The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
The endoplasmic reticulum as a protein-folding compartment
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Citations
Cites
Gething, M.-J., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,123
Speculations on the functions of the major heat shock and glucose-regulated proteins
Pelham, H. R. B. (1986) · Cell · doi:10.1016/0092-8674(86)90693-8 · Cited by 1,546
Ellis, R. J., & van der Vies, S. M. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.001541 · Cited by 1,120
Protein Oligomerization in the Endoplasmic Reticulum
Hurtley, S. M., & Helenius, A. (1989) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.05.110189.001425 · Cited by 994
Self-citationExperimental and Theoretical Aspects of Protein Folding
Anfinsen, C. B., & Scheraga, H. A. (1975) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60413-1 · Cited by 969
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M. K., & Hartl, F. U. (1992) · Nature · doi:10.1038/356683a0 · Cited by 953
Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
Rothman, J. E. (1989) · Cell · doi:10.1016/0092-8674(89)90005-6 · Cited by 879
Pines, J., & Hunter, T. (1991) · The Journal of cell biology · doi:10.1083/jcb.115.1.1 · Cited by 858
Immunoglobulin heavy chain binding protein
Haas, I. G., & Wabl, M. (1983) · Nature · doi:10.1038/306387a0 · Cited by 845
KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
Rose, M. D., Misra, L. M., & Vogel, J. P. (1989) · Cell · doi:10.1016/0092-8674(89)90058-5 · Cited by 674
Cited by
Yoshida, H., Okada, T., Haze, K., Yanagi, H., Yura, T., Negishi, M., & Mori, K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6755-6767.2000 · Cited by 934
Hammond, C., Braakman, I., & Helenius, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.3.913 · Cited by 841
Self-citationHow N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.
Helenius, A. (1994) · Molecular Biology of the Cell · doi:10.1091/mbc.5.3.253 · Cited by 623
Self-citationEndoplasmic reticulum of animal cells and its organization into structural and functional domains
Baumann, O., & Walz, B. (2001) · International Review of Cytology · doi:10.1016/s0074-7696(01)05004-5 · Cited by 458
Quality and quantity control at the endoplasmic reticulum
Hegde, R. S., & Ploegh, H. L. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.05.005 · Cited by 157
Metadata
- Authors
- Helenius, A., Marquardt, T., & Braakman, I.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 1992-08
- Volume
- 2
- Issue
- 8
- Pages
- 227-231
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W1992189713
- Cited by
- 301
- References
- 39
- FWCI
- 2.05
- Type
- journal article
- Language
- en
- Open access
- green
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- Helenius, A., Marquardt, T., & Braakman, I. (1992). The endoplasmic reticulum as a protein-folding compartment. Trends in Cell Biology. https://doi.org/10.1016/0962-8924(92)90309-b
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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.