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Volumn 15, Issue 4, 2004, Pages 197-204

The PDGF family: Four gene products form five dimeric isoforms

Author keywords

Dimeric isoforms; PDGF; Receptor

Indexed keywords

GENE PRODUCT; GENOMIC DNA; ISOPROTEIN; PLATELET DERIVED GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR A; PLATELET DERIVED GROWTH FACTOR B;

EID: 2942676788     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2004.03.007     Document Type: Article
Times cited : (668)

References (51)
  • 4
    • 0025767917 scopus 로고
    • A novel mechanism regulating growth factor association with the cell surface: Identification of a PDGF retention domain
    • LaRochelle W.J., May-Siroff M., Robbins K.C., Aaronson S.A. A novel mechanism regulating growth factor association with the cell surface: identification of a PDGF retention domain. Genes Dev. 5:1991;1191-1199
    • (1991) Genes Dev , vol.5 , pp. 1191-1199
    • Larochelle, W.J.1    May-Siroff, M.2    Robbins, K.C.3    Aaronson, S.A.4
  • 5
    • 0026182139 scopus 로고
    • Identification of a cell retention signal in the B-chain of platelet-derived growth factor and in the long splice version of the A-chain
    • Östman A., Andersson M., Betsholtz C., Westermark B., Heldin C.H. Identification of a cell retention signal in the B-chain of platelet-derived growth factor and in the long splice version of the A-chain. Cell Regulat. 2:1991;503-512
    • (1991) Cell Regulat , vol.2 , pp. 503-512
    • Östman, A.1    Andersson, M.2    Betsholtz, C.3    Westermark, B.4    Heldin, C.H.5
  • 7
    • 0035812719 scopus 로고    scopus 로고
    • Guidance of cell migration by the Drosophila PDGF/VEGF receptor
    • Duchek P., Somogyi K., Jekely G., Beccari S., Rorth P. Guidance of cell migration by the Drosophila PDGF/VEGF receptor. Cell. 107:2001;17-26
    • (2001) Cell , vol.107 , pp. 17-26
    • Duchek, P.1    Somogyi, K.2    Jekely, G.3    Beccari, S.4    Rorth, P.5
  • 9
    • 0037155683 scopus 로고    scopus 로고
    • Developmental control of blood cell migration by the Drosophila VEGF pathway
    • Cho N.K., Keyes L., Johnson E., Heller J., Ryner L., Karim F., et al. Developmental control of blood cell migration by the Drosophila VEGF pathway. Cell. 108:2002;865-876
    • (2002) Cell , vol.108 , pp. 865-876
    • Cho, N.K.1    Keyes, L.2    Johnson, E.3    Heller, J.4    Ryner, L.5    Karim, F.6
  • 10
    • 4644293902 scopus 로고    scopus 로고
    • PVF2, a PDGF/VEGF-like growth factor, induces hemocyte proliferation in Drosophila larvae
    • Munier A.I., Doucet D., Perrodou E., Zachary D., Meister M., Hoffmann J.A., et al. PVF2, a PDGF/VEGF-like growth factor, induces hemocyte proliferation in Drosophila larvae. EMBO Rep. 3:2002;1195-1200
    • (2002) EMBO Rep. , vol.3 , pp. 1195-1200
    • Munier, A.I.1    Doucet, D.2    Perrodou, E.3    Zachary, D.4    Meister, M.5    Hoffmann, J.A.6
  • 11
    • 0042977586 scopus 로고    scopus 로고
    • PVF1, a PDGF/VEGF homolog, is sufficient to guide border cells and interacts genetically with Taiman
    • McDonald J.A., Pinheiro E.M., Montell D.J. PVF1, a PDGF/VEGF homolog, is sufficient to guide border cells and interacts genetically with Taiman. Development. 130:2003;3469-3478
    • (2003) Development , vol.130 , pp. 3469-3478
    • McDonald, J.A.1    Pinheiro, E.M.2    Montell, D.J.3
  • 12
    • 0035955692 scopus 로고    scopus 로고
    • Molecular cloning and expression of a functional snake venom vascular endothelium growth factor (VEGF) from the Bothrops insularis pit viper. A new member of the VEGF family of proteins
