The protein p26 is a small heat shock protein that functions as a molecular chaperone to
protect embryos by preventing irreversible protein damage during embryonic development …

p26, a small heat shock protein, is thought to protect Artemia embryos from stress during
encystment and diapause. Full-length p26 cDNAs were compared and used to determine …

Molecular chaperones protect cells during stress by limiting the denaturation/aggregation of
proteins and facilitating their renaturation. In this context, brine shrimp embryos can endure …

Abstract p26, an abundantly expressed small heat shock protein, is thought to establish
stress resistance in oviparously developing embryos of the crustacean Artemia franciscana …

Artemia franciscana embryos undergo encystment, developmental arrest and diapause, the
last characterized by profound metabolic dormancy and extreme stress resistance. Encysted …

The small heat shock proteins function as molecular chaperones, an activity often requiring
reversible oligomerization and which protects against irreversible protein denaturation. An …

The role of the small heat shock/α-crystallin protein, p26, in transcription in Artemia
franciscana embryos was examined using isolated nuclei, containing either control or …

Encysted brine‐shrimp gastrulae bring their metabolism to a reversible standstill during
diapause and quiescence, demonstrating a remarkable resistance to unfavourable …

Oviparously developing embryos of the brine shrimp, Artemia franciscana, synthesize
abundant quantities of a small heat shock/α‐crystallin protein, termed p26. Wild‐type p26 …

Oviparous development in the extremophile crustacean, Artemia franciscana, generates
encysted embryos which enter a profound state of dormancy, termed diapause. Encystment …