Journal: Biochemical Society transactions
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Abbreviation
Biochem Soc Trans
Publisher
Portland Press
21 results
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Publications 1 - 10 of 21
- Targeting NRF2 to promote epithelial repairItem type: Review Article
Biochemical Society transactionsHiebert, Paul; Werner, Sabine (2023)The transcription factor NRF2 is well known as a master regulator of the cellular stress response. As such, activation of NRF2 has gained widespread attention for its potential to prevent tissue injury, but also as a possible therapeutic approach to promote repair processes. While NRF2 activation affects most or even all cell types, its effect on epithelial cells during repair processes has been particularly well studied. In response to tissue injury, these cells proliferate, migrate and/or spread to effectively repair the damage. In this review, we discuss how NRF2 governs repair of epithelial tissues, and we highlight the increasing number of NRF2 targets with diverse roles in regulating epithelial repair. - Akt/mTOR signalling in myelinationItem type: Journal Article
Biochemical Society transactionsNorrmén, Camilla; Suter, Ueli (2013) - Conserved activation pathways in G-protein-coupled receptorsItem type: Journal Article
Biochemical Society transactionsDeupi, Xavier; Standfuss, Jörg; Schertler, Gebhard (2012) - Building droplet-based microfluidic systems for biological analysisItem type: Journal Article
Biochemical Society transactionsNiu, Xize; deMello, Andrew J. (2012) - Evolving protocells to prototissuesItem type: Journal Article
Biochemical Society transactionsMantri, S.; Sapra, K. T. (2013) - Nucleosome recognition and spacing by chromatin remodelling factor ISW1aItem type: Journal Article
Biochemical Society transactionsRichmond, Timothy J. (2012) - Avoidance of the cytochrome c biogenesis system by periplasmic CXXCH motifsItem type: Journal Article
Biochemical Society transactionsMavridou, Despoina A. L.; Braun, Martin; Thoeny-Meyer, Linda; et al. (2008) - A molecular approach to the concerted action of kinases involved in energy homoeostasisItem type: Other Conference Item
Biochemical Society transactionsNeumann, D.; Schlattner, U.; Wallimann, T. (2003) - Eat it right: ER-phagy and recovER-phagyItem type: Review Article
Biochemical Society transactionsLoi, Marisa; Fregno, Ilaria; Guerra, Concetta; et al. (2018)The endoplasmic reticulum (ER) is the site of protein, lipid, phospholipid, steroid and oligosaccharide synthesis and modification, calcium ion storage, and detoxification of endogenous and exogenous products. Its volume (and activity) must be maintained under normal growth conditions, must be expanded in a controlled manner on activation of ER stress programs and must be reduced to pre-stress size during the recovery phase that follows ER stress termination. ER-phagy is the constitutive or regulated fragmentation and delivery of ER fragments to lysosomal compartments for clearance. It gives essential contribution to the maintenance of cellular homeostasis, proteostasis, lipidostasis and oligosaccharidostasis (i.e. the capacity to produce the proteome, lipidome and oligosaccharidome in appropriate quality and quantity). ER turnover is activated on ER stress, nutrient deprivation, accumulation of misfolded polypeptides, pathogen attack and by activators of macroautophagy. The selectivity of these poorly characterized catabolic pathways is ensured by proteins displayed at the limiting membrane of the ER subdomain to be removed from cells. These proteins are defined as ER-phagy receptors and engage the cytosolic macroautophagy machinery via specific modules that associate with ubiquitin-like, cytosolic proteins of the Atg8/LC3/GABARAP family. In this review, we give an overview on selective ER turnover and on the yeast and mammalian ER-phagy receptors identified so far. - Intramembrane proteolysis and post-targeting functions of signal peptidesItem type: Conference Paper
Biochemical Society transactionsMartoglio, B. (2003)
Publications 1 - 10 of 21