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

Translational repression of the disintegrin and metalloprotease ADAM10 by a stable G-quadruplex secondary structure in its 5'-untranslated region.

The Journal of biological chemistry - 30 Dec 2011

Lammich Sven, Kamp Frits, Wagner Judith, Nuscher Brigitte, Zilow Sonja, Ludwig Ann-Katrin, Willem Michael, Haass Christian

Abstract excerpt

Anti-amyloidogenic processing of the amyloid precursor protein APP by α-secretase prevents formation of the amyloid-β peptide, which accumulates in senile plaques of Alzheimer disease patients. α-Secretase belongs to the family of a disintegrin and metalloproteases (ADAMs), and ADAM10 is the prim...

Read the complete abstract on PubMed

Topics

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

Share to 5' Untranslated Regions
Share to ADAM Proteins
Share to Amyloid Precursor Protein Secretases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to Membrane Proteins

Share to Mutation

Share to Nucleic Acid Conformation

Share to Protein Biosynthesis

Source

Open in PubMed Open full text

Identifiers

PMID: 22065584
DOI: 10.1074/jbc.M111.296921
PMCID: PMC3248004

Genes

ADAM10
APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22065584-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Translational repression of the disintegrin and metalloprotease ADAM10 by a stable G-quadruplex secondary structure in its 5'-untranslated region.PMID 22065584Read ↗

5′-UTR G-Quadruplex-Mediated Translation Regulation in Eukaryotes: Current Understanding and Methodological ChallengesSemantic proximity Read ↗

Cosmosiin Increases ADAM10 Expression via Mechanisms Involving 5’UTR and PI3K SignalingSemantic proximity Read ↗

The G-quadruplex augments translation in the 5' untranslated region of transforming growth factor β2.Semantic proximity Read ↗

Expression of the Alzheimer protease BACE1 is suppressed via its 5'-untranslated region.Semantic proximity Read ↗

A stable RNA G-quadruplex within the 5'-UTR of Arabidopsis thaliana ATR mRNA inhibits translation.Semantic proximity Read ↗

Genomic structure and functional characterization of the human ADAM10 promoter.Semantic proximity Read ↗

In the sense of transcription regulation by G-quadruplexes: asymmetric effects in sense and antisense strands.Semantic proximity Read ↗

Helping Eve overcome ADAM: G-quadruplexes in the ADAM-15 promoter as new molecular targets for breast cancer therapeutics.Semantic proximity Read ↗

In vivo ribozyme targeting of betaAPP+ mRNAs.Semantic proximity Read ↗

A disintegrin and metalloproteinase (ADAM)-mediated ectodomain shedding of ADAM10.Semantic proximity Read ↗

RNA aptamers selectively modulate protein recruitment to the cytoplasmic domain of beta-secretase BACE1 in vitro.Semantic proximity Read ↗

Functional analysis of an ADAMTS10 signal peptide mutation in Weill-Marchesani syndrome demonstrates a long-range effect on secretion of the full-length enzyme.Semantic proximity Read ↗

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