[1] Lesot, H., Kuhl, U. and Mark, K.V. Isolation of a laminin-binding protein from muscle cell membranes. EMBO J.
2 (1983) 861–865. Google Scholar
[2] Malinoff, H.L. and Wicha, M.S. Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells. J. Cell Biol.
96 (1983) 1475–1479. http://dx.doi.org/10.1083/jcb.96.5.1475CrossrefGoogle Scholar
[3] Rao, N.C., Barsky, S.H., Terranova, V.P. and Liotta, L.A. Isolation of a tumor cell laminin receptor. Biochem. Biophys. Res. Commun.
111 (1983) 804–808. http://dx.doi.org/10.1016/0006-291X(83)91370-0CrossrefGoogle Scholar
[4] Rao, C.N., Castronovo, V., Schmitt, M.C., Wewer, U.M., Claysmith, A.P., Liotta, L.A. and Sobel, M.E. Evidence for a precursor of the high-affinity metastasis-associated murine laminin receptor. Biochemistry
28 (1989) 7476–7486. http://dx.doi.org/10.1021/bi00444a047CrossrefGoogle Scholar
[5] Yow, H.K., Wong, J.M., Chen, H.S., Lee, C.G., Davis, S., Steele, G.D., Jr. and Chen, L.B. Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein. Proc. Natl. Acad. Sci. USA
85 (1988) 6394–6398. http://dx.doi.org/10.1073/pnas.85.17.6394CrossrefGoogle Scholar
[6] Tohgo, A., Takasawa, S., Munakata, H., Yonekura, H., Hayashi, N. and Okamoto, H. Structural determination and characterization of a 40-kDa protein isolated from rat 40 S ribosomal subunit. FEBS Lett.
340 (1994) 133–138. http://dx.doi.org/10.1016/0014-5793(94)80188-6CrossrefGoogle Scholar
[7] Auth, D. and Brawerman, G. A 33-kDa polypeptide with homology to the laminin receptor: component of translation machinery. Proc. Natl. Acad. Sci. USA
89 (1992) 4368–4372. http://dx.doi.org/10.1073/pnas.89.10.4368CrossrefGoogle Scholar
[8] Sato, M., Kinoshita, K., Kaneda, Y., Saeki, Y., Iwamatsu, A. and Tanaka, K. Analysis of nuclear localization of laminin binding protein precursor p40 (LBP/p40). Biochem. Biophys. Res. Commun.
229 (1996) 896–901. http://dx.doi.org/10.1006/bbrc.1996.1899CrossrefGoogle Scholar
[9] Mecham, R.P., Hinek, A., Griffin, G.L., Senior, R.M. and Liotta, L.A. The elastin receptor shows structural and functional similarities to the 67-kDa tumor cell laminin receptor. J. Biol. Chem.
264 (1989) 16652–16657. Google Scholar
[10] McCaffery, P., Neve, R.L. and Drager, U.C. A dorso-ventral asymmetry in the embryonic retina defined by protein conformation. Proc. Natl. Acad. Sci. USA
87 (1990) 8570–8574. http://dx.doi.org/10.1073/pnas.87.21.8570CrossrefGoogle Scholar
[11] Rieger, R., Edenhofer, F., Lasmezas, C.I. and Weiss, S. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat. Med.
3 (1997) 1383–1388. http://dx.doi.org/10.1038/nm1297-1383CrossrefGoogle Scholar
[12] Gauczynski, S., Peyrin, J.M., Haik, S., Leucht, C., Hundt, C., Rieger, R., Krasemann, S., Deslys, J.P., Dormont, D., Lasmezas, C.I. and Weiss, S. The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein. EMBO J.
20 (2001) 5863–5875. http://dx.doi.org/10.1093/emboj/20.21.5863CrossrefGoogle Scholar
[13] Gauczynski, S., Nikles, D., El-Gogo, S., Papy-Garcia, D., Rey, C., Alban, S., Barritault, D., Lasmezas, C.I. and Weiss, S. The 37-kDa/67-kDa laminin receptor acts as a receptor for infectious prions and is inhibited by polysulfated glycanes. J. Infect. Dis.
194 (2006) 702–709. http://dx.doi.org/10.1086/505914CrossrefGoogle Scholar
[14] Ludewigs, H., Zuber, C., Vana, K., Nikles, D., Zerr, I. and Weiss, S. Therapeutic approaches for prion disorders. Expert Rev. Anti. Infect. Ther.
5 (2007) 613–630. http://dx.doi.org/10.1586/14787210.5.4.613CrossrefGoogle Scholar
[15] Vana, K., Zuber, C., Nikles, D. and Weiss, S. Novel aspects of prions, their receptor molecules, and innovative approaches for TSE therapy. Cell. Mol. Neurobiol.
27 (2007)107–128. http://dx.doi.org/10.1007/s10571-006-9121-1Web of ScienceCrossrefGoogle Scholar
[16] Zuber, C., Ludewigs, H. and Weiss, S. Therapeutic approaches targeting the prion receptor LRP/LR. Vet. Microbiol.
123 (2007) 387–393. http://dx.doi.org/10.1016/j.vetmic.2007.04.005Web of ScienceCrossrefGoogle Scholar
[17] Wang, K.S., Kuhn, R.J., Strauss, E.G., Ou, S. and Strauss, J.H. High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells. J. Virol.
