O-GlcNAcylation of α-Synuclein at Serine 87 Reduces Aggregation without Affecting Membrane Binding.
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The Sulfur-Linked Analogue of O-GlcNAc (S-GlcNAc) Is an Enzymatically Stable and Reasonable Structural Surrogate for O-GlcNAc at the Peptide and Protein Levels.The emerging link between O-GlcNAcylation and neurological disorders.O-GlcNAc modification inhibits the calpain-mediated cleavage of α-synuclein.Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein.Nutrient-driven O-GlcNAc in proteostasis and neurodegeneration.Advancing the Frontiers of Chemical Protein Synthesis-The 7th CPS Meeting, Haifa, Israel.
P2860
O-GlcNAcylation of α-Synuclein at Serine 87 Reduces Aggregation without Affecting Membrane Binding.
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name
O-GlcNAcylation of α-Synuclein ...... ut Affecting Membrane Binding.
@en
O-GlcNAcylation of α-Synuclein ...... ut Affecting Membrane Binding.
@nl
type
label
O-GlcNAcylation of α-Synuclein ...... ut Affecting Membrane Binding.
@en
O-GlcNAcylation of α-Synuclein ...... ut Affecting Membrane Binding.
@nl
prefLabel
O-GlcNAcylation of α-Synuclein ...... ut Affecting Membrane Binding.
@en
O-GlcNAcylation of α-Synuclein ...... ut Affecting Membrane Binding.
@nl
P2093
P2860
P1433
P1476
O-GlcNAcylation of α-Synuclein ...... ut Affecting Membrane Binding.
@en
P2093
Ana Galesic
Caroline K Brennan
Natalie Lamiri
Paul M Levine
Yuka E Lewis
P2860
P304
P356
10.1021/ACSCHEMBIO.7B00113
P577
2017-02-22T00:00:00Z