Oxidation-induced structural changes of ceruloplasmin foster NGR motif deamidation that promotes integrin binding and signaling.

Barbariga, Marco; Curnis, Flavio; Spitaleri, Andrea; Andolfo, Annapaola; Zucchelli, Chiara; Lazzaro, Massimo; Magnani, Giuseppe; Musco, Giovanna; Corti, Angelo; Alessio, Massimo

Barbariga, Marco; Curnis, Flavio; Spitaleri, Andrea; Andolfo, Annapaola; Zucchelli, Chiara; Lazzaro, Massimo; Magnani, Giuseppe; Musco, Giovanna; Corti, Angelo; Alessio, Massimo.

Affiliation

Barbariga M; From the Proteome Biochemistry.

J Biol Chem ; 289(6): 3736-48, 2014 Feb 07.

Article in En | MEDLINE | ID: mdl-24366863

Subject(s)

Ceruloplasmin/metabolism; Protein Processing, Post-Translational; Signal Transduction; Alzheimer Disease/cerebrospinal fluid; Alzheimer Disease/genetics; Amino Acid Motifs; Cell Adhesion/genetics; Cell Line, Tumor; Ceruloplasmin/chemistry; Ceruloplasmin/genetics; Humans; Integrins/genetics; Integrins/metabolism; Oxidation-Reduction; Protein Binding

Key words

Alzheimer Disease; Ceruloplasmin; Integrins; NGR Motif; Oxidative Stress; Protein Deamidation; Protein Misfolding; Structural Biology; isoNGR Motif

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Ceruloplasmin / Signal Transduction / Protein Processing, Post-Translational Limits: Humans Language: En Journal: J Biol Chem Year: 2014 Document type: Article Country of publication: United States

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