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Between immunosurveillance and immunopathology - Examples for mechanisms regulating cell-mediated cytotoxic activity [PDF]
, 2014 Ward, Beate
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Serpin structure, mechanism, and function.
Chemical Reviews, 2002AbstractFor Abstract see ChemInform Abstract in Full Text.
P. Gettins
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Serpin crystal structure and serpin polymer structure
Archives of Biochemistry and Biophysics, 2006Serpins are a family of structurally homologous proteins having metastable native structures. As a result, a serpin variant destabilized by mutation(s) has a tendency to undergo conformational changes leading to inactive forms, e.g., the latent form and polymer. Serpin polymers are involved in a number of conformational diseases.
Ewa Marszal, Andrew Shrake
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Methods, 2004
Mutagenesis represents a powerful methodology for the analysis of protein structural and functional relationships and dissection of complex protein-protein interactions. The suicide substrate-like inhibitory mechanism of the proteins of the serpin superfamily offers unique challenges for the design of mutagenesis studies.
Toni M, Antalis, Daniel A, Lawrence
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Mutagenesis represents a powerful methodology for the analysis of protein structural and functional relationships and dissection of complex protein-protein interactions. The suicide substrate-like inhibitory mechanism of the proteins of the serpin superfamily offers unique challenges for the design of mutagenesis studies.
Toni M, Antalis, Daniel A, Lawrence
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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.
Frank C. Church +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.
Frank C. Church +2 more
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Crystallography of Serpins and Serpin Complexes
2011The serpin superfamily of protease inhibitors undergoes a remarkable conformational change to inhibit target proteases. To date, over 80 different serpin crystal structures have been determined. These data reveal that the serpin monomer can adopt five different conformations (native, partially inserted native, δ-form, latent, and cleaved).
Michelle A. Dunstone +2 more
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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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, 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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