Identification of hydrophobic fragments of α1-antitrypsin and Cl protease inhibitor in human bile, plasma and spleen
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)80234-8/fullpdf
Reference26 articles.
1. Human α1-proteinase inhibitor
2. Implications of the three-dimensional structure of .alpha.1-antitrypsin for structure and function of serpins
3. The Serpins: Evolution and Adaptation in a Family of Protease Inhibitors
4. Plakalbumin, α1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis
5. Primary structure of the reactive site of human C1-inhibitor.
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1. Multiplex quantification of C-terminal alpha-1-antitrypsin peptides provides a novel approach for characterizing systemic inflammation;Scientific Reports;2022-03-09
2. Post-Translational Modifications of Circulating Alpha-1-Antitrypsin Protein;International Journal of Molecular Sciences;2020-12-02
3. CAAP48, a New Sepsis Biomarker, Induces Hepatic Dysfunction in an in vitro Liver-on-Chip Model;Frontiers in Immunology;2019-02-25
4. Identification of Novel Short C-Terminal Transcripts of Human SERPINA1 Gene;PLOS ONE;2017-01-20
5. Novel Biological Functions of A1AT;Alpha-1-antitrypsin Deficiency;2017
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