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

Benzer Materyaller

• Characterization of the Deoxynucleotide Triphosphate Triphosphohydrolase (dNTPase) Activity of the EF1143 Protein from Enterococcus faecalis and Crystal Structure of the Activator-Substrate Complex
  Yazar:: Vorontsov, Ivan I., ve diğerleri
  Baskı/Yayın Bilgisi: (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
  Baskı/Yayın Bilgisi: (2014)
• Substrate specificity of SAMHD1 triphosphohydrolase activity is controlled by deoxyribonucleoside triphosphates and phosphorylation at Thr592
  Yazar:: Jang, Sunbok, ve diğerleri
  Baskı/Yayın Bilgisi: (2016)
• Structural Basis of Allosteric Activation of Sterile α Motif and Histidine-Aspartate Domain-containing Protein 1 (SAMHD1) by Nucleoside Triphosphates
  Yazar:: Koharudin, Leonardus M. I., ve diğerleri
  Baskı/Yayın Bilgisi: (2014)
• Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity
  Yazar:: Vorontsov, Ivan I., ve diğerleri
  Baskı/Yayın Bilgisi: (2007)