Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.
about
Protein folding: then and nowStructure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy.Rapid Folding and Unfolding of Apaf-1 CARDTopology is the principal determinant in the folding of a complex all-alpha Greek key death domain from human FADDThe tandem CARDs of NOD2: intramolecular interactions and recognition of RIP2.Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formationStructural mechanisms in NLR inflammasome signaling.Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICKUbiquitin regulates caspase recruitment domain-mediated signaling by nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2.Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients.Assembly and regulation of ASC specks.
P2860
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P2860
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.
@en
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.
@nl
type
label
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.
@en
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.
@nl
prefLabel
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.
@en
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.
@nl
P2860
P356
P1433
P1476
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain
@en
P2093
A Clay Clark
P2860
P304
P356
10.1110/PS.03521504
P50
P577
2004-08-01T00:00:00Z