O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme
GAPDH colocalizes with viral RNA-dependentRNA polymerase in cells infected with Japanese encephalitis virus. GAPDH remains relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection and decreasing at 36 hours postinfection in the nuclear fraction of infected cells. There is no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of Japanese encephalitis virus. GAPDH binds to the minus-strand more efficiently than to the plus-strand of Japanese encephalitis virus RNAs
GAPDH colocalizes with viral RNA-dependentRNA polymerase in cells infected with Japanese encephalitis virus. GAPDH remains relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection and decreasing at 36 hours postinfection in the nuclear fraction of infected cells. There is no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of Japanese encephalitis virus. GAPDH binds to the minus-strand more efficiently than to the plus-strand of Japanese encephalitis virus RNAs
secreted GAPDH is located on the bacterial surface and released to the culture medium of enterohemorrhagic and enteropathogenic strains, secreted GAPDH remains associated with colonic Caco-2 epithelial cells after adhesion and binds human plasminogen and fribinogen, non-pathogenic Escherichia coli strains do not secrete GAPDH
GAPDH colocalizes with viral RNA-dependentRNA polymerase in cells infected with Japanese encephalitis virus. GAPDH remains relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection and decreasing at 36 hours postinfection in the nuclear fraction of infected cells. There is no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of Japanese encephalitis virus. GAPDH binds to the minus-strand more efficiently than to the plus-strand of Japanese encephalitis virus RNAs
GAPDH colocalizes with viral RNA-dependentRNA polymerase in cells infected with Japanese encephalitis virus. GAPDH remains relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection and decreasing at 36 hours postinfection in the nuclear fraction of infected cells. There is no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of Japanese encephalitis virus. GAPDH binds to the minus-strand more efficiently than to the plus-strand of Japanese encephalitis virus RNAs
O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme