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

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

European journal of biochemistry - 1 Dec 2001

Hansen M, Busse M N, Andreasen P A

Abstract excerpt

The serpins are of general protein chemical interest due to their ability to undergo a large conformational change consisting of the insertion of the reactive centre loop (RCL), which becomes strand 4, into the central beta sheet A. To make space for the incoming RCL, the 'shutter region' opens by the beta strands 3A and 5A sliding apart over the underlying alpha helix B. Loop insertion occurs during the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to In Vitro Techniques

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Plasminogen Activator Inhibitor 1

Share to Protein Structure, Secondary

Share to Recombinant Proteins

Share to Urokinase-Type Plasminogen Activator

Share to Vitronectin

Source

Identifiers

PMID: 11733024
DOI: 10.1046/j.0014-2956.2001.02582.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Importance of the amino-acid composition of the shutter region of plasminogen activator inhibitor-1 for its transitions to latent and substrate forms.PMID 11733024Read ↗

The Molecular Basis for Anti-Proteolytic and Non-Proteolytic Functions of Plasminogen Activator Inhibitor Type-1: Roles of the Reactive Centre Loop, the Shutter Region, the Flexible Joint Region and the Small Serpin FragmentSemantic proximity Read ↗

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

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

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

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

Remarkable extension of PAI-1 half-life surprisingly brings no changes to its structure.Semantic proximity Read ↗

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

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

The structural basis for the pathophysiological relevance of PAI-1 in cardiovascular diseases and the development of potential PAI-1 inhibitorsSemantic proximity Read ↗

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

Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease.Semantic proximity Read ↗

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