Results 81 to 90 of about 295,099 (303)
Protein stability can be monitored by many different techniques. However, these protocols are often lengthy, consume large amounts of protein, and require expensive and specialized instruments.
Kyle K. Biggar +2 more
doaj +1 more source
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane +11 more
wiley +1 more source
Fluorescence characterization of denatured proteins [PDF]
Characterization of unfolded states, while critical to a complete understanding of protein folding, is inherently difficult due to structural heterogeneity and dynamic interchange between states. The growing body of work focusing on single molecule fluorescence techniques for the study of protein folding, also highlights their potential for studies of ...
Huimin, Chen, Elizabeth, Rhoades
openaire +2 more sources
Acute caffeine treatment protects the developing retina from ischemia‐induced cell death
Caffeine reduces cell death in the developing retina under ischemia (OGD). This effect does not involve BDNF upregulation or antioxidant pathways (NRF2/VEGF). Neuroprotection occurs mainly through adenosine A2A receptor antagonism, decreasing glutamate release and excitotoxicity, highlighting caffeine's potential as an acute neuroprotective agent in ...
Amanda Alves Nascimento +6 more
wiley +1 more source
ORIGINAL ARTICLE: Membrane Stabilizing Activity and Protein Denaturation: A Possible Mechanism of Action for the Anti-Inflammatory Activity of Phyllanthus amarus [PDF]
Background: Previous studies confirm the anti-inflammatory potential of Phyllanthus amarus herb. Aim and objective: Primary aim of the present study was to investigate the possible anti-inflammatory mechanism of Phyllanthus amarus extract using in-vitro ...
Atul R. Chopade +2 more
doaj
Hyperthermophile protein behavior: partially-structured conformations of Pyrococcus furiosus rubredoxin monomers generated through forced cold-denaturation and refolding. [PDF]
Some years ago, we showed that thermo-chemically denatured, partially-unfolded forms of Pyrococcus furiosus triosephosphateisomerase (PfuTIM) display cold-denaturation upon cooling, and heat-renaturation upon reheating, in proportion with the extent of ...
Sanjeev Kumar Chandrayan +3 more
doaj +1 more source
TisIBP8, a fungal‐derived hyperactive ice‐binding protein, helps Caenorhabditis elegans survive dehydration. It localizes near cell membranes, reduces cell damage, and helps maintain membrane structure during drying. These results suggest that ice‐binding proteins can protect cells from dehydration stress as well as freezing stress.
Daiki Shimose +9 more
wiley +1 more source
The aim of the present study was to evaluate the effect of cooking (boiling, steaming, and frying) on anti-inflammation associated properties in vitro of six popularly consumed green leafy vegetables in Sri Lanka, namely: Centella asiatica, Cassia ...
K. D. P. P. Gunathilake +2 more
doaj +1 more source
Zein‐Based Adhesives: Sustainable Extraction and Application in Bioadhesive Technologies
Zein is extracted from corn gluten meal using a simple and scalable process with high yield (~90%). The resulting protein is applied in bioadhesives modified with Ca2+ and Fe3+ ions, exhibiting substrate‐dependent adhesion. The findings demonstrate competitive bonding performance and highlight the role of ionic interactions in tuning adhesion ...
Paula Bertolino Sanvezzo +3 more
wiley +1 more source
Feasibility of microfluidic routes to monitor protein stability as a tool for bioprocessing
During the bioprocessing of therapeutics, proteins may become damaged leading to modifications and changes in stability. This may, as a consequence, cause serious and potentially fatal side effects when administered to patients making damage ...
Remtulla, N.
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