The DOI matches its OpenAlex record; 34 of the 34 references it cites were found in a registry or an index.
Hsp47: a collagen-specific molecular chaperone
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Citations
Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Gething, M.-J., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,123
The Biology of heat shock proteins and molecular chaperones.
Morimoto, R. I., Tissieres, A., & Georgopoulos, C. P. (1994) · Cold Spring Harbor Laboratory eBooks · Cited by 1,243
Structure and Function of Collagen Types
(1987) · Elsevier eBooks · doi:10.1016/b978-0-12-481280-2.x5001-6 · Cited by 657
Berg, R. A., & Prockop, D. J. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)90961-3 · Cited by 582
Calnexin: a membrane-bound chaperone of the endoplasmic reticulum
Bergeron, J. J. M., Brenner, M. B., Thomas, D. Y., & Williams, D. B. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90205-4 · Cited by 532
The endoplasmic reticulum as a protein-folding compartment
Helenius, A., Marquardt, T., & Braakman, I. (1992) · Trends in Cell Biology · doi:10.1016/0962-8924(92)90309-b · Cited by 301
Bu, G., Geuze, H. J., Strous, G. J., & Schwartz, A. L. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07221.x · Cited by 274
BÄCHINGER, H. P., BRUCKNER, P., TIMPL, R., PROCKOP, D. J., & ENGEL, J. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb04610.x · Cited by 273
Engel, J. (1991) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.20.1.137 · Cited by 260
Cited by
ER quality control: towards an understanding at the molecular level
Ellgaard, L., & Helenius, A. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00233-7 · Cited by 388
Nagai, N., Hosokawa, M., Itohara, S., Adachi, E., Matsushita, T., Hosokawa, N., & Nagata, K. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1499 · Cited by 366
Self-citationBiology of Hsp47 (Serpin H1), a collagen-specific molecular chaperone
Ito, S., & Nagata, K. (2017) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2016.11.005 · Cited by 265
Self-citationHirao, K., Natsuka, Y., Tamura, T., Wada, I., Morito, D., Natsuka, S., Romero, P., Sleno, B., Tremblay, L. O., Herscovics, A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512191200 · Cited by 256
Self-citationHsp47 as a Collagen-Specific Molecular Chaperone
Ishida, Y., & Nagata, K. (2011) · Methods in Enzymology · doi:10.1016/b978-0-12-386471-0.00009-2 · Cited by 159
Self-citation
Metadata
- Authors
- Nagata, K.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 1996-01-01
- Volume
- 21
- Issue
- 1
- Pages
- 23-26
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2004422966
- Cited by
- 273
- References
- 34
- FWCI
- 5.44
- Type
- journal article
- Language
- en
- Open access
- closed
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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- CoChat. (2026). Citation check: Hsp47: a collagen-specific molecular chaperone. https://app.cochat.ai/papers/10.1016/0968-0004(96)80881-4
- The paper
- Nagata, K. (1996). Hsp47: a collagen-specific molecular chaperone. Trends in Biochemical Sciences. https://doi.org/10.1016/0968-0004(96)80881-4
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.