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