Characterizing the amyloid core region of the tumor suppressor protein p16INK4a using a limited proteolysis and peptide-based approach
Open Access
- 18 July 2024
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 300 (8) , 107590
Abstract
No abstract availableKeywords
Funding Information
- Royal Society of New Zealand Marsden Fund
- Canterbury Medical Research Foundation
- Health Research Council of New Zealand
- University of Canterbury Biomolecular Interaction Centre
This publication has 30 references indexed in Scilit:
- Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4ARedox Biology, 2020
- Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-AssembliesJournal of Molecular Biology, 2009
- Amyloid Fibril Formation from Full-Length and Fragments of AmylinJournal of Structural Biology, 2000
- The structural aspects of limited proteolysis of native proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
- Tumor Suppressor p16INK4A: Determination of Solution Structure and Analyses of Its Interaction with Cyclin-Dependent Kinase 4Molecular Cell, 1998
- Probing the partly folded states of proteins by limited proteolysisFolding and Design, 1997
- Structural characterization of the tumor suppressor p16, an ankyrin‐like repeat proteinProtein Science, 1996
- The Alzheimer A beta peptide develops protease resistance in association with its polymerization into fibrils.Journal of Biological Chemistry, 1994
- Letter to the editorsJournal of Mass Spectrometry, 1984
- A protease-resistant protein is a structural component of the Scrapie prionCell, 1983