Ontology highlight
ABSTRACT:
INSTRUMENT(S): Orbitrap Fusion
ORGANISM(S): Homo Sapiens (human) Escherichia Coli
SUBMITTER: Heike Stephanowitz
LAB HEAD: Janine Kirstein
PROVIDER: PXD031214 | Pride | 2022-10-15
REPOSITORIES: Pride
Action | DRS | |||
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All_crosslinks_spectra_merged.pdf | ||||
DNAJB1-HTTQ48_XL.csv | Csv | |||
F1_20171023_HS785_2.raw | Raw | |||
F1_20180122_HS_HS819_JK_7_SDAmethod.raw | Raw | |||
HTTQ23-HSP70_XL.csv | Csv |
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Ayala Mariscal S M SM Pigazzini M L ML Richter Y Y Özel M M Grothaus I L IL Protze J J Ziege K K Kulke M M ElBediwi M M Vermaas J V JV Colombi Ciacchi L L Köppen S S Liu F F Kirstein J J
Nature communications 20220810 1
Huntington's disease is a neurodegenerative disease caused by an expanded polyQ stretch within Huntingtin (HTT) that renders the protein aggregation-prone, ultimately resulting in the formation of amyloid fibrils. A trimeric chaperone complex composed of Hsc70, DNAJB1 and Apg2 can suppress and reverse the aggregation of HTTExon1Q<sub>48</sub>. DNAJB1 is the rate-limiting chaperone and we have here identified and characterized the binding interface between DNAJB1 and HTTExon1Q<sub>48</sub>. DNAJB ...[more]