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

Expression of linear permutated variants from circular enterocin AS-48.

Biochimie - 1 Mar 2011

Montalbán-López Manuel, Martínez-Bueno Manuel, Valdivia Eva, Maqueda Mercedes

Abstract excerpt

To confirm whether the head-to-tail circularization could be involved in the stability and activity of the circular bacteriocin AS-48, two permutated linear structural as-48A genes have been constructed by circular permutation. The absence of the leaderless linear AS(23/24) and AS(48/49) proteins in Escherichia coli, under all the conditions investigated, supports the idea that the circular backbone is important...

Read the complete abstract on PubMed

Topics

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

Share to Cloning, Molecular
Share to Bacteriocins
Share to Enterococcus faecalis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genetic Vectors

Share to Protein Engineering

Share to Protein Stability

Share to Recombinant Fusion Proteins

Share to Reverse Transcriptase Polymerase Chain Reaction

Source

Identifiers

PMID: 21130135
DOI: 10.1016/j.biochi.2010.11.011

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Expression of linear permutated variants from circular enterocin AS-48.PMID 21130135Read ↗

Conformational stability and activity of circular Enterocin AS-48 derivatives.Semantic proximity Read ↗

Mutations near the cleavage site of enterocin NKR-5-3B prepeptide reveal new insights into its biosynthesis.Semantic proximity Read ↗

Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA.Semantic proximity Read ↗

Circular permutation in proteins.Semantic proximity Read ↗

Engineering a circularly permuted GFP scaffold for peptide presentation.Semantic proximity Read ↗

An Enhanced Split Intein-Mediated Ligation (SIML) Platform for Rapid Discovery and Functional Screening of Circular BacteriocinsSemantic proximity Read ↗

Improving a circularly permuted TEM-1 beta-lactamase by directed evolution.Semantic proximity Read ↗

Functional Analysis of Genes Involved in the Biosynthesis of Enterocin NKR-5-3B, a Novel Circular BacteriocinSemantic proximity Read ↗

Capped acyclic permutants of the circular protein kalata B1.Semantic proximity Read ↗

Probing the functional mechanism of Escherichia coli GroEL using circular permutation.Semantic proximity Read ↗

Purification, characterization, and biological effects of a second bacteriocin from Enterococcus faecalis ssp. liquefaciens S-48 and its mutant strain B-48-28.Semantic proximity Read ↗

Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide.Semantic proximity Read ↗

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