Results 241 to 250 of about 3,068,795 (349)

Enzymatic degradation of biopolymers in amorphous and molten states: mechanisms and applications

open access: yesFEBS Open Bio, EarlyView.
This review explains how polymer morphology and thermal state shape enzymatic degradation pathways, comparing amorphous and molten biopolymer structures. By integrating structure–reactivity principles with insights from thermodynamics and enzyme engineering, it highlights mechanisms that enable efficient polymer breakdown.
Anđela Pustak, Aleksandra Maršavelski
wiley   +1 more source

The role of lipid metabolism in neuronal senescence

open access: yesFEBS Open Bio, EarlyView.
Disrupted lipid metabolism, through alterations in lipid species or lipid droplet accumulation, can drive neuronal senescence. However, lipid dyshomeostasis can also occur alongside neuronal senescence, further amplifying tissue damage. Delineating how lipid‐induced senescence emerges in neurons and glial cells, and how it contributes to ageing and ...
Dikaia Tsagkari   +2 more
wiley   +1 more source

Alcohol‐induced altered glycans in human tracheal epithelial cells promote bacterial adhesion

open access: yesFEBS Open Bio, EarlyView.
Alcohol induces altered glycans to promote bacteria adhesion. Heavy alcohol drinking is known to increase the risk of bacterial pneumonia. However, the link between alcohol levels and risk of infection remains underexplored. Recently, we found that alcohol induced α2‐6sialo mucin O‐glycans in human tracheobronchial epithelial cells, which mediated the ...
Pi‐Wan Cheng   +2 more
wiley   +1 more source

C2α‐carbanion‐protonating glutamate discloses tradeoffs between substrate accommodation and reaction rate in actinobacterial 2‐hydroxyacyl‐CoA lyase

open access: yesFEBS Open Bio, EarlyView.
Enzymes of the 2‐hydroxyacyl‐CoA lyase group catalyze the condensation of formyl‐CoA with aldehydes or ketones. Thus, by structural adaptation of active sites, practically any pharmaceutically and industrially important 2‐hydroxyacid could be biotechnologically synthesized. Combining crystal structure analysis, active site mutations and kinetic assays,
Michael Zahn   +4 more
wiley   +1 more source

Patatin‐domain‐containing (phospho)lipases under control: Mammalian co‐regulators and pathogenic activation mechanisms

open access: yesFEBS Open Bio, EarlyView.
Patatin domain‐containing (phospho)lipases are lipid‐hydrolyzing enzymes central to metabolism, membrane remodeling, and signaling. Their activity relies on precise co‐activation mechanisms involving protein–protein interactions and conformational rearrangements.
Noopur Dubey   +2 more
wiley   +1 more source

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