Folding and aggregation studies in the acylphosphatase-like family

Folding and misfolding of proteins are considered two sides of the same coin. The delicate equilibrium existing between these two processes is crucial for any living organism and its alterations can lead to the onset of several tremendous diseases, such as Alzheimer's and Parkinson's disease. The at...

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Tác giả chính: Bemporad, Francesco
Định dạng: Online
Ngôn ngữ:Tiếng Anh
Được phát hành: Firenze University Press 2022
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Truy cập trực tuyến:ONIX_20220531_9788884539465_149
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author Bemporad, Francesco
author_browse Bemporad, Francesco
author_facet Bemporad, Francesco
author_sort Bemporad, Francesco
collection Directory of Open Access Books
description Folding and misfolding of proteins are considered two sides of the same coin. The delicate equilibrium existing between these two processes is crucial for any living organism and its alterations can lead to the onset of several tremendous diseases, such as Alzheimer's and Parkinson's disease. The attainment of a profound knowledge of folding/misfolding processes is a key step to understand how life works and for discovering new therapies to these diseases. In this work the author shows that proteins can display enzymatic activity even in the absence of a compact three-dimensional structure, with important implications for the study of protein enzymes. Furthermore, the author investigates the formation of protein aggregates similar to those observed in patients of amyloid-related diseases.
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publisher Firenze University Press
publisherStr Firenze University Press
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spelling doab-20.500.12854ir-835242025-03-22T21:43:46Z Folding and aggregation studies in the acylphosphatase-like family Bemporad, Francesco Medicina Biologia Chimica Folding and misfolding of proteins are considered two sides of the same coin. The delicate equilibrium existing between these two processes is crucial for any living organism and its alterations can lead to the onset of several tremendous diseases, such as Alzheimer's and Parkinson's disease. The attainment of a profound knowledge of folding/misfolding processes is a key step to understand how life works and for discovering new therapies to these diseases. In this work the author shows that proteins can display enzymatic activity even in the absence of a compact three-dimensional structure, with important implications for the study of protein enzymes. Furthermore, the author investigates the formation of protein aggregates similar to those observed in patients of amyloid-related diseases. 2022-06-02T04:32:58Z 2022-06-02T04:32:58Z 2022-05-31T10:15:21Z 2009 book ONIX_20220531_9788884539465_149 OCN: 1229759119 2612-8020 https://library.oapen.org/handle/20.500.12657/54865 9788884539465 9788884539458 9788892737686 https://directory.doabooks.org/handle/20.500.12854/83524 eng Premio Tesi di Dottorato open access image/jpeg image/jpeg image/jpeg n/a n/a n/a https://library.oapen.org/bitstream/20.500.12657/54865/1/9788884539465.pdf https://library.oapen.org/bitstream/20.500.12657/54865/1/9788884539465.pdf https://library.oapen.org/bitstream/20.500.12657/54865/1/9788884539465.pdf Firenze University Press 10.36253/978-88-8453-946-5 10.36253/978-88-8453-946-5 2ec4474d-93b1-4cfa-b313-9c6019b51b1a 9788884539465 9788884539458 9788892737686 126 Firenze open access
spellingShingle Medicina
Biologia
Chimica
Bemporad, Francesco
Folding and aggregation studies in the acylphosphatase-like family
title Folding and aggregation studies in the acylphosphatase-like family
title_full Folding and aggregation studies in the acylphosphatase-like family
title_fullStr Folding and aggregation studies in the acylphosphatase-like family
title_full_unstemmed Folding and aggregation studies in the acylphosphatase-like family
title_short Folding and aggregation studies in the acylphosphatase-like family
title_sort folding and aggregation studies in the acylphosphatase like family
topic Medicina
Biologia
Chimica
topic_facet Medicina
Biologia
Chimica
url ONIX_20220531_9788884539465_149
work_keys_str_mv AT bemporadfrancesco foldingandaggregationstudiesintheacylphosphataselikefamily