Single amino acid replacement makes Aequorea victoria fluorescent proteins reversibly photoswitchable.

doi:10.1021/ja9014953

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Topics Community

Back to search

Article

Single amino acid replacement makes Aequorea victoria fluorescent proteins reversibly photoswitchable.

Journal of the American Chemical Society - 13 Jan 2010

Bizzarri Ranieri, Serresi Michela, Cardarelli Francesco, Abbruzzetti Stefania, Campanini Barbara, Viappiani Cristiano, Beltram Fabio

Abstract excerpt

Reversibly photoswitchable (i.e., photochromic) fluorescent proteins open the way to a number of advanced bioimaging techniques applicable to living-cell studies such as sequential photolabeling of distinct cellular regions, innovative FRET schemes, or nanoscopy. Owing to the relevance of fluorescent proteins from Aequorea victoria (AFPs) for cell biology, a photochromic "toolbox" constituted by several AFPs is...

Topics

Absorption
Amino Acid Substitution
Animals
Color
Darkness
Fluorescence Resonance Energy Transfer
Hydrozoa
Light
Luminescent Proteins
Models, Molecular
Molecular Imaging

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Photobleaching

Protein Conformation

Protein Folding

Protons

Stereoisomerism

Source

Open in PubMed

Identifiers

PMID: 19958004
DOI: 10.1021/ja9014953

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single amino acid replacement makes Aequorea victoria fluorescent proteins reversibly photoswitchable.PMID 19958004Read ↗

Fluorescent proteins and their applications in imaging living cells and tissues.Semantic proximity Read ↗

Chromophore chemistry of fluorescent proteins controlled by light.Semantic proximity Read ↗

[Fluorescent proteins: physical-chemical properties and application in cell biology].Semantic proximity Read ↗

Analysis of red-fluorescent proteins provides insight into dark-state conversion and photodegradation.Semantic proximity Read ↗

A unique series of reversibly switchable fluorescent proteins with beneficial properties for various applications.Semantic proximity Read ↗

Chimeric Autofluorescent Proteins as Photophysical Model System for Multicolor Bimolecular Fluorescence Complementation.Semantic proximity Read ↗

Improving the photostability of bright monomeric orange and red fluorescent proteins.Semantic proximity Read ↗

A stroboscopic approach for fast photoactivation-localization microscopy with Dronpa mutants.Semantic proximity Read ↗

The single T65S mutation generates brighter cyan fluorescent proteins with increased photostability and pH insensitivity.Semantic proximity Read ↗

Efficient photoconversion distorts the fluorescence lifetime of GFP in confocal microscopy: a model kinetic study on mutant Thr203Val.Semantic proximity Read ↗

Photoswitching of E222Q GFP mutants: "concerted" mechanism of chromophore isomerization and protonation.Semantic proximity Read ↗

Autofluorescent proteins in single-molecule research: applications to live cell imaging microscopy.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.