Results 81 to 90 of about 6,631,648 (289)

NADH‐Reductive Stress Induced by Dihydrolipoamide Dehydrogenase Activation Contributes to Cuproptosis

open access: yesAdvanced Science, EarlyView.
This study demonstrates a cuproptosis mechanism involving nicotinamide adenine dinucleotide (NADH)‐reductive stress in neural cells. Copper activates dihydrolipoamide dehydrogenase under mitochondrial pH, accumulating NADH. Copper also induces mitochondrial permeability transition pore opening, facilitating NADH translocation to the cytosol and ...
Si‐Yi Zhang   +3 more
wiley   +1 more source

Natural Peptides with Antimicrobial Activity

open access: yesCHIMIA, 1998
Antibiosis is a mechanism by which many cell types control potential environmental takeover or pathogenicity by microbes, especially bacteria. It is now clear that a large proportion of the antimicrobial compounds produced by various cells and ...
Ralph W. Jack, Günther Jung
doaj  

Beyond Toxin Transport: Novel Role of ABC Transporter for Enzymatic Machinery of Cereulide NRPS Assembly Line

open access: yesmBio, 2020
Nonribosomal peptide synthetases (NRPSs) and polyketide synthetases (PKSs) play a pivotal role in the production of bioactive natural products, such as antibiotics and cytotoxins. Despite biomedical and pharmaceutical importance, the molecular mechanisms
A. Gacek-Matthews   +5 more
doaj   +1 more source

Asymmetric Cu─N─Ru Bridgedsite Nanozyme‐Loaded Injectable Thermogel Boosts Cuproptosis‐Like Death for Multidrug‐Resistant Urinary Tract Infections

open access: yesAdvanced Science, EarlyView.
To address multidrug‐resistant urinary tract infections (MDR‐UTIs), we developed Cu‐ZIF8‐Ru nanozyme featuring an asymmetric Cu─N─Ru catalytic site. This unique structure enhances multienzyme‐mimetic activity, eradicating resistant bacteria by inducing a cuproptosis‐like death pathway through intracellular Cu2+ accumulation and energy depletion.
Guanlin Li   +9 more
wiley   +1 more source

BACILLUS SUBTILIS SJ01 PRODUCES HEMICELLULOSE DEGRADING MULTI-ENZYME COMPLEXES

open access: yesBioResources, 2012
Cellulose and hemicellulose account for a large portion of the world’s plant biomass. In nature, these polysaccharides are intertwined, forming complex materials that require multiple enzymes to degrade them.
Brett Ivan Pletschke   +2 more
doaj  

Colocalization and Disposition of Cellulosomes in Clostridium clariflavum as Revealed by Correlative Superresolution Imaging

open access: yesmBio, 2018
Cellulosomes are multienzyme complexes produced by anaerobic, cellulolytic bacteria for highly efficient breakdown of plant cell wall polysaccharides.
Lior Artzi   +6 more
doaj   +1 more source

Synthetic metabolons for metabolic engineering. [PDF]

open access: yes, 2014
Journal ArticleResearch Support, Non-U.S. Gov'tReviewThis is a pre-copyedited, author-produced PDF of an article accepted for publication in Journal of Experimental Botany following peer review. The definitive publisher-authenticated version J. Exp. Bot.
Howard, Thomas P.   +2 more
core   +1 more source

Microglial Membranes Wrapped Ultrasmall Medium‐Entropy Ru Single‐Atom Nanozyme: Enhanced Catalysis for Accelerating Inflammation/Redox Microenvironment Regulation in Intracerebral Hemorrhage

open access: yesAdvanced Science, EarlyView.
PtRhIr/Ru SAN@M nanozymes cross the blood–brain barrier and selectively accumulate in hemorrhagic brain regions. By mimicking multiple enzyme activities, they attenuate oxidative stress, modulate microglial polarization toward an anti‐inflammatory phenotype, inhibit ferroptosis, and promote neuronal repair.
Jiebo Li   +17 more
wiley   +1 more source

Reactive oxygen and nitrogen species generation features under conditions of acute hepatotoxicity

open access: yesVìsnik Dnìpropetrovsʹkogo Unìversitetu: Serìâ Bìologìâ, Ekologìâ, 2014
Development of the most of pathological conditions occurs by free radical mechanism which is characterized by increased free radical production at the cellular level, especially reactive oxygen and nitrogen species (ROS/RNS).
I. О. Shmarakov   +2 more
doaj   +1 more source

multienzyme complex

open access: yes, 2014
Citation: 'multienzyme complex' in the IUPAC Compendium of Chemical Terminology, 3rd ed.; International Union of Pure and Applied Chemistry; 2006. Online version 3.0.1, 2019. 10.1351/goldbook.M04047 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms.
openaire   +1 more source

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