The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates.
about
New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitinUbiquitylation Directly Induces Fold Destabilization of ProteinsObserving a late folding intermediate of Ubiquitin at atomic resolution by NMR.Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR.Ubiquitin-Binding Protein CG5445 Suppresses Aggregation and Cytotoxicity of Amyotrophic Lateral Sclerosis-linked TDP-43 in Drosophila.Intracellular tracing of amyloid vaccines through direct fluorescent labelling.p62 filaments capture and present ubiquitinated cargos for autophagy.Isolation and characterization of a minimal building block of polyubiquitin fibrils.Detection of Protein SUMOylation In Situ by Proximity Ligation Assays.Method for the Purification of Endogenous Unanchored Polyubiquitin Chains.It Pays To Be in Phase.
P2860
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P2860
The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates.
@en
type
label
The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates.
@en
prefLabel
The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates.
@en
P2093
P2860
P50
P356
P1476
The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates
@en
P2093
Erik Walinda
Harumi Fukada
Hikaru Tsuchiya
Keiichi Namba
Keiji Tanaka
Kyohei Arita
Mariko Ariyoshi
Masahiro Shirakawa
Masaru Hoshino
Shun Kageyama
P2860
P2888
P356
10.1038/NCOMMS7116
P407
P577
2015-01-20T00:00:00Z