    • Junqueira de Azevedo I.L., Farsky S.H., Oliveira M.L., Ho P.L. Molecular cloning and expression of a functional snake venom vascular endothelium growth factor (VEGF) from the Bothrops insularis pit viper. A new member of the VEGF family of proteins. J. Biol. Chem. 276:2001;39836-39842
    • (2001) J. Biol. Chem. , vol.276 , pp. 39836-39842
    • Junqueira De Azevedo, I.L.1    Farsky, S.H.2    Oliveira, M.L.3    Ho, P.L.4
  • 13
    • 0346101800 scopus 로고    scopus 로고
    • Snake venom vascular endothelial growth factors (VEGFs) exhibit potent activity through their specific recognition of KDR (VEGF receptor 2)
    • Yamazaki Y., Takani K., Atoda H., Morita T. Snake venom vascular endothelial growth factors (VEGFs) exhibit potent activity through their specific recognition of KDR (VEGF receptor 2). J. Biol Chem. 278:2003;51985-51988
    • (2003) J. Biol Chem. , vol.278 , pp. 51985-51988
    • Yamazaki, Y.1    Takani, K.2    Atoda, H.3    Morita, T.4
  • 14
    • 0027918158 scopus 로고
    • Topological similarities in TGF-β2, PDGF-BB and NGF define a superfamily of polypeptide growth factors
    • Murray-Rust J., McDonald N.Q., Blundell T.L., Hosang M., Oefner C., Winkler F., et al. Topological similarities in TGF-β2, PDGF-BB and NGF define a superfamily of polypeptide growth factors. Structure. 1:1993;153-159
    • (1993) Structure , vol.1 , pp. 153-159
    • Murray-Rust, J.1    McDonald, N.Q.2    Blundell, T.L.3    Hosang, M.4    Oefner, C.5    Winkler, F.6
  • 15
    • 0026744790 scopus 로고
    • Crystal structure of human platelet-derived growth factor BB
    • Oefner C., D'Arcy A., Winkler F.K., Eggimann B., Hosang M. Crystal structure of human platelet-derived growth factor BB. EMBO J. 11:1992;3921-3926
    • (1992) EMBO J. , vol.11 , pp. 3921-3926
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3    Eggimann, B.4    Hosang, M.5
  • 16
    • 0030795733 scopus 로고    scopus 로고
    • Vascular endothelial growth factor - Crystal structure and functional mapping of the kinase domain receptor binding site
    • Muller Y.A., Li B., Christinger H.W., Wells J.A., Cunningham B.C., Devos A.M. Vascular endothelial growth factor - crystal structure and functional mapping of the kinase domain receptor binding site. Proc. Natl. Acad. Sci. 94:1997;7192-7197
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 7192-7197
    • Muller, Y.A.1    Li, B.2    Christinger, H.W.3    Wells, J.A.4    Cunningham, B.C.5    Devos, A.M.6
  • 17
    • 0027190974 scopus 로고
    • The CUB domain. A widespread module in developmentally regulated proteins
    • Bork P., Beckmann G. The CUB domain. A widespread module in developmentally regulated proteins. J. Mol. Biol. 231:1993;539-545
    • (1993) J. Mol. Biol. , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 18
    • 0031565824 scopus 로고    scopus 로고
    • The 2.4 a resolution crystal structure of boar seminal plasma PSPI/PSP. II. A zona pellucida-binding glycoprotein heterodimer of the spermadhesin family built by a CUB domain architecture
    • Varela P.F., Romero A., Sanz L., Romao M.J., Topfer-Petersen E., Calvete J.J. The 2.4 A resolution crystal structure of boar seminal plasma PSPI/PSP. II. A zona pellucida-binding glycoprotein heterodimer of the spermadhesin family built by a CUB domain architecture. J. Mol. Biol. 274:1997;635-649
    • (1997) J. Mol. Biol. , vol.274 , pp. 635-649
    • Varela, P.F.1    Romero, A.2    Sanz, L.3    Romao, M.J.4    Topfer-Petersen, E.5    Calvete, J.J.6
  • 19
    • 0029965081 scopus 로고    scopus 로고
