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Hamada, H., Tsuruo, T. (1986) Functional role for the 170- to 180-kDa glycoprotein specific to drug-resistant tumor cells as revealed by monoclonal antibodies. Proceedings of the National Academy of Sciences, 83 (20) 7785-7789 doi:10.1073/pnas.83.20.7785

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Reference TypeJournal (article/letter/editorial)
TitleFunctional role for the 170- to 180-kDa glycoprotein specific to drug-resistant tumor cells as revealed by monoclonal antibodies.
JournalProceedings of the National Academy of Sciences
AuthorsHamada, H.Author
Tsuruo, T.Author
Year1986 (October 1)Volume83
Issue20
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.83.20.7785Search in ResearchGate
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Mindat Ref. ID1453337Long-form Identifiermindat:1:5:1453337:8
GUID0
Full ReferenceHamada, H., Tsuruo, T. (1986) Functional role for the 170- to 180-kDa glycoprotein specific to drug-resistant tumor cells as revealed by monoclonal antibodies. Proceedings of the National Academy of Sciences, 83 (20) 7785-7789 doi:10.1073/pnas.83.20.7785
Plain TextHamada, H., Tsuruo, T. (1986) Functional role for the 170- to 180-kDa glycoprotein specific to drug-resistant tumor cells as revealed by monoclonal antibodies. Proceedings of the National Academy of Sciences, 83 (20) 7785-7789 doi:10.1073/pnas.83.20.7785
In(1986, October) Proceedings of the National Academy of Sciences Vol. 83 (20) Proceedings of the National Academy of Sciences

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O'Neill, H. C. (1986) Monoclonal antibodies specific for H-2K and H-2D antigens on cytotoxic T cells can inhibit their function. Proceedings of the National Academy of Sciences, 83 (5) 1443-1447 doi:10.1073/pnas.83.5.1443
Honsik, C. J., Jung, G., Reisfeld, R. A. (1986) Lymphokine-activated killer cells targeted by monoclonal antibodies to the disialogangliosides GD2 and GD3 specifically lyse human tumor cells of neuroectodermal origin. Proceedings of the National Academy of Sciences, 83 (20) 7893-7897 doi:10.1073/pnas.83.20.7893
Shii, K., Roth, R. A. (1986) Inhibition of insulin degradation by hepatoma cells after microinjection of monoclonal antibodies to a specific cytosolic protease. Proceedings of the National Academy of Sciences, 83 (12) 4147-4151 doi:10.1073/pnas.83.12.4147
Yagita, H., Nakamura, T., Karasuyama, H., Okumura, K. (1989) Monoclonal antibodies specific for murine CD2 reveal its presence on B as well as T cells. Proceedings of the National Academy of Sciences, 86 (2) 645-649 doi:10.1073/pnas.86.2.645
Cornwell, M. M., Safa, A. R., Felsted, R. L., Gottesman, M. M., Pastan, I. (1986) Membrane vesicles from multidrug-resistant human cancer cells contain a specific 150- to 170-kDa protein detected by photoaffinity labeling. Proceedings of the National Academy of Sciences, 83 (11) 3847-3850 doi:10.1073/pnas.83.11.3847
FitzGerald, D. J., Willingham, M. C., Cardarelli, C. O., Hamada, H., Tsuruo, T., Gottesman, M. M., Pastan, I. (1987) A monoclonal antibody-Pseudomonas toxin conjugate that specifically kills multidrug-resistant cells. Proceedings of the National Academy of Sciences, 84 (12) 4288-4292 doi:10.1073/pnas.84.12.4288
Barclay, S. L., Smith, A. M. (1986) Rapid isolation of monoclonal antibodies specific for cell surface differentiation antigens. Proceedings of the National Academy of Sciences, 83 (12) 4336-4340 doi:10.1073/pnas.83.12.4336
Meiri, H., Goren, E., Bergmann, H., Zeitoun, I., Rosenthal, Y., Palti, Y. (1986) Specific modulation of sodium channels in mammalian nerve by monoclonal antibodies. Proceedings of the National Academy of Sciences, 83 (21) 8385-8389 doi:10.1073/pnas.83.21.8385
Georges, E., Bradley, G., Gariepy, J., Ling, V. (1990) Detection of P-glycoprotein isoforms by gene-specific monoclonal antibodies. Proceedings of the National Academy of Sciences, 87 (1) 152-156 doi:10.1073/pnas.87.1.152
Haruta, Y., Seon, B. K. (1986) Distinct human leukemia-associated cell surface glycoprotein GP160 defined by monoclonal antibody SN6. Proceedings of the National Academy of Sciences, 83 (20) 7898-7902 doi:10.1073/pnas.83.20.7898
Gottlieb, D. I., Chang, Y. C., Schwob, J. E. (1986) Monoclonal antibodies to glutamic acid decarboxylase. Proceedings of the National Academy of Sciences, 83 (22) 8808-8812 doi:10.1073/pnas.83.22.8808
 
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