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Kendall's Tau Test01:16

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All ortho–para directors, excluding halogens, are activating groups. These groups donate electrons to the ring, making the ring carbons electron-rich. Consequently, the reactivity of the aromatic ring towards electrophilic substitution increases. For instance, the nitration of anisole is about 10,000 times faster than the nitration of benzene. The electron-donating effect of the methoxy group in anisole activates the ortho and para positions on the ring and stabilizes the corresponding...
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Related Experiment Video

Updated: Jan 26, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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Sirtuin 3 Mediates Tau Deacetylation.

Shiping Li1,2, Junxiang Yin2, Megan Nielsen2,3

  • 1Department of Neurology, The Second Hospital of Hebei Medical University, Shijiazhuang, Hebei, China.

Journal of Alzheimer'S Disease : JAD
|April 9, 2019
PubMed
Summary
This summary is machine-generated.

Sirtuin 3 (Sirt3) reduces tau acetylation and accumulation in Alzheimer

Keywords:
AcetylationAlzheimer’s diseaseSirtuintau

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Tau acetylation is implicated in early Alzheimer's disease (AD) pathogenesis.
  • The role of the deacetylase Sirtuin 3 (Sirt3) in tau acetylation remains largely unknown.

Purpose of the Study:

  • To investigate the impact of Sirt3 on tau acetylation and aggregation.
  • To explore Sirt3 as a potential therapeutic target for AD.

Main Methods:

  • Examined Sirt3 and tangle tau protein levels in human postmortem brain slices (AD, MCI, controls) and AD model mice.
  • Assessed tau acetylation in HT22 cells following Sirt3 knockdown or overexpression.

Main Results:

  • Sirt3 levels were inversely correlated with tau protein in human brains and AD model mice.
  • Overexpression of Sirt3 significantly decreased tau acetylation.
  • Sirt3 knockdown led to increased tau acetylation in HT22 cells.

Conclusions:

  • Sirt3 plays a crucial role in regulating tau acetylation.
  • Sirt3 represents a promising therapeutic target for reducing tau accumulation in Alzheimer's disease.