    • Characterization of novel vascular endothelial growth factor (VEGF) receptors on tumor cells that bind VEGF165 via its exon 7-encoded domain
    • Soker S., Fidder H., Neufeld G., Klagsburn M. Characterization of novel vascular endothelial growth factor (VEGF) receptors on tumor cells that bind VEGF165 via its exon 7-encoded domain. J. Biol. Chem. 271:1996;5761-5767
    • (1996) J. Biol. Chem. , vol.271 , pp. 5761-5767
    • Soker, S.1    Fidder, H.2    Neufeld, G.3    Klagsburn, M.4
  • 20
    • 0032549799 scopus 로고    scopus 로고
    • Neurophilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor
    • Soker S., Takashima S., Quan Miao H., Neufeld G., Klagsbrun M. Neurophilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell. 92:1998;735-745
    • (1998) Cell , vol.92 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Quan Miao, H.3    Neufeld, G.4    Klagsbrun, M.5
  • 21
    • 0033597813 scopus 로고    scopus 로고
    • Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1
    • Mäkinen T., Olofsson B., Karpanen T., Hellman U., Soker S., Klagsburn M., et al. Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1. J. Biol. Chem. 274:1999;21217-21222
    • (1999) J. Biol. Chem. , vol.274 , pp. 21217-21222
    • Mäkinen, T.1    Olofsson, B.2    Karpanen, T.3    Hellman, U.4    Soker, S.5    Klagsburn, M.6
  • 22
    • 0034703022 scopus 로고    scopus 로고
    • Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165
    • Gluzman-Poltorak Z., Cohen T., Herzog Y., Neufeld G. Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165. J. Biol. Chem. 275:2000;29922
    • (2000) J. Biol. Chem. , vol.275 , pp. 29922
    • Gluzman-Poltorak, Z.1    Cohen, T.2    Herzog, Y.3    Neufeld, G.4
  • 23
    • 0037025311 scopus 로고    scopus 로고
    • Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain
    • Mamluk R., Gechtman Z., Kutcher M.E., Gasiunas N., Gallagher J., Klagsbrun M. Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain. J. Biol. Chem. 277:2002;24818-24825
    • (2002) J. Biol. Chem. , vol.277 , pp. 24818-24825
    • Mamluk, R.1    Gechtman, Z.2    Kutcher, M.E.3    Gasiunas, N.4    Gallagher, J.5    Klagsbrun, M.6
  • 24
    • 0032215144 scopus 로고    scopus 로고
    • Neuropilin-2 is a receptor for semaphorin IV: Insight into the structural basis of receptor function and specificity
    • Giger R.J., Urquhart E.R., Gillespie S.K., Levengood D.V., Ginty D.D., Kolodkin A.L. Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity. Neuron. 21:1998;1079-1092
    • (1998) Neuron , vol.21 , pp. 1079-1092
    • Giger, R.J.1    Urquhart, E.R.2    Gillespie, S.K.3    Levengood, D.V.4    Ginty, D.D.5    Kolodkin, A.L.6
  • 25
    • 0032215735 scopus 로고    scopus 로고
    • Neuropilin-1 extracellular domains mediate semaphorin D/III-induced growth cone collapse
    • Nakamura F., Tanaka M., Takahashi T., Kalb R.G., Strittmatter S.M. Neuropilin-1 extracellular domains mediate semaphorin D/III-induced growth cone collapse. Neuron. 21:1998;1093-1100
    • (1998) Neuron , vol.21 , pp. 1093-1100
    • Nakamura, F.1    Tanaka, M.2    Takahashi, T.3    Kalb, R.G.4    Strittmatter, S.M.5
  • 26
    • 0019923140 scopus 로고
    • Chromosomal localization of the human homolog (c-sis) of the simian sarcoma virus onc gene
    • Dalla-Favera R., Gallo R.C., Giallongo A., Croce C.M. Chromosomal localization of the human homolog (c-sis) of the simian sarcoma virus onc gene. Science. 218:1982;686-688
    • (1982) Science , vol.218 , pp. 686-688
    • Dalla-Favera, R.1    Gallo, R.C.2    Giallongo, A.3    Croce, C.M.4
  • 28
    • 0022447025 scopus 로고
    • CDNA sequence and chromosomal localization of human platelet-derived growth factor A-chain and its expression in tumour cell lines
