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Journal of Proteome Research|March 21, 2003
Insight into residues critical for antithrombin function from analysis of an expanded database of sequences that includes frog, turtle, and ostrich antithrombinsMarija Backovic, Peter G W GettinsMethods (San Diego, Calif.)|December 31, 2003
Use of NMR to study serpin functionPeter G W Gettins, Marija Backovic, Francis C PetersonProtein Science : a Publication of the Protein Society|April 23, 2002
Structural similarity of the covalent complexes formed between the serpin plasminogen activator inhibitor-1 and the arginine-specific proteinases trypsin, LMW u-PA, HMW u-PA, and t-PA: use of site-specific fluorescent probes of local environmentMarija Backovic, Efstratios Stratikos, Daniel A Lawrence, et al.FEBS Letters|July 19, 2002
The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanismPeter G W GettinsMethods in Molecular Biology (Clifton, N.J.)|January 29, 2016
Stable Drosophila Cell Lines: An Alternative Approach to Exogenous Protein ExpressionMarija Backovic, Thomas KreyCurrent Opinion in Structural Biology|April 10, 2009
Class III viral membrane fusion proteinsMarija Backovic, Theodore S JardetzkyThe Journal of Biological Chemistry|September 20, 2006
Three complement-like repeats compose the complete alpha2-macroglobulin binding site in the second ligand binding cluster of the low density lipoprotein receptor-related proteinKlavs Dolmer, Peter G W GettinsThe Journal of Biological Chemistry|November 1, 2003
alpha1-Proteinase inhibitor forms initial non-covalent and final covalent complexes with elastase analogously to other serpin-proteinase pairs, suggesting a common mechanism of inhibitionJózsef Dobó, Peter G W GettinsThe Biochemical Journal|December 21, 2011
A proximal pair of positive charges provides the dominant ligand-binding contribution to complement-like domains from the LRP (low-density lipoprotein receptor-related protein)Peter G W Gettins, Klavs DolmerThe Journal of Biological Chemistry|November 12, 2015
The High Affinity Binding Site on Plasminogen Activator Inhibitor-1 (PAI-1) for the Low Density Lipoprotein Receptor-related Protein (LRP1) Is Composed of Four Basic ResiduesPeter G W Gettins, Klavs DolmerPageof 9