The role of disulfide bonds and N-terminus in the structural properties of hepcidins: Insights from molecular dynamics simulations
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/bip.21499/fullpdf
Reference22 articles.
1. Hepcidin, a Urinary Antimicrobial Peptide Synthesized in the Liver
2. LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
3. A New Mouse Liver-specific Gene, Encoding a Protein Homologous to Human Antimicrobial Peptide Hepcidin, Is Overexpressed during Iron Overload
4. TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens
5. Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
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4. The effect of different disulfide connectivity patterns on hepcidin structure: Investigated by molecular dynamics simulation;Chemical Physics;2020-07
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