Diversity in the origins of proteostasis networks-a driver for protein function in evolution
Nature Reviews Molecular Cell Biology, ISSN: 1471-0072, Vol: 14, Issue: 4, Page: 237-248
2013
- 189Citations
- 352Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations189
- Citation Indexes189
- CrossRef189
- 181
- Captures352
- Readers352
- 352
Review Description
Although the sequence of a protein largely determines its function, proteins can adopt different folding states in response to changes in the environment, some of which may be deleterious to the organism. All organisms-Bacteria, Archaea and Eukarya-have evolved a protein homeostasis, or proteostasis, network comprising chaperones and folding factors, degradation components, signalling pathways and specialized compartmentalized modules that manage protein folding in response to environmental stimuli and variation. Surveying the origins of proteostasis networks reveals that they have co-evolved with the proteome to regulate the physiological state of the cell, reflecting the unique stresses that different cells or organisms experience, and that they have a key role in driving evolution by closely managing the link between the phenotype and the genotype. © 2013 Macmillan Publishers Limited. All rights reserved.
Bibliographic Details
Springer Science and Business Media LLC
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