Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
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Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.The p53 core domain is a molten globule at low pH: functional implications of a partially unfolded structure.Ligand binding and hydration in protein misfolding: insights from studies of prion and p53 tumor suppressor proteins.Assemblages: functional units formed by cellular phase separationReduced endogenous Ca2+ buffering speeds active zone Ca2+ signalingConformational Stability of the NH2-Terminal Propeptide of the Precursor of Pulmonary Surfactant Protein SP-B.Mutant p53 aggregates into prion-like amyloid oligomers and fibrils: implications for cancer.Ca2+-dependent inactivation of CaV1.2 channels prevents Gd3+ block: does Ca2+ block the pore of inactivated channels?Multiple cytosolic calcium buffers in posterior pituitary nerve terminalsAggregation tendencies in the p53 family are modulated by backbone hydrogen bonds.Expanding the prion concept to cancer biology: dominant-negative effect of aggregates of mutant p53 tumour suppressorAggregation and Prion-Like Properties of Misfolded Tumor Suppressors: Is Cancer a Prion Disease?The (1-63) region of the p53 transactivation domain aggregates in vitro into cytotoxic amyloid assemblies.Distinct modulatory role of RNA in the aggregation of the tumor suppressor protein p53 core domain.Loose coupling between Ca2+ channels and release sensors at a plastic hippocampal synapse.
P2860
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P2860
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
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2004 nî lūn-bûn
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2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2004 թվականի օգոստոսին հրատարակված գիտական հոդված
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2004年の論文
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name
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
@ast
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
@en
type
label
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
@ast
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
@en
prefLabel
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
@ast
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
@en
P2093
P2860
P1433
P1476
Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.
@en
P2093
Ana P Ano Bom
Ana P Valente
Daniella Ishimaru
Lenize F Maia
Luis M T R Lima
Priscila M Lopez
P2860
P304
P356
10.1529/BIOPHYSJ.104.044685
P407
P577
2004-08-06T00:00:00Z