New nucleolin-containing cytoplasmic bodies in an archamoebian protist Pelomyxa belevskii (Amoebozoa, Archamoebae, Pelobiontida).

The representatives of the archamoebian genus Pelomyxa are amoeboid anaerobic protists that inhabit fresh-water anoxic sediments, and most of them are usually multinucleate. The cytoplasm of these unicellular organisms is highly complicated and contains numerous vacuoles of different types, as well as a wide range of prokaryotic endocytobionts, agglomerations of glycogen, lipids, etc. Among the great variety of cytoplasmic structures in P.

Characterization of intermediate states in the fibrillogenesis of odorant-binding proteins.

The transition of β-barrel proteins from a soluble to an amyloid form is biologically significant in some cases but may lead to functional activity loss. In particular, odorant-binding proteins' (OBPs) fibrils are unable to bind odorant molecules potentially contributing to olfactory dysfunction. As shown previously, OBPs' fibrillogenesis is initiated by uncoupling of protein C-terminal fragment from the β-barrel and exposing amyloidogenic sites.

Correction: Sulatskaya et al. Structural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T. 2018, , 2762.

In the original publication [...

Correction: Stepanenko et al. Trypsin Induced Degradation of Amyloid Fibrils. , , 4828.

In the original [...