The Component Polypeptide Chains of Bovine Insulin Nucleate or Inhibit Aggregation of the Parent Protein in a Conformation-dependent Manner
- 17 May 2006
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 360 (2), 497-509
- https://doi.org/10.1016/j.jmb.2006.05.007
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Techniques to study amyloid fibril formation in vitroMethods, 2004
- Protein folding and misfoldingNature, 2003
- The alternative conformations of amyloidogenic proteins and their multi-step assembly pathwaysCurrent Opinion in Structural Biology, 1998
- Common core structure of amyloid fibrils by synchrotron X-ray diffractionJournal of Molecular Biology, 1997
- Toward Understanding Insulin FibrillationJournal of Pharmaceutical Sciences, 1997
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patientDiabetologia, 1988
- Assessment of gelling in insulin solutions for infusion pumpsJournal of Pharmacy and Pharmacology, 1985
- Insulin aggregation in artificial delivery systemsDiabetologia, 1980
- A Fibrous Modification of Insulin. I. The Heat Precipitate of InsulinJournal of the American Chemical Society, 1946