Results 41 to 50 of about 191,770 (239)

SIRT4 positively regulates autophagy via ULK1, but independently of HDAC6 and OPA1

open access: yesFEBS Open Bio, EarlyView.
Cells expressing SIRT4 (H161Y), a catalytically inactive mutant of the sirtuin SIRT4, fail to upregulate LC3B‐II and exhibit a reduced autophagic flux under stress conditions. Interestingly, SIRT4(H161Y) promotes phosphorylation of ULK1 at S638 and S758 that are associated with inhibition of autophagy initiation.
Isabell Lehmkuhl   +13 more
wiley   +1 more source

Smad1 Promotes Tumorigenicity and Chemoresistance of Glioblastoma by Sequestering p300 From p53

open access: yesAdvanced Science
Acetylation is critically required for p53 activation, though it remains poorly understood how p53 acetylation is regulated in glioblastoma (GBM). This study reveals that p53 acetylation is a favorable prognostic marker for GBM, regardless of p53 status,
Lingli Gong   +15 more
doaj   +1 more source

Natural Products as Geroprotective Modulators in Diabetic Nephropathy: A Mechanistic Framework Integrating Aging Hallmarks and the AMPK–SIRT1–Nrf2 Axis

open access: yesAging and Cancer, EarlyView.
Natural products target the aging kidney in diabetic nephropathy by restoring the AMPK–SIRT1–Nrf2 axis, reducing oxidative stress, inflammation, fibrosis, and cellular senescence while enhancing mitochondrial biogenesis and antioxidant defenses.
Sherif Hamidu   +8 more
wiley   +1 more source

Progressive mitochondrial protein lysine acetylation and heart failure in a model of Friedreich's ataxia cardiomyopathy.

open access: yesPLoS ONE, 2017
IntroductionThe childhood heart disease of Friedreich's Ataxia (FRDA) is characterized by hypertrophy and failure. It is caused by loss of frataxin (FXN), a mitochondrial protein involved in energy homeostasis.
Amanda R Stram   +5 more
doaj   +1 more source

Promotion of Lung Cancer Metastasis by SIRT2‐Mediated Extracellular Protein Deacetylation

open access: yesAdvanced Science, 2023
Acetylation of extracellular proteins has been observed in many independent studies where particular attention has been given to the dynamic change of the microenvironmental protein post‐translational modifications.
Meng Wu   +24 more
doaj   +1 more source

Acetylation Goes Global: The Emergence of Acetylation Biology [PDF]

open access: yesScience Signaling, 2009
Proteomic analysis shows protein acetylation to be more prevalent than previously appreciated.
Kristi L, Norris   +2 more
openaire   +2 more sources

Developmental and Epileptic Encephalopathy due to Biallelic Pathogenic Variants in PIGM

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective PIGM encodes a critical enzyme in the glycosylphosphatidylinositol (GPI)‐anchor biosynthesis pathway. While promoter‐region mutations in PIGM have been associated with a relatively mild phenotype characterized by portal vein thrombosis and absence seizures, recent evidence suggests that coding‐region mutations result in a more severe
Júlia Sala‐Coromina   +11 more
wiley   +1 more source

PRELIVE: A Framework for Predicting Lipid Nanoparticles In Vivo Efficacy and Reducing Reliance on Animal Testing

open access: yesAdvanced Functional Materials, EarlyView.
PREdicting LNP In Vivo Efficacy (PRELIVE) framework enables the prediction of lipid nanoparticle (LNPs) organ‐specific delivery through dual modeling approaches. Composition‐based models using formulation parameters and protein corona‐based models using biological fingerprints both achieve high predictive accuracy across multiple organs.
Belal I. Hanafy   +3 more
wiley   +1 more source

Cysteine S-acetylation is a widespread post-translational modification on metabolic proteins

open access: yesnpj Metabolic Health and Disease
Protein acetylation is a fundamental regulatory mechanism occurring primarily on lysine amino acids. Here we report systematic in vivo characterization of cysteine S-acetylation as a widespread post-translational modification in mammalian tissues.
E. Keith Keenan   +4 more
doaj   +1 more source

Acetyl-CoA synthetase regulates histone acetylation and hippocampal memory [PDF]

open access: yesNature, 2017
Metabolic production of acetyl coenzyme A (acetyl-CoA) is linked to histone acetylation and gene regulation, but the precise mechanisms of this process are largely unknown. Here we show that the metabolic enzyme acetyl-CoA synthetase 2 (ACSS2) directly regulates histone acetylation in neurons and spatial memory in mammals.
Mews, Philipp   +5 more
openaire   +2 more sources

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