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Related Concept Videos

Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
Cystic Fibrosis: Pathogenesis01:23

Cystic Fibrosis: Pathogenesis

Cystic fibrosis (CF), an autosomal recessive disorder, significantly affects the function of exocrine glands. This genetically inherited disease is characterized by the production of thick and sticky mucus, which can severely affect various organs and systems in the body.
CF is primarily caused by a genetic mutation in a chromosome 7 gene coding for the cystic fibrosis transmembrane conductance regulator (CFTR) protein. The most common gene mutation leading to CF is the ΔF508 mutation, but...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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.
Amino Acid Catabolism01:18

Amino Acid Catabolism

Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...

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Related Experiment Video

Updated: Jun 13, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Cysteine's metabolic fork: Sulfur partitioning shapes T cell function.

Melanie Grusdat1, Dirk Brenner2

  • 1Experimental and Molecular Immunology, Department of Infection and Immunity (DII), Luxembourg Institute of Health, Esch-sur-Alzette, Luxembourg.

Cell
|June 11, 2026
PubMed
Summary
This summary is machine-generated.

Cysteine metabolism is crucial for T cell survival and function. This study reveals how cysteine

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Multicolor Flow Cytometry-based Quantification of Mitochondria and Lysosomes in T Cells
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Multicolor Flow Cytometry-based Quantification of Mitochondria and Lysosomes in T Cells

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Last Updated: Jun 13, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

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

Multicolor Flow Cytometry-based Quantification of Mitochondria and Lysosomes in T Cells
06:22

Multicolor Flow Cytometry-based Quantification of Mitochondria and Lysosomes in T Cells

Published on: January 9, 2019

Area of Science:

  • Immunology
  • Cell Metabolism
  • Molecular Biology

Background:

  • T cell metabolism is critical for their function and survival.
  • Nutrient availability significantly impacts immune responses.

Purpose of the Study:

  • To investigate the role of cysteine metabolism in CD8+ T cell function.
  • To understand how cysteine's sulfur is utilized within T cells.

Main Methods:

  • Analysis of metabolic pathways in CD8+ T cells.
  • Tracking of sulfur incorporation into key biomolecules.

Main Results:

  • Cysteine's sulfur is routed to both glutathione and iron-sulfur cluster synthesis.
  • This metabolic routing is essential for CD8+ T cell proliferation.
  • Proper sulfur partitioning enhances effector functions and anti-tumor immunity.

Conclusions:

  • Cysteine metabolism plays a pivotal role in adaptive immunity.
  • Targeting cysteine metabolism could be a strategy to enhance T cell-based therapies.