Pages that link to "Q68189070"
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The following pages link to Conformational stability of the covalent complex between elastase and alpha 1-proteinase inhibitor (Q68189070):
Displaying 7 items.
- Structure of a serpin-protease complex shows inhibition by deformation (Q24290459) (← links)
- Active site distortion is sufficient for proteinase inhibition by serpins: structure of the covalent complex of alpha1-proteinase inhibitor with porcine pancreatic elastase (Q24297624) (← links)
- A serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism (Q30168478) (← links)
- Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles (Q34201670) (← links)
- The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium (Q43638841) (← links)
- A comparison between SDS-PAGE and size exclusion chromatography as analytical methods for determining product composition in protein conjugation reactions (Q44176552) (← links)
- Involvement of sulfhydryl groups in the stable fluorescent derivatization of proteins by o-phthalaldehyde (Q72289596) (← links)