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

You might also read

Related Articles

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

Sort by
Same author

Cytometric proteome profiling of GFP-tagged yeast for characterizing novel antifungals.

Communications biology·2026
Same author

On the Significance of the Terminal Location of Prion-Forming Regions of Yeast Proteins.

International journal of molecular sciences·2025
Same author

Development of a Wine Yeast Strain Capable of Malolactic Fermentation and Reducing the Ethyl Carbamate Content in Wine.

Foods (Basel, Switzerland)·2025
Same author

Mapping of Prion Structures in the Yeast Rnq1.

International journal of molecular sciences·2024
Same author

CAR1 as a new selective marker for genetic engineering of wine yeasts.

Journal of microbiological methods·2023
Same author

Structural Bases of Prion Variation in Yeast.

International journal of molecular sciences·2022

Related Experiment Video

Updated: May 19, 2026

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
15:23

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 13, 2010

DNA aptamers detecting generic amyloid epitopes.

Olga V Mitkevich1, Natalia V Kochneva-Pervukhova, Elizaveta R Surina

  • 1A.N. Bach Institute of Biochemistry, The Russian Academy of Sciences, Moscow, Russia.

Prion
|August 10, 2012
PubMed
Summary
This summary is machine-generated.

DNA aptamers can detect amyloid aggregates in yeast cells, including those formed by Sup35 and mouse PrP proteins. These aptamers recognize common conformational epitopes on various amyloid structures, suggesting broad applicability for amyloid detection.

More Related Videos

SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval
10:48

SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval

Published on: April 23, 2010

Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis
13:31

Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis

Published on: February 12, 2015

Related Experiment Videos

Last Updated: May 19, 2026

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
15:23

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 13, 2010

SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval
10:48

SDS-PAGE/Immunoblot Detection of Aβ Multimers in Human Cortical Tissue Homogenates using Antigen-Epitope Retrieval

Published on: April 23, 2010

Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis
13:31

Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis

Published on: February 12, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Aggregation

Background:

  • Amyloids are protein aggregates formed by polymerization.
  • DNA aptamers have been developed to bind specific amyloid fibrils.
  • The conformational epitopes of intracellular amyloid aggregates are not well understood.

Purpose of the Study:

  • To investigate if DNA aptamers selected against in vitro amyloid fibrils can detect intracellular amyloid aggregates.
  • To determine if these aptamers can recognize amyloid aggregates of different proteins in yeast cells.

Main Methods:

  • Selection of DNA aptamers against in vitro assembled Sup35 amyloid fibrils.
  • Testing aptamer binding to SDS-insoluble amyloid aggregates of Sup35 and mouse PrP in yeast.
  • Analysis of common conformational epitopes between in vitro and in vivo amyloid aggregates.

Main Results:

  • DNA aptamers successfully detected SDS-insoluble amyloid aggregates of Sup35 protein in yeast.
  • The same aptamers also detected amyloid aggregates of mouse PrP in yeast cells.
  • Data suggest common conformational epitopes are shared between in vitro and in vivo amyloid aggregates.

Conclusions:

  • Selected DNA aptamers can detect intracellular amyloid aggregates in yeast.
  • These aptamers recognize common epitopes on diverse amyloid structures.
  • The findings indicate potential for using these aptamers for broad amyloid detection in various organisms.