The formation of ordered Z (Glu342Lys) α1‐antitrypsin polymers in hepatocytes is central to liver disease in α1‐antitrypsin deficiency. In vitro experiments have identified an intermediate conformational state (M*) that precedes polymer formation but this has yet to be identified in vivo. Moreover, the mechanism of polymer formation and their fate in cells have been incompletely characterised. We have used cell models of disease in conjunction with conformation‐selective monoclonal antibodies and a small molecule inhibitor of polymerization to define the dynamics of polymer formation, accumulation and secretion. Pulse‐chase experiments demonstrate that Z α1‐antitrypsin accumulates as short chain polymers that partition with soluble cellular...
Mutant Z α1-antitrypsin (E342K) accumulates as polymers within the endoplasmic reticulum (ER) of hep...
α1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pulmonary ...
The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self...
The formation of ordered Z (Glu342Lys) α1 -antitrypsin polymers in hepatocytes is central to liver d...
Severe α1‐antitrypsin deficiency results from the Z allele (Glu342Lys) that causes the accumulation ...
Abstract Severe α1‐antitrypsin deficiency results from the Z allele (Glu342Lys) that causes the accu...
The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self...
The common severe Z mutation (E342K) of α1-antitrypsin forms intracellular polymers that are associa...
Severe α1 -antitrypsin deficiency results from the Z allele (Glu342Lys) that causes the accumulation...
The common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that are reta...
The Z mutant of α1-antitrypsin (Glu342Lys) causes a domain swap and the formation of intrahepatic po...
The common severe Z mutation (E342K) of alpha(1)-antitrypsin forms intracellular polymers that are a...
AbstractThe common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that ...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
α1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pulmonary ...
Mutant Z α1-antitrypsin (E342K) accumulates as polymers within the endoplasmic reticulum (ER) of hep...
α1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pulmonary ...
The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self...
The formation of ordered Z (Glu342Lys) α1 -antitrypsin polymers in hepatocytes is central to liver d...
Severe α1‐antitrypsin deficiency results from the Z allele (Glu342Lys) that causes the accumulation ...
Abstract Severe α1‐antitrypsin deficiency results from the Z allele (Glu342Lys) that causes the accu...
The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self...
The common severe Z mutation (E342K) of α1-antitrypsin forms intracellular polymers that are associa...
Severe α1 -antitrypsin deficiency results from the Z allele (Glu342Lys) that causes the accumulation...
The common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that are reta...
The Z mutant of α1-antitrypsin (Glu342Lys) causes a domain swap and the formation of intrahepatic po...
The common severe Z mutation (E342K) of alpha(1)-antitrypsin forms intracellular polymers that are a...
AbstractThe common Z mutant (Glu342Lys) of α1-antitrypsin results in the formation of polymers that ...
The serpinopathies result from the ordered polymerization of mutants of members of the serine protei...
α1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pulmonary ...
Mutant Z α1-antitrypsin (E342K) accumulates as polymers within the endoplasmic reticulum (ER) of hep...
α1-Antitrypsin is primarily synthesised in the liver, circulates to the lung and protects pulmonary ...
The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self...