A 2.6 å structure of a serpin polymer and implications for conformational disease
- 29 October 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 293 (3) , 449-455
- https://doi.org/10.1006/jmbi.1999.3184
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationActa Crystallographica Section D-Biological Crystallography, 1998
- Conformational diseaseThe Lancet, 1997
- MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid ProteinsAnnual Review of Biochemistry, 1997
- Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpinsProtein Science, 1997
- Probing serpin reactive-loop conformations by proteolytic cleavageBiochemical Journal, 1996
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Domain swapping: entangling alliances between proteins.Proceedings of the National Academy of Sciences, 1994
- The S variant of human α1-antitrypsin, structure and implications for function and metabolismProtein Engineering, Design and Selection, 1989
- A fast algorithm for rendering space-filling molecule picturesJournal of Molecular Graphics, 1988
- Immunochemical identification of the serine protease inhibitor α1-antichymotrypsin in the brain amyloid deposits of Alzheimer's diseaseCell, 1988