Results 261 to 270 of about 20,002 (295)
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Journal of Leukocyte Biology, 2008
AbstractSerine protease inhibitors (serpins) are a family of proteins that are important in the regulation of several biological processes. This mainly involves the inhibition of serine proteases, although some serpins inhibit a different class of proteases or even function without inhibitory activity.
Michael Bots, Jan Paul Medema
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AbstractSerine protease inhibitors (serpins) are a family of proteins that are important in the regulation of several biological processes. This mainly involves the inhibition of serine proteases, although some serpins inhibit a different class of proteases or even function without inhibitory activity.
Michael Bots, Jan Paul Medema
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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.
James C. Whisstock +2 more
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Serpins: Development for Therapeutic Applications.
Methods in molecular biology, 2018Serine protease inhibitors, or serpins, function as central regulators for many vital processes in the mammalian body, maintaining homeostasis for clot formation and breakdown, immune responses, lung function, and hormone or central nervous system activity, among many others.
A. Lucas +4 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
Joanna Boncela, Czeslaw S. Cierniewski
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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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Structural insights into serpin—protease complexes reveal the inhibitory mechanism of serpins [PDF]
Nature Structural & Molecular Biology, 1997 Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins.
Jan Karolin +5 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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The Drosophila serpins: multiple functions in immunity and morphogenesis.
Methods in Enzymology, 2011Members 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 ...
J. Reichhart, D. Gubb, V. Leclerc
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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.
Péter Závodszky +6 more
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Serpins for diagnosis and therapy in cancer.
Cardiovascular & Haematological Disorders - Drug Targets, 2013Serine protease inhibitors (Serpins) play an important role in regulating a wide array of diverse biological activities, representing up to 2-10% of circulating plasma proteins.
Donghang Zheng +4 more
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