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Related Concept Videos

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.
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Protein Glycosylation01:25

Protein Glycosylation

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...
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.
Oxidations of Aldehydes and Ketones to Carboxylic Acids01:15

Oxidations of Aldehydes and Ketones to Carboxylic Acids

Oxidation of aldehydes and ketones results in the formation of carboxylic acids. Aldehydes, bearing hydrogen next to the carbonyl group, are easily oxidized compared to ketones. This is because an aldehydic proton can easily be abstracted during oxidation.
Aldehydes readily undergo oxidation in strong oxidizing agents such as potassium permanganate and chromic acid. The oxidation can also be carried out using mild oxidizing agents such as silver oxide. In fact, aldehydes can be easily oxidized...
Phosphorylation01:02

Phosphorylation

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.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

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Updated: May 13, 2026

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations
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Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations

Published on: April 26, 2024

Pathophysiological relevance of aldehydic protein modifications.

Neven Zarkovic1, Ana Cipak, Morana Jaganjac

  • 1Laboratory for Oxidative Stress, Rudjer Boskovic Institute, Zagreb, Croatia.

Journal of Proteomics
|February 27, 2013
PubMed
Summary

Oxidative stress generates reactive aldehydes that modify proteins, forming adducts. These aldehydic-protein adducts, like those from 4-hydroxy-2-nonenal, serve as biomarkers for diseases linked to lipid peroxidation.

Keywords:
4-Hydroxy-2-nonenal (HNE)Acrolein (ACR)ImmunochemistryMalondialdehyde (MDA)Non-enzymatic protein modificationsOxidative stress

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Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method
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Published on: October 23, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pathophysiology

Background:

  • Oxidative stress involves excess reactive oxygen species production.
  • Reactive aldehydes, byproducts of lipid peroxidation, modify proteins.
  • These modifications alter protein structure and function, acting as free radical messengers.

Purpose of the Study:

  • To explore the role of aldehydic-protein adducts in pathophysiological processes.
  • To highlight the significance of specific adducts (4-hydroxy-2-nonenal, malondialdehyde, acrolein) as biomarkers.
  • To discuss the impact of immunochemical methods and knowledge of aldehyde bioactivity on disease understanding.

Main Methods:

  • Review of existing literature on oxidative stress and protein modification.
  • Focus on immunochemical techniques for detecting aldehydic-protein adducts.
  • Analysis of the bioactivity of reactive aldehydes and their adducts.

Main Results:

  • Aldehydic-protein adducts are formed via covalent modification of proteins by reactive aldehydes.
  • Specific adducts involving 4-hydroxy-2-nonenal, malondialdehyde, and acrolein are identified.
  • These adducts can serve as valuable biomarkers for various pathophysiological conditions.

Conclusions:

  • Aldehydic-protein adducts are significant indicators of oxidative stress and lipid peroxidation.
  • Advancements in immunochemical methods enhance the study of these non-enzymatic modifications.
  • Understanding aldehyde bioactivity can improve disease prevention, diagnosis, and treatment.