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

Generation of a novel TRAIL mutant by proline to arginine substitution based on codon bias and its antitumor effects.

Molecular medicine reports - 1 Oct 2017

Zhu Aijing, Wang Xiuyun, Huang Min, Chen Chen, Yan Juan, Xu Qi, Wei Lijia, Huang Xianzhou, Zhu Hong, Yi Cheng

Abstract excerpt

TNF ligand superfamily member 10 (TRAIL) is a member of the tumor necrosis factor superfamily. The present study was performed in an effort to increase the expression of soluble (s)TRAIL by rebuilding the gene sequence of TRAIL. Three principles based on the codon bias of Escherichia coli were put forward to design the rebuild strategy. Relying on these three principles, a P7R mutation near the N‑terminal region...

Read the complete abstract on PubMed

Topics

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

Share to Antineoplastic Agents
Share to Arginine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Survival

Share to Plasmids

Share to Proline

Share to Recombinant Proteins

Share to TNF-Related Apoptosis-Inducing Ligand

Source

Identifiers

PMID: 28791342
DOI: 10.3892/mmr.2017.7146

Genes

TNF

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

Generation of a novel TRAIL mutant by proline to arginine substitution based on codon bias and its antitumor effects.PMID 28791342Read ↗

DR4-selective tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) variants obtained by structure-based design.Semantic proximity Read ↗

2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity.Semantic proximity Read ↗

Therapeutic applications of TRAIL receptor agonists in cancer and beyondSemantic proximity Read ↗

The TRAIL apoptotic pathway in cancer onset, progression and therapy.Semantic proximity Read ↗

TRAIL mutant membrane penetrating peptide alike-MuR6-TR enhances the antitumor effects of TRAIL in pancreatic carcinoma both in vitro and in vivo.Semantic proximity Read ↗

Rapid and efficient cancer cell killing mediated by high-affinity death receptor homotrimerizing TRAIL variants.Semantic proximity Read ↗

TRAIL as a target in anti-cancer therapy.Semantic proximity Read ↗

Generation of new TRAIL mutants DR5-A and DR5-B with improved selectivity to death receptor 5.Semantic proximity Read ↗

Apoptosis-Inducing TNF Superfamily Ligands for Cancer TherapySemantic proximity Read ↗

Trimeric coiled-coil domain of human pulmonary surfactant protein D enhances zinc-binding ability and biologic activity of soluble TRAIL.Semantic proximity Read ↗

Targeted delivery of a designed sTRAIL mutant results in superior apoptotic activity towards EGFR-positive tumor cells.Semantic proximity Read ↗

Mutations Enhancing Selectivity of Antitumor Cytokine TRAIL to DR5 Receptor Increase Its Cytotoxicity against Tumor Cells.Semantic proximity Read ↗

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