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Related Concept Videos

Flow Cytometry01:23

Flow Cytometry

The development of flow cytometry techniques began in 1934 with initial attempts by Andrew Moldavan, a bacteriologist who counted the cells in a flowing capillary system. Moldavan pumped cells through a capillary tube focused under a microscope for visualization. The invention of photometry allowed the measurement of differentially-stained cells, and Louis Kamentsky developed the first multiparameter flow cytometer in 1965 to identify and count the cancer cells in cervical tissue specimens.
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Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry
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Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Published on: December 8, 2015

Measuring FRET in flow cytometry and microscopy.

Péter Nagy1, György Vereb, Sándor Damjanovich

  • 1University of Debrecen, Debrecen, Hungary.

Current Protocols in Cytometry
|September 5, 2008
PubMed
Summary
This summary is machine-generated.

This study details methods for measuring protein interactions using Förster Resonance Energy Transfer (FRET) via flow and image cytometry. These protocols enable precise quantification of protein associations in biological samples.

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Last Updated: Jul 2, 2026

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry
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Published on: December 8, 2015

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Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction
11:11

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Published on: August 15, 2013

Area of Science:

  • Biophysics
  • Cell Biology
  • Biochemistry

Background:

  • Protein-protein interactions are crucial for cellular functions.
  • Fluorescence techniques offer powerful tools for studying these interactions in situ.
  • Förster Resonance Energy Transfer (FRET) is a biophysical method to detect molecular proximity.

Purpose of the Study:

  • To present detailed protocols for measuring protein associations using FRET.
  • To adapt FRET measurements for both flow cytometry and image cytometry.
  • To provide guidance on data interpretation and address potential limitations.

Main Methods:

  • Utilizing fluorescently labeled proteins (via antibodies or fluorescent proteins).
  • Employing flow cytometry to measure FRET through donor quenching (population-based) or multi-channel intensity analysis (cell-by-cell).
  • Implementing image cytometry for FRET determination via donor photobleaching, including autofluorescence correction.

Main Results:

  • Established protocols for FRET-based protein association measurement using cytometry.
  • Demonstrated cell-by-cell FRET quantification with autofluorescence correction.
  • Provided an algorithm applicable to both flow and image cytometric FRET analysis.

Conclusions:

  • Flow and image cytometry provide robust platforms for FRET-based protein interaction studies.
  • Careful consideration of experimental parameters and data interpretation is essential for accurate FRET measurements.
  • These protocols offer valuable tools for researchers investigating molecular interactions in complex biological systems.