Refolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase

Ítems similars

• S-Adenosyl-Homocysteine Is a Weakly Bound Inhibitor for a Flaviviral Methyltransferase
  per: Chen, Hui, et al.
  Publicat: (2013)
• Novel Broad Spectrum Inhibitors Targeting the Flavivirus Methyltransferase
  per: Brecher, Matthew, et al.
  Publicat: (2015)
• Using S-adenosyl-L-homocysteine capture compounds to characterize S-adenosyl-L-methionine and S-adenosyl-L-homocysteine binding proteins
  per: Brown, Lindsey J., et al.
  Publicat: (2014)
• Identification and Characterization of Novel Broad-Spectrum Inhibitors of the Flavivirus Methyltransferase
  per: Brecher, Matthew, et al.
  Publicat: (2015)
• Uptake and Utilization of S-Adenosyl-l-Methionine and S-Adenosyl-l-Homocysteine in an Adenine Mutant of Saccharomyces cerevisiae
  per: Knudsen, Richard C., et al.
  Publicat: (1969)