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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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 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.
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2° Amines to N-Nitrosamines: Reaction with NaNO201:20

2° Amines to N-Nitrosamines: Reaction with NaNO2

Secondary amines react with nitrous acid to form N-nitrosamines, as depicted in Figure 1. Nitrous acid, a weak and unstable acid, is formed in situ from an aqueous solution of sodium nitrite and strong acids, such as hydrochloric acid or sulfuric acid, in cold conditions. In the presence of an acid, the nitrous acid gets protonated. The subsequent loss of water results in the formation of the electrophile known as nitrosonium ion.
Nitric Oxide Signaling Pathway01:28

Nitric Oxide Signaling Pathway

Nitric oxide (NO), an inorganic gas, acts as a potent second messenger in most animal and plant tissues. NO diffuses out of the cells that produce it and enters the neighboring cells to generate a downstream response. NO synthase (NOS) catalyzes NO production by the deamination of the amino acid arginine. There are three isoforms of NOS. Endothelial cells have endothelial NOS (eNOS), nerve and muscle cells have neuronal NOS (nNOS), and macrophages produce inducible NOS (iNOS) upon exposure to...
Biosynthesis of Nucleic Acids01:28

Biosynthesis of Nucleic Acids

Nucleic acid biosynthesis is a fundamental biochemical process that produces the purine and pyrimidine nucleotides essential for DNA and RNA synthesis. This pathway maintains a balanced nucleotide pool, preventing imbalances that could jeopardize genetic integrity and cellular function. Given the crucial role of nucleotides, their synthesis is tightly regulated to ensure proper cellular homeostasis.Purine BiosynthesisThe biosynthesis of purine nucleotides begins with ribose-5-phosphate, a...

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Nitropeptide Profiling and Identification Illustrated by Angiotensin II
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Published on: June 16, 2019

Protein S-nitrosylation: purview and parameters.

Douglas T Hess1, Akio Matsumoto, Sung-Oog Kim

  • 1Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA.

Nature Reviews. Molecular Cell Biology
|February 3, 2005
PubMed
Summary

S-nitrosylation, a key protein modification, dynamically regulates cellular functions by attaching nitrogen monoxide to cysteine. This process is crucial for nitric oxide signaling and redox-based physiological control.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • S-nitrosylation is a post-translational modification involving the covalent attachment of a nitrogen monoxide (NO) group to cysteine residues.
  • This modification plays a significant role in regulating protein function and cellular processes.

Purpose of the Study:

  • To elucidate the fundamental mechanisms and broad implications of S-nitrosylation in cellular regulation.
  • To highlight the role of S-nitrosylation in mediating the effects of nitric oxide (NO).

Main Methods:

  • Review and synthesis of existing literature on S-nitrosylation.
  • Analysis of the biochemical pathways involved in S-nitrosylation.
  • Examination of the functional consequences of S-nitrosylation in various biological contexts.

Main Results:

  • S-nitrosylation is a widespread regulatory mechanism affecting most protein classes.
  • It is a primary means by which nitric oxide (NO) exerts its influence on cellular signaling.
  • S-nitrosylation provides a critical link between redox status and physiological regulation.

Conclusions:

  • S-nitrosylation is an essential post-translational modification for dynamic protein regulation.
  • It underpins the diverse physiological roles of nitric oxide (NO) in cellular systems.
  • Understanding S-nitrosylation is key to comprehending redox-based cellular control mechanisms.