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Related Concept Videos

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.
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

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Related Experiment Video

Updated: May 20, 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

RedoxDB--a curated database for experimentally verified protein oxidative modification.

Ming-an Sun1, Yejun Wang, Han Cheng

  • 1School of Life Sciences, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China.

Bioinformatics (Oxford, England)
|July 27, 2012
PubMed
Summary

Researchers have developed RedoxDB, a new database for experimentally validated redox proteins. This resource aids in understanding protein oxidative modification and its role in cellular processes.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Signaling
  • Proteomics

Background:

  • Redox regulation and signaling are crucial cellular processes.
  • Cysteine thiol groups are key targets for reversible oxidation in redox regulation.
  • Existing research has identified numerous redox proteins and modified cysteines, but a centralized database was lacking.

Purpose of the Study:

  • To create a manually curated database for experimentally validated redox proteins.
  • To provide a centralized resource for information on protein oxidative modification.
  • To support research in redox biology and computational analyses.

Main Methods:

  • Manual curation of literature for experimentally validated redox proteins.
  • Inclusion of data on protein identity, organism, sequence, and cysteine modification details.
  • Development of a database (RedoxDB version 1.0) with search, blast, and download functionalities.

Main Results:

  • RedoxDB version 1.0 contains 2157 redox proteins and 2203 modified cysteine residues.
  • Detailed information includes cysteine position, modification type, flanking sequence, gene name, organism, and literature references.
  • The database provides links to UniProt and PDB for integrated data access.

Conclusions:

  • RedoxDB serves as a valuable resource for the growing field of redox biology.
  • The database facilitates both experimental and computational studies on protein oxidative modification.
  • It addresses the need for a centralized repository of information on redox-sensitive proteins.