An integrative approach to studying sphingolipid metabolism reveals p53 as a master regulator of the pathway. [PDF]
Ghandour B +10 more
europepmc +1 more source
A review of recent advances in exosome-mediated drug delivery for regenerative therapy and immunomodulation. [PDF]
Azhar MA +5 more
europepmc +1 more source
Glycolytic Enzyme HK2 Phosphorylates nSMase1 to Promote Astrocytic Exosomes Biogenesis Contributing to Acute Ischemic Stroke Injury. [PDF]
Chen C +12 more
europepmc +1 more source
"Zombie virus" like pyroptosis: Extracellular vesicles spread pyroptosis by transferring functional N-GSDMD pore. [PDF]
Zhang Y, Jin S, Tian Y, Qi J.
europepmc +1 more source
HSP70 is a chaperone for IL-33 activity in chronic airway disease. [PDF]
Osorio OA +11 more
europepmc +1 more source
Neutral sphingomyelinases and nSMase2: Bridging the gaps
There is strong evidence indicating a role for ceramide as a second messenger in processes such as apoptosis, cell growth and differentiation, and cellular responses to stress. Ceramide formation from the hydrolysis of sphingomyelin is considered to be a major pathway of stress-induced ceramide production with magnesium-dependent neutral ...
Christopher Clarke, Yusuf Hannun
exaly +3 more sources
Suppression of tau propagation using an inhibitor that targets the DK-switch of nSMase2 [PDF]
Targeting of molecular pathways involved in the cell-to-cell propagation of pathological tau species is a novel approach for development of disease-modifying therapies that could block tau pathology and attenuate cognitive decline in patients with Alzheimer's disease and other tauopathies. We discovered cambinol through a screening effort and show that
Varghese John +2 more
exaly +5 more sources
Neutral Sphingomyelinase 2 (nSMase2) Is a Phosphoprotein Regulated by Calcineurin (PP2B) [PDF]
We previously reported that exposure of human airway epithelial cells to oxidative stress increased ceramide generation via specific activation of neutral sphingomyelinase2 (nSMase2). Here we show that nSMase2 is a phosphoprotein exclusively phosphorylated at serine residues.
Anne Knowlton +2 more
exaly +3 more sources

