping the heparin-binding sites on type I collagen monomers and fibrils
    • San Antonio, J. D., Lander, A. D., Karnovsky, M. J., and Slayter, H. S. (1994) Mapping the heparin-binding sites on type I collagen monomers and fibrils, J. Cell Biol. 125, 1179-1188.
    • (1994) J. Cell Biol. , vol.125 , pp. 1179-1188
    • San Antonio, J.D.1    Lander, A.D.2    Karnovsky, M.J.3    Slayter, H.S.4
  • 60
    • 0034603836 scopus 로고    scopus 로고
    • Mechanisms of fibroblast growth factor 2 intracellular processing: A kinetic analysis of the role of heparan sulfate proteoglycans
    • Sperinde, G. V., and Nugent, M. A. (2000) Mechanisms of fibroblast growth factor 2 intracellular processing: A kinetic analysis of the role of heparan sulfate proteoglycans, Biochemistry 39, 3788-3796.
    • (2000) Biochemistry , vol.39 , pp. 3788-3796
    • Sperinde, G.V.1    Nugent, M.A.2


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