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Correction: First Report of the Human-Pathogenic Enterocytozoon bieneusi from Red-Bellied Tree Squirrels (Callosciurus erythraeus) in Sichuan, China
[This corrects the article DOI: 10.1371/journal.pone.0163605.].
Journal Article
Squirrels
\"Developed by literacy experts for students in kindergarten through grade three, this book introduces squirrels to young readers through leveled text and related photos\"--Provided by publisher.
Book
Squirrels
\"Identify specific squirrel species. Explore their behavior, life cycle, mating habits, geographical location, anatomy, enemies, and defenses\"--Provided by publisher.
Book
Paraxerus cepapi (Rodentia: Sciuridae)
Paraxerus cepapi (A. Smith, 1836) is a rodent commonly called Smith's bush squirrel. Pelage color varies throughout its distribution, with grayer individuals in the western reaches of its distribution and more brown individuals in eastern areas. Paraxerus cepapi is 1 of 11 species in the genus Paraxerus and is found throughout sub-Saharan Africa. The International Union for the Conservation of Nature (IUCN) considers P. cepapi to be a species of “Least Concern” (LC), listing no major threats.
Journal Article
Squirrels
Readers will learn about this favorite common animal while strengthening reading skills.
Book
Red squirrels
\"Simple text and full-color photography introduce beginning readers to red squirrels. Developed by literacy experts for students in kindergarten through third grade\"-- Provided by publisher.
Book
Extracellular cap domain is an essential component of the TRPV1 gating mechanism
Transient receptor potential (TRP) channels are polymodal molecular sensors involved in numerous physiological processes and implicated in a variety of human diseases. Several structures of the founding member of the TRP channel family, TRPV1, are available, all of which were determined for the protein missing the N- and C-termini and the extracellular S5-P-loop. Here, we present structures of the full-length thirteen-lined ground squirrel TRPV1 solved by cryo-EM. Our structures resolve the extracellular cap domain formed by the S5-P-loops and the C-terminus that wraps around the three-stranded β-sheet connecting elements of the TRPV1 intracellular skirt. The cap domain forms a dome above the pore’s extracellular entrance, with four portals leading to the ion conductance pathway. Deletion of the cap increases the TRPV1 average conductance, reduces the open probability and affects ion selectivity. Our data show that both the termini and the cap domain are critical determinants of TRPV1 function.
Structural and functional characterization of the full-length TRPV1 channel from the thirteen-lined ground squirrel reveal the architecture of the extracellular cap domain and the intracellular C-terminus, and suggest a role of the cap domain in TRPV1 conductance and ion selectivity.
Journal Article