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Related Concept Videos

The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

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Related Experiment Video

Updated: Jun 21, 2026

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

Selenoproteins.

Jun Lu1, Arne Holmgren

  • 1Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE-17177 Stockholm, Sweden.

The Journal of Biological Chemistry
|September 2, 2008
PubMed
Summary
This summary is machine-generated.

Selenium is vital for health, forming the 21st amino acid, selenocysteine (Sec). Selenoproteins, containing Sec, are crucial for antioxidant defense and thyroid function, impacting diseases like cancer and infertility.

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Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
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Last Updated: Jun 21, 2026

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
03:09

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O

Published on: August 9, 2024

Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach
04:25

Enriching Subcellular Proteins in Leptospira Using a Triton X-114-Based Fractionation Approach

Published on: August 8, 2025

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Nutritional Science

Background:

  • Selenium is an essential micronutrient for humans and animals.
  • Its primary role is as the 21st amino acid, selenocysteine (Sec), incorporated into selenoproteins.
  • Selenocysteine incorporation utilizes a unique co-translational mechanism decoding the UGA codon.

Purpose of the Study:

  • To elucidate the significance of selenium and selenoproteins in biological systems.
  • To highlight the role of selenocysteine in protein function and its genetic encoding.
  • To explore the connection between selenoproteins and various human diseases.

Main Methods:

  • Identification of 25 selenoprotein genes in the human genome.
  • Analysis of the unique UGA codon decoding mechanism for selenocysteine incorporation.
  • Review of the catalytic and biological functions of key selenoproteins.

Main Results:

  • Selenoproteins are integral to redox reactions, antioxidant defense, and thyroid hormone metabolism.
  • Selenocysteine is an essential active-site residue for the catalytic activity of many selenoproteins.
  • 25 selenoprotein genes have been identified in the human genome.

Conclusions:

  • Selenoproteins play critical roles in oxidoreduction, redox signaling, and immune responses.
  • Dysfunction or deficiency in selenium/selenoproteins is linked to diseases including cancer, Keshan disease, and infertility.
  • Understanding selenoprotein function is key to addressing various health conditions.