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• W2023960897 abstract "Integral membrane proteins (IMPs) are essential components of the plasma and organellar membranes of the eukaryotic cell. Non-native IMPs, which can arise as a result of mutations, errors during biosynthesis or cellular stress, can disrupt these membranes and potentially lead to cell death. To protect against this outcome, the cell possesses quality control (QC) systems that detect and dispose of non-native IMPs from cellular membranes. Recent studies suggest that recognition of non-native IMPs by the QC machinery is correlated with the thermodynamic stability of these proteins. Consistent with this, small molecules known as chemical and pharmacological chaperones have been identified that stabilize non-native IMPs and enable them to evade QC. These findings have far-reaching implications for treating human diseases caused by defective IMPs. Integral membrane proteins (IMPs) are essential components of the plasma and organellar membranes of the eukaryotic cell. Non-native IMPs, which can arise as a result of mutations, errors during biosynthesis or cellular stress, can disrupt these membranes and potentially lead to cell death. To protect against this outcome, the cell possesses quality control (QC) systems that detect and dispose of non-native IMPs from cellular membranes. Recent studies suggest that recognition of non-native IMPs by the QC machinery is correlated with the thermodynamic stability of these proteins. Consistent with this, small molecules known as chemical and pharmacological chaperones have been identified that stabilize non-native IMPs and enable them to evade QC. These findings have far-reaching implications for treating human diseases caused by defective IMPs." @default.
• W2023960897 created "2016-06-24" @default.
• W2023960897 creator A5029396985 @default.
• W2023960897 creator A5056406602 @default.
• W2023960897 creator A5069261270 @default.
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• W2023960897 date "2004-12-01" @default.
• W2023960897 modified "2023-09-29" @default.
• W2023960897 title "Quality control of integral membrane proteins" @default.
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• W2023960897 doi "https://doi.org/10.1016/j.tibs.2004.10.009" @default.
• W2023960897 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15544951" @default.
• W2023960897 hasPublicationYear "2004" @default.
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