Metal Binding Ability of Cysteine-Rich Peptide Domain of ZIP13 Zn2+ Ions Transporter
Author:
Affiliation:
1. Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, 50-383 Wroclaw, Poland
2. Department of Chemistry, University of Siena, Via Aldo Moro 2, Siena 53100, Italy
Publisher
American Chemical Society (ACS)
Subject
Inorganic Chemistry,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/ic200270p
Reference37 articles.
1. Evolutionary Descent of Prion Genes from the ZIP Family of Metal Ion Transporters
2. Effect of metal ions on de novo aggregation of full-length prion protein
3. Copper and Zinc Binding Modulates the Aggregation and Neurotoxic Properties of the Prion Peptide PrP106−126
4. ZupT Is a Zn(II) Uptake System in Escherichia coli
5. The Acrodermatitis Enteropathica Gene ZIP4 Encodes a Tissue-specific, Zinc-regulated Zinc Transporter in Mice
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