Jun 25, 2019 · The Functional Mammalian CRES (Cystatin-Related Epididymal Spermatogenic) Amyloid is Antiparallel β-Sheet Rich and Forms a Metastable Oligomer During Assembly. Sci Rep 9 , 9210 (2019). https ...

The CRES oligomer was resistant to further assembly and only over extended time transitioned into higher ordered antiparallel β-sheet rich amyloids. However, the addition of CRES amyloid seeds, generated in vitro or in the form of endogenous epididymal …

CRes is unique in that its amyloids are rich in antiparallel β-sheets instead of the more common parallel β-sheets. taken together, our studies suggest that early metastable oligomers may serve ...

Accumulating evidence shows that amyloids perform biological roles. We previously showed that an amyloid matrix composed of four members of the CRES subgroup of reproductive family 2 cystatins is a normal component of the mouse epididymal lumen. The cellular mechanisms that control the assembly of these and other functional amyloid structures, however, remain unclear. We speculated that cross ...

Jun 25, 2019 · However, CRES is unique in that its amyloids are rich in antiparallel β-sheets instead of the more common parallel β-sheets. Taken together, our studies suggest that early metastable oligomers may serve as building blocks for functional amyloid assembly and further reveal that antiparallel β-sheet-rich amyloids can be functional forms.

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Download scientific diagram | CRES structural conversion involves α-helix to antiparallel β-sheet transition. (a) CD was performed approximately once a week for 12 weeks (W0-W12) on the same ...

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