Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species.
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The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation.Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers.HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.Propagation of an Aβ Dodecamer Strain Involves a Three-Step Mechanism and a Key Intermediate.27-Hydroxycholesterol increases α-synuclein protein levels through proteasomal inhibition in human dopaminergic neurons.Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms
P2860
Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species.
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name
Inhibition of α-Synuclein Fibr ...... n between α-Synuclein Species.
@en
Inhibition of α-Synuclein Fibr ...... n between α-Synuclein Species.
@nl
type
label
Inhibition of α-Synuclein Fibr ...... n between α-Synuclein Species.
@en
Inhibition of α-Synuclein Fibr ...... n between α-Synuclein Species.
@nl
prefLabel
Inhibition of α-Synuclein Fibr ...... n between α-Synuclein Species.
@en
Inhibition of α-Synuclein Fibr ...... n between α-Synuclein Species.
@nl
P2093
P50
P1433
P1476
Inhibition of α-Synuclein Fibr ...... n between α-Synuclein Species.
@en
P2093
Anne Dhulesia
Giuliana Fusco
Janet R Kumita
Nunilo Cremades
Paolo Arosio
Tuomas P J Knowles
P304
P356
10.1021/ACS.BIOCHEM.6B01178
P407
P577
2017-02-23T00:00:00Z