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Article

A trimeric structural fusion of an antagonistic tumor necrosis factor-α mutant enhances molecular stability and enables facile modification.

The Journal of biological chemistry - 21 Apr 2017

Inoue Masaki, Ando Daisuke, Kamada Haruhiko, Taki Shintaro, Niiyama Mayumi, Mukai Yohei, Tadokoro Takashi, Maenaka Katsumi, Nakayama Taisuke, Kado Yuji, Inoue Tsuyoshi, Tsutsumi Yasuo, Tsunoda Shin-Ichi

Abstract excerpt

Tumor necrosis factor-α (TNF) exerts its biological effect through two types of receptors, p55 TNF receptor (TNFR1) and p75 TNF receptor (TNFR2). An inflammatory response is known to be induced mainly by TNFR1, whereas an anti-inflammatory reaction is thought to be mediated by TNFR2 in some autoimmune diseases. We have been investigating the use of an antagonistic TNF mutant (TNFR1-selective antagonistic TNF...

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Source

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Identifiers

PMID: 28235800
DOI: 10.1074/jbc.M117.779686
PMCID: PMC5399098

Genes

TNF

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.

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