CD47 does not mediate amyloid-β(1–42) protofibril-stimulated microglial cytokine release

Nordihydroguaiaretic acid does not disaggregate beta-amyloid(1-40) protofibrils but does inhibit growth arising from direct protofibril association.

Nordihydroguaiaretic acid (NDGA) was observed by Ono et al. (J Neurochem 87:172-181, 2002) to decrease the fluorescence of thioflavin T associated with freshly extended amyloid beta-protein (Abeta) fibrils. They concluded that NDGA could disaggregate Abeta fibrils into aggregates that were larger than monomers or oligomers and did not bind thioflavin T. Such an effect could be of therapeutic im...

Amyloid protofibril is highly voluminous and compressible.

We report here results of the first direct measurement of partial volume and compressibility changes of a protein as it forms an amyloid protofibril. We use a high precision density meter and an ultrasonic velocity meter on a solution of intrinsically denatured, disulfide-deficient variant of hen lysozyme, and follow the time-dependent changes in volume and compressibility, as the protein spont...

Transmigration but Attenuates Polymorphonuclear Neutrophil CD47 Deficiency Does Not Impede

The Amyloid-β-SDR5C1(ABAD) Interaction Does Not Mediate a Specific Inhibition of Mitochondrial RNase P

The amyloid-β peptide (Aβ) is suggested to cause mitochondrial dysfunction in Alzheimer's disease. The mitochondrial dehydrogenase SDR5C1 (also known as ABAD) was shown to bind Aβ and was proposed to thereby mediate mitochondrial toxicity, but the molecular mechanism has not been clarified. We recently identified SDR5C1 as an essential component of human mitochondrial RNase P and its associated...

Amyloid-β Protofibril Formation and Neurotoxicity Implications for Alzheimer’s Disease