66 (1992) 4992–5001. Google Scholar
[18] Thepparit, C. and Smith, D.R. Serotype-specific entry of dengue virus into liver cells: identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor. J. Virol.
78 (2004) 12647–12656. http://dx.doi.org/10.1128/JVI.78.22.12647-12656.2004CrossrefGoogle Scholar
[19] Akache, B., Grimm, D., Pandey, K., Yant, S.R., Xu, H. and Kay, M.A. The 37/67-kilodalton laminin receptor is a receptor for adeno-associated virus serotypes 8, 2, 3, and 9. J. Virol.
80 (2006) 9831–9836. http://dx.doi.org/10.1128/JVI.00878-06CrossrefGoogle Scholar
[20] Coggin, J.H. Jr., Barsoum, A.L. and Rohrer, J.W. 37 kiloDalton oncofetal antigen protein and immature laminin receptor protein are identical, universal T-cell inducing immunogens on primary rodent and human cancers. Anticancer Res.
19 (1999) 5535–5542. Google Scholar
[21] Zelle-Rieser, C., Barsoum, A.L., Sallusto, F., Ramoner, R., Rohrer, J.W., Holtl, L., Bartsch, G., Coggin, J.J. and Thurnher, M. Expression and immunogenicity of oncofetal antigen-immature laminin receptor in human renal cell carcinoma. J. Urol.
165 (2001) 1705–1709. http://dx.doi.org/10.1016/S0022-5347(05)66398-7CrossrefGoogle Scholar
[22] Castronovo, V. Laminin receptors and laminin-binding proteins during tumor invasion and metastasis. Invasion Metastasis
13 (1993) 1–30. Google Scholar
[23] Castronovo, V., Claysmith, A.P., Barker, K.T., Cioce, V., Krutzsch, H.C. and Sobel, M.E. (1991). Biosynthesis of the 67 kDa high affinity laminin receptor. Biochem. Biophys. Res. Commun.
177 (1991) 177–183. http://dx.doi.org/10.1016/0006-291X(91)91965-FCrossrefGoogle Scholar
[24] Buto, S., Tagliabue, E., Ardini, E., Magnifico, A., Ghirelli, C., van den Brule, F., Castronovo, V., Colnaghi, M.I., Sobel, M.E. and Menard, S. Formation of the 67-kDa laminin receptor by acylation of the precursor. J. Cell. Biochem.
69 (1998) 244–251. http://dx.doi.org/10.1002/(SICI)1097-4644(19980601)69:3<244::AID-JCB2>3.0.CO;2-RCrossrefGoogle Scholar
[25] Narumi, K., Inoue, A., Tanaka, M., Isemura, M., Shimo-Oka, T., Abe, T., Nukiwa, T. and Satoh, K. Inhibition of experimental metastasis of human fibrosarcoma cells by anti-recombinant 37-kDa laminin binding protein antibody. Jpn. J. Cancer Res.
90 (1999) 425–431. Google Scholar
[26] Kaneda, Y., Kinoshita, K., Sato, M., Saeki, Y., Yamada, R., Wataya-Kaneda, M., and Tanaka, K. The induction of apoptosis in HeLa cells by the loss of LBP-p40. Cell Death Differ.
5 (1998) 20–28. http://dx.doi.org/10.1038/sj.cdd.4400315CrossrefGoogle Scholar
[27] Leucht, C., Simoneau, S., Rey, C., Vana, K., Rieger, R., Lasmezas, C.I. and Weiss, S. The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells. EMBO Rep.
4 (2003) 290–295. http://dx.doi.org/10.1038/sj.embor.embor768CrossrefGoogle Scholar
[28] Leucht, C., Vana, K., Renner-Muller, I., Dormont, D., Lasmezas, C.I., Wolf, E. and Weiss, S. Knock-down of the 37-kDa/67-kDa laminin receptor in mouse brain by transgenic expression of specific antisense LRP RNA. Transgenic Res. 13 (2004) 81–85. http://dx.doi.org/10.1023/B:TRAG.0000017177.35197.89CrossrefGoogle Scholar
[29] Ardini, E., Pesole, G., Tagliabue, E., Magnifico, A., Castronovo, V., Sobel, M.E., Colnaghi, M.I. and Menard, S. The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution. Mol. Biol. Evol.
15 (1998) 1017–1025. Google Scholar
[30] Knowles B.B., Howe, C.C. and Aden D.P. Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis B surface antigen. Science
209 (1980) 497–499. http://dx.doi.org/10.1126/science.6248960CrossrefGoogle Scholar
[31] Elbashir, S.M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K. and Tuschl, T. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature
411 (2001) 494–498. http://dx.doi.org/10.1038/35078107Web of ScienceCrossrefGoogle Scholar
[32] Hannon, G.J. RNA interference. Nature
418 (2002) 244–251. http://dx.doi.org/10.1038/418244aCrossrefGoogle Scholar
[33] Hurtado, A., Tseng, J.C. and Meruelo, D. Gene therapy that safely targets and kills tumor cells throughout the body. Rejuvenation Res.
9 (2006) 36–44. http://dx.doi.org/10.1089/rej.2006.9.36CrossrefGoogle Scholar
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