This transition is known to happen via partially folded intermediates and soluble oligomers. Natively structured or unstructured peptides/proteins undergo structural transition to form cross-β-sheet rich amyloids. The Funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: The authors have declared that no competing interests exist.Īmyloids are highly ordered protein/peptide aggregates that are associated with a number of human diseases including Alzheimer's and Parkinson's. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.įunding: This work was supported by the Council of Scientific and Industrial Research (37(1404)/10/EMR-11, Department of Science and Technology (SR/FR/LS-032/2009) and Department of Biotechnology, Government of India for financial support. Received: OctoAccepted: JanuPublished: March 5, 2012Ĭopyright: © 2012 Ranganathan et al. Uversky, University of South Florida College of Medicine, United States of America Citation: Ranganathan S, Singh PK, Singh U, Singru PS, Padinhateeri R, Maji SK (2012) Molecular Interpretation of ACTH-β-Endorphin Coaggregation: Relevance to Secretory Granule Biogenesis.
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