Mechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalis

Eitemau Tebyg

• Characterization of the Deoxynucleotide Triphosphate Triphosphohydrolase (dNTPase) Activity of the EF1143 Protein from Enterococcus faecalis and Crystal Structure of the Activator-Substrate Complex
  gan: Vorontsov, Ivan I., et al.
  Cyhoeddwyd: (2011)
• Figuring out How a Deoxyribonucleoside Triphosphate Triphosphohydrolase Functions in a Pathogenic Bacterium♦: Mechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalis
  Cyhoeddwyd: (2014)
• Substrate specificity of SAMHD1 triphosphohydrolase activity is controlled by deoxyribonucleoside triphosphates and phosphorylation at Thr592
  gan: Jang, Sunbok, et al.
  Cyhoeddwyd: (2016)
• Structural Basis of Allosteric Activation of Sterile α Motif and Histidine-Aspartate Domain-containing Protein 1 (SAMHD1) by Nucleoside Triphosphates
  gan: Koharudin, Leonardus M. I., et al.
  Cyhoeddwyd: (2014)
• Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity
  gan: Vorontsov, Ivan I., et al.
  Cyhoeddwyd: (2007)