The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Repression of the Heat Shock Response Is a Programmed Event at the Onset of Reproduction
Open accessAbstract
Summary The heat shock response (HSR) is essential for proteostasis and cellular health. In metazoans, aging is associated with a decline in quality control, thus increasing the risk for protein conformational disease. Here, we show that in C. elegans, the HSR declines precipitously over a four hour period in early adulthood coincident with the onset of reproductive maturity. Repression of the HSR occurs due to an increase in H3K27me3 marks at stress gene loci, the timing of which is determined by reduced expression of the H3K27 demethylase jmjd-3.1. This results in a repressed chromatin state that interferes with HSF-1 binding and suppresses transcription initiation in response to stress. The removal of germ line stem cells preserves jmjd-3.1 expression, suppresses the accumulation of H3K27me3 at stress gene loci and maintains the HSR. These findings suggest that competing requirements of the germ line and soma dictate organismal stress resistance as animals begin reproduction.
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
Regulation of aging and age-related disease by DAF-16 and heat-shock factor
Hsu, A.-L., Murphy, C. T., & Kenyon, C. (2003) · Science · doi:10.1126/science.1083701 · Cited by 1,513
The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
Self-citationDirect inhibition of the longevity-promoting factor SKN-1 by insulin-like signaling in C. elegans
Tullet, J. M. A., Hertweck, M., An, J. H., Baker, J., Hwang, J. Y., Liu, S., Oliveira, R. P., Baumeister, R., & Blackwell, T. K. (2008) · Cell · doi:10.1016/j.cell.2008.01.030 · Cited by 923
Stress-activated cap’n’collar transcription factors in aging and human disease
Sykiotis, G. P., & Bohmann, D. (2010) · Science Signaling · doi:10.1126/scisignal.3112re3 · Cited by 776 · cited 2×
“…responses (UPRs), and the antioxidant stress response, which rapidly upregulate molecular chaperones and detoxification enzymes to diminish the consequences of protein damage across cellular compartments (Akerfelt et al., 2010; Haynes et al., 2013; Sykiotis and Bohmann, 2010; Walter and Ron, 2011).”
BackgroundWidespread protein aggregation as an inherent part of aging in C. elegans
David, D. C., Ollikainen, N., Trinidad, J. C., Cary, M. P., Burlingame, A. L., & Kenyon, C. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000450 · Cited by 627
RPN-6 determines C. elegans longevity under proteotoxic stress conditions
Vilchez, D., Morantte, I., Liu, Z., Douglas, P. M., Merkwirth, C., Rodrigues, A. P. C., Manning, G., & Dillin, A. (2012) · Nature · doi:10.1038/nature11315 · Cited by 413
Autophagy and Lipid Metabolism Coordinately Modulate Life Span in Germline-less C. elegans
Lapierre, L. R., Gelino, S., Meléndez, A., & Hansen, M. (2011) · Current Biology · doi:10.1016/j.cub.2011.07.042 · Cited by 343
Jin, C., Li, J., Green, C. D., Yu, X., Tang, X., Han, D., Xian, B., Wang, D., Huang, X., Cao, X., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.001 · Cited by 258
Polycomb Repressive Complex 2 and Trithorax modulate Drosophila longevity and stress resistance
Siebold, A. P., Banerjee, R., Tie, F., Kiss, D. L., Moskowitz, J., & Harte, P. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907739107 · Cited by 216
Reis‐Rodrigues, P., Czerwieniec, G., Peters, T. W., Evani, U. S., Alavez, S., Gaman, E. A., Vantipalli, M., Mooney, S. D., Gibson, B. W., Lithgow, G. J., et al. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2011.00765.x · Cited by 174
Cited by
The proteostasis network and its decline in ageing
Hipp, M. S., Kasturi, P., & Hartl, F. U. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0101-y · Cited by 1,642
Booth, L. N., & Brunet, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.013 · Cited by 499
C. elegans neurons jettison protein aggregates and mitochondria under neurotoxic stress
Melentijevic, I., Toth, M. L., Arnold, M. L., Guasp, R. J., Harinath, G., Nguyen, K. C., Taub, D., Parker, J. A., Neri, C., Gabel, C. V., et al. (2017) · Nature · doi:10.1038/nature21362 · Cited by 454
Two conserved histone demethylases regulate mitochondrial stress-induced longevity
Merkwirth, C., Jovaisaite, V., Durieux, J., Matilainen, O., Jordan, S. D., Quiros, P. M., Steffen, K. K., Williams, E. G., Mouchiroud, L., Tronnes, S. U., et al. (2016) · Cell · doi:10.1016/j.cell.2016.04.012 · Cited by 363
“1 is also necessary and sufficient for UPRmt induction and lifespan extension and has overlapping roles in ER stress regulation (Labbadia and Morimoto, 2015).”
InfluentialEpigenetic changes during aging and their reprogramming potential
Kane, A. E., & Sinclair, D. A. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1570075 · Cited by 283
Metadata
- Authors
- Labbadia, J., & Morimoto, R. I.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2015-08
- Volume
- 59
- Issue
- 4
- Pages
- 639-650
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W1847809821
- Cited by
- 329
- References
- 10
- FWCI
- 10.42
- Type
- journal article
- Language
- en
- Open access
- bronze
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: Repression of the Heat Shock Response Is a Programmed Event at the Onset of Reproduction. https://app.cochat.ai/papers/10.1016/j.molcel.2015.06.027
- The paper
- Labbadia, J., & Morimoto, R. I. (2015). Repression of the Heat Shock Response Is a Programmed Event at the Onset of Reproduction. Molecular Cell. https://doi.org/10.1016/j.molcel.2015.06.027
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.
