Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

6.7K
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...
6.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Elevated Asporin expression in human atherosclerotic plaques promotes their stability and reduces the risk for cardiovascular events.

Cardiovascular research·2026
Same author

Isoform-specific oxidative modifications of tropoelastin by HOCl and MPO alter protein self-assembly.

Redox report : communications in free radical research·2025
Same author

Peroxidase-Catalyzed and Photo-Oxidation of Tryptophan Results in Distinct Isomeric Tryptophan Dimers.

ACS omega·2025
Same author

Parthenolide disrupts mitosis by inhibiting ZNF207/BUGZ-promoted kinetochore-microtubule attachment.

The EMBO journal·2025
Same author

N-Terminal Proteomics Reveals Distinct Protein Degradation Patterns in Different Types of Human Atherosclerotic Plaques.

Journal of proteome research·2024
Same author

Macromolecular crowding and bicarbonate enhance the hydrogen peroxide-induced inactivation of glyceraldehyde-3-phosphate dehydrogenase.

The Biochemical journal·2024

Related Experiment Video

Updated: Jan 4, 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

2.1K

Detection, identification, and quantification of oxidative protein modifications.

Clare L Hawkins1, Michael J Davies2

  • 1Department of Biomedical Sciences, Panum Institute, University of Copenhagen, Copenhagen 2200, Denmark.

The Journal of Biological Chemistry
|November 2, 2019
PubMed
Summary

Protein oxidation, a common cellular event, damages proteins and is linked to aging and disease. New methods are emerging to detect these oxidative modifications, aiding research into their role in health and injury.

Keywords:
carbonyldisulfidehydroperoxideoxidative stressoxygen radicalspost-translational modificationprotein chemical modificationprotein cross-linkingreactive oxygen species

More Related Videos

Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
10:12

Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications

Published on: April 21, 2023

3.4K
Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes
07:38

Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes

Published on: September 1, 2020

5.6K

Related Experiment Videos

Last Updated: Jan 4, 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

2.1K
Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
10:12

Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications

Published on: April 21, 2023

3.4K
Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes
07:38

Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes

Published on: September 1, 2020

5.6K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Oxidative stress arises from endogenous and exogenous sources, generating reactive species.
  • Proteins are primary targets of oxidative damage, leading to altered structure, function, and turnover.
  • Accumulation of damaged proteins is implicated in aging and various diseases.

Purpose of the Study:

  • To review advances in understanding protein oxidation chemistry.
  • To highlight methods for detecting and quantifying oxidative modifications in biological systems.
  • To assess the current state and future needs in protein oxidation research.

Main Methods:

  • Review of scientific literature on protein oxidation.
  • Summary of analytical techniques for detecting post-translational modifications.
  • Discussion of methods for identifying and quantifying oxidized amino acids, peptides, and proteins.

Main Results:

  • Oxidative damage to proteins is diverse, with characteristic modifications depending on the oxidant.
  • Kinetics of damage formation vary significantly.
  • Various methods exist to detect oxidative modifications at different biological levels (amino acid, peptide, protein).

Conclusions:

  • Reliable methods are crucial for studying protein oxidation in complex biological systems.
  • Despite progress, further development is needed to fully understand the role of protein oxidation in disease.
  • Distinguishing cause from consequence in protein oxidation requires advanced analytical capabilities.