Hepcidin Revisited, Disulfide Connectivity, Dynamics, and Structure

Hepcidin is a tightly folded 25-residue peptide hormone containing four disulfide bonds, which has been shown to act as the principal regulator of iron homeostasis in vertebrates. We used multiple techniques to demonstrate a disulfide bonding pattern for hepcidin different from that previously publi...

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Dades bibliogràfiques
Autors principals: Jordan, John B., Poppe, Leszek, Haniu, Mitsuru, Arvedson, Tara, Syed, Rashid, Li, Vivian, Kohno, Hiko, Kim, Helen, Schnier, Paul D., Harvey, Timothy S., Miranda, Les P., Cheetham, Janet, Sasu, Barbra J.
Format: Artigo
Idioma:Inglês
Publicat: American Society for Biochemistry and Molecular Biology 2009
Matèries:
Protein Structure and Folding
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC2782009/
https://ncbi.nlm.nih.gov/pubmed/19553669
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.017764
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