Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature.
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Characterization of the oligomerization and aggregation of human Serum Amyloid APathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2.Amyloid fibril formation by a normally folded protein in the absence of denaturants and agitation.
P2860
Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature.
description
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2011年の論文
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2011年論文
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2011年論文
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name
Inflammation protein SAA2.2 sp ...... at physiological temperature.
@en
type
label
Inflammation protein SAA2.2 sp ...... at physiological temperature.
@en
prefLabel
Inflammation protein SAA2.2 sp ...... at physiological temperature.
@en
P2093
P2860
P356
P1433
P1476
Inflammation protein SAA2.2 sp ...... at physiological temperature.
@en
P2093
Diane Bayron Poueymiroy
J Javier Aguilera
Saipraveen Srinivasan
Wilfredo Colón
P2860
P304
P356
10.1021/BI200856V
P407
P577
2011-10-05T00:00:00Z