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Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

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Related Experiment Video

Updated: Apr 7, 2026

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

Using proteomics to probe neurons.

Yunee Kim¹, Thomas Kislinger²

¹Department of Medical Biophysics, University of Toronto, Toronto, Canada.

|July 3, 2015

Summary

This summary is machine-generated.

Researchers used mass spectrometry to measure different forms of three related proteins in mouse neurons. This technique allows for precise quantification of protein variants within specific brain cells.

Keywords:

MRM SRM alternative splicing cell biology mouse neuroligin neuroscience recognition synapse

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Related Experiment Videos

Last Updated: Apr 7, 2026

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

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Published on: June 23, 2022

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Published on: May 23, 2019

Cell Subtype-specific Analysis of Neuronal Membrane Proteasome in Somatosensory Neurons

Cell Subtype-specific Analysis of Neuronal Membrane Proteasome in Somatosensory Neurons

Published on: October 10, 2025

Area of Science:

Neuroscience
Proteomics
Biochemistry

Background:

Understanding protein expression is crucial for neuronal function.
Closely related proteins can have distinct roles and regulatory mechanisms.
Mass spectrometry-based proteomics offers high sensitivity and specificity for protein quantification.

Purpose of the Study:

To quantify the abundances of different protein forms.
To investigate the expression patterns of three specific, closely related proteins.
To analyze these proteins within the context of mouse neurons.

Main Methods:

Utilized advances in mass spectrometry-based proteomics.
Employed quantitative proteomics techniques.
Focused analysis on neuronal tissue from mice.

Main Results:

Successfully quantified the abundances of distinct protein forms.
Determined the relative levels of three closely related proteins.
Provided quantitative data on protein expression in mouse neurons.

Conclusions:

Mass spectrometry is a powerful tool for analyzing protein isoforms in complex biological systems.
The study provides a quantitative foundation for understanding the roles of these specific proteins in neuronal function.
Further research can build upon these findings to explore the functional implications of differential protein expression.