The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin.
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Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,221
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
The mechanism of action of cyclosporin A and FK506
Schreiber, S. L., & Crabtree, G. R. (1992) · Immunology Today · doi:10.1016/0167-5699(92)90111-j · Cited by 2,127
Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
Clipstone, N. A., & Crabtree, G. R. (1992) · Nature · doi:10.1038/357695a0 · Cited by 1,637
Chemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
Schreiber, S. L. (1991) · Science · doi:10.1126/science.1702904 · Cited by 1,494
Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A
Flanagan, W. M., Corthésy, B., Bram, R. J., & Crabtree, G. R. (1991) · Nature · doi:10.1038/352803a0 · Cited by 1,056
FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin
O'Keefe, S. J., Tamura, J., Kincaid, R. L., Tocci, M. J., & O'Neill, E. A. (1992) · Nature · doi:10.1038/357692a0 · Cited by 841
Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A.
Fruman, D. A., Klee, C. B., Bierer, B. E., & Burakoff, S. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.9.3686 · Cited by 823
Cited by
ER stress and the unfolded protein response
Schröder, M., & Kaufman, R. J. (2005) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2004.06.056 · Cited by 1,747
Mammalian sweet taste receptors
Nelson, G., Hoon, M. A., Chandrashekar, J., Zhang, Y., Ryba, N. J. P., & Zuker, C. S. (2001) · Cell · doi:10.1016/s0092-8674(01)00451-2 · Cited by 1,702
Self-citationBI-DIRECTIONAL PROTEIN TRANSPORT BETWEEN THE ER AND GOLGI
Lee, M. C. S., Miller, E. A., Goldberg, J., Orci, L., & Schekman, R. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.010403.105307 · Cited by 813
Poyner, D. R., Sexton, P. M., Marshall, I., Smith, D. M., Quirion, R., Born, W., Muff, R., Fischer, J. A., & Foord, S. M. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.2.233 · Cited by 804
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706
Metadata
- Authors
- Baker, E. K., Colley, N. J., & Zuker, C. S.
- Venue
- The EMBO Journal
- Published
- 1994-10
- Volume
- 13
- Issue
- 20
- Pages
- 4886-4895
- ISSN
- 0261-4189 (ISSN-L)
- OpenAlex
- W323363336
- Cited by
- 302
- References
- 48
- FWCI
- 7.35
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. https://app.cochat.ai/papers/10.1002/j.1460-2075.1994.tb06816.x
- The paper
- Baker, E. K., Colley, N. J., & Zuker, C. S. (1994). The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. The EMBO Journal. https://doi.org/10.1002/j.1460-2075.1994.tb06816.x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.