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β-Amyloid Monomers Are Neuroprotective
TLDR
Synthetic Aβ1-42 monomers support the survival of developing neurons under conditions of trophic deprivation and protect mature neurons against excitotoxic death, a process that contributes to the overall neurodegeneration associated with AD. Expand
The Monomer State of Beta-Amyloid: Where the Alzheimer's Disease Protein Meets Physiology
TLDR
The emerging evidence for the physiological functions of A beta is summarized, including the recent demonstration that Abeta monomers are endowed with neuroprotective activity, and it is proposed that A beta aggregation might contribute to AD pathology through a "loss-of-function" process. Expand
Design and synthesis of new trehalose‐conjugated pentapeptides as inhibitors of Aβ(1–42) fibrillogenesis and toxicity
TLDR
Three new trehalose‐conjugated peptides of the well known β‐sheet breaker peptide iAβ5p, were synthesized and tested as inhibitors of Aβ toxicity toward pure cultures of rat cortical neurons. Expand
The telomere-binding protein Rif2 and ATP-bound Rad50 have opposing roles in the activation of yeast Tel1ATM kinase
TLDR
A model in which Rif2 attenuates Tel1 activity at telomeres by acting directly on Rad50 and discharging its activated ATP-bound state, thereby rendering the MRX complex incompetent for Tel1 activation is proposed. Expand
Nickel(II) complexes of the multihistidine peptide fragments of human prion protein.
TLDR
It was found that the peptides can bind as many nickel(II) ions as the number of independent histidyl residues, and that the complex formation processes of nickel( II) are very similar to those of copper(II), but with a significantly reduced stability for nickel(ii), which shifts thecomplex formation reactions into the slightly alkaline pH range. Expand
Nickel(II) and mixed metal complexes of amyloid-beta N-terminus.
TLDR
It was found that the hexadecapeptide and its fragments are effective nickel(II) binding ligands and complex formation processes of nickel( II) ions are quite similar to those of copper(II), but both metal ions are able to alter the distribution of copper-II ions among the various binding sites. Expand
Copper(II) complexes of rat amylin fragments.
TLDR
Data support that rIAPP(17-29) can interact with copper(II) ions under physiological conditions and the SSNN tetrapeptide fragment can be considered as the shortest sequence responsible for metal binding. Expand
Structural studies of a signal peptide in complex with signal peptidase I cytoplasmic domain: The stabilizing effect of membrane‐mimetics on the acquired fold
TLDR
This work has assessed the conformation of the signal peptide when bound to signal peptidase by solution nuclear magnetic resonance and found clear evidence of a weak peptide‐enzyme complex formation, consistent with proteolysis of the preprotein occurring while the sign peptide remains in the bilayer and the enzyme active site functioning at the membrane surface. Expand
The Wrapping Loop and Rap1 C-terminal (RCT) Domain of Yeast Rap1 Modulate Access to Different DNA Binding Modes*
TLDR
The ability of the DBD to form higher stoichiometry complexes on DNA is maintained also in larger Rap1 constructs, indicating that transition between at least two DNA-binding modes is a general property of the protein and not a specific feature of theDBD in isolation. Expand
The mitochondrial single-stranded DNA binding protein from S. cerevisiae, Rim1, does not form stable homo-tetramers and binds DNA as a dimer of dimers
TLDR
It is discovered that while Rim1 forms tetramers at high protein concentration, it dissociates into a smaller oligomeric species at low protein concentrations, which provides support for a dimer–tetramer oligomerization model. Expand
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