In recent years, we have witnessed several important paradigm shifts in understanding the molecular basis of liver disease in alpha-1-antitrypsin (AT) deficiency. These shifts have become possible as a result of a number of advances in research on the cell biology of aggregation-prone mutant protein
Molecular pathogenesis of liver disease in α1-antitrypsin deficiency
✍ Scribed by J H Teckman; D Qu; D H Perlmutter
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 320 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0270-9139
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✦ Synopsis
alpha-1-antitrypsin; PiZZ, a1-ATZ phenotype; ER, endoplasmic acts with the target P 1 -P 1 residues of the reactive center loop, reticulum; MHC, major histocompatibility complex.
the loop inserts further into the gap in the A sheet, generating From the: Departments of Pediatrics, Cell Biology, and Physiology, Washington Univera ''locked'' conformation and inactivating the cognate enzyme.
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We present our experience with 18 pediatric patients with a,-antitrypsin deficiency of the PiZZ phenotype. Fifteen patients (83%) presented with neonatal cholestatic jaundice at a mean age of 2 f 0.6 months (2S.D.). The ma1e:female ratio was 15:3, indicating a male predominance. All metabolic, infec
## Abstract Protein aggregation is the cause of several human diseases. Understanding the molecular mechanisms involved in protein aggregation requires knowledge of the kinetics and structures populated during the reaction. Arguably, the best structurally characterized misfolding reaction is that o
## Abstract Mechanism of α1 AT polymerization. See Serpin Polymerization and Its Role in Disease—the Molecular Basis of α~1~‐Antitrypsin Deficiency by Knaupp and Bottomley, pp. 1–5.