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

Nuclear import and export signals control the subcellular localization of Nurr1 protein in response to oxidative stress.

The Journal of biological chemistry - 22 Feb 2013

García-Yagüe Ángel Juan, Rada Patricia, Rojo Ana I, Lastres-Becker Isabel, Cuadrado Antonio

Abstract excerpt

Orphan receptor Nurr1 participates in the acquisition and maintenance of the dopaminergic cell phenotype, modulation of inflammation, and cytoprotection, but little is known about its regulation. In this study, we report that Nurr1 contains a bipartite nuclear localization signal (NLS) within its DNA binding domain and two leucine-rich nuclear export signals (NES) in its ligand binding domain. Together, these...

Read the complete abstract on PubMed

Topics

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

Share to Active Transport, Cell Nucleus
Share to Arsenites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biological Transport

Share to Cytosol

Share to Microscopy, Fluorescence

Share to Nuclear Localization Signals

Share to Nuclear Receptor Subfamily 4, Group A, Member 2

Share to Subcellular Fractions

Source

Open in PubMed Open full text

Identifiers

PMID: 23283970
DOI: 10.1074/jbc.M112.439190
PMCID: PMC3581400

Genes

NES

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

Nuclear import and export signals control the subcellular localization of Nurr1 protein in response to oxidative stress.PMID 23283970Read ↗

Retinoid X receptor regulates Nur77/TR3-dependent apoptosis [corrected] by modulating its nuclear export and mitochondrial targeting.Semantic proximity Read ↗

FMRP and its Multifunctionality: From Cytosol to Nucleolus and BackSemantic proximity Read ↗

Nur77 forms novel nuclear structures upon DNA damage that cause transcriptional arrest.Semantic proximity Read ↗

Comprehensive insights into the function and molecular and pharmacological regulation of neuron-derived orphan receptor 1, an orphan receptorSemantic proximity Read ↗

Defining requirements for heterodimerization between the retinoid X receptor and the orphan nuclear receptor Nurr1.Semantic proximity Read ↗

Nurr1 deficiency impairs autophagy-lysosomal function through GBA-dependent transcriptional regulation in Parkinson’s disease pathogenesisSemantic proximity Read ↗

The N-terminal region of Nurr1 (a.a 1-31) is essential for its efficient degradation by the ubiquitin proteasome pathway.Semantic proximity Read ↗

Nuclear import and export signals in control of Nrf2.Semantic proximity Read ↗

Continuous Nuclear Export of p62/SQSTM1 Is Essential for Kidney HomeostasisSemantic proximity Read ↗

A novel conserved nuclear localization signal is recognized by a group of yeast importins.Semantic proximity Read ↗

Heterogeneous Nuclear Ribonucleoprotein A2 Is a Common Transcriptional Coactivator in the Nuclear Transcription Response to Mitochondrial Respiratory StressSemantic proximity Read ↗

Targeting NR1D1 in organ injury: challenges and prospectsSemantic proximity Read ↗

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