Pulse Explorar nav.journalClub Debates Tendencias Investigadores Revistas

Join discussions, follow papers, and never miss your next session.

Download on theApp Store

Inicio Explorar nav.journalClub Tendencias

⌘+K

Structural Basis of Glycoform Selectivity in Prion Strains | Synapse

January 25, 2026

Ver artículo completo

Structural Basis of Glycoform Selectivity in Prion Strains

FPFrancesca PeccatiIkerbasque

Puntos clave

To elucidate the structural mechanisms underlying glycoform selectivity in prion strains.
Analyzed the conformational differences of PrP C and PrP Sc
Examined the aggregation propensity of various glycoforms
Utilized structural biology techniques to assess conformational stability
Identified distinct structural features that influence glycoform selectivity
Showed varying aggregation rates corresponding to glycoform variations
Revealed insights into the relationship between glycoform structure and pathogenicity

Resumen

Prion diseases originate from the pathological misfolding of the cellular sialoglycoprotein prion protein (PrP C ), universally found across mammalian species, into an aberrant conformation termed PrP Sc , which exhibits high aggregation propensity...

Preguntar a la IA

Me gusta

Guardar

Compartir

Ver artículo completo

Preguntar a la IA

Me gusta

Guardar

Compartir

Ver artículo completo

Cite This Study

Francesca Peccati (Thu,) studied this question.

synapsesocial.com/papers/6975b1eafeba4585c2d6d6a5 https://doi.org/https://doi.org/10.1039/d5cp04286k