Comparison of the properties of rare variants of alpha1-proteinase inhibitor expressed in COS-1 cells and assessment of their potential as risk factors in human disease.

doi:10.1016/j.bbadis.2005.03.010

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

Back to search

Article

Comparison of the properties of rare variants of alpha1-proteinase inhibitor expressed in COS-1 cells and assessment of their potential as risk factors in human disease.

Biochimica et biophysica acta - 10 Jun 2005

Ray Shahla, Mickleborough Timothy D, Brown Jerry L

Abstract excerpt

Among the more than 75 known variants of alpha(1)-proteinase inhibitor, a sub-population of rare, point mutations causing single amino acid replacements have been identified and classified as "at risk" alleles for development of pulmonary disease. In most cases, it is not clear how the amino acid replacements typical of these variants change the properties of the inhibitor to increase risk of disease in the...

Topics

Amino Acid Substitution
Animals
COS Cells
Chlorocebus aethiops
Electrophoresis, Polyacrylamide Gel
Fluorescent Antibody Technique
Genetic Predisposition to Disease
Genetic Variation
Immunoprecipitation
Lung Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Oligonucleotides

Plasmids

Point Mutation

Transfection

alpha 1-Antitrypsin

Source

Open in PubMed

Identifiers

PMID: 15949707
DOI: 10.1016/j.bbadis.2005.03.010

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

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

discussions

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

Comparison of the properties of rare variants of alpha1-proteinase inhibitor expressed in COS-1 cells and assessment of their potential as risk factors in human disease.PMID 15949707Read ↗

Characterization of Novel Missense Variants of SERPINA1 Gene Causing Alpha-1 Antitrypsin DeficiencySemantic proximity Read ↗

The role of proteases, endoplasmic reticulum stress and SERPINA1 heterozygosity in lung disease and α-1 anti-trypsin deficiency.Semantic proximity Read ↗

Construction and expression of alpha 1-proteinase inhibitor mutants and the effects of these mutations on secretion of the variant inhibitors.Semantic proximity Read ↗

Molecular characterisation of the defective alpha 1-antitrypsin alleles PI Mwurzburg (Pro369Ser), Mheerlen (Pro369Leu), and Q0lisbon (Thr68Ile).Semantic proximity Read ↗

Deletion of Serpina1a, a murine α1-antitrypsin ortholog, results in embryonic lethality.Semantic proximity Read ↗

Molecular mechanisms of alpha1-antitrypsin null alleles.Semantic proximity Read ↗

Probing of the reactive center loop region of alpha-1-antitrypsin by mutagenesis predicts new type-2 dysfunctional variants.Semantic proximity Read ↗

Serine proteinase inhibitor therapy in alpha(1)-antitrypsin inhibitor deficiency and cystic fibrosis.Semantic proximity Read ↗

A novel SERPINA1 mutation causing serum alpha(1)-antitrypsin deficiency.Semantic proximity Read ↗

alpha1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies.Semantic proximity Read ↗

Degradation of mutant proteins, underlying "loss of function" phenotypes, plays a major role in genetic disease.Semantic proximity Read ↗

A naturally occurring nonpolymerogenic mutant of alpha 1-antitrypsin characterized by prolonged retention in the endoplasmic reticulum.Semantic proximity Read ↗

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