Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Proteomics01:33

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 proteomics...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Aspirin and fibrin clot modulation in vascular pharmacology: Fibrinogen acetylation, disease context, and translational uncertainty.

Vascular pharmacology·2026
Same author

Oleuropein and hydroxytyrosol enhance mitochondrial function and biogenesis in SH-SY5Y cells through estrogen-like mechanisms.

Food & function·2026
Same author

Chemobrain as a Neuroimmune Syndrome: Mechanisms, Modifiers, and Emerging Multi-Target Therapeutic Strategies.

Molecules (Basel, Switzerland)·2026
Same author

PBMC DEG/miRNA biomarkers of TDP-43 pathology in ALS.

Neurobiology of disease·2026
Same author

Unraveling in vitro phase separation and aggregation properties of the structured region of FMRP and the impact of Fragile X syndrome-linked mutations.

The FEBS journal·2026
Same author

Energy-efficient selection of high-yield PHA producers via microaerophilic uncoupled feeding.

Bioresource technology·2026

Related Experiment Video

Updated: Jun 28, 2026

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

Aggregation propensity of the human proteome.

Elodie Monsellier1, Matteo Ramazzotti, Niccolò Taddei

  • 1Dipartimento di Scienze Biochimiche, Università degli studi di Firenze, Florence, Italy.

Plos Computational Biology
|October 18, 2008
PubMed
Summary

Protein aggregation, common in diseases, is a general property of proteins. This study analyzed the human proteome, finding sequence features that modulate aggregation propensity, revealing links between protein structure, biology, and disease.

More Related Videos

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

Related Experiment Videos

Last Updated: Jun 28, 2026

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
07:28

JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics

Published on: October 19, 2021

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

Area of Science:

  • Biochemistry
  • Proteomics
  • Computational Biology

Background:

  • Amyloid-like fibril formation is implicated in human protein deposition diseases.
  • Protein aggregation is an intrinsic property of polypeptide chains, analyzable at large scales.

Purpose of the Study:

  • To analyze the aggregation propensity of the entire human proteome using a predictive algorithm.
  • To investigate the relationship between protein sequence, structure, cellular localization, and aggregation propensity.

Main Methods:

  • Utilized a previously developed predictive algorithm to analyze 34,180 human protein sequences.
  • Compared aggregation propensities across different protein types (membrane, disordered, folded) and subcellular localizations.
  • Identified gatekeeper residues that confer protection against aggregation.

Main Results:

  • Longer proteins generally exhibit less intense aggregation peaks than shorter ones.
  • Proteins involved in deposition diseases show aggregation propensities not significantly different from the general proteome.
  • Aggregation propensities vary with subcellular localization, protein structure, and cellular environment.
  • Specific gatekeeper residues act as protective elements against aggregation.

Conclusions:

  • Protein aggregation propensity is intrinsically linked to protein biology and is modulated by negative selection pressure.
  • Computational tools can reliably predict aggregation propensities, with results consistent across different algorithms.
  • Understanding protein aggregation mechanisms is crucial for comprehending protein deposition diseases and protein function.