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

Human tra2-beta1 autoregulates its protein concentration by influencing alternative splicing of its pre-mRNA.

Human molecular genetics - 1 Mar 2004

Stoilov Peter, Daoud Rosette, Nayler Oliver, Stamm Stefan

Abstract excerpt

HTRA2-BETA1 is an SR-like protein that regulates alternative splice site selection in a concentration-dependent manner. Its proper concentration is important as several pathological states are associated with its change. We investigated the mechanism that controls the cellular HTRA2-BETA1 concentration and found it utilizes a negative feedback loop to regulate the splicing of its exon 2. TRA2-BETA1 binds to four...

Read the complete abstract on PubMed

Topics

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

Share to Alternative Splicing
Share to Amino Acid Motifs
Share to Enhancer Elements, Genetic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immune Sera

Share to Protein-Tyrosine Kinases

Share to RNA-Binding Proteins

Share to RNA Precursors

Share to Serine-Arginine Splicing Factors

Source

Identifiers

PMID: 14709600
DOI: 10.1093/hmg/ddh051

Genes

HTRA2
CLK2

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

Human tra2-beta1 autoregulates its protein concentration by influencing alternative splicing of its pre-mRNA.PMID 14709600Read ↗

Bichromatic Splicing Detector Allows Quantification of THRA1 and THRA2 Splicing Isoforms in Single Cells by Fluorescent Live-Cell ImagingSemantic proximity Read ↗

HnRNP G and Tra2beta: opposite effects on splicing matched by antagonism in RNA bindingSemantic proximity Read ↗

Clinical phenotype and mutant TRα1.Semantic proximity Read ↗

A novel splice variant involving the 5' untranslated region of thyroid hormone receptor beta1 (TRbeta1).Semantic proximity Read ↗

Tau exons 2 and 10, which are misregulated in neurodegenerative diseases, are partly regulated by silencers which bind a SRp30c.SRp55 complex that either recruits or antagonizes htra2beta1.Semantic proximity Read ↗

A purine-rich intronic element enhances alternative splicing of thyroid hormone receptor mRNA.Semantic proximity Read ↗

A point mutation in the activation function 2 domain of thyroid hormone receptor alpha1 expressed after CRE-mediated recombination partially recapitulates hypothyroidism.Semantic proximity Read ↗

A New Mechanism in THRA Resistance: The First Disease-Associated Variant Leading to an Increased Inhibitory Function of THRA2.Semantic proximity Read ↗

Protein phosphatase 1 binds to the RNA recognition motif of several splicing factors and regulates alternative pre-mRNA processingSemantic proximity Read ↗

HR3/RORα-mediated cholesterol sensing regulates TOR signalingSemantic proximity Read ↗

Regulation of thyroid hormone receptor alpha2 RNA binding and subcellular localization by phosphorylation.Semantic proximity Read ↗

A natural transactivation mutation in the thyroid hormone beta receptor: impaired interaction with putative transcriptional mediators.Semantic proximity Read ↗

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