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

Identifying cytoplasmic proteins that affect receptor clustering using fluorescence resonance energy transfer and RNA interference.

Analytical and bioanalytical chemistry - 1 Dec 2009

Dibya Deepak, Sander Suzanne, Smith Emily A

Abstract excerpt

Unraveling the complex, dynamic organization of the cell membrane can provide vital information about many aspects of cellular functions. Reported herein is a method for identifying cytoplasmic proteins that affect cell membrane protein organization. RNA interference (RNAi) is used to reduce the expression of select cytoplasmic proteins and a fluorescence resonance energy transfer (FRET) assay is used to measure...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line
Share to Cytoplasm
Share to Drosophila

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drosophila Proteins

Share to Fluorescence Resonance Energy Transfer

Share to Integrins

Share to Mutation

Share to RNA Interference

Source

Identifiers

PMID: 19806349
DOI: 10.1007/s00216-009-3146-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identifying cytoplasmic proteins that affect receptor clustering using fluorescence resonance energy transfer and RNA interference.PMID 19806349Read ↗

Dynamic regulation of integrin β1 phosphorylation supports invasion of breast cancer cellsSemantic proximity Read ↗

Multiparametric analysis of focal adhesion formation by RNAi-mediated gene knockdownSemantic proximity Read ↗

Molecular mechanism of vinculin activation and nanoscale spatial organization in focal adhesions.Semantic proximity Read ↗

RNAi screen identifies KIF15 as a novel regulator of integrin endocytic traffickingSemantic proximity Read ↗

Structural and functional analysis of LIM domain-dependent recruitment of paxillin to αvβ3 integrin-positive focal adhesions.Semantic proximity Read ↗

Flow cytometric analysis of fluorescence resonance energy transfer: a tool for high-throughput screening of molecular interactions in living cells.Semantic proximity Read ↗

Bifunctional small molecules that induce nuclear localization and targeted transcriptional regulationSemantic proximity Read ↗

Nuclear cytoplasmic shuttling by thyroid hormone receptors. multiple protein interactions are required for nuclear retention.Semantic proximity Read ↗

Deciphering the nuclear import pathway for the cytoskeletal red cell protein 4.1R.Semantic proximity Read ↗

Proteomic and functional evidence for a P2X7 receptor signalling complex.Semantic proximity Read ↗

EFR3A: a new raft domain organizing protein?Semantic proximity Read ↗

Visualization of Rab5 activity in living cells by FRET microscopy and influence of plasma-membrane-targeted Rab5 on clathrin-dependent endocytosis.Semantic proximity Read ↗

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