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Serpin polymerization and its role in disease—The molecular basis of α 1 ‐antitrypsin deficiency
Author(s) -
Knaupp Anja S.,
Bottomley Stephen P.
Publication year - 2009
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.127
Subject(s) - serpin , alpha 1 antitrypsin deficiency , protein folding , protein aggregation , chemistry , disease , mechanism (biology) , population , biochemistry , biology , medicine , immunology , gene , environmental health , philosophy , epistemology
Protein aggregation is the cause of several human diseases. Understanding the molecular mechanisms involved in protein aggregation requires knowledge of the kinetics and structures populated during the reaction. Arguably, the best structurally characterized misfolding reaction is that of α 1 ‐antitrypsin. α 1 ‐Antitrypsin misfolding leads to both liver disease and emphysema and affect approximately 1 in 2000 of the population. This review will focus on the mechanism of α 1 ‐antitrypsin misfolding and the development of potential therapeutic strategies. © 2008 IUBMB IUBMB Life, 61(1): 1–5, 2009