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Cited by 411

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability

Open access
Leuenberger, Pascal, Ganscha, Stefan, Kahraman, Abdullah, Cappelletti, Valentina, Boersema, Paul J., von Mering, Christian, Claassen, Manfred, Picotti, Paola·2017·Science

Abstract

How proteomes take the heat: Living organisms are very sensitive to temperature, and much of this is attributed to its effect on the structure and function of proteins. Leuenberger et al. explored thermostability on a proteome-wide scale in bacteria, yeast, and human cells by using a combination of limited proteolysis and mass spectrometry (see the Perspective by Vogel). Their results suggest that temperature-induced cell death is caused by the loss of a subset of proteins with key functions. The study also provides insight into the molecular and evolutionary bases of protein and proteome stability. Science , this issue p. eaai7825 ; see also p. 794

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Crossref · 10.1126/science.aai7825

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Metadata

Authors
Leuenberger, P., Ganscha, S., Kahraman, A., Cappelletti, V., Boersema, P. J., von Mering, C., Claassen, M., & Picotti, P.
Venue
Science
Published
2017-02-24
Volume
355
Issue
6327
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2590059905
Cited by
411
References
7
FWCI
13.59
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability. https://app.cochat.ai/papers/10.1126/science.aai7825
The paper
Leuenberger, P., Ganscha, S., Kahraman, A., Cappelletti, V., Boersema, P. J., von Mering, C., Claassen, M., & Picotti, P. (2017). Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability. Science. https://doi.org/10.1126/science.aai7825

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.