Acid Denaturation of α1-Antitrypsin: Characterization of a Novel Mechanism of Serpin Polymerization

This publication has 50 references indexed in Scilit:

• Probing the equilibrium denaturation of the serpin α1-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state
  Journal of Molecular Biology, 2001
• Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling
  Biophysical Journal, 2000
• α1-Antitrypsin Polymerisation Can Occur by both Loop A and C Sheet Mechanisms
  Biochemical and Biophysical Research Communications, 1998
• Wild-type α1-antitrypsin is in the canonical inhibitory conformation
  Journal of Molecular Biology, 1998
• Folding Pathway of Human α1-Antitrypsin: Characterization of an Intermediate That Is Active but Prone to Aggregation
  Biochemical and Biophysical Research Communications, 1996
• Fluorescence-detected polymerization kinetics of human α1-antitrypsin
  Protein Journal, 1996
• Trypsin complexed with α₁‐proteinase inhibitor has an increased structural flexibility
  FEBS Letters, 1995
• The molecular basis of α1-antichymotrypsin deficiency in a heterozygote with liver and lung disease
  Journal of Hepatology, 1993
• Effects of glycosylation on the folding and stability of human, recombinant and cleaved α1-antitrypsin
  Journal of Molecular Biology, 1992
• Risk of Cirrhosis and Primary Liver Cancer in Alpha₁-Antitrypsin Deficiency
  New England Journal of Medicine, 1986