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

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.1K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.1K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.0K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.0K
Amyloid Fibrils03:03

Amyloid Fibrils

9.6K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.6K

You might also read

Related Articles

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

Sort by
Same author

A Glimpse into the Initial Microsecond of Biomolecular Condensation.

Journal of the American Chemical Society·2026
Same author

Electrostatic bimodality of human cytosolic DNA sensor cGAS-dsDNA condensates revealed by millisecond flashing electrophoretic separation.

Nature communications·2026
Same author

Cellular water-potential sensing through biomolecular condensation.

Nature·2026
Same author

Pathogenic Characterization of a Novel G47R Transthyretin Mutation in Early-Onset Amyloid Cardiomyopathy.

Journal of the American Heart Association·2026
Same author

Distinct RNA Physical Microenvironments Shape Unique Properties and Functions within Biomolecular Condensates.

Journal of the American Chemical Society·2026
Same author

Bridging hydrogen-bond-stabilized polymeric coacervate core micelles for high-efficiency drug encapsulation and delivery.

Nature communications·2026

Related Experiment Video

Updated: Jul 12, 2025

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.4K

Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments.

Yulong Bai1,2, Shengnan Zhang3, Hui Dong3,4

  • 1Department of Chemistry, Research Center for Industries of the Future, Westlake University, 600 Dunyu Road, Hangzhou 310030, Zhejiang Province, China.

Chemical Reviews
|October 24, 2023
PubMed
Summary

Visualizing protein misfolding in living cells is crucial for understanding neurodegenerative diseases. This review covers advanced imaging techniques that offer deeper insights than in vitro studies.

More Related Videos

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

9.8K
Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

12.1K

Related Experiment Videos

Last Updated: Jul 12, 2025

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.4K
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

9.8K
Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

12.1K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Protein misfolding and aggregation are central to neurodegenerative diseases, leading to cellular dysfunction.
  • In vitro studies provide insights but often fail to replicate the complex cellular environment.
  • In-cell imaging offers greater physiological and pathological relevance for studying protein behavior.

Purpose of the Study:

  • To review methodologies for visualizing protein misfolding within living cells.
  • To highlight advancements in in-cell imaging techniques for studying disease mechanisms.
  • To underscore the importance of in-cell studies for therapeutic development.

Main Methods:

  • Optical imaging techniques
  • Mass spectrometry-based strategies
  • In-cell nuclear magnetic resonance (NMR)
  • Cryo-electron microscopy (cryo-EM)

Main Results:

  • Recent advancements have significantly enhanced the ability to study protein misfolding in cellular contexts.
  • These techniques provide detailed information on misfolding processes and aberrant protein species.
  • In-cell methods reveal complexities not observed in simplified in vitro models.

Conclusions:

  • In-cell visualization techniques are vital for advancing our understanding of neurodegenerative disease mechanisms.
  • Progress in these imaging modalities promises new therapeutic strategies.
  • Bridging the gap between in vitro and in-cell studies is key for future research.