    • Betsholtz C., Johnsson A., Heldin C.H., Westermark B., Lind P., Urdea M.S., et al. cDNA sequence and chromosomal localization of human platelet-derived growth factor A-chain and its expression in tumour cell lines. Nature. 320:1986;695-699
    • (1986) Nature , vol.320 , pp. 695-699
    • Betsholtz, C.1    Johnsson, A.2    Heldin, C.H.3    Westermark, B.4    Lind, P.5    Urdea, M.S.6
  • 29
    • 0035826891 scopus 로고    scopus 로고
    • Chromosomal location, exon structure, and vascular expression patterns of the human PDGFC and PDGFD genes
    • Uutela M., Lauren J., Bergsten E., Li X., Horelli-Kuitunen N., Eriksson U., et al. Chromosomal location, exon structure, and vascular expression patterns of the human PDGFC and PDGFD genes. Circulation. 103:2001;2242-2247
    • (2001) Circulation , vol.103 , pp. 2242-2247
    • Uutela, M.1    Lauren, J.2    Bergsten, E.3    Li, X.4    Horelli-Kuitunen, N.5    Eriksson, U.6
  • 30
    • 0021430551 scopus 로고
    • The c-sis gene encodes a precursor of the B chain of platelet-derived growth factor
    • Johnsson A., Heldin C.H., Wasteson A., Westermark B., Deuel T.F., Huang J.S., et al. The c-sis gene encodes a precursor of the B chain of platelet-derived growth factor. EMBO J. 3:1984;921-928
    • (1984) EMBO J. , vol.3 , pp. 921-928
    • Johnsson, A.1    Heldin, C.H.2    Wasteson, A.3    Westermark, B.4    Deuel, T.F.5    Huang, J.S.6
  • 31
    • 0026648227 scopus 로고
    • Platelet-derived growth factor a chain: Confirmation of localization of PDGFA to chromosome 7p22 and description of an unusual minisatellite
    • Bonthron D., Collins T., Grzeschik K.H., van Roy N., Speleman F. Platelet-derived growth factor A chain: confirmation of localization of PDGFA to chromosome 7p22 and description of an unusual minisatellite. Genomics. 13:1992;257-263
    • (1992) Genomics , vol.13 , pp. 257-263
    • Bonthron, D.1    Collins, T.2    Grzeschik, K.H.3    Van Roy, N.4    Speleman, F.5
  • 32
    • 0026700690 scopus 로고
    • Characterization of the mouse PDGF A-chain gene. Evolutionary conservation of gene structure
    • Rorsman F., Leveen P., Betsholtz C. Characterization of the mouse PDGF A-chain gene. Evolutionary conservation of gene structure. Growth Factors. 7:1992;241-251
    • (1992) Growth Factors , vol.7 , pp. 241-251
    • Rorsman, F.1    Leveen, P.2    Betsholtz, C.3
  • 33
    • 0041347558 scopus 로고    scopus 로고
    • A novel murine PDGF-D splicing variant results in significant differences in peptide expression and function
    • Zhuo Y., Hoyle G.W., Zhang J., Morris G., Lasky J.A. A novel murine PDGF-D splicing variant results in significant differences in peptide expression and function. Biochem Biophys Res Commun. 308:2003;126-132
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 126-132
    • Zhuo, Y.1    Hoyle, G.W.2    Zhang, J.3    Morris, G.4    Lasky, J.A.5
  • 34
    • 0032875460 scopus 로고    scopus 로고
    • Mechanism of action and in vivo role of platelet-derived growth factor
    • Heldin C.H., Westermark B. Mechanism of action and in vivo role of platelet-derived growth factor. Physiol. Rev. 79:1999;1283-1316
    • (1999) Physiol. Rev. , vol.79 , pp. 1283-1316
    • Heldin, C.H.1    Westermark, B.2
  • 35
    • 0026446402 scopus 로고
    • Platelet-derived growth factor-A and its receptor are expressed in separate, but adjacent cell layers of the mouse embryo
    • Orr-Urtreger A., Lonai P. Platelet-derived growth factor-A and its receptor are expressed in separate, but adjacent cell layers of the mouse embryo. Development. 115:1992;1045-1058
