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Article

The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study.

Blood - 1 Jan 2006

Nemeth Elizabeta, Preza Gloria C, Jung Chun-Ling, Kaplan Jerry, Waring Alan J, Ganz Tomas

Abstract excerpt

Hepcidin is the principal iron-regulatory hormone. It acts by binding to the iron exporter ferroportin, inducing its internalization and degradation, thereby blocking cellular iron efflux. The bioactive 25 amino acid (aa) peptide has a hairpin structure stabilized by 4 disulfide bonds. We synthesized a series of hepcidin derivatives and determined their bioactivity in a cell line expressing ferroportin-GFP fusion...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 16141345
DOI: 10.1182/blood-2005-05-2049
PMCID: PMC1895343

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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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