Point mutations cause members of the serine protease inhibitor (serpin) superfamily to
undergo a novel conformational transition, forming ordered polymers. These polymers …

The molecular basis of α1-antitrypsin deficiency is reviewed and is shown to be due to the
accumulation of mutant protein as ordered polymers within the endoplasmic reticulum of …

INTRODUCTION Enzymes possess extraordinary catalytic proficiency and specificity. These
properties ultimately derive from interactions not just between the active-site residues and …

The low molecular weight plasma proteome and its biological relevance are not well
defined; therefore, experiments were conducted to directly sequence and identify peptides …

Serpins are a widely distributed family of high molecular mass protein proteinase inhibitors
that can inhibit both serine and cysteine proteinases by a remarkable mechanism-based …

Computational simulations of protein folding can be used to interpret experimental folding
results, to design new folding experiments, and to test the effects of mutations and small …

Proteinases and their inhibitors play important roles in neural development, homeostasis
and disease. Neuroserpin is a member of the serine proteinase inhibitor (serpin) superfamily …

Serpins use an extraordinary mechanism of protease inhibition that depends on a rapid and
marked conformational change and causes destruction of the covalently linked protease …

The serpinopathies are among a diverse set of conformational diseases that involve the
aberrant self-association of proteins into ordered aggregates. α1-Antitrypsin deficiency is the …

The serpins (serine proteinase inhibitors) are structurally similar but functionally diverse
proteins that fold into a conserved structure and employ a unique suicide substrate‐like …