Site-specific fluorescence dynamics of α-synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations.
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Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretionFamilial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein.Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation.Anti-amyloid compounds inhibit α-synuclein aggregation induced by protein misfolding cyclic amplification (PMCA)Coupling of the non-amyloid-component (NAC) domain and the KTK(E/Q)GV repeats stabilize the α-synuclein fibrils.Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synuclein.
P2860
Site-specific fluorescence dynamics of α-synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations.
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2014 nî lūn-bûn
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2014年の論文
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2014年学术文章
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name
Site-specific fluorescence dyn ...... disease-associated mutations.
@en
Site-specific fluorescence dyn ...... disease-associated mutations.
@nl
type
label
Site-specific fluorescence dyn ...... disease-associated mutations.
@en
Site-specific fluorescence dyn ...... disease-associated mutations.
@nl
prefLabel
Site-specific fluorescence dyn ...... disease-associated mutations.
@en
Site-specific fluorescence dyn ...... disease-associated mutations.
@nl
P356
P1433
P1476
Site-specific fluorescence dyn ...... disease-associated mutations.
@en
P2093
G Krishnamoorthy
Shruti Sahay
P304
P356
10.1021/BI401543Z
P407
P577
2014-01-27T00:00:00Z