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Peter G W Gettins

Showing results (1-10 of 48) with videos related to

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FEBS Letters|July 19, 2002
The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanismPeter G W Gettins
Chemical Reviews|December 12, 2002
Serpin structure, mechanism, and functionPeter G W Gettins
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 Gettins
The 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 Gettins
The 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 Gettins
Thescientificworldjournal|July 6, 2018
Insight into Residues Critical for Antithrombin Function from an Expanded Database of Sequences That Includes Frog, Turtle and Ostrich AntithrombinsMarija Backovic, Peter G W Gettins
The 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 Dolmer
The 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 Dolmer
The Journal of Biological Chemistry|February 16, 2012
How the serpin α1-proteinase inhibitor foldsKlavs Dolmer, Peter G W Gettins
The Biochemical Journal|July 5, 2007
Human alpha2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3Ninh Doan, Peter G W Gettins
Pageof 5

Showing results (1-10 of 48) with videos related to

Sort By:
Pageof 5
FEBS Letters|July 19, 2002
The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanismPeter G W Gettins
Chemical Reviews|December 12, 2002
Serpin structure, mechanism, and functionPeter G W Gettins
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 Gettins
The 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 Gettins
The 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 Gettins
Thescientificworldjournal|July 6, 2018
Insight into Residues Critical for Antithrombin Function from an Expanded Database of Sequences That Includes Frog, Turtle and Ostrich AntithrombinsMarija Backovic, Peter G W Gettins
The 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 Dolmer
The 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 Dolmer
The Journal of Biological Chemistry|February 16, 2012
How the serpin α1-proteinase inhibitor foldsKlavs Dolmer, Peter G W Gettins
The Biochemical Journal|July 5, 2007
Human alpha2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3Ninh Doan, Peter G W Gettins
Pageof 5