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

SERPINA1 long transcripts produce non-secretory alpha1-antitrypsin isoform: In vitro translation in living cells.

International journal of biological macromolecules - 30 Jun 2023

Maslakova A A, Golyshev S A, Potashnikova D M, Moisenovich A M, Orlovsky I V, Smirnova O V, Rubtsov M A

Abstract excerpt

SERPINA1 is a well-studied serpin gene due to its dramatic impact on human health. Translation initiation at the main SERPINA1 start codon produces the only known alpha1-antitrypsin (AAT) isoform intended for secretion. AAT performs essential functions by inhibiting proteases and modulating immunity. However, SERPINA1 expression at the level of translation is not sufficiently studied. Here we hypothesize that the...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to alpha 1-Antitrypsin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to alpha 1-Antitrypsin Deficiency

Share to Codon, Initiator

Share to Protein Isoforms

Source

Identifiers

PMID: 37086761
DOI: 10.1016/j.ijbiomac.2023.124433

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

SERPINA1 long transcripts produce non-secretory alpha1-antitrypsin isoform: In vitro translation in living cells.PMID 37086761Read ↗

Towards unveiling the nature of short SERPINA1 transcripts: Avoiding the main ORF control to translate alpha1-antitrypsin C-terminal peptides.Semantic proximity Read ↗

Altered polyadenylation site usage in SERPINA1 3’UTR in response to cellular stress affects A1AT protein expressionSemantic proximity Read ↗

Translational Control of Secretory Proteins in Health and Disease.Semantic proximity Read ↗

Shortening of 3’ UTRs in most cell types composing tumor tissues implicates alternative polyadenylation in protein metabolismSemantic proximity Read ↗

A quantitative study on splice variants of N-acylethanolamine acid amidase in human prostate cancer cells and other cells.Semantic proximity Read ↗

Translational regulation of cell invasion through extracellular matrix—an emerging role for ribosomesSemantic proximity Read ↗

Exploring STEAP1 Expression in Prostate Cancer Cells in Response to Androgen Deprivation and in Small Extracellular VesiclesSemantic proximity Read ↗

A translation control reporter system (TCRS) for the analysis of translationally controlled processes in the vertebrate cell.Semantic proximity Read ↗

The assembly of cancer-specific ribosomes by the lncRNA <i>LISRR</i> suppresses melanoma anti-tumour immunitySemantic proximity Read ↗

Alternative transcripts of the SERPINA1 gene in alpha-1 antitrypsin deficiency.Semantic proximity Read ↗

Human protein secretory pathway genes are expressed in a tissue-specific pattern to match processing demands of the secretomeSemantic proximity Read ↗

Translational control in endothelial cells.Semantic proximity Read ↗

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