LEADER 02288nam  2200469z- 450 
001 9910261132603321
005 20210211
035   $a(CKB)4100000002484760
035   $a(oapen)https://directory.doabooks.org/handle/20.500.12854/53828
035   $a(oapen)doab53828
035   $a(EXLCZ)994100000002484760
100   $a20202102d2017      |y         0
101 0 $aeng
135   $aurmn|---annan
181   $ctxt$2rdacontent
182   $cc$2rdamedia
183   $acr$2rdacarrier
200 00$aMolecular Chaperones and Neurodegeneration
210   $cFrontiers Media SA$d2017
215   $a1 online resource (180 p.)
225 1 $aFrontiers Research Topics
311 08$a2-88945-342-1 
330   $aMolecular chaperones or heat-shock proteins (HSPs) play essential roles in safeguarding structural stability and preventing misfolding and aggregation of proteins, and maintaining the proteome functionality in the cell. For over two decades until the present time, new functions have been discovered and several molecular mechanisms have been elucidated for many chaperones, while the field is being continuously challenged by new open questions. Probably as a consequence of the increasing research on the molecular bases of neurodegenerative diseases, and the realisation that many such disorders are linked to protein misfolding processes, unleashing the roles and mechanisms of chaperones in the context of neurodegeneration has become a prime scientific goal. This e-book contains a diversity of reviews, perspective and original research articles highlighting the importance and potential of this emerging subject.
606   $aNeurosciences$2bicssc
610   $aamyloid protein
610   $aheat-shock protein
610   $aheat-shock response
610   $amolecular chaperone
610   $aneurodegeneration
610   $aneurodegenerative disease
610   $aneuroprotection
610   $aprotein misfolding
610   $aproteostasis
610   $atherapeutics
615  7$aNeurosciences
700   $aCintia Roodveldt$4auth$01320418
702   $aJanice E. Braun$4auth
702   $aTiago F. Outeiro$4auth
906   $aBOOK
912   $a9910261132603321
996   $aMolecular Chaperones and Neurodegeneration$93034283
997   $aUNINA