Folding and aggregation studies in the acylphosphatase-like family (Record no. 74912)
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| 000 -LEADER | |
|---|---|
| fixed length control field | 01841naaaa2200253uu 4500 |
| 001 - CONTROL NUMBER | |
| control field | https://directory.doabooks.org/handle/20.500.12854/47794 |
| 005 - DATE AND TIME OF LATEST TRANSACTION | |
| control field | 20220220080453.0 |
| 020 ## - INTERNATIONAL STANDARD BOOK NUMBER | |
| International Standard Book Number | 978-88-8453-946-5 |
| 020 ## - INTERNATIONAL STANDARD BOOK NUMBER | |
| International Standard Book Number | 9788884539465 |
| 024 7# - OTHER STANDARD IDENTIFIER | |
| Standard number or code | 10.36253/978-88-8453-946-5 |
| Terms of availability | doi |
| 042 ## - AUTHENTICATION CODE | |
| Authentication code | dc |
| 100 1# - MAIN ENTRY--PERSONAL NAME | |
| Personal name | Francesco Bemporad |
| Relationship | auth |
| 245 10 - TITLE STATEMENT | |
| Title | Folding and aggregation studies in the acylphosphatase-like family |
| 260 ## - PUBLICATION, DISTRIBUTION, ETC. | |
| Name of publisher, distributor, etc. | Firenze University Press |
| Date of publication, distribution, etc. | 2009 |
| 300 ## - PHYSICAL DESCRIPTION | |
| Extent | 1 electronic resource (126 p.) |
| 506 0# - RESTRICTIONS ON ACCESS NOTE | |
| Terms governing access | Open Access |
| Source of term | star |
| Standardized terminology for access restriction | Unrestricted online access |
| 520 ## - SUMMARY, ETC. | |
| Summary, etc. | 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. |
| 540 ## - TERMS GOVERNING USE AND REPRODUCTION NOTE | |
| Terms governing use and reproduction | Creative Commons |
| Use and reproduction rights | https://creativecommons.org/licenses/by-nc-nd/4.0/ |
| Source of term | cc |
| -- | https://creativecommons.org/licenses/by-nc-nd/4.0/ |
| 653 ## - INDEX TERM--UNCONTROLLED | |
| Uncontrolled term | Chimica |
| 653 ## - INDEX TERM--UNCONTROLLED | |
| Uncontrolled term | Medicina |
| 653 ## - INDEX TERM--UNCONTROLLED | |
| Uncontrolled term | Biologia |
| 856 40 - ELECTRONIC LOCATION AND ACCESS | |
| Host name | www.oapen.org |
| Uniform Resource Identifier | <a href="https://www.fupress.com/redir.ashx?RetUrl=3851.pdf">https://www.fupress.com/redir.ashx?RetUrl=3851.pdf</a> |
| Access status | 0 |
| Public note | DOAB: download the publication |
| 856 40 - ELECTRONIC LOCATION AND ACCESS | |
| Host name | www.oapen.org |
| Uniform Resource Identifier | <a href="https://directory.doabooks.org/handle/20.500.12854/47794">https://directory.doabooks.org/handle/20.500.12854/47794</a> |
| Access status | 0 |
| Public note | DOAB: description of the publication |
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