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Infectious parvovirus B19 circulates in the blood coated with active host protease inhibitors. [PDF]
Nat CommunLee H +9 more
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Morphotype-Specific Antifungal Defense in <i>Cacopsylla chinensis</i> Arises from Metabolic and Immune Network Restructuring. [PDF]
InsectsJi J, Gao X, Hu Z, Ma R, Zhao L.
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Exploring Genetic Determinants: A Comprehensive Analysis of Serpin B Family SNPs and Prognosis in Glioblastoma Multiforme Patients. [PDF]
Cancers (Basel)Al-Khatib SM +7 more
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Integrative view of serpins in health and disease: the contribution of serpinA3.
American Journal of Physiology - Cell Physiology, 2020Serpins are a superfamily of proteins characterized by their common function as serine protease inhibitors. So far, 36 serpins from nine clades have been identified.
Andrea Sánchez-Navarro +3 more
semanticscholar +1 more source
, 2015
The serpins are a family of structurally conserved protease inhibitors found mainly in the animal and plant kingdoms. This chapter will focus on the evolution of plant serpins brought to light by mining of the growing number of whole plant genomes. Our analysis shows remarkable diversification of plant serpins as compared to those in animals. Indeed, a
Maja Cohen, T. H. Roberts, R. Fluhr
semanticscholar +3 more sources
The serpins are a family of structurally conserved protease inhibitors found mainly in the animal and plant kingdoms. This chapter will focus on the evolution of plant serpins brought to light by mining of the growing number of whole plant genomes. Our analysis shows remarkable diversification of plant serpins as compared to those in animals. Indeed, a
Maja Cohen, T. H. Roberts, R. Fluhr
semanticscholar +3 more sources
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
openaire +3 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +3 more sources
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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