Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Specific interactions of serpins in their native forms attenuate their conformational transitions.

Protein science : a publication of the Protein Society - 1 Aug 2007

Na Yu-Ran, Im Hana

Abstract excerpt

Plasminogen activator inhibitor-1 (PAI-1) belongs to the serine protease inhibitor (serpin) protein superfamily. Serpins are unique in that their native forms are not the most thermodynamically stable conformation; instead, a more stable, latent conformation exists. During the transition to the latent form, the first strand of beta-sheet C (s1C) in the serpin is peeled away from the beta-sheet, and the reactive...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Kinetics
Share to Mutagenesis, Site-Directed
Share to Plasminogen Activator Inhibitor 1

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Conformation

Share to Protein Denaturation

Share to Protein Folding

Share to Recombinant Proteins

Share to Serine Proteinase Inhibitors

Source

Open in PubMed Open full text

Identifiers

PMID: 17600149
DOI: 10.1110/ps.072838107
PMCID: PMC2203359

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Specific interactions of serpins in their native forms attenuate their conformational transitions.PMID 17600149Read ↗

Structural factors affecting the choice between latency transition and polymerization in inhibitory serpins.Semantic proximity Read ↗

Single fluorescence probes along the reactive center loop reveal site-specific changes during the latency transition of PAI-1.Semantic proximity Read ↗

Importance of the amino-acid composition of the shutter region of plasminogen activator inhibitor-1 for its transitions to latent and substrate forms.Semantic proximity Read ↗

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

The native metastability and misfolding of serine protease inhibitors.Semantic proximity Read ↗

Cellular folding pathway of a metastable serpin.Semantic proximity Read ↗

A protein family under 'stress' - serpin stability, folding and misfolding.Semantic proximity Read ↗

The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion.Semantic proximity Read ↗

Regulation of protein function by native metastability.Semantic proximity Read ↗

Structural differences between active forms of plasminogen activator inhibitor type 1 revealed by conformationally sensitive ligands.Semantic proximity Read ↗

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

Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.