Results 191 to 200 of about 12,528 (235)
Hemolymph protease-17b activates proHP6 to stimulate melanization and Toll signaling in Manduca sexta. [PDF]
Insect Biochem Mol BiolWang Y, Jiang H.
europepmc +1 more source
Applications of Surface Plasmon Resonance in Heparan Sulfate Interactome Research. [PDF]
BiomedicinesDatta P, Dordick JS, Zhang F.
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IJMS Special Issue-Molecular Mechanisms of Diabetic Kidney Disease 2.0. [PDF]
Int J Mol SciPetrica L.
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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
Thomas Hugh Roberts, Robert Fluhr
exaly +2 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
Thomas Hugh Roberts, Robert Fluhr
exaly +2 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
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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
openaire +2 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
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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).
M A, Dunstone, James C, Whisstock
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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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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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