A promising therapeutic potential of extract in mitigating ethanol-induced working memory impairments and hippocampal oxidative stress in rats.

This study explored the therapeutic potential hydroalcoholic extract derived from Origanum vulgare leaf in mitigating ethanol-induced working memory impairments and hippocampal oxidative stress in rats. Eight groups, including controls, ethanol-exposed rats, and those treated with extract (100, 200, and 300 mg/kg) alone or combined with ethanol, were assessed using the radial arm maze (RAM) for behavioral tests. Ethanol increased working memory errors and time spent in error zones, effects notably reduced by the extract, especially at 300 mg/kg dose (P≤0.

Insight Into Factors Influencing the Aggregation Process in Wild-Type and P66R Mutant SOD1: Computational and Spectroscopic Approaches.

Disturbances in metal ion homeostasis associated with amyotrophic lateral sclerosis (ALS) have been described for several years, but the exact mechanism of involvement is not well understood. To elucidate the role of metalation in superoxide dismutase (SOD1) misfolding and aggregation, we comprehensively characterized the structural features (apo/holo forms) of WT-SOD1 and P66R mutant in loop IV. Using computational and experimental methodologies, we assessed the physicochemical properties of these variants and their correlation with protein aggregation at the molecular level.

Bisdemethoxycurcumin, a novel potent polyphenolic compound, effectively inhibits the formation of amyloid aggregates in ALS-associated hSOD1 mutant (L38R).

Protein misfolding is a biological process that leads to protein aggregation. Anomalous misfolding and aggregation of human superoxide dismutase (hSOD1) into amyloid aggregates is a characteristic feature of amyotrophic lateral sclerosis (ALS), a neurodegenerative illness. Thus, focusing on the L38R mutant may be a wise decision to comprehend the SOD1 disease process in ALS.

Mutation/metal deficiency in the "electrostatic loop" enhanced aggregation process in apo/holo SOD1 variants: implications for ALS diseases.

Despite the many mechanisms it has created to prevent unfolding and aggregation of proteins, many diseases are caused by abnormal folding of proteins, which are called misfolding diseases. During this process, proteins undergo structural changes and become stable, insoluble beta-sheet aggregates called amyloid fibrils. Mutations/disruptions in metal ion homeostasis in the ALS-associated metalloenzyme superoxide dismutase (SOD1) reduce conformational stability, consistent with the protein aggregation hypothesis for neurodegenerative diseases.

GSTP1-A313G genetic polymorphism and the risk of preeclampsia in pregnant women: A study in the northern population of Iran.

Preeclampsia or high blood pressure in pregnancy is one of the special disorders during pregnancy. It seems that oxidative stress plays an important role in the occurrence of this disease. The purpose of this study is to investigate the relationship between the A313G polymorphism in exon five of the glutathione S-transferase gene (GSTP1) and the risk of preeclampsia in a case-control study.

Catharanthine, an anticancer vinca alkaloid: an in silico and in vitro analysis of the autophagic system as the major mechanism of cell death in liver HepG2 cells.

Catharanthine, a component of the anticancer drug vinblastine along with vindoline, disrupts the cell cycle by interfering with mitotic spindle formation. Apart from their antioxidant properties, vinca alkaloids like catharanthine inhibit phosphodiesterase activity and elevate intracellular cAMP levels. The aim of this study was to investigate how catharantine affects apoptosis and autophagy.

Implications of ALS-Associated Mutations on Biochemical and Biophysical Features of hSOD1 and Aggregation Formation.

One of the recognized motor neuron degenerative disorders is amyotrophic lateral sclerosis (ALS). By now, several mutations have been reported and linked to ALS patients, some of which are induced by mutations in the human superoxide dismutase (hSOD1) gene. The ALS-provoking mutations are located throughout the structure of hSOD1 and promote the propensity to aggregate.

Polyphenolic flavonoid compounds act as the inhibitory potential of aggregation process: Implications for the prevention and therapeutics against FALS-associated D101G SOD1 mutant.

Aggregation of proteins is a biological phenomenon caused by misfolded proteins. Human superoxide dismutase (hSOD1) misfolding and aggregation underlie the neurological illness amyotrophic lateral sclerosis (ALS). The most significant contributing factor to ALS is genetic point mutations in SOD1.

Role of charged residues of the "electrostatic loop" of hSOD1 in promotion of aggregation: Implications for the mechanism of ALS-associated mutations under amyloidogenic conditions.

Protein misfolding and amyloid formation are hallmarks of numerous diseases, including amyotrophic lateral sclerosis (ALS), in which hSOD1 aggregation is involved in pathogenesis. We used two point mutations in the electrostatic loop, G138E and T137R, to analyze charge distribution under destabilizing circumstances to gain more about how ALS-linked mutations affect SOD1 protein stability or net repulsive charge. We show that protein charge is important in the ALS disease process using bioinformatics and experiments.

