Serpin structure, mechanism, and function

PGW Gettins - Chemical reviews, 2002 - ACS Publications
Serpins are a superfamily of proteins, whose membership is based on the presence of a
single common core domain consisting of three β-sheets and 8-9 R-helices, and with a set of …

Cell-mediated immunity in arthropods: hematopoiesis, coagulation, melanization and opsonization

P Jiravanichpaisal, BL Lee, K Söderhäll - Immunobiology, 2006 - Elsevier
Cell-mediated immunity in arthropods: Hematopoiesis, coagulation, melanization and
opsonization - ScienceDirect Skip to main contentSkip to article Elsevier logo Journals & Books …

Innate immune responses of a lepidopteran insect, Manduca sexta

MR Kanost, H Jiang, XQ Yu - Immunological reviews, 2004 - Wiley Online Library
Many innate immune mechanisms are conserved throughout the animal kingdom. Manduca
sexta, a widely used model for insect biochemical research, employs these mechanisms to …

Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function

JA Irving, RN Pike, AM Lesk, JC Whisstock - Genome research, 2000 - genome.cshlp.org
We present a comprehensive alignment and phylogenetic analysis of the serpins, a
superfamily of proteins with known members in higher animals, nematodes, insects, plants …

Structure and properties of ovalbumin

JA Huntington, PE Stein - … of Chromatography B: Biomedical Sciences and …, 2001 - Elsevier
Ovalbumin is a protein of unknown function found in large quantities in avian egg-white.
Surprisingly, ovalbumin belongs to the serpin family although it lacks any protease inhibitory …

Serine proteinase inhibitors in arthropod immunity

MR Kanost - Developmental & Comparative Immunology, 1999 - Elsevier
Arthropod hemolymph contains proteins with serine proteinase inhibitory activity. These
inhibitors may exist in plasma or in hemocyte granules. Serine proteinase inhibitors from the …

The clip-domain family of serine proteinases in arthropods

H Jiang, MR Kanost - Insect biochemistry and molecular biology, 2000 - Elsevier
Extracellular serine proteinase cascades have evolved in vertebrates and invertebrates to
mediate rapid, local reactions to physiological or pathological cues. In mammalian plasma, a …

Serpins in arthropod biology

DA Meekins, MR Kanost, K Michel - Seminars in cell & developmental …, 2017 - Elsevier
Serpins are the largest known family of serine proteinase inhibitors and perform a variety of
physiological functions in arthropods. Herein, we review the field of serpins in arthropod …

Structural basis of the endoproteinase–protein inhibitor interaction

W Bode, R Huber - Biochimica et Biophysica Acta (BBA)-Protein Structure …, 2000 - Elsevier
Proteolytic enzymes are potentially hazardous to their protein environment, so that their
activity must be carefully controlled. Living organisms use protein inhibitors as a major tool …

Topography of a 2.0 Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease

PR Elliott, XY Pei, TR Dafforn, DA Lomas - Protein Science, 2000 - cambridge.org
Members of the serpin family of serine proteinase inhibitors play important roles in the
inflammatory, coagulation, fibrinolytic, and complement cascades. An inherent part of their …