Amyloid diseases display the presence, in targeted tissues and organs, of fibrillar deposits of
specific peptides or proteins. Increasing efforts are presently spent in investigating the …

Several human degenerative diseases involve amyloidogenic peptides/proteins with high
conformational plasticity and propensity to self-aggregate into polymeric fibrillar assemblies …

Glycosaminoglycans (GAGs), which are found in association with all extracellular amyloid
deposits in humans, are known to accelerate the aggregation of various amyloidogenic …

Recently, it was suggested that maternal T and potentially B cells transferred during
pregnancy and/or the breast milk feeding and their encounter with the antigen in mesenteric …

Polyanionic candidate microbicides, including cellulose sulfate, carrageenan, PRO 2000,
were proven ineffective in preventing HIV-1 transmission and even cellulose sulfate showed …

Protein aggregation and amyloid formation are associated with both pathological conditions
in humans such as Alzheimer's disease and native functions such as peptide hormone …

Many human diseases are caused by the conversion of proteins from their native state into
amyloid fibrils that deposit in the extracellular space. Heparan sulfate, a component of the …

Prion diseases are transmissible neurodegenerative disorders associated with the
conversion of the cellular prion protein, PrPC, to a misfolded isoform called PrPSc. Although …

Glycosaminoglycans (GAGs) are related to multiple biological functions and diseases. There
is growing evidence that GAG concentration and sulfate content increase with age. The …

Chondroitin sulfate proteoglycans (CSPGs) are complex biomolecules that are known to
facilitate patterning of axonal direction and cell migration during the early growth and …