Computational insight into in silico analysis and molecular dynamics simulation of the dimer interface residues of ALS-linked hSOD1 forms in apo/holo states: a combined experimental and bioinformatic perspective.

The aggregation of misfolded SOD1 proteins in neurodegenerative illnesses is a key pathological hallmark in amyotrophic lateral sclerosis (ALS). SOD1 is stabilized and enzymatically activated after binding to Cu/Zn and forming intramolecular disulfide. SOD1 aggregation/oligomerization is triggered by the dissociation of Cu and/or Zn ions.

A double point mutation of SOD1 targeting net charge promotes aggregation under destabilizing conditions: Correlation of charge distribution and ALS-provoking mutation.

A progressive neurodegenerative illness such as amyotrophic lateral sclerosis (ALS) is characterized by the misfolding and aggregation of human CuZn superoxide dismutase (hSOD1) into amyloid aggregates. Thus, designing strategies for the choice of WT-SOD1 and double mutant (G12D/G138E) with an increased net negative charge can be a good idea to elucidate the pathological mechanism of SOD1 in ALS under some destabilizing conditions. Consequently, we show evidence that protein charge, together with other destabilizing conditions, plays an important role in ALS disease.

Human DT-diaphorase expression in : optimization, purification and structural stability.

Expression and purification of human DT-diaphorase, also referred to as NAD(P)H quinone oxidoreductase 1 (NQO1; EC. 1.6.

Development of Analysis and Molecular Dynamics Simulation on L67P and D76Y Mutants of the Human Superoxide Dismutase 1(hSOD1) Related to Amyotrophic Lateral Sclerosis.

Background: One neurodegenerative disorder that is caused by a mutation in the hSOD1 gene is Amyotrophic lateral sclerosis (ALS).

Objectives: The current study was developed in order to evaluate the effect exerted by two ALS-associated point mutations, L67P and D76Y are located in the metal-binding loop, on structural characterization of hSOD1 protein using molecular dynamics (MD) simulations and computational predictions.

Materials And Methods: In this study, GROMACS was utilized to perform molecular dynamics simulations along with 9 different algorithms such as Predict SNP, PhD-SNP, MAPP, PolyPhen-1, Polyphen-2, SNP, SIFT, SNP&GO, and PMUT for predicting and also evaluating the mutational effect on the structural and conformational characterization of hSOD1.

Zinc binding loop mutations of hSOD1 promote amyloid fibrils under physiological conditions: Implications for initiation of amyotrophic lateral sclerosis.

Neurotoxic species of misfolded hSOD1 are involved in the process of causing amyotrophic lateral sclerosis (ALS), which is a devastating neurodegenerative disease. Considerable evidence exists on that hSOD1 mutants-mediated toxicity is resulted from gain-of-function, while the mechanism of this toxicity is unknown yet. In the present study, we focused on the possible mechanism of two point-mutations (namely L67P and D76Y) on metal-binding sites and their possible consequent effects on ALS progress.

Lipase immobilization on a novel class of Zr-MOF/electrospun nanofibrous polymers: Biochemical characterization and efficient biodiesel production.

In this study, due to the favorable properties of MOF compounds and fibrous materials, new nanostructures of Zr-MOF/PVP nanofibrous composites were synthesized by electrospinning procedure. The related features of these samples were characterized by relevant analyzes, including SEM, BET surface area analysis, XRD, and FTIR spectroscopy. The final product showed significant properties such as small particle size distribution, large surface area, and high crystallinity.

Antioxidant, histopathological and biochemical outcomes of short-term exposure to acetamiprid in liver and brain of rat: The protective role of N-acetylcysteine and S-methylcysteine.

The present study was conducted to investigate the protective effects of N-Acetyl-L-cysteine (NAC) and S-methyl- L-cysteine (SMC) against hepatic oxidative stress and brain damage induced by acetamiprid (ACP) in rats, which were evaluated by histopathological changes, measuring serum biomarkers and antioxidant defense systems. In this study, 42 rats were randomly divided into 6 groups and administered by intraperitoneally for one week: the control group, the sham group (normal saline), ACP alone (5 mg/kg) (group1), NAC alone (160 mg/kg) (group2), ACP + SMC (100 mg/kg) (group3), ACP + NAC (group 4) and ACP + NAC + SMC (group 5). Our results showed that acetamiprid induces liver injures including infiltration of inflammatory cells, congestion and altered histo-architecture and brain damages including gliosis, hyperemia and necrosis.

Copper nanoparticles promote rapid wound healing in acute full thickness defect via acceleration of skin cell migration, proliferation, and neovascularization.

Worldwide, impaired wound healing leads to a large burden of morbidity and mortality. Current treatments have several limitations. Recently, nanomaterials such as copper nanoparticles (CuNPs) have attracted considerable research interest.