Mohammed Moudjou

Prion protein is secreted in soluble forms in the epididymal fluid and proteolytically processed and transported in seminal plasma.

Glycan-controlled epitopes of prion protein include a major determinant of susceptibility to sheep scrapie.

Prion proteins from susceptible and resistant sheep exhibit some distinct cell biological features.

Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep.

Glycan chains modulate prion protein binding to immobilized metal ions.

The respiratory syncytial virus M2-1 protein forms tetramers and interacts with RNA and P in a competitive manner.

Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent.

PB1-F2 influenza A virus protein adopts a beta-sheet conformation and forms amyloid fibers in membrane environments.

Characterization of spontaneously generated prion-like conformers in cultured cells.

Integrity of helix 2-helix 3 domain of the PrP protein is not mandatory for prion replication.

Nucleoprotein nanostructures combined with adjuvants adapted to the neonatal immune context: a candidate mucosal RSV vaccine.

Mammalian prions: tolerance to sequence changes-how far?

Glycoform-selective prion formation in sporadic and familial forms of prion disease.

Plasminogen-based capture combined with amplification technology for the detection of PrP(TSE) in the pre-clinical phase of infection.

Shadoo binds lipid membranes and undergoes aggregation and fibrillization.

Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.

Highly infectious prions generated by a single round of microplate-based protein misfolding cyclic amplification.

Preclinical detection of variant CJD and BSE prions in blood.

Identification and characterization of the binding site of the respiratory syncytial virus phosphoprotein to RNA-free nucleoprotein.

Interaction between Shadoo and PrP Affects the PrP-Folding Pathway.

C-Nap1 mutation affects centriole cohesion and is associated with a Seckel-like syndrome in cattle.

Mutated but not deleted ovine PrPC N-terminal polybasic region strongly interferes with prion propagation in transgenic mice.