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Volumn 54, Issue 12, 2015, Pages 2149-2159

Thalidomide (5HPP-33) suppresses microtubule dynamics and depolymerizes the microtubule network by binding at the vinblastine binding site on tubulin

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Indexed keywords

CYTOLOGY;

EID: 84926067379     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501429j     Document Type: Article
Times cited : (28)

References (65)
  • 1
    • 53549098210 scopus 로고    scopus 로고
    • Thalidomide as a multi-template for development of biologically active compounds
    • Hashimoto, Y. (2008) Thalidomide as a multi-template for development of biologically active compounds Arch. Pharm. (Weinheim, Ger.) 341, 536-547
    • (2008) Arch. Pharm. (Weinheim, Ger.) , vol.341 , pp. 536-547
    • Hashimoto, Y.1
  • 2
    • 79958765360 scopus 로고    scopus 로고
    • Teratogenic effects of thalidomide: Molecular mechanisms
    • Ito, T., Ando, H., and Handa, H. (2011) Teratogenic effects of thalidomide: Molecular mechanisms Cell. Mol. Life Sci. 68, 1569-1579
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1569-1579
    • Ito, T.1    Ando, H.2    Handa, H.3
  • 3
    • 37849052222 scopus 로고    scopus 로고
    • Thalidomide induces limb anomalies by PTEN stabilization, Akt suppression, and stimulation of caspase-dependent cell death
    • Knobloch, J., Schmitz, I., Gotz, K., Schulze-Osthoff, K., and Ruther, U. (2008) Thalidomide induces limb anomalies by PTEN stabilization, Akt suppression, and stimulation of caspase-dependent cell death Mol. Cell. Biol. 28, 529-538
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 529-538
    • Knobloch, J.1    Schmitz, I.2    Gotz, K.3    Schulze-Osthoff, K.4    Ruther, U.5
  • 4
    • 0028285369 scopus 로고
    • Enhancement of phorbol ester-induced production of tumor necrosis factor α by thalidomide
    • Nishimura, K., Hashimoto, Y., and Iwasaki, S. (1994) Enhancement of phorbol ester-induced production of tumor necrosis factor α by thalidomide Biochem. Biophys. Res. Commun. 199, 455-460
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 455-460
    • Nishimura, K.1    Hashimoto, Y.2    Iwasaki, S.3
  • 5
    • 0034936211 scopus 로고    scopus 로고
    • Thymidine phosphorylase inhibitors with a homophthalimide skeleton
    • Kita, T., Takahashi, H., and Hashimoto, Y. (2001) Thymidine phosphorylase inhibitors with a homophthalimide skeleton Biol. Pharm. Bull. 24, 860-862
    • (2001) Biol. Pharm. Bull. , vol.24 , pp. 860-862
    • Kita, T.1    Takahashi, H.2    Hashimoto, Y.3
  • 6
    • 10644272105 scopus 로고    scopus 로고
    • N-Phenylphthalimide-type cyclooxygenase (COX) inhibitors derived from thalidomide: Substituent effects on subtype selectivity
    • Sano, H., Noguchi, T., Tanatani, A., Miyachi, H., and Hashimoto, Y. (2004) N-Phenylphthalimide-type cyclooxygenase (COX) inhibitors derived from thalidomide: Substituent effects on subtype selectivity Chem. Pharm. Bull. 52, 1021-1022
    • (2004) Chem. Pharm. Bull. , vol.52 , pp. 1021-1022
    • Sano, H.1    Noguchi, T.2    Tanatani, A.3    Miyachi, H.4    Hashimoto, Y.5
  • 7
    • 33749430243 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of cyclic amide/imide-bearing hydroxamic acid derivatives as class-selective histone deacetylase (HDAC) inhibitors
