The DOI matches its Crossref record; 105 of the 105 references it cites were found in a registry or an index.
Protein Folding in the Endoplasmic Reticulum and the Unfolded Protein Response
Abstract
In all eukaryotic cells, the endoplasmic reticulum (ER) is an intracellular organelle where folding and assembly occurs for proteins destined to the extracellular space, plasma membrane, and the exo/endocytic compartments (Kaufman 1999). As a protein-folding compartment, the ER is exquisitely sensitive to alterations in homeostasis, and provides stringent quality control systems to ensure that only correctly folded proteins transit to the Golgi and unfolded or misfolded proteins are retained and ultimately degraded. A number of biochemical and physiological stimuli, such as perturbation in calcium homeostasis or redox status, elevated secretory protein synthesis, expression of misfolded proteins, sugar/glucose deprivation, altered glycosylation, and overloading of cholesterol can disrupt ER homeostasis, impose stress to the ER, and subsequently lead to accumulation of unfolded or misfolded proteins in the ER lumen. The ER has evolved highly specific signaling pathways called the unfolded protein response (UPR) to cope with the accumulation of unfolded or misfolded proteins. Elucidation of the molecular mechanisms by which accumulation of unfolded proteins in the ER transmits a signal to the cytoplasm and nucleus has led to major new insights into the diverse cellular and physiological processes that are regulated by the UPR. This chapter summarizes how cells respond to the accumulation of unfolded proteins in the cell and the relevance of these signaling pathways to human physiology and disease.
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“Periods of high lipid exposure, glucose deprivation, or increased synthesis of secretory proteins, lead to the accumulation of unfolded or misfolded proteins within the ER lumen [59].”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [59]
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The Role for Endoplasmic Reticulum Stress in Diabetes Mellitus
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Metadata
- Authors
- Zhang, K., & Kaufman, R. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Kaufman, R.J.
- Venue
- Handbook of Experimental Pharmacology
- Publisher
- Springer-Verlag
- Published
- 2005-12-28
- Issue
- 172
- Pages
- 69-91
- OpenAlex
- W136234913
- Cited by
- 152
- References
- 105
- Citations by year
- 2026: 3 · 2024: 3 · 2023: 2 · 2022: 7 · 2021: 4 · 2020: 3 · 2019: 7 · 2018: 6 · 2017: 5 · 2016: 4 · 2015: 11 · 2014: 7 · 2013: 16 · 2012: 6
- FWCI
- 24.70
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Springer eBooks (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK42394)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- endoplasmic reticulum, unfolded protein response, protein folding, endoplasmic reticulum stress, ER homeostasis, misfolded proteins, calcium homeostasis, redox state, secretory protein synthesis, glucose deprivation, glycosylation
- MeSH terms
- Animals, Cell Differentiation, Diabetes Mellitus, Endoplasmic Reticulum, Glucose, Humans, Nervous System Diseases, Proteins, Transcription, Genetic, Protein Biosynthesis, Apoptosis, Protein Folding
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