The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Chaperoning signaling pathways: molecular chaperones as stress-sensing`heat shock' proteins
Abstract
Heat shock proteins interact with multiple key components of signaling pathways that regulate growth and development. The molecular relationships between heat shock proteins, various signaling proteins and partner proteins appear to be critical for the normal function of signal transduction pathways. The relative levels of these proteins may be important, as too little or too much Hsp70 or Hsp90 can result in aberrant growth control, developmental malformations and cell death. Although the functions of heat shock proteins as molecular chaperones have been well characterized, their complementary role as a `stress-induced' proteins to monitor changes and alter the biochemical environment of the cell remains elusive. Genetic and molecular interactions between heat shock proteins, their co-chaperones and components of signaling pathways suggest that crosstalk between these proteins can regulate proliferation and development by preventing or enhancing cell growth and cell death as the levels of heat shock proteins vary in response to environmental stress or disease.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444
Increasing complexity of Ras signaling
Campbell, S. L., Khosravi-Far, R., Rossman, K. L., Clark, G. J., & Der, C. J. (1998) · Oncogene · doi:10.1038/sj.onc.1202174 · Cited by 1,079
Takayama, S., Sato, T., Krajewski, S., Kochel, K., Irie, S., Milian, J. A., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90410-7 · Cited by 857
Reduced levels of hsp90 compromise steroid receptor action in vivo
Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787
A New First Step in Activation of Steroid Receptors
Davies, T. H., Ning, Y.-M., & Sánchez, E. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100531200 · Cited by 427
Heat-shock protein hsp90 governs the activity of pp60v-src kinase.
Xu, Y., & Lindquist, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7074 · Cited by 416
Cited by
Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
Wang, W., Vinocur, B., Shoseyov, O., & Altman, A. (2004) · Trends in Plant Science · doi:10.1016/j.tplants.2004.03.006 · Cited by 2,759
Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
Morimoto, R. I. (2008) · Genes & Development · doi:10.1101/gad.1657108 · Cited by 872
Self-citationMassey, A. J., Williamson, D. S., Browne, H., Murray, J. B., Dokurno, P., Shaw, T., Macias, A. T., Daniels, Z., Geoffroy, S., Dopson, M., et al. (2010) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-009-1194-3 · Cited by 313
(2020) · doi:10.1038/s42003-020-0763-1 · Cited by 309
Heat shock protein–based therapy as a potential candidate for treating the sphingolipidoses
Kirkegaard, T., Gray, J., Priestman, D. A., Wallom, K.-L., Atkins, J., Olsen, O. D., Klein, A., Drndarski, S., Petersen, N. H. T., Ingemann, L., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad9823 · Cited by 173
Metadata
- Authors
- Nollen, E. A. A., & Morimoto, R. I.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2002-07-15
- Volume
- 115
- Issue
- 14
- Pages
- 2809-2816
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1901873593
- Cited by
- 653
- References
- 7
- FWCI
- 12.31
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Chaperoning signaling pathways: molecular chaperones as stress-sensing`heat shock' proteins. https://app.cochat.ai/papers/10.1242/jcs.115.14.2809
- The paper
- Nollen, E. A. A., & Morimoto, R. I. (2002). Chaperoning signaling pathways: molecular chaperones as stress-sensing`heat shock' proteins. Journal of Cell Science. https://doi.org/10.1242/jcs.115.14.2809
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.
