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

Altered specificities of genetically engineered alpha 1 antitrypsin variants.

Protein engineering - 1 Jan 2000

Jallat S, Carvallo D, Tessier L H, Roecklin D, Roitsch C, Ogushi F, Crystal R G, Courtney M

Abstract excerpt

Seven active site variants of human alpha 1-antitrypsin (alpha 1AT) were produced in Escherichia coli following site-specific mutagenesis of the alpha 1AT complementary DNA. alpha 1AT (Ala358), alpha 1AT (Ile358) and alpha 1AT (Val358) were efficient inhibitors of both neutrophil and pancreatic elastases, but not of cathepsin G. alpha 1AT (Ala356, Val358) and alpha 1AT (Phe358) specifically inhibited pancreatic...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence
Share to Binding Sites

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

Share to SDS gene

Share to Genetic Variation

Share to In Vitro Techniques

Share to Molecular Sequence Data

Share to Serine Endopeptidases

Source

Identifiers

PMID: 3509863
DOI: 10.1093/protein/1.1.29

Genes

SDS

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

Altered specificities of genetically engineered alpha 1 antitrypsin variants.PMID 3509863Read ↗

Synthesis in E. coli of alpha 1-antitrypsin variants of therapeutic potential for emphysema and thrombosis.Semantic proximity Read ↗

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

Application of directed evolution and back-to-consensus algorithms to human alpha1-antitrypsin leads to diminished anti-protease activity and augmented anti-inflammatory activities.Semantic proximity Read ↗

Detection of genetic variants of alpha 1-antitrypsin with site-specific monoclonal antibodies.Semantic proximity Read ↗

Purification and biochemical characterization of recombinant alpha 1-antitrypsin variants expressed in Escherichia coli.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 ↗

Bioengineering: alpha 1-proteinase inhibitor site-specific mutagenesis. The prospect for improving the inhibitor.Semantic proximity Read ↗

Evaluation of phage display system and leech-derived tryptase inhibitor as a tool for understanding the serine proteinase specificities.Semantic proximity Read ↗

Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins.Semantic proximity Read ↗

Impact of mutations at the P4 and P5 positions on the reaction of antithrombin with thrombin and elastase.Semantic proximity Read ↗

A new library of alpha-lytic protease S1 mutants generated by combinatorial random substitution.Semantic proximity Read ↗

Alpha 1-antitrypsin variants produced by recombinant DNA: differences in elastase inhibitory activity and resistance to oxidant agents.Semantic proximity Read ↗

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