    • Shinji, C., Maeda, S., Imai, K., Yoshida, M., Hashimoto, Y., and Miyachi, H. (2006) Design, synthesis, and evaluation of cyclic amide/imide-bearing hydroxamic acid derivatives as class-selective histone deacetylase (HDAC) inhibitors Bioorg. Med. Chem. 14, 7625-7651
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 7625-7651
    • Shinji, C.1    Maeda, S.2    Imai, K.3    Yoshida, M.4    Hashimoto, Y.5    Miyachi, H.6
  • 11
    • 33746802786 scopus 로고    scopus 로고
    • Tubulin polymerization inhibitors with a fluorinated phthalimide skeleton derived from thalidomide
    • Yanagawa, T., Noguchi, T., Miyachi, H., Kobayashi, H., and Hashimoto, Y. (2006) Tubulin polymerization inhibitors with a fluorinated phthalimide skeleton derived from thalidomide Bioorg. Med. Chem. Lett. 16, 4748-4751
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 4748-4751
    • Yanagawa, T.1    Noguchi, T.2    Miyachi, H.3    Kobayashi, H.4    Hashimoto, Y.5
  • 12
    • 84916238331 scopus 로고    scopus 로고
    • Thalidomide Embryopathy: An Enigmatic Challenge
    • Vargesson, N. (2013) Thalidomide Embryopathy: An Enigmatic Challenge ISRN Developmental Biology 2013, 18
    • (2013) ISRN Developmental Biology , vol.2013 , pp. 18
    • Vargesson, N.1
  • 13
    • 61349192318 scopus 로고    scopus 로고
    • Thalidomide resistance is based on the capacity of the glutathione-dependent antioxidant defense
    • Knobloch, J., Reimann, K., Klotz, L. O., and Ruther, U. (2008) Thalidomide resistance is based on the capacity of the glutathione-dependent antioxidant defense Mol. Pharmaceutics 5, 1138-1144
    • (2008) Mol. Pharmaceutics , vol.5 , pp. 1138-1144
    • Knobloch, J.1    Reimann, K.2    Klotz, L.O.3    Ruther, U.4
  • 15
    • 84857319432 scopus 로고    scopus 로고
    • Deciphering the mystery of thalidomide teratogenicity
    • Ito, T. and Handa, H. (2012) Deciphering the mystery of thalidomide teratogenicity Congenital Anomalies 52, 1-7
    • (2012) Congenital Anomalies , vol.52 , pp. 1-7
    • Ito, T.1    Handa, H.2
  • 16
    • 0023729816 scopus 로고
    • Proposed mechanisms of action in thalidomide embryopathy
    • Stephens, T. D. (1988) Proposed mechanisms of action in thalidomide embryopathy Teratology 38, 229-239
    • (1988) Teratology , vol.38 , pp. 229-239
    • Stephens, T.D.1
  • 17
    • 0032920883 scopus 로고    scopus 로고
    • Free radical-mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity
    • Parman, T., Wiley, M. J., and Wells, P. G. (1999) Free radical-mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity Nat. Med. 5, 582-585
    • (1999) Nat. Med. , vol.5 , pp. 582-585
    • Parman, T.1    Wiley, M.J.2    Wells, P.G.3
  • 20
    • 1942438028 scopus 로고    scopus 로고
    • Microtubules as a target for anticancer drugs
    • Jordan, M. A. and Wilson, L. (2004) Microtubules as a target for anticancer drugs Nat. Rev. Cancer 4, 253-265
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 253-265
    • Jordan, M.A.1    Wilson, L.2
  • 21
    • 0032933622 scopus 로고    scopus 로고
    • Taxol suppresses dynamics of individual microtubules in living human tumor cells
    • Yvon, A. M., Wadsworth, P., and Jordan, M. A. (1999) Taxol suppresses dynamics of individual microtubules in living human tumor cells Mol. Biol. Cell 10, 947-959
    • (1999) Mol. Biol. Cell , vol.10 , pp. 947-959
    • Yvon, A.M.1    Wadsworth, P.2    Jordan, M.A.3
  • 24
    • 38949128693 scopus 로고    scopus 로고
