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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...

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Autores principales: Egorov, Vladimir, Grudinina, Natalia, Vasin, Andrey, Lebedev, Dmitry
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2015
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.
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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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