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The Journal of biological chemistry, ISSN 0021-9258, 01/2020, Volume 295, Issue 8, pp. 2438 - 2448
How and when disulfides bonds form in proteins relative to the stage of their folding is a fundamental question in cell biology. Two models describe this... 
Journal Article
The EMBO Journal, ISSN 0261-4189, 08/2019, Volume 38, Issue 15
Journal Article
The EMBO journal, 06/2019
Activation of the ATF6α signaling pathway is initiated by trafficking of ATF6α from the ER to the Golgi apparatus. Its subsequent proteolysis releases a... 
Journal Article
Journal of Hypertension, ISSN 0263-6352, 10/2018, Volume 36 Suppl 3, pp. e57 - e58
OBJECTIVES:Nox-derived ROS and ER stress are implicated in vascular dysfunction in hypertension. Evidence suggests a cross-talk between these processes;... 
Hypertension | Oxidative stress | Care and treatment | Development and progression | Genetic aspects | Health aspects | Endoplasmic reticulum
Journal Article
07/2018, 1st, Chemical biology, ISBN 1782629904, Volume 9
The formation of disulphide bonds is probably the most influential modification of proteins. These bonds are unique among post-translational modifications of... 
SCIENCE / Chemistry / Organic | Protein folding
eBook
Hypertension (Dallas, Tex. : 1979), ISSN 0194-911X, 7/2018, Volume 72, Issue 1, pp. 235 - 246
Vascular Nox-derived ROS and ER stress have been implicated in hypertension. However relationships between these processes is unclear. We hypothesized that Nox... 
compartmentalization | Reactive oxygen species | vascular smooth muscle
Journal Article
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 01/2018, Volume 43, Issue 1, pp. 32 - 43
The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for protein folding, degradation, chaperone function, and the ER... 
ER chaperones | disulfides | protein folding | ER-associated degradation | thiol reduction | endoplasmic reticulum | ERAD PATHWAY | DISULFIDE-ISOMERASE | OXIDATIVE STRESS | STRUCTURAL BASIS | PDI FAMILY | BIOCHEMISTRY & MOLECULAR BIOLOGY | REDOX | REDUCTASE | DEGRADATION | CYTOSOL | QUALITY-CONTROL | Proteins
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 01/2018, Volume 43, Issue 1, p. 32
The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for protein folding, degradation, chaperone function, and the ER... 
Studies | Proteins | Reduction | Homesteading | Protein folding | Homeostasis | Oxidation | Catalysis | Endoplasmic reticulum | Cytosol
Journal Article
Wellcome Open Research, ISSN 2398-502X, 2017, Volume 2, p. 36
Background: The mammalian endoplasmic reticulum (ER) continuously adapts to the cellular secretory load by the activation of an unfolded protein response... 
Enzymes | Phosphorylation | Transcription factors | Protein folding | Funding | Cloning | Homeostasis | Kinases | Endoplasmic reticulum | Cellular Death & Stress Responses
Journal Article
Wellcome Open Research, ISSN 2398-502X, 2017, Volume 2, p. 36
: The mammalian endoplasmic reticulum (ER) continuously adapts to the cellular secretory load by the activation of an unfolded protein response (UPR).  This... 
Journal Article
Journal Article
Biophysics Reports, ISSN 2364-3439, 8/2015, Volume 1, Issue 1, pp. 14 - 17
The activity of typical 2-cys peroxiredoxin (Prxs) can be regulated by hyperoxidation with a consequent loss of redox activity. Here we developed a simple... 
Biochemistry, general | Peroxiredoxin | Biotechnology | Biophysics and Biological Physics | Hyperoxidation | Isoelectric focusing | Physics
Journal Article