000			01841naaaa2200253uu 4500
001			https://directory.doabooks.org/handle/20.500.12854/47794
005			20220220080453.0
020			_a978-88-8453-946-5
020			_a9788884539465
024	7		_a10.36253/978-88-8453-946-5 _cdoi
042			_adc
100	1		_aFrancesco Bemporad _4auth
245	1	0	_aFolding and aggregation studies in the acylphosphatase-like family
260			_bFirenze University Press _c2009
300			_a1 electronic resource (126 p.)
506	0		_aOpen Access _2star _fUnrestricted online access
520			_aFolding 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			_aCreative Commons _fhttps://creativecommons.org/licenses/by-nc-nd/4.0/ _2cc _4https://creativecommons.org/licenses/by-nc-nd/4.0/
653			_aChimica
653			_aMedicina
653			_aBiologia
856	4	0	_awww.oapen.org _uhttps://www.fupress.com/redir.ashx?RetUrl=3851.pdf _70 _zDOAB: download the publication
856	4	0	_awww.oapen.org _uhttps://directory.doabooks.org/handle/20.500.12854/47794 _70 _zDOAB: description of the publication
999			_c74912 _d74912