Results 251 to 260 of about 992,662 (310)
Bioprosthetic aortic valves have revolutionized the treatment of aortic stenosis, but their durability is limited by structural valve deterioration (SVD). This review focuses on the pericardial tissue at the heart of these valves, examining how its mechanical properties and calcification drive fatigue and failure.
Gabriele Greco +7 more
wiley +1 more source
In Situ 3D Bioprinting: Impact of Cross‐Linking on the Adhesive Properties of Hydrogels
In situ 3D bioprinting enables the direct deposition of cell‐laden, adhesive biomaterials for on‐site tissue regeneration. This review provides a comprehensive overview of how cross‐linking influences the bioadhesive properties of hydrogels used in 3D bioprinting, highlighting cross‐linking triggers, bioadhesion mechanisms, polymer interpenetration ...
Odile Romero Fernandez +4 more
wiley +1 more source
4D‐Printed Magneto‐Plasmonic Microrobots for Programmable Spatiotemporal De‐Icing
A 4D‐printing strategy is introduced to achieve programmable de‐icing devices. By aligning gold–magnetite nanofillers within a photosensitive resin, the printed structures exhibit dual magnetic and plasmonic functionalities, enabling precise spatio‐temporal ice removal through thermoplasmonic effects.
Amélie Pérot +7 more
wiley +1 more source
Shaping of Biohybrid Functional Living Materials
This work demonstrates a strategy for shaping living mycelium into functional materials by directing its natural growth. Nanoparticles armor hyphae, micron‐scale particles entangle within the network, and printed hydrogel architectures steer expansion, creating defined geometries.
Sarah Schyck +3 more
wiley +1 more source
Characterization of the Effects of Low-Sodium Salt Substitution on Sensory Quality, Protein Oxidation, and Hydrolysis of Air-Dried Chicken Meat and Its Molecular Mechanisms Based on Tandem Mass Tagging-Labeled Quantitative Proteomics. [PDF]
Li J +8 more
europepmc +1 more source
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Annals of the New York Academy of Sciences, 2000
Abstract: The oxidative modification of proteins by reactive species, especially reactive oxygen species, is implicated in the etiology or progression of a panoply of disorders and diseases. These reactive species form through a large number of physiological and non‐physiological reactions.
E R, Stadtman, R L, Levine
openaire +2 more sources
Abstract: The oxidative modification of proteins by reactive species, especially reactive oxygen species, is implicated in the etiology or progression of a panoply of disorders and diseases. These reactive species form through a large number of physiological and non‐physiological reactions.
E R, Stadtman, R L, Levine
openaire +2 more sources
Protein oxidation and proteolysis
bchm, 2006Abstract One of the hallmarks of chronic or severe oxidative stress is the accumulation of oxidized proteins, which tend to form high-molecular-weight aggregates. The major proteolytic system responsible for the removal of oxidized cytosolic and nuclear proteins is the proteasome.
Nicolle, Bader, Tilman, Grune
openaire +2 more sources
Experimental Gerontology, 2001
Organisms produce reactive oxygen species (ROS) throughout their lives. The activities of a number of key antioxidant enzymes, such as catalase, superoxide dismutase and glutathione peroxidase, which protect against the damaging effects of ROS, have been reported to decrease with increasing age, though this is not unequivocal.
Linton, S +2 more
openaire +3 more sources
Organisms produce reactive oxygen species (ROS) throughout their lives. The activities of a number of key antioxidant enzymes, such as catalase, superoxide dismutase and glutathione peroxidase, which protect against the damaging effects of ROS, have been reported to decrease with increasing age, though this is not unequivocal.
Linton, S +2 more
openaire +3 more sources
Accounts of Chemical Research, 2000
The oxidative folding of proteins is reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). The mutual effects of conformational folding and disulfide bond regeneration are emphasized, particularly the "locking in" of native disulfide bonds by stable tertiary structure in disulfide intermediates.
M, Narayan +3 more
openaire +2 more sources
The oxidative folding of proteins is reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). The mutual effects of conformational folding and disulfide bond regeneration are emphasized, particularly the "locking in" of native disulfide bonds by stable tertiary structure in disulfide intermediates.
M, Narayan +3 more
openaire +2 more sources
Photochemical & Photobiological Sciences, 2012
Photo-induced damage to proteins occurs via multiple pathways. Direct damage induced by UVB (λ 280-320 nm) and UVA radiation (λ 320-400 nm) is limited to a small number of amino acid residues, principally tryptophan (Trp), tyrosine (Tyr), histidine (His) and disulfide (cystine) residues, with this occurring via both excited state species and radicals ...
David I, Pattison +2 more
openaire +2 more sources
Photo-induced damage to proteins occurs via multiple pathways. Direct damage induced by UVB (λ 280-320 nm) and UVA radiation (λ 320-400 nm) is limited to a small number of amino acid residues, principally tryptophan (Trp), tyrosine (Tyr), histidine (His) and disulfide (cystine) residues, with this occurring via both excited state species and radicals ...
David I, Pattison +2 more
openaire +2 more sources

