Discover Community Create You

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

Article

Fluctuation-based imaging of nuclear Rac1 activation by protein oligomerisation.

Scientific reports - 27 Feb 2014

Hinde Elizabeth, Yokomori Kyoko, Gaus Katharina, Hahn Klaus M, Gratton Enrico

Abstract excerpt

Here we describe a fluctuation-based method to quantify how protein oligomerisation modulates signalling activity of a multifunctional protein. By recording fluorescence lifetime imaging microscopy (FLIM) data of a FRET biosensor in a format that enables concomitant phasor and cross Number and Brightness (cN&B) analysis, we measure the nuclear dynamics of a Rac1 FRET biosensor and assess how Rac1 homo-oligomers...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to alpha Karyopherins
Share to Cytoplasm
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence Resonance Energy Transfer

Share to Microscopy, Fluorescence

Share to NIH 3T3 Cells

Share to Protein Multimerization

Share to rac1 GTP-Binding Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 24573109
DOI: 10.1038/srep04219
PMCID: PMC3936235

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fluctuation-based imaging of nuclear Rac1 activation by protein oligomerisation.PMID 24573109Read ↗

A precise and general FRET-based method for monitoring structural transitions in protein self-organizationSemantic proximity Read ↗

Oligomerization of G protein-coupled receptors: biochemical and biophysical methods.Semantic proximity Read ↗

Combining FRET and super-resolution microscopy reveals kinase activation and mitochondrial activity at the nanoscaleSemantic proximity Read ↗

Cofilin nuclear-cytoplasmic shuttling affects cofilin-actin rod formation during stress.Semantic proximity Read ↗

Multiplexed biochemical imaging reveals the extent and complexity of non-genetic heterogeneity in DNA damage-induced caspase dynamicsSemantic proximity Read ↗

Quantitative live-cell imaging and computational modeling shed new light on endogenous WNT/CTNNB1 signaling dynamics.Semantic proximity Read ↗

Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study.Semantic proximity Read ↗

Monitoring peripheral protein oligomerization on biological membranes.Semantic proximity Read ↗

Confocal fluorescence anisotropy and FRAP imaging of α-synuclein amyloid aggregates in living cells.Semantic proximity Read ↗

Single-molecule imaging reveals the oligomeric state of functional TNFα-induced plasma membrane TNFR1 clusters in cells.Semantic proximity Read ↗

Oligomerization of the yeast alpha-factor receptor: implications for dominant negative effects of mutant receptors.Semantic proximity Read ↗

An improved Ras sensor for highly sensitive and quantitative FRET-FLIM imaging.Semantic proximity Read ↗

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