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Molecular mechanism of the interaction between MDM2 and p53.
We have investigated the kinetic and thermodynamic basis of the p53-MDM2 interaction using a set of peptides based on residues 15-29 of p53. Wild-type p53 peptide bound MDM2 with a dissociationExpand
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The C-terminus of p53 binds the N-terminal domain of MDM2
The p53 tumor suppressor interacts with its negative regulator Mdm2 via the former's N-terminal region and core domain, yet the extreme p53 C-terminal region contains lysine residues ubiquitinated byExpand
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The structure of an FF domain from human HYPA/FBP11.
The FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 andExpand
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Revealing the Ligand Binding Site of NhaA Na+/H+ Antiporter and Its pH Dependence*
Background: Cell pH and Na+ homeostasis requires Na+/H+ antiporters such as NhaA. Results: Mutational analysis and ITC measurements revealed the NhaA-Li+ binding site. Conclusion: Binding of Li+ toExpand
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A peptide that binds and stabilizes p53 core domain: Chaperone strategy for rescue of oncogenic mutants
Conformationally compromised oncogenic mutants of the tumor suppressor protein p53 can, in principle, be rescued by small molecules that bind the native, but not the denatured state. We describe aExpand
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Butyrylcholinesterase attenuates amyloid fibril formation in vitro.
In Alzheimer's disease, both acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) colocalize with brain fibrils of amyloid-beta (Abeta) peptides, and synaptic AChE-S facilitates fibrilExpand
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Oxidation of Helix-3 Methionines Precedes the Formation of PK Resistant PrPSc
While elucidating the peculiar epitope of the α-PrP mAb IPC2, we found that PrPSc exhibits the sulfoxidation of residue M213 as a covalent signature. Subsequent computational analysis predicted thatExpand
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Modulation of binding of DNA to the C-terminal domain of p53 by acetylation.
The binding of nonspecific DNA to the C-terminal negative regulatory domain (CTD) of p53 modulates its activity. The CTD is a natively unfolded region, which is subject to acetylation andExpand
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Binding of p53-derived ligands to MDM2 induces a variety of long range conformational changes.
We have used NMR to study the effects of peptide binding on the N-terminal p53-binding domain of human MDM2 (residues 25-109). There were changes in HSQC-chemical shifts throughout the domain onExpand
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Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope
Degradation of mutant Ndc10 is mediated by the E3 ligase Doa10 at the endoplasmic reticulum/nuclear envelope membrane. An autonomous degradation motif was localized to the C-terminal region of Ndc10.Expand
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