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

Exploration of the arrest peptide sequence space reveals arrest-enhanced variants.

The Journal of biological chemistry - 17 Apr 2015

Cymer Florian, Hedman Rickard, Ismail Nurzian, von Heijne Gunnar

Abstract excerpt

Translational arrest peptides (APs) are short stretches of polypeptides that induce translational stalling when synthesized on a ribosome. Mechanical pulling forces acting on the nascent chain can weaken or even abolish stalling. APs can therefore be used as in vivo force sensors, making it possible to measure the forces that act on a nascent chain during translation with single-residue resolution. It is also...

Read the complete abstract on PubMed

Topics

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

Share to Biomechanical Phenomena
Share to Escherichia coli
Share to Gene Expression Regulation, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Peptide Chain Elongation, Translational

Share to Peptide Elongation Factors

Share to Peptides

Share to Ribosomes

Source

Open in PubMed Open full text

Identifiers

PMID: 25713070
DOI: 10.1074/jbc.M115.641555
PMCID: PMC4400336

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploration of the arrest peptide sequence space reveals arrest-enhanced variants.PMID 25713070Read ↗

Mutational analysis of the human Xbp1 translational arrest peptide and construction of arrest-enhanced variantsSemantic proximity Read ↗

The plasticity of a translation arrest motif yields insights into nascent polypeptide recognition inside the ribosome tunnel.Semantic proximity Read ↗

The ribosomal exit tunnel functions as a discriminating gate.Semantic proximity Read ↗

Search for translation arrest peptides encoded upstream of genes for components of protein localization pathways.Semantic proximity Read ↗

Structural and mutational analysis of the ribosome-arresting human XBP1uSemantic proximity Read ↗

Translation arrest requires two-way communication between a nascent polypeptide and the ribosome.Semantic proximity Read ↗

Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing.Semantic proximity Read ↗

Probing interplays between human XBP1u translational arrest peptide and 80S ribosomeSemantic proximity Read ↗

Nascent SecM chain interacts with outer ribosomal surface to stabilize translation arrest.Semantic proximity Read ↗

Sequence diversity of apidaecin-like peptides arresting the terminating ribosome.Semantic proximity Read ↗

Prion Protein Folding Mechanism Revealed by Pulling Force StudiesSemantic proximity Read ↗

The folding and unfolding behavior of ribonuclease H on the ribosomeSemantic proximity Read ↗

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