Results 191 to 200 of about 23,239 (235)
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2011
Members of the serpin superfamily of proteins have been found in all living organisms, although rarely in bacteria or fungi. They have been extensively studied in mammals, where many rapid physiological responses are regulated by inhibitory serpins. In addition to the inhibitory serpins, a large group of noninhibitory proteins with a conserved serpin ...
Jean Marc Reichhart +2 more
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Members of the serpin superfamily of proteins have been found in all living organisms, although rarely in bacteria or fungi. They have been extensively studied in mammals, where many rapid physiological responses are regulated by inhibitory serpins. In addition to the inhibitory serpins, a large group of noninhibitory proteins with a conserved serpin ...
Jean Marc Reichhart +2 more
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Methods, 2004
One of the more common features of serpins is the ability to bind various ligands. Ligand binding can occur so that the inhibitory properties of the serpin are regulated, so that the serpin can be localized, or to produce or modulate some other biological function of the serpin.
Philip A, Patston +2 more
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One of the more common features of serpins is the ability to bind various ligands. Ligand binding can occur so that the inhibitory properties of the serpin are regulated, so that the serpin can be localized, or to produce or modulate some other biological function of the serpin.
Philip A, Patston +2 more
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An atlas of serpin conformations
Trends in Biochemical Sciences, 1998The serpins are a family of proteins that inhibit chymotrypsin-like serine proteinases, with an unusual mechanism involving a large conformational change known as the stressed-->relaxed (S-->R) transition. This article is a guide to the known serpin conformations and their biological significance.
J, Whisstock, R, Skinner, A M, Lesk
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Serpin Polymerization In Vitro
2011Serpin polymerization is an event which generally occurs within living tissue as a consequence of a folding defect caused by point mutations. Major advances in cell biology and imaging have allowed detailed studies into subcellular localization, processing, and clearance of serpin polymers, but to understand the molecular basis of the misfolded state ...
James A, Huntington, Masayuki, Yamasaki
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Serpins and the Complement System
2011C1-inhibitor (serpin G1) is a 105 kDa inhibitor which functions as a major antiinflammatory protein in the body. It has its effects via inhibition of the proteases of the complement system and contact system of coagulation, as well as several direct effects mediated by its unique highly glycosylated N-terminal domain.
László, Beinrohr +6 more
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Serpin–Glycosaminoglycan Interactions
2011Serpins (serine protease inhibitors) have traditionally been grouped together based on structural homology. They share common structural features of primary sequence, but not all serpins require binding to cofactors in order to achieve maximal protease inhibition. In order to obtain physiologically relevant rates of inhibition of target proteases, some
Chantelle M, Rein +2 more
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Maspin: A Tumor Suppressing Serpin
1996Maspin, a serpin found in mammary epithelial cells, has been shown to have tumor suppressor activity. The gene is expressed in normal human mammary epithelial cells but down-regulated in invasive breast carcinomas. Similar patterns of expression at the RNA and protein levels are seen by Northern analysis with cells grown in culture and by ...
R, Sager +3 more
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2013
Serpins (serine proteinase inhibitors) are the largest superfamily of protease inhibitors. The serpins are structurally similar but functionally diverse proteins that fold into a conserved structure and employ a unique suicide substrate-like inhibitory mechanism. Most of them act as classical protease inhibitors, but there are also serpins that inhibit
Czeslaw S. Cierniewski, Joanna Boncela
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Serpins (serine proteinase inhibitors) are the largest superfamily of protease inhibitors. The serpins are structurally similar but functionally diverse proteins that fold into a conserved structure and employ a unique suicide substrate-like inhibitory mechanism. Most of them act as classical protease inhibitors, but there are also serpins that inhibit
Czeslaw S. Cierniewski, Joanna Boncela
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Genetic engineering and the serpins
BioEssays, 1988D R, Boswell, R W, Carrell
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