Salivary Cystatins: Exploring New Post-Translational Modifications and Polymorphisms by Top-Down High-Resolution Mass Spectrometry-Reference-Cited by-同舟云学术

Salivary Cystatins: Exploring New Post-Translational Modifications and Polymorphisms by Top-Down High-Resolution Mass Spectrometry

Published:2017-10-26 Issue:11 Volume:16 Page:4196-4207
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Manconi Barbara¹^ORCID,Liori Barbara¹,Cabras Tiziana¹^ORCID,Vincenzoni Federica²,Iavarone Federica²,Castagnola Massimo²³,Messana Irene²³,Olianas Alessandra¹

Affiliation:

1. Department of Life and Environmental Sciences, Biomedical Section, University of Cagliari, Monserrato Campus, 09042 Monserrato, Cagliari, Italy

2. Biochemistry and Clinical Biochemistry Institute, Medicine Faculty, Catholic University of Rome, L.go F. Vito 1, 00168 Rome, Italy

3. Institute of Chemistry of the Molecular Recognition CNR, L.go F. Vito 1, 00168 Rome, Italy

Funder

Universit? di Cagliari

Nando and Elsa Peretti Foundation

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.7b00567

Reference61 articles.

1. Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease

2. Cystatins: Biochemical and structural properties, and medical relevance

3. RP-HPLC–ESI-MS evidenced that salivary cystatin B is detectable in adult human whole saliva mostly as S-modified derivatives: S-Glutathionyl, S-cysteinyl and S–S 2-mer

4. Localization of the human SH-protease inhibitor in the epidermis

5. Localization of three inhibitors of cysteineproteinases in the human oral mucosa

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