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

Reactivity of alpha 1-antitrypsin mutants against proteolytic enzymes of the kallikrein-kinin, complement, and fibrinolytic systems.

The Journal of biological chemistry - 25 Jun 1990

Patston P A, Roodi N, Schifferli J A, Bischoff R, Courtney M, Schapira M

Abstract excerpt

Increased extracellular proteolysis because of unregulated activation of blood coagulation, complement, and fibrinolysis is observed in thrombosis, shock, and inflammation. In the present study, we have examined whether the plasma kallikrein-kinin system, the classical pathway of complement, and the fibrinolytic system could be inhibited by alpha 1-antitrypsin reactive site mutants. Wild-type alpha 1-antitrypsin...

Topics

Amino Acid Sequence
Complement Inactivator Proteins
Fibrinolysis
Hemolysis
Humans
Kallikreins
Kinins
Molecular Sequence Data
Mutation
Peptide Hydrolases
Serpins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

alpha 1-Antitrypsin

Source

Identifiers

PMID: 2191958

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2191958-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Reactivity of alpha 1-antitrypsin mutants against proteolytic enzymes of the kallikrein-kinin, complement, and fibrinolytic systems.PMID 2191958Read ↗

The M358R variant of α(1)-proteinase inhibitor inhibits coagulation factor VIIa.Semantic proximity Read ↗

Recombinant C1 inhibitor P5/P3 variants display resistance to catalytic inactivation by stimulated neutrophils.Semantic proximity Read ↗

Altered specificities of genetically engineered alpha 1 antitrypsin variants.Semantic proximity Read ↗

Mutants of plasminogen activator inhibitor-1 designed to inhibit neutrophil elastase and cathepsin G are more effective in vivo than their endogenous inhibitors.Semantic proximity Read ↗

Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity.Semantic proximity Read ↗

Inhibition of activated protein C by recombinant alpha 1-antitrypsin variants with substitution of arginine or leucine for methionine358.Semantic proximity Read ↗

Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway.Semantic proximity Read ↗

Basic residues in the 37-loop of activated protein C modulate inhibition by protein C inhibitor but not by alpha(1)-antitrypsin.Semantic proximity Read ↗

COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization.Semantic proximity Read ↗

Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.Semantic proximity Read ↗

α1 -antitrypsin Pittsburgh and plasmin-mediated proteolysis.Semantic proximity Read ↗

Contributions of basic amino acids in the autolysis loop of factor XIa to serpin specificity.Semantic proximity Read ↗

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