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Related Concept Videos

Proteomics01:33

Proteomics

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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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Subcellular Fractionation01:32

Subcellular Fractionation

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The homogenate obtained after cell lysis contains various membrane-bound organelles that can be further separated into pure fractions by subcellular fractionation. These isolates are used to study specific cellular components, analyze localized protein activity, and are even employed in diagnostics. Fractionation is typically achieved using centrifugation methods, the most common being density-gradient and differential centrifugation.
Differential Centrifugation
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The Proteasome02:18

The Proteasome

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The Proteasome Structure01:17

The Proteasome Structure

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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
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JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
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The 15-min (Sub)Cellular Proteome.

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    This study introduces a rapid method for analyzing single-cell proteomes using capillary electrophoresis-mass spectrometry (CE-MS) with data-independent acquisition (DIA). This technique achieves high molecular coverage, significantly advancing cell biology research.

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    Area of Science:

    • Cell biology
    • Proteomics
    • Analytical chemistry

    Background:

    • Single-cell mass spectrometry (MS) provides insights into cellular functions.
    • Characterizing subcellular proteomes at the single-cell level is challenging due to sample limitations.

    Approach:

    • Integrated subcellular capillary microsampling, fast capillary electrophoresis (CE), and orbitrap tandem MS.
    • Employed data-independent acquisition (DIA) for enhanced proteome detection.
    • Demonstrated rapid analysis within a 15-min separation window.

    Key Points:

    • CE-MS with DIA identified 1,161 proteins from single HeLa-cell-equivalent digests, surpassing data-dependent acquisition (DDA) (401 proteins).
    • Successfully profiled 1,242 proteins from subcellular niches in identified *Xenopus laevis* embryonic cells.
    • The method achieved high molecular coverage and speed for subcellular proteome analysis.

    Conclusions:

    • CE-MS with DIA offers a fast, sensitive, and deep profiling solution for (sub)cellular proteomes.
    • This approach expands the analytical capabilities for cell biology research.
    • Enables detailed investigation of organelle components within single cells.