2 results match your criteria: "University of Massachusetts Chan Medial School[Affiliation]"
A phase transition reduces the threshold for nicotinamide mononucleotide-based activation of SARM1, an NAD(P) hydrolase, to physiologically relevant levels.
J Biol Chem
November 2023
Program in Chemical Biology, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA; Department of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medial School, Worcester, Massachusetts, USA. Electronic address:
Article Synopsis
- * SARM1 is normally inactive in healthy neurons but gets activated upon damage through two proposed mechanisms: increased NMN levels and a phase transition that stabilizes SARM1's active form.
- * This research demonstrates that the phase transition can significantly lower the NMN concentration needed to activate SARM1, merging both activation ideas and highlighting potential therapeutic targets.
SARM1, an Enzyme Involved in Axon Degeneration, Catalyzes Multiple Activities through a Ternary Complex Mechanism.
Biochemistry
July 2023
Program in Chemical Biology, University of Massachusetts Chan Medical School, Worcester, Massachusetts 01605, United States.
Sterile alpha and toll/interleukin receptor (TIR) motif containing protein 1 (SARM1) is an NAD hydrolase and cyclase involved in axonal degeneration. In addition to NAD hydrolysis and cyclization, SARM1 catalyzes a base exchange reaction between nicotinic acid (NA) and NADP to generate NAADP, which is a potent calcium signaling molecule. Herein, we describe efforts to characterize the hydrolysis, cyclization, and base exchange activities of TIR-1, the ortholog of SARM1; TIR-1 also catalyzes NAD(P) hydrolysis and/or cyclization and regulates axonal degeneration in worms.
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