Genetic variations resulting in a change of amino acid sequence can have a dramatic effect
on stability, hydrogen bond network, conformational dynamics, activity and many other …

Alpha-1 antitrypsin (A1AT) is an acute-phase protein, and is best known as an inhibitor of
the serine proteases, specifically, neutrophil elastase, proteinase 3, and cathepsin G. The …

Since the discovery of alpha‐1 antitrypsin in the early 1960s, several new genes have been
suggested to play a role in chronic obstructive pulmonary disease (COPD) pathogenesis …

Abstract Leukotriene B 4 (LTB 4) contributes to many inflammatory diseases, including
genetic and nongenetic forms of chronic obstructive pulmonary disease. α-1 Antitrypsin …

Serine proteinase inhibitors (serpins), typically fold to a metastable native state and undergo
a major conformational change in order to inhibit target proteases. However, conformational …

Abstract α1-Antitrypsin (A1AT) purified from human plasma upregulates expression and
release of angiopoietin-like protein 4 (Angptl4) in adherent human blood monocytes and in …

Abstract The α-1-antitrypsin (or alpha-1-antitrypsin, A1AT) Z variant is the primary cause of
severe A1AT deficiency and forms polymeric chains that aggregate in the endoplasmic …

UDP-glucose: glycoprotein glucosyltransferase 1 (UGT1) is a central quality control
gatekeeper in the mammalian endoplasmic reticulum (ER). The reglucosylation of …

The Z mutation (E342K) of α1-antitrypsin (α1-AT), carried by 4% of Northern Europeans,
predisposes to early onset of emphysema due to decreased functional α1-AT in the lung and …

The rugged folding landscapes of functional proteins puts them at risk of misfolding and
aggregation. Serine protease inhibitors, or serpins, are paradigms for this delicate balance …