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Peptide-Induced Amyloid-Like Conformational Transitions in Proteins
Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amylo...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4578744/ https://www.ncbi.nlm.nih.gov/pubmed/26435719 http://dx.doi.org/10.1155/2015/723186 |
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author | Egorov, Vladimir Grudinina, Natalia Vasin, Andrey Lebedev, Dmitry |
author_facet | Egorov, Vladimir Grudinina, Natalia Vasin, Andrey Lebedev, Dmitry |
author_sort | Egorov, Vladimir |
collection | PubMed |
description | Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can cause the conformational transitions in the protein. Short peptides which could be produced during the protein life cycle or which are encoded by short open reading frames can affect the protein conformation and function. |
format | Online Article Text |
id | pubmed-4578744 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-45787442015-10-04 Peptide-Induced Amyloid-Like Conformational Transitions in Proteins Egorov, Vladimir Grudinina, Natalia Vasin, Andrey Lebedev, Dmitry Int J Pept Review Article Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can cause the conformational transitions in the protein. Short peptides which could be produced during the protein life cycle or which are encoded by short open reading frames can affect the protein conformation and function. Hindawi Publishing Corporation 2015 2015-09-08 /pmc/articles/PMC4578744/ /pubmed/26435719 http://dx.doi.org/10.1155/2015/723186 Text en Copyright © 2015 Vladimir Egorov et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Egorov, Vladimir Grudinina, Natalia Vasin, Andrey Lebedev, Dmitry Peptide-Induced Amyloid-Like Conformational Transitions in Proteins |
title | Peptide-Induced Amyloid-Like Conformational Transitions in Proteins |
title_full | Peptide-Induced Amyloid-Like Conformational Transitions in Proteins |
title_fullStr | Peptide-Induced Amyloid-Like Conformational Transitions in Proteins |
title_full_unstemmed | Peptide-Induced Amyloid-Like Conformational Transitions in Proteins |
title_short | Peptide-Induced Amyloid-Like Conformational Transitions in Proteins |
title_sort | peptide-induced amyloid-like conformational transitions in proteins |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4578744/ https://www.ncbi.nlm.nih.gov/pubmed/26435719 http://dx.doi.org/10.1155/2015/723186 |
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