    • (1992) Development , vol.115 , pp. 1045-1058
    • Orr-Urtreger, A.1    Lonai, P.2
  • 36
    • 0030730837 scopus 로고    scopus 로고
    • Alveogenesis failure in PDGF-A-deficient mice is coupled to lack of distal spreading of alveolar smooth muscle cell progenitors during lung development
    • Lindahl P., Karlsson L., Hellström M., Gebre-Medhin S., Willetts K., Heath J.K., et al. Alveogenesis failure in PDGF-A-deficient mice is coupled to lack of distal spreading of alveolar smooth muscle cell progenitors during lung development. Development. 124:1997;3943-3953
    • (1997) Development , vol.124 , pp. 3943-3953
    • Lindahl, P.1    Karlsson, L.2    Hellström, M.3    Gebre-Medhin, S.4    Willetts, K.5    Heath, J.K.6
  • 37
    • 0032774661 scopus 로고    scopus 로고
    • Roles for PDGF-A and sonic hedgehog in development of mesenchymal components of the hair follicle
    • Karlsson L., Bondjers C., Betsholtz C. Roles for PDGF-A and sonic hedgehog in development of mesenchymal components of the hair follicle. Development. 126:1999;2611-2621
    • (1999) Development , vol.126 , pp. 2611-2621
    • Karlsson, L.1    Bondjers, C.2    Betsholtz, C.3
  • 38
    • 0033832891 scopus 로고    scopus 로고
    • Abnormal gastrointestinal development in PDGF-A and PDGFR-(alpha) deficient mice implicates a novel mesenchymal structure with putative instructive properties in villus morphogenesis
    • Karlsson L., Lindahl P., Heath J.K., Betsholtz C. Abnormal gastrointestinal development in PDGF-A and PDGFR-(alpha) deficient mice implicates a novel mesenchymal structure with putative instructive properties in villus morphogenesis. Development. 127:2000;3457-3466
    • (2000) Development , vol.127 , pp. 3457-3466
    • Karlsson, L.1    Lindahl, P.2    Heath, J.K.3    Betsholtz, C.4
  • 39
    • 0032768156 scopus 로고    scopus 로고
    • Role of PDGF-B and PDGFR-beta in recruitment of vascular smooth muscle cells and pericytes during embryonic blood vessel formation in the mouse
    • Hellström M., Kalén M., Lindahl P., Abramsson A., Betsholtz C. Role of PDGF-B and PDGFR-beta in recruitment of vascular smooth muscle cells and pericytes during embryonic blood vessel formation in the mouse. Development. 126:1999;3047-3055
    • (1999) Development , vol.126 , pp. 3047-3055
    • Hellström, M.1    Kalén, M.2    Lindahl, P.3    Abramsson, A.4    Betsholtz, C.5
  • 40
    • 0034706020 scopus 로고    scopus 로고
    • The mouse Pdgfc gene: Dynamic expression in embryonic tissues during organogenesis
    • Ding H., Wu X., Kim I., Tam P.P., Koh G.Y., Nagy A. The mouse Pdgfc gene: dynamic expression in embryonic tissues during organogenesis. Mech. Dev. 96:2000;209-213
    • (2000) Mech. Dev. , vol.96 , pp. 209-213
    • Ding, H.1    Wu, X.2    Kim, I.3    Tam, P.P.4    Koh, G.Y.5    Nagy, A.6
  • 41
    • 0035663713 scopus 로고    scopus 로고
    • Expression analysis of PDGF-C in adult and developing mouse tissues
    • Aase K., Abramsson A., Karlsson L., Betsholtz C., Eriksson U. Expression analysis of PDGF-C in adult and developing mouse tissues. Mech. Dev. 110:2002;187-191
    • (2002) Mech. Dev. , vol.110 , pp. 187-191
    • Aase, K.1    Abramsson, A.2    Karlsson, L.3    Betsholtz, C.4    Eriksson, U.5
  • 42
    • 0036175903 scopus 로고    scopus 로고
    • The expression of SCDGF/PDGFC/fallotein and SCDGF-B/PDGF-D in the rat central nervous system
    • Hamada T., Ui-Tei K., Imaki J., Takahashi F., Onodera H., Mishima T., et al. The expression of SCDGF/PDGFC/fallotein and SCDGF-B/PDGF-D in the rat central nervous system. Mech. Dev. 112:2002;161-164
