Mammalian cytidine 5'-monophosphate N-acetylneuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs.

@article{Mnster1998MammalianC5,
  title={Mammalian cytidine 5'-monophosphate N-acetylneuraminic acid synthetase: a nuclear protein with evolutionarily conserved structural motifs.},
  author={Agnieszka M{\"u}nster and Matthias Eckhardt and Barry Potvin and Martina M{\"u}hlenhoff and Pamela Stanley and Rita Gerardy-Schahn},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 16},
  pages={9140-5}
}
Sialic acids of cell surface glycoproteins and glycolipids play a pivotal role in the structure and function of animal tissues. The pattern of cell surface sialylation is species- and tissue-specific, is highly regulated during embryonic development, and changes with stages of differentiation. A prerequisite for the synthesis of sialylated glycoconjugates is the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), which provides a substrate for Golgi… CONTINUE READING