The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
TCP1 complex is a molecular chaperone in tubulin biogenesis
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Citations
Cites
Gething, M.-J., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,123
Munro, S., & Pelham, H. R. B. (1986) · Cell · doi:10.1016/0092-8674(86)90746-4 · Cited by 1,449
Beyond self-assembly: From microtubules to morphogenesis
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Interaction of Hsp 70 with Newly Synthesized Proteins: Implications for Protein Folding and Assembly
Beckmann, R. P., Mizzen, L. E., & Welch, W. J. (1990) · Science · doi:10.1126/science.2188360 · Cited by 1,291
Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
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Diverse effects of beta-tubulin mutations on microtubule formation and function.
Huffaker, T. C., Thomas, J. H., & Botstein, D. (1988) · The Journal of cell biology · doi:10.1083/jcb.106.6.1997 · Cited by 366
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Trent, J. D., Nimmesgern, E., Wall, J. S., Hartl, F.-U., & Horwich, A. L. (1991) · Nature · doi:10.1038/354490a0 · Cited by 336
Self-citationT-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
Lewis, V. A., Hynes, G. M., Zheng, D., Saibil, H., & Willison, K. (1992) · Nature · doi:10.1038/358249a0 · Cited by 308
Cited by
Yam, A. Y., Xia, Y., Lin, H.-T. J., Burlingame, A., Gerstein, M., & Frydman, J. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1515 · Cited by 420
The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo
Sternlicht, H., Farr, G. W., Sternlicht, M. L., Driscoll, J. K., Willison, K., & Yaffe, M. B. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9422 · Cited by 341
Self-citationGupta, R. S. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.tb02216.x · Cited by 299
Heat Shock Proteins as Ligands of Toll-Like Receptors
Vabulas, R. M., Wagner, H., & Schild, H. (2002) · Current Topics in Microbiology and Immunology · doi:10.1007/978-3-642-59430-4_11 · Cited by 276
SALMON: survival analysis learning with multi-omics neural networks on breast cancer
Huang, Z., Zhan, X., Xiang, S., Johnson, T. S., Helm, B., Yu, C. Y., Zhang, J., Salama, P., Rizkalla, M., Han, Z., et al. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00166 · Cited by 262
“In module #51, TCP1 functioned as a cytosolic chaperone in the biogenesis of tubulin (Yaffe et al., 1992), which has been proved to have an association with breast cancer (Bassiouni et al.”
Background
Metadata
- Authors
- Yaffe, M. B., Farr, G. W., Miklos, D., Horwich, A. L., Sternlicht, M. L., & Sternlicht, H.
- Venue
- Nature
- Published
- 1992-07-16
- Volume
- 358
- Issue
- 6383
- Pages
- 245-248
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2037094686
- Cited by
- 462
- References
- 25
- FWCI
- 13.87
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: TCP1 complex is a molecular chaperone in tubulin biogenesis. https://app.cochat.ai/papers/10.1038/358245a0
- The paper
- Yaffe, M. B., Farr, G. W., Miklos, D., Horwich, A. L., Sternlicht, M. L., & Sternlicht, H. (1992). TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature. https://doi.org/10.1038/358245a0
Data sources
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.
