Copper-ion interaction with the 106–113 domain of the prion protein: a solution-equilibria study on model peptides
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
Inorganic Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2005/DT/B505314E
Reference36 articles.
1. Cellular prion protein: on the road for functions
2. Nobel Lecture: Prions
3. Neurodegenerative Diseases and Prions
4. Copper Binding to the N-Terminal Tandem Repeat Regions of Mammalian and Avian Prion Protein
5. Copper Binding to the N-Terminal Tandem Repeat Region of Mammalian and Avian Prion Protein: Structural Studies Using Synthetic Peptides
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1. Methionine 109 plays a key role in Cu(II) binding to His111 in the 92–115 fragment of the human prion protein;Inorganica Chimica Acta;2018-09
2. Conformation-dependent affinity of Cu(II) ions peptide complexes derived from the human Pin1 protein;Journal of Thermal Analysis and Calorimetry;2016-04-04
3. Spectroscopic and Theoretical Study of CuI Binding to His111 in the Human Prion Protein Fragment 106–115;Inorganic Chemistry;2016-03-01
4. Investigations of copper(II) complexation by fragments of the FBP28 protein using isothermal titration (ITC) and differential scanning calorimetry (DSC);Journal of Thermal Analysis and Calorimetry;2015-04-04
5. Cross-Talk Between the Octarepeat Domain and the Fifth Binding Site of Prion Protein Driven by the Interaction of Copper(II) with the N-terminus;Chemistry - A European Journal;2015-02-03
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