Structural studies and SH3 domain binding properties of a human antiviral salivary proline-rich peptide-Reference-Cited by-同舟云学术

Structural studies and SH3 domain binding properties of a human antiviral salivary proline-rich peptide

Published:2016-09 Issue:5 Volume:106 Page:714-725
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Righino Benedetta¹,Pirolli Davide¹,Radicioni Giorgia¹,Marzano Valeria¹,Longhi Renato²,Arcovito Alessandro¹,Sanna Maria Teresa³,De Rosa Maria Cristina⁴,Paoluzi Serena⁵,Cesareni Gianni⁵,Messana Irene³,Castagnola Massimo¹⁴,Vitali Alberto⁴

Affiliation:

1. Istituto di Biochimica e Biochimica Clinica, Facoltà di Medicina, Università Cattolica; L.Go F. Vito, 1 Rome 00168 Italy

2. Istituto di Chimica del Riconoscimento Molecolare; C.N.R, via Mario Bianco, 9 Milan 20100 Italy

3. Dipartimento di Scienze della Vita e dell'Ambiente, Monserrato, 09042, Italy, Università di Cagliari, Cittadella Universitaria; Cagliari

4. Istituto di Chimica di Riconoscimento Molecolare; C.N.R. Rome, L.Go F. Vito, 1 Rome 00168 Italy

5. Dipartimento di Biologia; Università di Tor Vergata; Rome 00173 Italy

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference73 articles.

1. Proline-Rich Peptides: Multifunctional Bioactive Molecules as New Potential Therapeutic Drugs

2. The short proline-rich antibacterial peptide family

3. Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria

4. PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to Src homology 3 domains of p47 phox.

5. PR-39, a Syndecan-inducing Antimicrobial Peptide, Binds and Affects p130Cas

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