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Reversible inhibition of protein import into the nucleus by wheat germ agglutinin injected into cultured cells.
Purification, Cloning, and Expression of Murine Uridine Phosphorylase (*)
- Shin‐ichi Watanabe, A. Hino, K. Wada, J. Eliason, T. Uchida
- Biology, ChemistryThe Journal of Biological Chemistry
- 19 May 1995
expression of uridine phosphorylase mRNA in these cell lines was further enhanced by treating the cells with the inflammatory cytokines, tumor necrosis factor-α, interleukin 1α, and interferon, and high levels of mRNA expression in Colon-26.
Direct measurement of phagosomal reactive oxygen by luminol-binding microspheres.
ATP-dependent association of nuclear proteins with isolated rat liver nuclei.
- N. Imamoto-Sonobe, Y. Yoneda, R. Iwamoto, H. Sugawa, T. Uchida
- Biology, PhysicsProceedings of the National Academy of Sciences…
- 1 May 1988
In vitro association of Xenopus nucleoplasmin and mammalian nonhistone chromosomal high mobility group 1 (HMG1) protein with nuclei isolated from rat liver was examined. Efficient association of…
Synthetic peptides containing a region of SV 40 large T-antigen involved in nuclear localization direct the transport of proteins into the nucleus.
A monoclonal antibody against the nucleus reveals the presence of a common protein in the nuclear envelope, the perichromosomal region, and cytoplasmic vesicles
- M. Wataya-Kaneda, Y. Kaneda, T. Sakurai, H. Sugawa, T. Uchida
- BiologyThe Journal of cell biology
- 1 January 1987
Immunofluorescence studies and immunoblot analysis showed that this monoclonal antibody prepared against the nucleus recognized a protein of approximately 40 kD both in the cytoplasm and in the perichromosomal regions.
Binding properties of monoclonal antibody to the cytoplasmic domain of transferrin receptor.
One of these antibodies, U-1, recognized the cytoplasmic domain of TFR and the others, N-2 and W-3, recognized its cell surface domains, but only antibody W- 3 competed with transferrin (TF) for binding to TFR.
Polymer microbeads bound to C3 fragments for detecting and labeling cells with C3 receptors.
C3hu-, C3mu- and C3bhu-mbs were stable for more than 4 months and formed rosettes with cells which had the corresponding receptor and cap formation of each receptor was observed under a microscope.
Antibodies to Asp-Asp-Glu-Asp can inhibit transport of nuclear proteins into the nucleus.
- Y. Yoneda, N. Imamoto-Sonobe, Y. Matsuoka, R. Iwamoto, Y. Kiho, T. Uchida
- 14 October 1988
Rabbit antibodies to a synthetic peptide containing the negatively charged amino acid sequence Asp-Asp- asp-Glu-As p were obtained and blocked transport of nuclear proteins into the nucleus.