    • 5HPP-33, a Novel Tubulin-Polymerization Inhibitor Derived from Thalidomide, Directly Inhibits Proliferation and Induces Apoptosis of Human Multiple Myeloma Cells
    • Iguchi, T., Oda-Nakazato, S., Noguchi, T., Hashimoto, Y., Hattori, Y., Yamada, T., Ikeda, Y., and Kizaki, M. (2008) 5HPP-33, a Novel Tubulin-Polymerization Inhibitor Derived from Thalidomide, Directly Inhibits Proliferation and Induces Apoptosis of Human Multiple Myeloma Cells Int. J. Mol. Med. 21, 163-168
    • (2008) Int. J. Mol. Med. , vol.21 , pp. 163-168
    • Iguchi, T.1    Oda-Nakazato, S.2    Noguchi, T.3    Hashimoto, Y.4    Hattori, Y.5    Yamada, T.6    Ikeda, Y.7    Kizaki, M.8
  • 26
    • 84859492942 scopus 로고    scopus 로고
    • Kinetic stabilization of microtubule dynamics by indanocine perturbs EB1 localization, induces defects in cell polarity and inhibits migration of MDA-MB-231 cells
    • Kapoor, S. and Panda, D. (2012) Kinetic stabilization of microtubule dynamics by indanocine perturbs EB1 localization, induces defects in cell polarity and inhibits migration of MDA-MB-231 cells Biochem. Pharmacol. 83, 1495-1506
    • (2012) Biochem. Pharmacol. , vol.83 , pp. 1495-1506
    • Kapoor, S.1    Panda, D.2
  • 27
    • 84880835558 scopus 로고    scopus 로고
    • The suppression effects of thalidomide on human lung fibroblasts: Cell proliferation, vascular endothelial growth factor release, and collagen production
    • Tseng, C. M., Hsiao, Y. H., Su, V. Y., Su, K. C., Wu, Y. C., Chang, K. T., and Perng, D. W. (2013) The suppression effects of thalidomide on human lung fibroblasts: Cell proliferation, vascular endothelial growth factor release, and collagen production Lung 191, 361-368
    • (2013) Lung , vol.191 , pp. 361-368
    • Tseng, C.M.1    Hsiao, Y.H.2    Su, V.Y.3    Su, K.C.4    Wu, Y.C.5    Chang, K.T.6    Perng, D.W.7
  • 30
    • 84864409103 scopus 로고    scopus 로고
    • CIL-102 binds to tubulin at colchicine binding site and triggers apoptosis in MCF-7 cells by inducing monopolar and multinucleated cells
    • Gireesh, K. K., Rashid, A., Chakraborti, S., Panda, D., and Manna, T. (2012) CIL-102 binds to tubulin at colchicine binding site and triggers apoptosis in MCF-7 cells by inducing monopolar and multinucleated cells Biochem. Pharmacol. 84, 633-645
    • (2012) Biochem. Pharmacol. , vol.84 , pp. 633-645
    • Gireesh, K.K.1    Rashid, A.2    Chakraborti, S.3    Panda, D.4    Manna, T.5
  • 31
    • 84865635380 scopus 로고    scopus 로고
    • An antitubulin agent BCFMT inhibits proliferation of cancer cells and induces cell death by inhibiting microtubule dynamics
    • Rai, A., Surolia, A., and Panda, D. (2012) An antitubulin agent BCFMT inhibits proliferation of cancer cells and induces cell death by inhibiting microtubule dynamics PLoS One 7, e44311
    • (2012) PLoS One , vol.7
    • Rai, A.1    Surolia, A.2    Panda, D.3
  • 32
    • 51049098503 scopus 로고    scopus 로고
    • Kinetic stabilization of microtubule dynamics by estramustine is associated with tubulin acetylation, spindle abnormalities, and mitotic arrest
    • Mohan, R. and Panda, D. (2008) Kinetic stabilization of microtubule dynamics by estramustine is associated with tubulin acetylation, spindle abnormalities, and mitotic arrest Cancer Res. 68, 6181-6189
    • (2008) Cancer Res. , vol.68 , pp. 6181-6189
    • Mohan, R.1    Panda, D.2
  • 33
    • 56549120027 scopus 로고    scopus 로고
