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

Thermodynamic and kinetic characterization of the protein Z-dependent protease inhibitor (ZPI)-protein Z interaction reveals an unexpected role for ZPI Lys-239.

The Journal of biological chemistry - 10 Apr 2015

Huang Xin, Zhou Jian, Zhou Aiwu, Olson Steven T

Abstract excerpt

The anticoagulant serpin, protein Z-dependent protease inhibitor (ZPI), circulates in blood as a tight complex with its cofactor, protein Z (PZ), enabling it to function as a rapid inhibitor of membrane-associated factor Xa. Here, we show that N,N'-dimethyl-N-(acetyl)-N'-(7-nitrobenz-3-oxa-1,3-diazol-4-yl)ethylenediamine (NBD)-fluorophore-labeled K239C ZPI is a sensitive, moderately perturbing reporter of the...

Read the complete abstract on PubMed

Topics

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

Share to Azoles
Share to Binding, Competitive

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Blood Proteins

Share to Factor Xa

Share to Fluorescent Dyes

Share to Osmolar Concentration

Share to Serpins

Share to Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 25713144
DOI: 10.1074/jbc.M114.633479
PMCID: PMC4392287

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Thermodynamic and kinetic characterization of the protein Z-dependent protease inhibitor (ZPI)-protein Z interaction reveals an unexpected role for ZPI Lys-239.PMID 25713144Read ↗

Structural basis for catalytic activation of protein Z-dependent protease inhibitor (ZPI) by protein Z.Semantic proximity Read ↗

Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.Semantic proximity Read ↗

Identification of factor Xa residues critical for interaction with protein Z-dependent protease inhibitor: both active site and exosite interactions are required for inhibition.Semantic proximity Read ↗

Characterization of the protein Z-dependent protease inhibitor interactive-sites of protein Z.Semantic proximity Read ↗

Protein Z-dependent protease inhibitor deficiency produces a more severe murine phenotype than protein Z deficiency.Semantic proximity Read ↗

Tapping Into the Natural PZ-Independent Anticoagulant Function of ZPI to Inhibit Thrombosis With Minimal Effect on Hemostasis.Semantic proximity Read ↗

Two missense mutations identified in venous thrombosis patients impair the inhibitory function of the protein Z dependent protease inhibitor.Semantic proximity Read ↗

Protein Z, an anticoagulant protein with expanding role in reproductive biology.Semantic proximity Read ↗

Prothrombotic phenotype of protein Z deficiency.Semantic proximity Read ↗

Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity.Semantic proximity Read ↗

Interaction of factor IXa with factor VIIIa. Effects of protease domain Ca2+ binding site, proteolysis in the autolysis loop, phospholipid, and factor X.Semantic proximity Read ↗

Role of the activation peptide in the mechanism of protein C activation.Semantic proximity Read ↗

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