Results 61 to 70 of about 22,350 (290)

Phosphorylation‐Facilitated CKB Lactylation At K11 By GCN5 Enhances Creatine Kinase Activity and Mitigates Neuronal Damage After Cerebral Ischemia‐Reperfusion

open access: yesAdvanced Science, EarlyView.
This study uncovers hierarchical coordination between K11 lactylation and S199 phosphorylation of CKB in cerebral ischemia‐reperfusion injury. Such dual modifications potentiate CKB enzymatic function, remodel energy metabolism, alleviate oxidative stress and neuronal damage, and represent a viable therapeutic target for stroke treatment.
Chao Duan   +17 more
wiley   +1 more source

Conserved Metabolic Regulatory Functions of Sirtuins [PDF]

open access: yes, 2008
SummarySilent information regulator 2 (Sir2) proteins, or sirtuins, are protein deacetylases/mono-ADP-ribosyltransferases found in organisms ranging from bacteria to humans.
Verdin, Eric, Schwer, Bjoern
core   +1 more source

The sirtuin family in cancer [PDF]

open access: yesCell Cycle, 2019
Sirtuins are a family of protein deacylases and ADP-ribosyl-transferases, homologs to the yeast SIR2 protein. Seven sirtuin paralogs have been described in mammals, with different subcellular locations, targets, enzymatic activities, and regulatory mechanisms.
Luis Filipe Costa-Machado   +1 more
openaire   +2 more sources

Histone H3K18 Lactylation Promotes the Malignant Progression of Wilms Tumor via a PSRC1/AKT/HIF‐1α Positive Feedback Loop

open access: yesAdvanced Science, EarlyView.
In nephroblastoma, aberrant glycolysis drives lactate accumulation, which elevates histone H3K18 lactylation via p300. Lactylation of the PSRC1 promoter activates its transcription. PSRC1 competitively binds AKT, relieving PTEN‐mediated inhibition and triggering AKT/mTOR/HIF‐1α signaling.
Yanping Wang   +6 more
wiley   +1 more source

Sirtuins: guardians of mammalian healthspan

open access: yes, 2014
•Overexpression of the mammalian sirtuins SIRT1 and SIRT6 increases lifespan in mouse models.•Sirtuin activity is protective against a variety of age-associated diseases.•Sirtuins affect tumor initiation and maintenance via diverse mechanisms.•Small ...
Skinner, Mary E.   +2 more
core   +1 more source

Assaying Chromatin Sirtuins [PDF]

open access: yes, 2013
Most of the sirtuins' nuclear substrates identified so far are histones or other chromatin-associated proteins and, thus, it is of special relevance the development of good biochemical techniques to analyze the biology of these proteins in the context of chromatin.
Zhong, Lei   +4 more
openaire   +4 more sources

Miro1 Protects Against Acute Kidney Injury Through Modulating Mitochondrial Homeostasis via Interaction With Sirt6

open access: yesAdvanced Science, EarlyView.
Ischemia‐reperfusion reduces Sirt6 activity, thereby increasing Miro1 acetylation. Hyperacetylated Miro1 exhibits perinuclear distribution and degradation, thereby inducing mitochondrial dysfunction and promoting apoptosis in renal tubular epithelial cells. This pathway reveals a mechanistic link between Sirt6‐mediated deacetylation and Miro1 stability
Lin Wu   +12 more
wiley   +1 more source

SnapShot: Sirtuins, NAD, and Aging [PDF]

open access: yes, 2014
Sirtuins are highly conserved nicotinamide adenine dinucleotide (NAD)-dependent enzymes that regulate a wide range of biological processes, including aging, in several species.
Guarente, Leonard, Nakagawa, Takashi
core   +1 more source

Rhoifolin Alleviates Ulcerative Colitis by Targeting NMNAT1 and Activating SIRT1‐FOXO1 Signaling to Enhance ILC3s Effector Function

open access: yesAdvanced Science, EarlyView.
Rhoifolin directly targets NMNAT1, thereby activating nicotinamide salvage pathway and promoting intracellular NAD+ biosynthesis. Elevated NAD+ levels enhance SIRT1 activity, leading to FOXO1 deacetylation and nuclear translocation. Nuclear FOXO1 subsequently binds to the IL‐22 promoter, upregulating IL‐22 transcription and potentiating ILC3 effector ...
Hongqiong Yang   +12 more
wiley   +1 more source

Sirtuins in tumorigenesis [PDF]

open access: yes, 2014
Sirtuins (SIRT) are group of enzymes that require nicotinamide adenine dinucleotide (NAD+) to catalyze their reactions. These chemical compounds have mono (ADP-ribosyl) transferase or deacetylases activities, and they can be found in nearly all species.
SAŠA KRALIK-OGUIĆ   +13 more
core   +1 more source

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