    • Kinetic stabilization of microtubule dynamic instability by benomyl increases the nuclear transport of p53
    • Rathinasamy, K. and Panda, D. (2008) Kinetic stabilization of microtubule dynamic instability by benomyl increases the nuclear transport of p53 Biochem. Pharmacol. 76, 1669-1680
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1669-1680
    • Rathinasamy, K.1    Panda, D.2
  • 34
    • 0024094432 scopus 로고
    • Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies
    • Walker, R. A., O'Brien, E. T., Pryer, N. K., Soboeiro, M. F., Voter, W. A., Erickson, H. P., and Salmon, E. D. (1988) Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies J. Cell Biol. 107, 1437-1448
    • (1988) J. Cell Biol. , vol.107 , pp. 1437-1448
    • Walker, R.A.1    O'Brien, E.T.2    Pryer, N.K.3    Soboeiro, M.F.4    Voter, W.A.5    Erickson, H.P.6    Salmon, E.D.7
  • 35
    • 0019513433 scopus 로고
    • Glutamate-induced polymerization of tubulin: Characteristics of the reaction and application to the large-scale purification of tubulin
    • Hamel, E. and Lin, C. M. (1981) Glutamate-induced polymerization of tubulin: Characteristics of the reaction and application to the large-scale purification of tubulin Arch. Biochem. Biophys. 209, 29-40
    • (1981) Arch. Biochem. Biophys. , vol.209 , pp. 29-40
    • Hamel, E.1    Lin, C.M.2
  • 36
    • 77952290395 scopus 로고    scopus 로고
    • HMBA depolymerizes microtubules, activates mitotic checkpoints and induces mitotic block in MCF-7 cells by binding at the colchicine site in tubulin
    • Chatterji, B. P., Banerjee, M., Singh, P., and Panda, D. (2010) HMBA depolymerizes microtubules, activates mitotic checkpoints and induces mitotic block in MCF-7 cells by binding at the colchicine site in tubulin Biochem. Pharmacol. 80, 50-61
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 50-61
    • Chatterji, B.P.1    Banerjee, M.2    Singh, P.3    Panda, D.4
  • 37
    • 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
  • 39
    • 77955291726 scopus 로고    scopus 로고
    • Fluorescence spectroscopic methods to analyze drug-tubulin interactions
    • Bhattacharyya, B., Kapoor, S., and Panda, D. (2010) Fluorescence spectroscopic methods to analyze drug-tubulin interactions Methods Cell Biol. 95, 301-329
    • (2010) Methods Cell Biol. , vol.95 , pp. 301-329
    • Bhattacharyya, B.1    Kapoor, S.2    Panda, D.3
  • 41
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf, A. W. and van Aalten, D. M. (2004) PRODRG: A tool for high-throughput crystallography of protein-ligand complexes Acta Crystallogr. D60, 1355-1363
    • (2004) Acta Crystallogr. , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 42
    • 84885050645 scopus 로고    scopus 로고
    • Ansamitocin P3 depolymerizes microtubules and induces apoptosis by binding to tubulin at the vinblastine site
    • Venghateri, J. B., Gupta, T. K., Verma, P. J., Kunwar, A., and Panda, D. (2013) Ansamitocin P3 depolymerizes microtubules and induces apoptosis by binding to tubulin at the vinblastine site PLoS One 8 (10) e75182
    • (2013) PLoS One , vol.8 , Issue.10
    • Venghateri, J.B.1    Gupta, T.K.2    Verma, P.J.3    Kunwar, A.4    Panda, D.5
  • 43
    • 0036084259 scopus 로고    scopus 로고
    • Efficient docking of peptides to proteins without prior knowledge of the binding site
    • Hetenyi, C. and van der Spoel, D. (2002) Efficient docking of peptides to proteins without prior knowledge of the binding site Protein Sci. 11, 1729-1737
