Copper binding to naturally occurring, lactam form of angiogenin differs from that to recombinant protein, affecting their activity

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(2015) Chiara Giacomelli et al.   INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY

Angiogenin in Parkinson Disease Models: Role of Akt Phosphorylation and Evaluation of AAV-Mediated Angiogenin Expression in MPTP Treated Mice

(2013) Trent U. Steidinger et al.   PLoS One

Copper(II) interaction with peptide fragments of histidine–proline-rich glycoprotein: Speciation, stability and binding details

(2012) Diego La Mendola et al.   JOURNAL OF INORGANIC BIOCHEMISTRY

Probing the Copper(II) Binding Features of Angiogenin. Similarities and Differences between a N-Terminus Peptide Fragment and the Recombinant Human Protein

(2011) Diego La Mendola et al.   INORGANIC CHEMISTRY

Copper(ii) complex formation with a linear peptide encompassing the putative cell binding site of angiogenin

(2010) Diego La Mendola et al.   DALTON TRANSACTIONS

Copper Transport in Mammalian Cells: Special Care for a Metal with Special Needs

(2009) Jack H. Kaplan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

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