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Glycoprotein-folding quality control in the endoplasmic reticulum
(De Gruyter, 2012)
Nearly one third of proteins synthesized by eukaryotic cells belong to the secretory pathway, gaining access to the endoplasmic reticulum (ER) either co- or post-translationally. In the ER disulfide bonds are formed, ...
The Molecular Chaperone Hsp70 Family Members Function by a Bidirectional Heterotrophic Allosteric Mechanism
(BENTHAM SCIENCE PUBL LTD, 2011)
The Hsp70 family is one of the most important and conserved molecular chaperone families. It is well documented that Hsp70 family members assist many cellular processes involving protein quality control, as follows: protein ...
TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis
(Elsevier Science, 2021-08)
The Endoplasmic Reticulum (ER) is responsible for the folding and post-translational modification of secretory proteins, as well as for triaging misfolded proteins. During folding, there is a complex yet only partially ...
UDP-Glucose: Glycoprotein Glucosyltransferase 1,2 (UGGT1,2)
(Springer, 2014)
Almost one-third of proteins synthesized by eukaryotic cells belong to the secretory pathway, entering the endoplasmic reticulum (ER) either co- or posttranslationally. In the ER, proteins acquire their native tertiary ...
Endoplasmic reticulum stress in autoimmune diseases: Can altered protein quality control and/or unfolded protein response contribute to autoimmunity? A critical review on Sjogren's syndrome
(ELSEVIER SCIENCE BV, 2018)
For many years, researchers in the field of autoimmunity have focused on the role of the immune components in the etiopathogenesis of autoimmune diseases. However, some studies have demonstrated the importance of target ...
The stress rheostat: an interplay between the unfolded protein response (UPR) and autophagy in neurodegeneration
(2008)
The unfolded protein response (UPR) is a conserved adaptive reaction that increases cell survival under conditions of endoplasmic reticulum (ER) stress. The UPR controls diverse processes such as protein folding, secretion, ...
The Endoplasmic Reticulum Glucosyltransferase Recognizes Nearly Native Glycoprotein Folding Intermediates
(American Society for Biochemistry and Molecular Biology, 2004-10)
The UDP-Glc:glycoprotein glucosyltransferase (GT), a key player in the endoplasmic reticulum (ER) quality control of glycoprotein folding, only glucosylates glycoproteins displaying non-native conformations. To determine ...
Endoplasmic reticulum stress in autoimmune diseases : Can altered protein quality control and/or unfolded protein response contribute to autoimmunity? A critical review on Sjögren's syndrome
(2018-08)
For many years, researchers in the field of autoimmunity have focused on the role of the immune components in the etiopathogenesis of autoimmune diseases. However, some studies have demonstrated the importance of target ...
ER Proteostasis Control of Neuronal Physiology and Synaptic Function
(Elsevier Ltd, 2018)
© 2018 Elsevier Ltd Neuronal proteostasis is maintained by the dynamic integration of different processes that regulate the synthesis, folding, quality control, and localization of proteins. The endoplasmic reticulum (ER) ...
ER stress and the unfolded protein response in neurodegeneration
(Nature Publishing Group, 2017)
The clinical manifestation of neurodegenerative diseases is initiated by the selective alteration in the functionality of distinct neuronal populations. The pathology of many neurodegenerative diseases includes accumulation ...