    • (2002) Mech. Dev. , vol.112 , pp. 161-164
    • Hamada, T.1    Ui-Tei, K.2    Imaki, J.3    Takahashi, F.4    Onodera, H.5    Mishima, T.6
  • 43
    • 0026685187 scopus 로고
    • PDGF-AA and PDGF-BB biosynthesis: Proprotein processing in the Golgi complex and lysosomal degradation of PDGF-BB retained intracellularly
    • Östman A., Thyberg J., Westermark B., Heldin C.-H. PDGF-AA and PDGF-BB biosynthesis: proprotein processing in the Golgi complex and lysosomal degradation of PDGF-BB retained intracellularly. J. Cell Biol. 118:1992;509-519
    • (1992) J. Cell Biol. , vol.118 , pp. 509-519
    • Östman, A.1    Thyberg, J.2    Westermark, B.3    Heldin, C.-H.4
  • 44
    • 0042125242 scopus 로고    scopus 로고
    • Endothelial PDGF-B retention is required for proper investment of pericytes in the microvessel wall
    • Lindblom P., Gerhardt H., Liebner S., Abramsson A., Enge M., Hellström M., et al. Endothelial PDGF-B retention is required for proper investment of pericytes in the microvessel wall. Genes Dev. 17:2003;1835-1840
    • (2003) Genes Dev. , vol.17 , pp. 1835-1840
    • Lindblom, P.1    Gerhardt, H.2    Liebner, S.3    Abramsson, A.4    Enge, M.5    Hellström, M.6
  • 45
    • 0037379743 scopus 로고    scopus 로고
    • The proteolytic processing of pro-platelet-derived growth factor-A at RRKR(86) by members of the proprotein convertase family is functionally correlated to platelet-derived growth factor-A-induced functions and tumorigenicity
    • Siegfried G., Khatib A.M., Benjannet S., Chretien M., Seidah N.G. The proteolytic processing of pro-platelet-derived growth factor-A at RRKR(86) by members of the proprotein convertase family is functionally correlated to platelet-derived growth factor-A-induced functions and tumorigenicity. Cancer Res. 63:2003;1458-1463
    • (2003) Cancer Res. , vol.63 , pp. 1458-1463
    • Siegfried, G.1    Khatib, A.M.2    Benjannet, S.3    Chretien, M.4    Seidah, N.G.5
  • 48
    • 0009121951 scopus 로고    scopus 로고
    • Platelet-derived growth factor C (PDGF-C) a novel growth factor that binds to PDGF {alpha} and {beta} receptor
    • Gilbertson D.G., Duff M.E., West J.W. Platelet-derived growth factor C (PDGF-C) a novel growth factor that binds to PDGF {alpha} and {beta} receptor. J. Biol. Chem. 10:2001;10
    • (2001) J. Biol. Chem. , vol.10 , pp. 10
    • Gilbertson, D.G.1    Duff, M.E.2    West, J.W.3
  • 49
    • 0035242001 scopus 로고    scopus 로고
    • PDGF-C is an EWS/FLI induced transforming growth factor in Ewing family tumors
    • Zwerner J.P., May W.A. PDGF-C is an EWS/FLI induced transforming growth factor in Ewing family tumors. Oncogene. 20:2001;626-633
    • (2001) Oncogene , vol.20 , pp. 626-633
    • Zwerner, J.P.1    May, W.A.2
  • 50
    • 0036793520 scopus 로고    scopus 로고
    • Angiogenesis stimulated by PDGFCC, a novel member in the PDGF family, involves activation of PDGFR-alphaalpha and -alphabeta receptors
    • Cao R., Bråkenhielm E., Li X. Angiogenesis stimulated by PDGFCC, a novel member in the PDGF family, involves activation of PDGFR-alphaalpha and -alphabeta receptors. FASEB J. 16:2002;1575-1583
    • (2002) FASEB J. , vol.16 , pp. 1575-1583
    • Cao, R.1    Bråkenhielm, E.2    Li, X.3
  • 51
    • 0037380709 scopus 로고    scopus 로고
    • Novel PDGF family members: PDGF-C and PDGFD
    • Li X., Eriksson U. Novel PDGF family members: PDGF-C and PDGFD. Cytokine Growth Factor Rev. 14:2003;91-98
    • (2003) Cytokine Growth Factor Rev. , vol.14 , pp. 91-98
    • Li, X.1    Eriksson, U.2


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