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 disea...

Full description

Saved in:
Bibliographic Details
Superior document:Premio Tesi di Dottorato
:
Year of Publication:2009
Language:English
Series:Premio Tesi di Dottorato
Physical Description:1 electronic resource (126 p.)
Tags: Add Tag
No Tags, Be the first to tag this record!
id 993603842304498
ctrlnum (CKB)5860000000046971
(oapen)https://directory.doabooks.org/handle/20.500.12854/83524
(EXLCZ)995860000000046971
collection bib_alma
record_format marc
spelling Bemporad, Francesco auth
Folding and aggregation studies in the acylphosphatase-like family
Firenze Firenze University Press 2009
1 electronic resource (126 p.)
text txt rdacontent
computer c rdamedia
online resource cr rdacarrier
Premio Tesi di Dottorato
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.
English
Medicine bicssc
Medicina
Biologia
Chimica
88-927-3768-6
language English
format eBook
author Bemporad, Francesco
spellingShingle Bemporad, Francesco
Folding and aggregation studies in the acylphosphatase-like family
Premio Tesi di Dottorato
author_facet Bemporad, Francesco
author_variant f b fb
author_sort Bemporad, Francesco
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_auth Folding and aggregation studies in the acylphosphatase-like family
title_new Folding and aggregation studies in the acylphosphatase-like family
title_sort folding and aggregation studies in the acylphosphatase-like family
series Premio Tesi di Dottorato
series2 Premio Tesi di Dottorato
publisher Firenze University Press
publishDate 2009
physical 1 electronic resource (126 p.)
isbn 88-927-3768-6
illustrated Not Illustrated
work_keys_str_mv AT bemporadfrancesco foldingandaggregationstudiesintheacylphosphataselikefamily
status_str n
ids_txt_mv (CKB)5860000000046971
(oapen)https://directory.doabooks.org/handle/20.500.12854/83524
(EXLCZ)995860000000046971
carrierType_str_mv cr
hierarchy_parent_title Premio Tesi di Dottorato
is_hierarchy_title Folding and aggregation studies in the acylphosphatase-like family
container_title Premio Tesi di Dottorato
_version_ 1796653242154745856
fullrecord <?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01726nam-a2200313z--4500</leader><controlfield tag="001">993603842304498</controlfield><controlfield tag="005">20231214133309.0</controlfield><controlfield tag="006">m o d </controlfield><controlfield tag="007">cr|mn|---annan</controlfield><controlfield tag="008">202206s2009 xx |||||o ||| 0|eng d</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(CKB)5860000000046971</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(oapen)https://directory.doabooks.org/handle/20.500.12854/83524</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(EXLCZ)995860000000046971</subfield></datafield><datafield tag="041" ind1="0" ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Bemporad, Francesco</subfield><subfield code="4">auth</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Folding and aggregation studies in the acylphosphatase-like family</subfield></datafield><datafield tag="260" ind1=" " ind2=" "><subfield code="a">Firenze</subfield><subfield code="b">Firenze University Press</subfield><subfield code="c">2009</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">1 electronic resource (126 p.)</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">computer</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">online resource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="490" ind1="1" ind2=" "><subfield code="a">Premio Tesi di Dottorato</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">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.</subfield></datafield><datafield tag="546" ind1=" " ind2=" "><subfield code="a">English</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Medicine</subfield><subfield code="2">bicssc</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Medicina</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Biologia</subfield></datafield><datafield tag="653" ind1=" " ind2=" "><subfield code="a">Chimica</subfield></datafield><datafield tag="776" ind1=" " ind2=" "><subfield code="z">88-927-3768-6</subfield></datafield><datafield tag="906" ind1=" " ind2=" "><subfield code="a">BOOK</subfield></datafield><datafield tag="ADM" ind1=" " ind2=" "><subfield code="b">2023-12-15 05:49:36 Europe/Vienna</subfield><subfield code="f">system</subfield><subfield code="c">marc21</subfield><subfield code="a">2022-06-08 16:08:14 Europe/Vienna</subfield><subfield code="g">false</subfield></datafield><datafield tag="AVE" ind1=" " ind2=" "><subfield code="i">DOAB Directory of Open Access Books</subfield><subfield code="P">DOAB Directory of Open Access Books</subfield><subfield code="x">https://eu02.alma.exlibrisgroup.com/view/uresolver/43ACC_OEAW/openurl?u.ignore_date_coverage=true&amp;portfolio_pid=5337700040004498&amp;Force_direct=true</subfield><subfield code="Z">5337700040004498</subfield><subfield code="b">Available</subfield><subfield code="8">5337700040004498</subfield></datafield></record></collection>