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

Self-Assembling NanoLuc Luciferase Fragments as Probes for Protein Aggregation in Living Cells.

ACS chemical biology - 15 Jan 2016

Zhao Jia, Nelson Travis J, Vu Quyen, Truong Tiffany, Stains Cliff I

Abstract excerpt

Given the clear role of protein aggregation in human disease, there is a critical need for assays capable of quantifying protein aggregation in living systems. We hypothesized that the inherently low background and biocompatibility of luminescence signal readouts could provide a potential solution to this problem. Herein, we describe a set of self-assembling NanoLuc luciferase (Nluc) fragments that produce a...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid beta-Peptides
Share to Bacteria
Share to Biological Assay

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Blotting, Western

Share to Luciferases

Share to NIH 3T3 Cells

Share to Peptide Fragments

Share to Protein Aggregation, Pathological

Source

Open in PubMed Open full text

Identifiers

PMID: 26492083
DOI: 10.1021/acschembio.5b00758
PMCID: PMC5110118

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

Self-Assembling NanoLuc Luciferase Fragments as Probes for Protein Aggregation in Living Cells.PMID 26492083Read ↗

A genetically encoded selection for amyloid-β oligomer bindersSemantic proximity Read ↗

A slow but steady nanoLuc: R162A mutation results in a decreased, but stable, nanoLuc activity.Semantic proximity Read ↗

Q-DOAS: A Proximity Quenching Assay for Real-Time Detection of Early Protein Aggregation EventsSemantic proximity Read ↗

Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis.Semantic proximity Read ↗

Novel repertoire of tau biosensors to monitor pathological tau transformation and seeding activity in living cellsSemantic proximity Read ↗

Detection and manipulation of live antigen-expressing cells using conditionally stable nanobodiesSemantic proximity Read ↗

A FRET Sensor for Non‐Invasive Imaging of Amyloid Formation in VivoSemantic proximity Read ↗

Design of non-aggregating variants of Aβ peptide.Semantic proximity Read ↗

A novel small molecule screening platform for disrupting toxic tau oligomers in cellsSemantic proximity Read ↗

An in vivo platform to select and evolve aggregation-resistant proteins.Semantic proximity Read ↗

Mutations enhance the aggregation propensity of the Alzheimer's A beta peptide.Semantic proximity Read ↗

Development of new fusion proteins for visualizing amyloid-β oligomers in vivoSemantic proximity Read ↗

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