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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 …
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 …
opsonization - ScienceDirect Skip to main contentSkip to article Elsevier logo Journals & Books …
Innate immune responses of a lepidopteran insect, Manduca sexta
Many innate immune mechanisms are conserved throughout the animal kingdom. Manduca
sexta, a widely used model for insect biochemical research, employs these mechanisms to …
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
We present a comprehensive alignment and phylogenetic analysis of the serpins, a
superfamily of proteins with known members in higher animals, nematodes, insects, plants …
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 …
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 …
inhibitors may exist in plasma or in hemocyte granules. Serine proteinase inhibitors from the …
Serpins in arthropod biology
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 …
physiological functions in arthropods. Herein, we review the field of serpins in arthropod …
The clip-domain family of serine proteinases in arthropods
Extracellular serine proteinase cascades have evolved in vertebrates and invertebrates to
mediate rapid, local reactions to physiological or pathological cues. In mammalian plasma, a …
mediate rapid, local reactions to physiological or pathological cues. In mammalian plasma, a …
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 …
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
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 …
inflammatory, coagulation, fibrinolytic, and complement cascades. An inherent part of their …