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Hsp104 dissolves ASPA aggregates to promote protein folding..:

Sarah K. Gersing (8594898) ; Yong Wang (12837) ; Martin Grønbæk-Thygesen (9592332)...
https://figshare.com/articles/figure/Hsp104_dissolves_ASPA_aggregates_to_promote_protein_folding_and_inclusion_body_formation_/14512405. , 2021

Link: https://doi.org/10.1371/journal.pgen.1009539.g005

RT Journal
T1 <Title>Hsp104 dissolves ASPA aggregates to promote protein folding and inclusion body formation</Title>

UL https://suche.suub.uni-bremen.de/peid=base-ftsmithonian:oai:figshare.com:article_14512405&Exemplar=1&LAN=DE
				
A1 Sarah K. Gersing (8594898)
A1 Yong Wang (12837)
A1 Martin Grønbæk-Thygesen (9592332)
A1 Caroline Kampmeyer (8594889)
A1 Lene Clausen (9592329)
A1 Martin Willemoës (559349)
A1 Claes Andréasson (42156)
A1 Amelie Stein (5664)
A1 Kresten Lindorff-Larsen (317515)
A1 Rasmus Hartmann-Petersen (117664)
YR 2021
K1 Biochemistry
K1 Genetics
K1 Molecular Biology
K1 Neuroscience
K1 Physiology
K1 Biotechnology
K1 Biological Sciences not elsewhere classified
K1 use ASPA C 152W
K1 proteasomal degradation
K1 degradation pathway
K1 C 152W substitution
K1 wild-type ASPA
K1 disease-linked aspartoacylase varia
K1 ASPA C 152W
K1 quality control E 3 ubiquitin-prote
K1 protein quality control components
K1 co-chaperone Hsp 110
K1 aggregated ASPA C 152W
K1 disaggregase Hsp 104
K1 substitution C 152W ASPA C 152W
K1 disease-causing protein variant
JF https://figshare.com/articles/figure/Hsp104_dissolves_ASPA_aggregates_to_promote_protein_folding_and_inclusion_body_formation_/14512405
LK http://dx.doi.org/https://doi.org/10.1371/journal.pgen.1009539.g005
DO https://doi.org/10.1371/journal.pgen.1009539.g005
SF ELIB - SuUB Bremen

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