Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.
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The DNA-binding domain mediates both nuclear and cytosolic functions of p53Noncanonical DNA motifs as transactivation targets by wild type and mutant p53Mutant p53 aggregates into prion-like amyloid oligomers and fibrils: implications for cancer.Molecular dynamic simulation insights into the normal state and restoration of p53 function.Searching for factors that distinguish disease-prone and disease-resistant prions via sequence analysisLarge-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteomeThe tumor suppressor p53: from structures to drug discovery.A fluid salt-bridging cluster and the stabilization of p53.Therapeutic targeting of p53: all mutants are equal, but some mutants are more equal than others.Resveratrol prevents p53 aggregation and in breast cancer cells
P2860
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P2860
Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.
description
2005 nî lūn-bûn
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2005年の論文
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name
Disruption of an intermonomer ...... nsity to form amyloid fibrils.
@ast
Disruption of an intermonomer ...... nsity to form amyloid fibrils.
@en
type
label
Disruption of an intermonomer ...... nsity to form amyloid fibrils.
@ast
Disruption of an intermonomer ...... nsity to form amyloid fibrils.
@en
prefLabel
Disruption of an intermonomer ...... nsity to form amyloid fibrils.
@ast
Disruption of an intermonomer ...... nsity to form amyloid fibrils.
@en
P2860
P356
P1433
P1476
Disruption of an intermonomer ...... ensity to form amyloid fibrils
@en
P2093
Prentice Bowman
Richard W Kriwacki
P2860
P304
P356
10.1110/PS.051622005
P577
2005-10-31T00:00:00Z