Results 201 to 210 of about 34,502 (251)
High-throughput amino acid-level characterization of the interactions of plasminogen activator inhibitor-1 with variably divergent proteases. [PDF]
Protein SciHaynes LM +4 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
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
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 +2 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).
M A, Dunstone, James C, Whisstock
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.
Philip A, Patston +2 more
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources