Results 271 to 280 of about 102,380 (310)

Chaperone‐Mediated Autophagic Degradation of USP9X in Macrophages Exacerbates Postmyocardial Infarction Inflammation and Cardiac Dysfunction

open access: yesAdvanced Science, Volume 13, Issue 19, 2 April 2026.
This study demonstrates that inflammatory stimuli induce the acetylation‐triggered, chaperone‐mediated autophagic degradation of ubiquitin‐specific peptidase 9 X‐linked (USP9X) in macrophages. USP9X acts as a macrophage “inflammation switch” after myocardial infarction (MI). USP9X loss destabilizes tumor necrosis factor receptor‐associated factor (TRAF)
Biqing Wang   +7 more
wiley   +1 more source

The possible role of sirtuins and MiRNAs in gastrointestinal cancers: special focus on Sirt1. [PDF]

open access: yesCancer Cell Int
Meybodi SM   +4 more
europepmc   +1 more source

Autophagy-Lysosomal Axis Stimulation by Beta-Hydroxybutyrate in Astrocytes. [PDF]

open access: yesMol Neurobiol
Coronado-Monroy P   +4 more
europepmc   +1 more source
Some of the next articles are maybe not open access.

Related searches:

[SIRT1].

Nihon rinsho. Japanese journal of clinical medicine, 2016
Silent information regulator 2 homolog 1 (SIRT1), a product of the so called "longevity gene", is a protein deacetylase that has been reported to suppress cardiovascular pathologies such as myocardial infarction, and neurodegenerative diseases such as Alzheimer's disease, amyotrophic lateral sclerosis, and Parkinson's disease via anti-apoptosis, anti ...
Yorito, Hattori, Masafumi, Ihara
openaire   +3 more sources

Metabolic benefits from Sirt1 and Sirt1 activators

Current Opinion in Clinical Nutrition and Metabolic Care, 2009
To evaluate the role of mammalian Sirt1 and Sirt1 activators in the protection from metabolic disorders such as diet-induced obesity, diabetes type 2, or nonalcoholic fatty liver disease.Sirtuins are highly conserved nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases that are activated by NAD+ and inhibited by NAD in its reduced form (NADH)
Nilika, Chaudhary, Paul T, Pfluger
openaire   +2 more sources

Bivalent SIRT1 inhibitors

Bioorganic & Medicinal Chemistry Letters, 2017
In the current study, bivalent compounds 1-17 constructed by covalently linking the ɛ-amino group of lysine in a tripeptidic scaffold to a functionality via a linker were prepared and examined for their inhibitory potencies against SIRT1, a prototypical member of the β-nicotinamide adenine dinucleotide (β-NAD+)-dependent sirtuin family of protein Nε ...
Juan, Wang   +3 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy