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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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Interactions Between Signaling Pathways01:19

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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
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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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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Redox Reactions

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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...
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Redox Reactions01:27

Redox Reactions

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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...
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Related Experiment Video

Updated: Dec 23, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Cross-talk between redox signalling and protein aggregation.

Loes van Dam1, Tobias B Dansen1

  • 1Center for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584CG Utrecht, The Netherlands.

Biochemical Society Transactions
|April 21, 2020
PubMed
Summary
This summary is machine-generated.

Reactive oxygen species (ROS) and protein aggregation are linked to aging and neurodegenerative diseases. This review explores how ROS signaling influences protein aggregation, and proposes elevated ROS production may be a protective response to curb aggregation.

Keywords:
amyloidprotein aggregationreactive oxygen speciesredox signalling

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Area of Science:

  • Biochemistry
  • Cellular Biology
  • Neuroscience

Background:

  • Aging and proteinopathies like Alzheimer's and Parkinson's disease are associated with increased reactive oxygen species (ROS) and protein aggregation.
  • The causal relationship between ROS and protein aggregation remains unclear.
  • ROS encompass superoxide (O2•−), hydrogen peroxide (H2O2), and hydroxyl radicals (OH•).

Purpose of the Study:

  • To review the current understanding of how redox signaling affects protein aggregation and vice versa.
  • To explore the hypothesis that elevated ROS production during aging is a stress response to mitigate protein aggregation and toxicity.

Main Methods:

  • Literature review of studies investigating the interplay between redox signaling and protein aggregation.
  • Analysis of the roles of ROS-induced damage and redox signaling in protein aggregation pathways.
  • Examination of the impact of aggregation stages on toxicity.

Main Results:

  • Redox signaling, downstream of H2O2, influences protein aggregation.
  • ROS-induced damage also affects protein aggregation.
  • Redox signaling impacts multiple stages of protein aggregation and amyloid formation, from initiation to oligomerization.
  • Larger amyloid aggregates are generally less toxic than smaller, prefibrillar oligomers.

Conclusions:

  • Redox signaling plays a significant role in protein aggregation processes.
  • Age-associated increases in ROS may represent a protective stress response aimed at controlling protein aggregation and reducing cellular toxicity.