The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases
Open accessAbstract
Receptor accessory peptidyl prolyl cis/trans isomerases (PPIases) of the FKBP and cyclophilin types form receptor heterocomplexes with different stabilities. PPIases have been found to associate with other receptor heterocomplex constituents via either proline‐directed active sites or additional domains of the enzymes. The single‐domain PPIases FKBP12 and FKBP12.6 are shown to interact with receptor protein kinases and calcium channels at their active sites. In contrast, heterooligomeric nuclear receptors contain multi‐domain PPIases like FKBP51, FKBP52 or cyclophilin 40 that directly interact with the chaperone hsp90 via the tetratricopeptide repeat modules of the folding helper enzymes. PPIases play a critical role in the functional arrangement of components within receptor heterocomplexes.
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Cites
Polypeptide Flux through Bacterial Hsp70
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Gene–Stress–Epigenetic regulation of FKBP5: clinical and translational implications
Zannas, A. S., Wiechmann, T., Gassen, N. C., & Binder, E. B. (2016) · Neuropsychopharmacology · doi:10.1038/npp.2015.235 · Cited by 622
Proteome Map of the Chloroplast Lumen of Arabidopsis thaliana
Schubert, M., Petersson, U. A., Haas, B. J., Funk, C., Schröder, W. P., & Kieselbach, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108575200 · Cited by 438
Metadata
- Authors
- Schiene-Fischer, C., & Yu, C.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2001-04-19
- Volume
- 495
- Issue
- 1-2
- Pages
- 1-6
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2093693347
- Cited by
- 182
- References
- 7
- FWCI
- 4.45
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Schiene-Fischer, C., & Yu, C. (2001). Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. FEBS Letters. https://doi.org/10.1016/s0014-5793(01)02326-2
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