Misfolding of transthyretin in vivo is controlled by the redox environment and macromolecular crowding.

Transthyretin (TTR) amyloidosis is a progressive disorder characterized by peripheral neuropathy, autonomic dysfunction, and cardiomyopathy. The precise mechanism by which TTR misfolds and forms fibrils in vivo remains incompletely understood, posing challenges to the development of effective therapeutics. In this study, we reveal that the recently identified nonnative pathological species of TTR (NNTTR), which is enriched in the plasma of ttr-val30met gene carriers, exhibits strong amyloidogenic properties, making it a promising therapeutic target.

Site-specific sulfations regulate the physicochemical properties of papillomavirus-heparan sulfate interactions for entry.

Certain human papillomaviruses (HPVs) are etiological agents for several anogenital and oropharyngeal cancers. During initial infection, HPV16, the most prevalent cancer-causing type, specifically interacts with heparan sulfates (HSs), not only enabling initial cell attachment but also triggering a crucial conformational change in viral capsids termed structural activation. It is unknown, whether these HPV16-HS interactions depend on HS sulfation patterns.

Jejunal amyloidosis: a rare case presented with sudden weight loss and altered bowel habits.

Amyloidosis is a multisystem disease characterized by the extracellular deposition of abnormal protein fibrils in various tissues and organs. It is a systemic disease mainly affecting the kidneys, liver, and spleen. In the GI tract, the duodenum is most commonly involved, followed by the stomach.