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Proteins that fail to attain or maintain their structure reduce fitness in part through toxic gain of function mechanisms referred to as "proteotoxicity". The latter conspicuously affects poorly-renewable tissues of long-lived organisms in which the threat of protein misfolding can exert its deleterious consequences over extended periods of time. Protein misfolding is compartment-specific and its extent is influenced by the burden of newly-synthesized unfolded proteins presented to given compartment (cytosol, endoplasmic reticulum, mitochondria) and by the protein folding environment in that compartment. The latter is influenced by structural elements operating within and on the compartment and by its metabolic state. Both parameters are regulated by complex homeostatic pathways, constituting a proteostasis network in which compartment-specific unfolded protein responses (UPR) are important.
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Nature (2020)
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mag(2015)
mag(2013)
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Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature (2006)
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature (2004)
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature (2003)
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