The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
P59, an hsp 90-binding protein. Cloning and sequencing of its cDNA and preparation of a peptide-directed polyclonal antibody.
Open accessAbstract
The primary sequence of the rabbit liver cDNA coding for protein p59 has been determined. The protein binds to the 90-kDa heat shock protein (hsp 90) and is associated with it, including when hsp 90 participates in hetero-oligomeric complexes of untransformed mammalian steroid receptors that sediment at 8-10 S. The cloned cDNA codes for an open reading frame of 458 amino acids defining a yet unknown protein. However, 55% amino acid homology to peptidyl-prolyl isomerase is found between amino acids 41 and 137, suggesting rotamase activity for p59, which speculatively may apply to bound hsp 90 and thus be implied in the intracellular trafficking of hetero-oligomeric forms of steroid hormone receptors. A polyclonal antibody derived from the COOH-terminal peptide 441-458 demonstrates a good affinity for rabbit, rat, and human "p59" protein. It interacts with at least one epitope, available in 8-10 S untransformed steroid receptor complexes and different from that recognized by the monoclonal antibody KN382/EC-1.
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Citations
Cites
A 59-kilodalton protein associated with progestin, estrogen, androgen and glucocorticoid receptors
Tai, P. K. K., Maeda, Y., Nakao, K., Wakim, N. G., Duhring, J. L., & Faber, L. E. (1986) · Biochemistry · doi:10.1021/bi00366a043 · Cited by 257
HSP56: a novel heat shock protein associated with untransformed steroid receptor complexes
Sanchez, E. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45667-0 · Cited by 214
Cited by
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*
Pratt, W. B., & Toft, D. O. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0303 · Cited by 1,791
Inhibition of nuclear hormone receptor activity by calreticulin
Dedhar, S., Rennie, P. S., Shago, M., Hagesteijn, C.-Y. L., Yang, H., Filmus, J., Hawley, R. G., Bruchovsky, N., Cheng, H., Matusik, R. J., et al. (1994) · Nature · doi:10.1038/367480a0 · Cited by 375
Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70.
Smith, D. F., Sullivan, W. P., Marion, T. N., Zaitsu, K., Madden, B., McCormick, D. J., & Toft, D. O. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.869 · Cited by 269
Silverstein, A. M., Galigniana, M. D., Kanelakis, K. C., Radanyi, C., Renoir, J.-M., & Pratt, W. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.36980 · Cited by 186
Self-citationPirkl, F., & Buchner, J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4595 · Cited by 179
Metadata
- Authors
- Lebeau, M. C., Massol, N., Herrick, J., Faber, L. E., Renoir, J. M., Radanyi, C., & Baulieu, E. E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-03
- Volume
- 267
- Issue
- 7
- Pages
- 4281-4284
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1584384646
- Cited by
- 179
- References
- 2
- FWCI
- 11.32
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: P59, an hsp 90-binding protein. Cloning and sequencing of its cDNA and preparation of a peptide-directed polyclonal antibody. https://app.cochat.ai/papers/10.1016/s0021-9258(18)42827-x
- The paper
- Lebeau, M. C., Massol, N., Herrick, J., Faber, L. E., Renoir, J. M., Radanyi, C., & Baulieu, E. E. (1992). P59, an hsp 90-binding protein. Cloning and sequencing of its cDNA and preparation of a peptide-directed polyclonal antibody. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)42827-x
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