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Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

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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.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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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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Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

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Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
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Sulfur Assimilation01:20

Sulfur Assimilation

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Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
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Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

Phase II Reactions: Sulfation and Conjugation with α-Amino Acids

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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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Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation01:22

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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.
Several distinctive characteristics distinguish glutathione conjugation from other phase II...
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Related Experiment Video

Updated: Aug 6, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Protein Persulfidation: Recent Progress and Future Directions.

Shanshan Luo1, Chuiyu Kong1, Danyu Ye1

  • 1Key Laboratory of Cardiovascular and Cerebrovascular Medicine, Nanjing Medical University, Nanjing, China.

Antioxidants & Redox Signaling
|March 21, 2023
PubMed
Summary
This summary is machine-generated.

Hydrogen sulfide (H2S) regulates biological activities through S-sulfhydration, modifying proteins. Understanding protein persulfidation is key to H2S functions and therapeutic development.

Keywords:
H2Slabeling methodsmolecular mechanismspersulfidationprotein S-sulfhydration

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • Hydrogen sulfide (H2S) is a gasotransmitter regulating physiological and pathological processes.
  • S-sulfhydration (persulfidation) is a key mechanism for H2S biological functions, involving cysteine residue modification.
  • Protein persulfides are crucial for understanding H2S roles.

Purpose of the Study:

  • To review the mechanism and detection methods of protein persulfidation.
  • To summarize recent findings on persulfidation selectivity and its impact on protein function and signaling.
  • To highlight areas for future research in H2S biology and therapeutics.

Main Methods:

  • Review of existing literature on H2S, S-sulfhydration, and persulfidation.
  • Discussion of various methods developed for detecting protein persulfides.
  • Synthesis of recent discoveries regarding persulfidation's role in biological processes.

Main Results:

  • Protein persulfidation regulates ion channels, enzymes, transcription factors, and protein-protein interactions.
  • Persulfidation is implicated in diverse biological processes.
  • Several technical and theoretical questions regarding persulfidation remain unresolved.

Conclusions:

  • Optimizing persulfidation detection methods is crucial.
  • Further elucidation of persulfidation's properties and molecular functions will advance therapeutics.
  • Understanding persulfidation is vital for H2S-related research.