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Article

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.

Structure (London, England : 1993) - 4 Mar 2014

Kojima Rieko, Okumura Masaki, Masui Shoji, Kanemura Shingo, Inoue Michio, Saiki Masatoshi, Yamaguchi Hiroshi, Hikima Takaaki, Suzuki Mamoru, Akiyama Shuji, Inaba Kenji

Abstract excerpt

The mammalian endoplasmic reticulum (ER) contains a diverse oxidative protein folding network in which ERp46, a member of the protein disulfide isomerase (PDI) family, serves as an efficient disulfide bond introducer together with Peroxiredoxin-4 (Prx4). We revealed a radically different molecular architecture of ERp46, in which the N-terminal two thioredoxin (Trx) domains with positively charged patches near...

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PMID: 24462249
DOI: 10.1016/j.str.2013.12.013

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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.

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