    • (2002) Protein Sci. , vol.11 , pp. 1729-1737
    • Hetenyi, C.1    Van Der Spoel, D.2
  • 45
    • 84884576648 scopus 로고    scopus 로고
    • CXI-benzo-84 reversibly binds to tubulin at colchicine site and induces apoptosis in cancer cells
    • Rai, A., Gupta, T. K., Kini, S., Kunwar, A., Surolia, A., and Panda, D. (2013) CXI-benzo-84 reversibly binds to tubulin at colchicine site and induces apoptosis in cancer cells Biochem. Pharmacol. 86, 378-391
    • (2013) Biochem. Pharmacol. , vol.86 , pp. 378-391
    • Rai, A.1    Gupta, T.K.2    Kini, S.3    Kunwar, A.4    Surolia, A.5    Panda, D.6
  • 47
    • 0029115509 scopus 로고
    • Vinblastine suppresses dynamics of individual microtubules in living interphase cells
    • Dhamodharan, R., Jordan, M. A., Thrower, D., Wilson, L., and Wadsworth, P. (1995) Vinblastine suppresses dynamics of individual microtubules in living interphase cells Mol. Biol. Cell 6, 1215-1229
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1215-1229
    • Dhamodharan, R.1    Jordan, M.A.2    Thrower, D.3    Wilson, L.4    Wadsworth, P.5
  • 48
    • 42049099005 scopus 로고    scopus 로고
    • New tubulin polymerization inhibitor derived from thalidomide: Implications for anti-myeloma therapy
    • Kizaki, M. and Hashimoto, Y. (2008) New tubulin polymerization inhibitor derived from thalidomide: Implications for anti-myeloma therapy Curr. Med. Chem. 15, 754-765
    • (2008) Curr. Med. Chem. , vol.15 , pp. 754-765
    • Kizaki, M.1    Hashimoto, Y.2
  • 49
    • 0023112960 scopus 로고
    • Photoaffinity labeling of tubulin subunits with a photoactive analogue of vinblastine
    • Safa, A. R., Hamel, E., and Felsted, R. L. (1987) Photoaffinity labeling of tubulin subunits with a photoactive analogue of vinblastine Biochemistry 26, 97-102
    • (1987) Biochemistry , vol.26 , pp. 97-102
    • Safa, A.R.1    Hamel, E.2    Felsted, R.L.3
  • 50
    • 0016701089 scopus 로고
    • Interaction of Vinblastine with Calf Brain Microtubule Protein
    • Lee, J. C., Harrison, D., and Timasheff, S. N. (1975) Interaction of Vinblastine with Calf Brain Microtubule Protein J. Biol. Chem. 250, 9276-9282
    • (1975) J. Biol. Chem. , vol.250 , pp. 9276-9282
    • Lee, J.C.1    Harrison, D.2    Timasheff, S.N.3
  • 51
    • 77955289715 scopus 로고    scopus 로고
    • The binding of vinca domain agents to tubulin: Structural and biochemical studies
    • Cormier, A., Knossow, M., Wang, C., and Gigant, B. (2010) The binding of vinca domain agents to tubulin: Structural and biochemical studies Methods Cell Biol. 95, 373-390
    • (2010) Methods Cell Biol. , vol.95 , pp. 373-390
    • Cormier, A.1    Knossow, M.2    Wang, C.3    Gigant, B.4
  • 52
    • 84886135220 scopus 로고    scopus 로고
    • A vinblastine fluorescent probe for pregnane X receptor in a time-resolved fluorescence resonance energy transfer assay
    • Lin, W. and Chen, T. (2013) A vinblastine fluorescent probe for pregnane X receptor in a time-resolved fluorescence resonance energy transfer assay Anal. Biochem. 443, 252-260
    • (2013) Anal. Biochem. , vol.443 , pp. 252-260
    • Lin, W.1    Chen, T.2
  • 54
    • 33749565180 scopus 로고    scopus 로고
    • Microtubule-targeting agents inhibit angiogenesis at subtoxic concentrations, a process associated with inhibition of Rac1 and Cdc42 activity and changes in the endothelial cytoskeleton
