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Article

The distal hinge of the reactive site loop and its proximity: a target to modulate plasminogen activator inhibitor-1 activity.

The Journal of biological chemistry - 30 Nov 2001

Bijnens A P, Gils A, Stassen J M, Komissarov A A, Knockaert I, Brouwers E, Shore J D, Declerck P J

Abstract excerpt

The serpin plasminogen activator inhibitor type 1 (PAI-1) plays a regulatory role in various physiological processes (e.g. fibrinolysis and pericellular proteolysis) and forms a potential target for therapeutic interventions. In this study we identified the epitopes of three PAI-1 inhibitory monoclonal antibodies (MA-44E4, MA-42A2F6, and MA-56A7C10). Differential cross-reactivities of these monoclonals with PAI-1...

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PMID: 11559698
DOI: 10.1074/jbc.M103077200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The distal hinge of the reactive site loop and its proximity: a target to modulate plasminogen activator inhibitor-1 activity.PMID 11559698Read ↗

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Discovery and characterisation of an antibody that selectively modulates the inhibitory activity of plasminogen activator inhibitor-1Semantic proximity Read ↗

Subtle structural differences between human and mouse PAI-1 reveal the basis for biochemical differences.Semantic proximity Read ↗

Elucidation of the binding regions of PAI-1 neutralizing antibodies using chimeric variants of human and rat PAI-1.Semantic proximity Read ↗

Plasminogen activator inhibitor-2 is highly tolerant to P8 residue substitution--implications for serpin mechanistic model and prediction of nsSNP activities.Semantic proximity Read ↗

Distal hinge of plasminogen activator inhibitor-1 involves its latency transition and specificities toward serine proteases.Semantic proximity Read ↗

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