Back to search

Article

Both terminal misfolding and polymerisation contribute to disease-relevant responses in cell models of α <sub>1</sub> -antitrypsin deficiency-associated liver disease

2025-10-01

Abstract excerpt

Polymerisation of α 1 -antitrypsin within hepatocytes is considered central to the pathogenesis of α 1 -antitrypsin deficiency-associated liver fibrosis, most commonly in homozygotes for the Z (p.Glu342Lys) allele. Polymerisation proceeds via self-association of monomeric intermediate states. In parallel, >50% of synthesised Z α 1 -antitrypsin is instead recognized as terminally-misfolded and degraded. It is un...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
f6f03a5a-2b42-59ec-8398-eb9bbea54825
DOI
10.1101/2025.09.30.679226
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Both terminal misfolding and polymerisation contribute to disease-relevant responses in cell models of α <sub>1</sub> -antitrypsin deficiency-associated liver diseaseDOI 10.1101/2025.09.30.679226
Z-AAT impairs organelle homeostasis and reduces adaptive response to lipids in alpha-1 antitrypsin deficiency modelsSemantic proximity
Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha1-antitrypsin deficiency.Semantic proximity
hiPSC hepatocyte model demonstrates the role of unfolded protein response and inflammatory networks in α1-antitrypsin deficiencySemantic proximity
Liver organoids reproduce alpha-1 antitrypsin deficiency-related liver diseaseSemantic proximity
Endoplasmic reticulum stress--a double edged sword for Z alpha-1 antitrypsin deficiency hepatoxicity.Semantic proximity
The pathological Trento variant of alpha-1-antitrypsin (E75V) shows nonclassical behaviour during polymerization.Semantic proximity
Preventing and reversing the cellular consequences of Z alpha-1 antitrypsin accumulation by targeting s4A.Semantic proximity
Alpha1-antitrypsin deficiency. 4: Molecular pathophysiology.Semantic proximity
Three new alpha1-antitrypsin deficiency variants help to define a C-terminal region regulating conformational change and polymerization.Semantic proximity
Alpha-1-antitrypsin deficiency: diagnosis, pathophysiology, and management.Semantic proximity
Development of a small molecule that corrects misfolding and increases secretion of Z α <sub>1</sub> -antitrypsinSemantic proximity
Liver disease in alpha-1 antitrypsin deficiency: current understanding and future therapy.Semantic proximity
Select a neighboring publication to make it the new centre.