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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Glutathione, a tripeptide made up of glutamate, cysteine, and glycine, is a critical player in the detoxification of drugs and xenobiotics via a process known as glutathione conjugation or mercapturic acid formation. This phase II biotransformation reaction involves the covalent binding of glutathione to a drug or its metabolite, enhancing the compound's water solubility and enabling its excretion.
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

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Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme...
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Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Related Experiment Video

Updated: Apr 26, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Protein S-glutathionylation: from current basics to targeted modifications.

Doina Popov1

  • 1Institute of Cellular Biology and Pathology "N. Simionescu" of the Romanian Academy , 8, B.P. Hasdeu Street, Bucharest 050568 , Romania.

Archives of Physiology and Biochemistry
|August 13, 2014
PubMed
Summary

Protein S-glutathionylation, a reversible modification, protects cells from oxidative stress. This redox switch regulates cell survival and death, offering potential therapeutic strategies for cardiovascular diseases.

Keywords:
Cysteineglutaredoxinglutathioneprotein tyrosine phosphatases (PTPs)thioredoxin

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Protein S-glutathionylation is a redox-dependent post-translational modification involving antioxidant glutathione and protein thiols.
  • This modification is crucial for cellular homeostasis and plays a role in oxidative stress-related cardiovascular pathology due to redox imbalance.

Purpose of the Study:

  • To review recent advancements in protein S-glutathionylation.
  • Focus areas include its chemistry, cellular functions, quantification methods, and therapeutic potential.

Main Methods:

  • Literature review of Medline and PubMed databases.
  • Search terms included 'glutathionylation' for articles published between 2009 and 2014.

Main Results:

  • Protein S-glutathionylation protects protein thiols from irreversible oxidation.
  • It acts as a biological redox switch, influencing cell survival pathways (kinases, phosphatases) and cell death (apoptosis).
  • This modification interacts with phosphorylation and S-nitrosylation.

Conclusions:

  • Protein S-glutathionylation is a key regulator of cellular redox state.
  • It serves as a valuable biomarker for oxidative stress.
  • It holds significant potential for developing novel therapeutic strategies.