Destabilization of Green Fluorescent Protein by Substitution of Its Amino-Terminal Residue

Lesmana, Jessica; Friedl, Peter

doi:10.1007/978-94-010-0369-8_2

Search citation statements

Order By: Relevance

Paper Sections

Select...

Introduction1

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2016

2020

Publication Types

Select...

Article1

Book1

Relationship

Self Cite0

Independent2

Authors

Journals

Cited by 2 publications

(1 citation statement)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, FP-based FRET sensors are stable in cells for long time due to high intracellular stability of FPs. For example, EGFP has a half-life time of greater than 24 h in cells [ 6 ]. Lastly, stable cell lines expressing FRET biosensors are easily achievable in the presence of antibiotic pressure, which reduces cell-cell viability in FRET imaging and facilitates high-throughput drug screening [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

A Guide to Fluorescent Protein FRET Pairs

Bajar

Wang

Zhang

et al. 2016

Sensors

389

364

View full text Add to dashboard Cite

Förster or fluorescence resonance energy transfer (FRET) technology and genetically encoded FRET biosensors provide a powerful tool for visualizing signaling molecules in live cells with high spatiotemporal resolution. Fluorescent proteins (FPs) are most commonly used as both donor and acceptor fluorophores in FRET biosensors, especially since FPs are genetically encodable and live-cell compatible. In this review, we will provide an overview of methods to measure FRET changes in biological contexts, discuss the palette of FP FRET pairs developed and their relative strengths and weaknesses, and note important factors to consider when using FPs for FRET studies.

show abstract

Section: Introductionmentioning

confidence: 99%