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Related Concept Videos

Redox Reactions01:24

Redox Reactions

Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...
Redox Reactions01:27

Redox Reactions

Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
Protein Modifications in the RER01:26

Protein Modifications in the RER

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 sequences.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
These groups modify specific amino acids in a protein.
Redox Titration: Other Oxidizing and Reducing Agents01:26

Redox Titration: Other Oxidizing and Reducing Agents

Besides iodine, other oxidizing or reducing agents can serve as titrants in redox titrations. Common oxidizing titrants include KMnO4, cerium(IV), and K2Cr2O7. The choice of oxidizing titrants depends on factors like stability, cost, analyte strength, and reaction rate between the analyte and titrant. KMnO4 is a strong oxidizing titrant that reduces from Mn(VII) to Mn(II) in a highly acidic solution, simultaneously oxidizing the analyte to a higher oxidation state. In this case, KMnO4 acts as a...

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Related Experiment Video

Updated: Jun 28, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Thiol-based redox switches in eukaryotic proteins.

Nicolas Brandes1, Sebastian Schmitt, Ursula Jakob

  • 1Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.

Antioxidants & Redox Signaling
|November 13, 2008
PubMed
Summary
This summary is machine-generated.

Oxidative thiol modifications in proteins are now recognized as crucial redox switches regulating cellular functions. This review highlights key examples in gene transcription, metabolism, and signal transduction.

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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
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Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
12:07

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

Related Experiment Videos

Last Updated: Jun 28, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
12:07

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Oxidative thiol modifications in cytosolic proteins were historically dismissed as artifacts.
  • Recent advancements in in vivo thiol trapping and mass spectrometry reveal their biological significance.

Purpose of the Study:

  • To review the role of thiol-based redox switches in regulating protein function.
  • To examine three eukaryotic proteins (Yap1p, glyceraldehyde-3-phosphate dehydrogenase, PTP1B) demonstrating thiol-based regulation.

Main Methods:

  • In vivo thiol trapping technology
  • Mass spectrometric analysis
  • Review of literature on specific proteins

Main Results:

  • Thiol modifications act as molecular switches, regulated by reactive oxygen and nitrogen species.
  • These modifications impact diverse pathways including gene transcription, metabolism, signal transduction, and apoptosis.
  • Yap1p's function is modulated without altering its activity.
  • Glyceraldehyde-3-phosphate dehydrogenase's active site cysteine modification redirects metabolism and induces apoptosis.
  • PTP1B exemplifies the reversible nature of redox-regulation.

Conclusions:

  • Thiol-based redox switches are vital regulatory mechanisms in eukaryotic cells.
  • Reversibility is a key characteristic of redox-sensitive proteins.
  • Understanding these switches is crucial for comprehending cellular responses to oxidative stress.