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

Reductive methylation and mutation of an anthrax toxin fusion protein modulates its stability and cytotoxicity.

Scientific reports - 23 Apr 2014

Bachran Christopher, Gupta Pradeep K, Bachran Silke, Leysath Clinton E, Hoover Benjamin, Fattah Rasem J, Leppla Stephen H

Abstract excerpt

We characterized an anti-cancer fusion protein consisting of anthrax lethal factor (LF) and the catalytic domain of Pseudomonas exotoxin A by (i) mutating the N-terminal amino acids and by (ii) reductive methylation to dimethylate all lysines. Dimethylation of lysines was achieved quantitatively and specifically without affecting binding of the fusion protein to PA or decreasing the enzymatic activity of the...

Read the complete abstract on PubMed

Topics

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

Share to ADP Ribose Transferases
Share to Bacterial Toxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytosol

Share to Exotoxins

Share to Methylation

Share to Protein Interaction Domains and Motifs

Share to Protein Stability

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 24755540
DOI: 10.1038/srep04754
PMCID: PMC3996465

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

Reductive methylation and mutation of an anthrax toxin fusion protein modulates its stability and cytotoxicity.PMID 24755540Read ↗

Engineering anthrax toxin variants that exclusively form octamers and their application to targeting tumors.Semantic proximity Read ↗

A protease-resistant immunotoxin against CD22 with greatly increased activity against CLL and diminished animal toxicity.Semantic proximity Read ↗

Mapping the anthrax protective antigen binding site on the lethal and edema factors.Semantic proximity Read ↗

Characterization of dominant-negative forms of anthrax protective antigen.Semantic proximity Read ↗

Monitoring endocytic trafficking of anthrax lethal factor by precise and quantitative protein labeling.Semantic proximity Read ↗

Anthrax toxin: receptor binding, internalization, pore formation, and translocation.Semantic proximity Read ↗

A "dock and lock" approach to preparation of targeted liposomes.Semantic proximity Read ↗

An anthrax lethal factor mutant that is defective at causing pyroptosis retains proapoptotic activity.Semantic proximity Read ↗

An approach to characterizing single-subunit mutations in multimeric prepores and pores of anthrax protective antigen.Semantic proximity Read ↗

Identification of new dominant-negative mutants of anthrax protective antigen using directed evolution.Semantic proximity Read ↗

Catalytically inactive anthrax toxin(s) are potential prophylactic agents.Semantic proximity Read ↗

A recombinant immunotoxin engineered for increased stability by adding a disulfide bond has decreased immunogenicity.Semantic proximity Read ↗

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