Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer.
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Colocalization of serum amyloid a with microtubules in human coronary artery endothelial cellsDivergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid ACharacterization 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.Serum amyloid A 2.2 refolds into a octameric oligomer that slowly converts to a more stable hexamer.Could antibodies against serum amyloid A function as physiological regulators in humans?
P2860
Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer.
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name
Urea-induced denaturation of a ...... marginal stability of hexamer.
@en
Urea-induced denaturation of a ...... marginal stability of hexamer.
@nl
type
label
Urea-induced denaturation of a ...... marginal stability of hexamer.
@en
Urea-induced denaturation of a ...... marginal stability of hexamer.
@nl
prefLabel
Urea-induced denaturation of a ...... marginal stability of hexamer.
@en
Urea-induced denaturation of a ...... marginal stability of hexamer.
@nl
P2860
P356
P1433
P1476
Urea-induced denaturation of a ...... marginal stability of hexamer.
@en
P2093
Limin Wang
Wilfredo Colón
P2860
P304
P356
10.1110/PS.051387005
P577
2005-06-03T00:00:00Z