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Related Concept Videos

Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
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Various carboxylic acid derivatives (such as acid chlorides, esters, and anhydrides) can be used for the acylation of amines to yield amides. The reaction requires two equivalents of amines. The first amine molecule functions as a nucleophile and attacks the carbonyl carbon to produce a tetrahedral intermediate. This is followed by the loss of the leaving group and restoration of the C=O bond.
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Acidity of 1-Alkynes02:42

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The acidic strength of hydrocarbons follows the order: Alkynes > Alkenes > Alkanes. The strength of an acid is commonly expressed in units of pKa — the lower the pKa, the stronger the acid. Among the hydrocarbons, terminal alkynes have lower pKa values and are, therefore, more acidic. For example, the pKa values for ethane, ethene, and acetylene are 51, 44, and 25, respectively, as shown here.
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  3. S-acylation Of Tdp-43: Palming Down Aggregation?
  1. Home
  3. S-acylation Of Tdp-43: Palming Down Aggregation?

Related Experiment Video

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
08:31

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

Published on: April 10, 2020

S-acylation of TDP-43: PALMing down aggregation?

Ruonan Yang1, Yanshan Fang1

  • 1Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China; University of Chinese Academy of Sciences, Beijing 100049, China.

Cell Chemical Biology
|June 18, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

S-acylation, a protein modification, prevents the aggregation of TDP-43. This finding suggests reduced S-acylation may contribute to Amyotrophic Lateral Sclerosis (ALS) pathogenesis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • S-acylation is a known posttranslational modification regulating protein stability and trafficking.
  • The RNA-binding protein TDP-43 is implicated in neurodegenerative diseases.

Purpose of the Study:

  • To investigate the function of S-acylation on TDP-43.
  • To explore the role of S-acylation in the context of ALS pathogenesis.

Main Methods:

  • The study utilized biochemical assays to examine the interaction between S-acylation and TDP-43.
  • Researchers investigated the impact of S-acylation on TDP-43 condensation driven by poly(ADP-ribose).

Main Results:

  • S-acylation of TDP-43 was found to suppress its aggregation.
  • This lipid modification antagonizes poly(ADP-ribose)-induced condensation of TDP-43.
  • Reduced S-acylation levels were correlated with ALS pathogenesis.

    • Conclusions:

    • S-acylation has a distinct function in preventing TDP-43 aggregation.
    • Dysregulation of S-acylation may play a role in the development of ALS.