Folding and Stability of the Z and Siiyama Genetic Variants of Human α1-Antitrypsin
Open Access
- 1 January 1997
- journal article
- Published by Elsevier
- Vol. 272 (1) , 510-516
- https://doi.org/10.1074/jbc.272.1.510
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Probing the native strain in α1-antitrypsinNature Structural & Molecular Biology, 1996
- The Endoplasmic Reticulum Degradation Pathway for Mutant Secretory Proteins α1-Antitrypsin Z and S Is Distinct from That for an Unassembled Membrane ProteinPublished by Elsevier ,1996
- Specificity of Abnormal Assembly in Immunoglobulin Light Chain Deposition Disease and AmyloidosisJournal of Molecular Biology, 1996
- ReviewBiological Chemistry Hoppe-Seyler, 1996
- α1-Antitrypsin Mmalton (Phe52-deleted) Forms Loop-Sheet Polymers in Vivo.Published by Elsevier ,1995
- Defective protein folding as a cause of diseaseNature Structural & Molecular Biology, 1995
- The Z type variation of human α1-antitrypsin causes a protein folding defectNature Structural & Molecular Biology, 1995
- The mechanism of Z α1-antitrypsin accumulation in the liverNature, 1992
- Protein Oligomerization In The Endoplasmic ReticulumAnnual Review of Cell and Developmental Biology, 1989
- Antielastases of the human alveolar structures. Implications for the protease-antiprotease theory of emphysema.Journal of Clinical Investigation, 1981