Giuseppe MichieliJan 23
Intra-patient #neuraminidase #mutations in avian #H5N1 #influenza virus reduce #sialidase activity to complement weaker hemagglutinin binding and facilitate #human infection, https://etidiohnew.blogspot.com/2026/01/intra-patient-neuraminidase-mutations.html
Intra-patient #neuraminidase #mutations in avian #H5N1 #influenza virus reduce #sialidase activity to complement weaker hemagglutinin binding and facilitate #human infection

StructBiolCommunicationsApr 18, 2023
The structure of the sialidase SiaPG complexed with tartrate, along with a product-binding simulation and kinetic analysis of mutants, establishes key residues required for its enzymatic activity. #Sialidase #PorphyromonasGingivalis #Crystallography https://doi.org/10.1107/S2053230X23001735
Structural and enzymatic characterization of the sialidase SiaPG from Porphyromonas gingivalis

The crystal structure of the sialidase SiaPG from Porphyromonas gingivalis, a pathogenic bacterium which causes human periodontal disease, is reported.

Acta Crystallographica Section F
StructBiolCommunicationsMar 31, 2023
WenBo Dong et al.: Structural and enzymatic characterization of the sialidase SiaPG from Porphyromonas gingivalis #Sialidase #PorphyromonasGingivalis #Crystallography ... #IUCr http://scripts.iucr.org/cgi-bin/paper?S2053230X23001735
Structural and enzymatic characterization of the sialidase SiaPG from Porphyromonas gingivalis

The crystal structure of the sialidase SiaPG from Porphyromonas gingivalis, a pathogenic bacterium which causes human periodontal disease, is reported.

Acta Crystallographica Section F