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Article

Deep mutational scanning and massively parallel kinetics of plasminogen activator inhibitor-1 functional stability to probe its latency transition.

The Journal of biological chemistry - 1 Dec 2022

Haynes Laura M, Huttinger Zachary M, Yee Andrew, Kretz Colin A, Siemieniak David R, Lawrence Daniel A, Ginsburg David

Abstract excerpt

Plasminogen activator inhibitor-1 (PAI-1), a member of the serine protease inhibitor superfamily of proteins, is unique among serine protease inhibitors for exhibiting a spontaneous conformational change to a latent or inactive state. The functional half-life for this transition at physiologic temperature and pH is ∼1 to 2 h. To better understand the molecular mechanisms underlying this transition, we now report...

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Identifiers

PMID: 36257408
DOI: 10.1016/j.jbc.2022.102608
PMCID: PMC9667310

Provenance

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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