Results 191 to 200 of about 220,248 (385)

Anti‐Inflammatory/Antioxidant Features of Adipose Tissue Mesenchymal Stem Cells Conditioned Media for Doped TiO2 Nanoparticles in Induced Inflammation

open access: yesChemistryOpen, EarlyView.
The PI3K/AKT pathway is triggered when lipopolysaccharide (LPS) binds to TLR4 on the cell membrane. This causes the NF‐κB complex to get phosphorylated and IKB to degrade, allowing NF‐κB to go into the nucleus. Pro‐inflammatory genes including interleukin‐4 (IL‐4), IL‐6, and tumor necrosis factor α are triggered by this.
Ahmed A. Abd‐Rabou   +4 more
wiley   +1 more source

Effect of metal-complexing agents on the oxygenase activity of sheep vesicular glands [PDF]

open access: green, 1973
Paul R. LeTellier   +2 more
openalex   +1 more source

Comparative Proteomics of Salinity Stress Responses in Fish and Aquatic Invertebrates

open access: yesPROTEOMICS, EarlyView.
ABSTRACT Fluctuating salinity is symptomatic of climate change challenging aquatic species. The melting of polar ice, rising sea levels, coastal surface and groundwater salinization, and increased evaporation in arid habitats alter salinity worldwide. Moreover, the frequency and intensity of extreme weather events such as rainstorms and floods increase,
Maxime Leprêtre   +3 more
wiley   +1 more source

Interactions of rare earth elements with living organisms and emerging biotechnical applications

open access: yesPLANTS, PEOPLE, PLANET, EarlyView.
Rare earth elements (REEs) are critical resources required to achieve net‐zero carbon emission targets and energy security. However, rising demand for REEs coupled with significant extraction and processing challenges and geopolitical risks restricts access to REE resources.
Samantha A. McGaughey   +6 more
wiley   +1 more source

Targeting heme oxygenase-1 and carbon monoxide for therapeutic modulation of inflammation.

open access: yesTranslational research : the journal of laboratory and clinical medicine, 2016
S. Ryter, A. Choi
semanticscholar   +1 more source

Binding Differences of the Peptide‐Substrate–Binding Domain of Collagen Prolyl 4‐Hydroxylases I and II for Proline‐ and Hydroxyproline‐Rich Peptides

open access: yesProteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Collagen prolyl 4‐hydroxylase (C‐P4H) catalyzes the 4‐hydroxylation of Y‐prolines of the XYG‐repeat of procollagen. C‐P4Hs are tetrameric α2β2 enzymes. The α‐subunit provides the N‐terminal dimerization domain, the middle peptide‐substrate–binding (PSB) domain, and the C‐terminal catalytic (CAT) domain.
M. Mubinur Rahman   +8 more
wiley   +1 more source

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