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

Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins.

Molecular cell - 1 Sept 2003

Liu Shihui, Leppla Stephen H

Abstract excerpt

Retroviral insertional mutagenesis was used to produce a mutant Chinese hamster ovary cell line that is completely resistant to several different bacterial ADP-ribosylating toxins. The gene responsible for toxin resistance, termed diphtheria toxin (DT) and Pseudomonas exotoxin A (ETA) sensitivity required gene 1 (DESR1), encodes two small protein isoforms of 82 and 57 residues. DESR1 is evolutionally conserved...

Read the complete abstract on PubMed

Topics

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

Share to ADP-Ribosylation Factors
Share to Bacterial Infections

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

Share to Bacterial Toxins

Share to CHO Cells

Share to Eukaryotic Cells

Share to Histidine

Share to Molecular Weight

Share to Retroviridae

Source

Identifiers

PMID: 14527407
DOI: 10.1016/j.molcel.2003.08.003

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

Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins.PMID 14527407Read ↗

Characterization of a Chinese hamster ovary cell mutant having a mutation in elongation factor-2.Semantic proximity Read ↗

Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2.Semantic proximity Read ↗

The role of the diphthamide-containing loop within eukaryotic elongation factor 2 in ADP-ribosylation by Pseudomonas aeruginosa exotoxin A.Semantic proximity Read ↗

Inactivation of the elongation factor Tu by mosquitocidal toxin-catalyzed mono-ADP-ribosylation.Semantic proximity Read ↗

The family of toxin‐related ecto‐ADP‐ribosyltransferases in humans and the mouseSemantic proximity Read ↗

ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological PerspectivesSemantic proximity Read ↗

Molecular Mechanisms of the Cytotoxicity of ADP-Ribosylating ToxinsSemantic proximity Read ↗

An abundance of bacterial ADP-ribosyltransferases — implications for the origin of exotoxins and their human homologuesSemantic proximity Read ↗

Insights into diphthamide, key diphtheria toxin effector.Semantic proximity Read ↗

Gene trap mutagenesis-based forward genetic approach reveals that the tumor suppressor OVCA1 is a component of the biosynthetic pathway of diphthamide on elongation factor 2.Semantic proximity Read ↗

Selection of diphtheria toxin active-site mutants in yeast. Rediscovery of glutamic acid-148 as a key residue.Semantic proximity Read ↗

Novel bacterial ADP-ribosylating toxins: structure and functionSemantic proximity Read ↗

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