Results 91 to 100 of about 7,369 (220)
Frontiers in Bioengineering and Biotechnology, 2019 Peptides and proteins containing disulfide bonds can be produced in Escherichia coli by targeting the oxidizing periplasm, co-expressing isomerases or chaperons, refolding from inclusion bodies, or by using redox-engineered E. coli strains.
Mathias Joachim +7 more
doaj +1 more source
Analysis of the interaction of calcitriol with the disulfide isomerase ERp57 [PDF]
, 2016 Calcitriol, the active form of vitamin D3, can regulate the gene expression through the binding to the nuclear receptor VDR, but it can also display nongenomic actions, acting through a membrane- associated receptor, which has been discovered as the ...
Altieri, Fabio +7 more
core +1 more source
Journal of Clinical Periodontology, EarlyView.ABSTRACT Introduction This explanatory pilot study presents a workflow to identify approved drugs, which could be repurposed for periodontitis therapy using salivary proteomics combined with drug‐target database screening. Methods Proteomic analyses of saliva using LC–MS/MS were conducted in two independent settings: a cohort (sub‐study I, N = 187) and
Taisir Bozo +11 more
wiley +1 more source
DsbG, a Protein Disulfide Isomerase with Chaperone Activity [PDF]
Journal of Biological Chemistry, 2000 DsbG, a protein disulfide isomerase present in the periplasm of Escherichia coli, is shown to function as a molecular chaperone. Stoichiometric amounts of DsbG are sufficient to prevent the thermal aggregation of two classical chaperone substrate proteins, citrate synthase and luciferase.
F, Shao +3 more
openaire +2 more sources
The Role of Oxidative Stress in Periodontitis
Journal of Periodontal Research, EarlyView.Oxidative stress is involved in multiple chemical reactions that take place in different intracellular organelles: mitochondria, rough endoplasmic reticulum, peroxisomes, autophagy, and aging, and can be influenced by exogenous factors: nutrition, physical activity, psychological status, environmental conditions, microbiome, and drugs.
Pedro Bullon +3 more
wiley +1 more source
Compact Conformations of Human Protein Disulfide Isomerase
PLoS ONE, 2014 Protein disulfide isomerase (PDI) composed of four thioredoxin-like domains a, b, b', and a', is a key enzyme catalyzing oxidative protein folding in the endoplasmic reticulum. Large scale molecular dynamics simulations starting from the crystal structures of human PDI (hPDI) in the oxidized and reduced states were performed.
Shang Yang +8 more
openaire +4 more sources
LUCID: An Integrative Approach for Target Discovery and dsRNA Design in Plant Fungal Pathogens
Plant Biotechnology Journal, EarlyView.LUCID: A computational pipeline for RNAi‐based biofungicide design. ABSTRACT Phytopathogenic fungi pose an escalating threat to global food security and ecosystem stability, as resistance and environmental concerns diminish the effectiveness of conventional fungicides.
Lucía Jiménez‐Castro +4 more
wiley +1 more source
eLife, 2018 Pharmacologic arm-selective unfolded protein response (UPR) signaling pathway activation is emerging as a promising strategy to ameliorate imbalances in endoplasmic reticulum (ER) proteostasis implicated in diverse diseases.
Ryan Paxman +6 more
doaj +1 more source
Conformational Resilience of Protein Disulfide Isomerase
The FASEB Journal, 2019 Protein disulfide isomerase (PDI) is a 57 kDa protein with both oxidoreductase and chaperone activities that is mainly localized to the endoplasmic reticulum. It is a U‐shaped protein with an abb'xa’ structural organization where the a and
Jessica Guyette +3 more
openaire +1 more source
ER Dysfunction and Protein Folding Stress in ALS [PDF]
, 2013 Amyotrophic lateral sclerosis (ALS) is the most frequent paralytic disease in adults. Most ALS cases are considered sporadic with no clear genetic component.
Hetz, Claudio +3 more
core +3 more sources