    • Bijman, M. N., van Nieuw Amerongen, G. P., Laurens, N., van Hinsbergh, V. W., and Boven, E. (2006) Microtubule-targeting agents inhibit angiogenesis at subtoxic concentrations, a process associated with inhibition of Rac1 and Cdc42 activity and changes in the endothelial cytoskeleton Mol. Cancer Ther. 5, 2348-2357
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 2348-2357
    • Bijman, M.N.1    Van Nieuw Amerongen, G.P.2    Laurens, N.3    Van Hinsbergh, V.W.4    Boven, E.5
  • 55
    • 0024310174 scopus 로고
    • Role of microtubule assembly in phenytoin teratogenic action in the sea urchin (Arbacia punctulata) embryo
    • Estus, S. and Blumer, J. L. (1989) Role of microtubule assembly in phenytoin teratogenic action in the sea urchin (Arbacia punctulata) embryo Mol. Pharmacol. 36, 708-715
    • (1989) Mol. Pharmacol. , vol.36 , pp. 708-715
    • Estus, S.1    Blumer, J.L.2
  • 56
    • 0007276205 scopus 로고
    • Congenital malformations in hamster embryos after treatment with vinblastine and vincristine
    • Ferm, V. H. (1963) Congenital malformations in hamster embryos after treatment with vinblastine and vincristine Science 141, 426
    • (1963) Science , vol.141 , pp. 426
    • Ferm, V.H.1
  • 57
    • 0026040213 scopus 로고
    • Colchicine: A state-of-the-art review
    • Levy, M., Spino, M., and Read, S. E. (1991) Colchicine: A state-of-the-art review Pharmacotherapy 11, 196-211
    • (1991) Pharmacotherapy , vol.11 , pp. 196-211
    • Levy, M.1    Spino, M.2    Read, S.E.3
  • 59
    • 33845640597 scopus 로고    scopus 로고
    • Teratogen-induced activation of p53 in early postimplantation mouse embryos
    • Hosako, H., Little, S. A., Barrier, M., and Mirkes, P. E. (2007) Teratogen-induced activation of p53 in early postimplantation mouse embryos Toxicol. Sci. 95, 257-269
    • (2007) Toxicol. Sci. , vol.95 , pp. 257-269
    • Hosako, H.1    Little, S.A.2    Barrier, M.3    Mirkes, P.E.4
  • 61
    • 34548008152 scopus 로고    scopus 로고
    • p53 regulates cyclophosphamide teratogenesis by controlling caspases 3, 8, 9 activation and NF-κB DNA binding
    • Pekar, O., Molotski, N., Savion, S., Fein, A., Toder, V., and Torchinsky, A. (2007) p53 regulates cyclophosphamide teratogenesis by controlling caspases 3, 8, 9 activation and NF-κB DNA binding Reproduction 134, 379-388
    • (2007) Reproduction , vol.134 , pp. 379-388
    • Pekar, O.1    Molotski, N.2    Savion, S.3    Fein, A.4    Toder, V.5    Torchinsky, A.6
  • 62
    • 84877146937 scopus 로고    scopus 로고
    • p53 family and VEGF regulation: "It's complicated"
    • Farhang Ghahremani, M., Goossens, S., and Haigh, J. J. (2013) p53 family and VEGF regulation: "It's complicated" Cell Cycle 12, 1331-1332
    • (2013) Cell Cycle , vol.12 , pp. 1331-1332
    • Farhang Ghahremani, M.1    Goossens, S.2    Haigh, J.J.3
  • 65
    • 0026593331 scopus 로고
    • Expression of vascular endothelial growth factor during embryonic angiogenesis and endothelial cell differentiation
    • Breier, G., Albrecht, U., Sterrer, S., and Risau, W. (1992) Expression of vascular endothelial growth factor during embryonic angiogenesis and endothelial cell differentiation Development 114, 521-532
    • (1992) Development , vol.114 , pp. 521-532
    • Breier, G.1    Albrecht, U.2    Sterrer, S.3    Risau, W.4


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