Selected article for: "polymerase domain and thumb domain"

Author: Al-Mulla, Hawaa M. N.; Turrell, Lauren; Smith, Nicola M.; Payne, Luke; Baliji, Surendranath; Züst, Roland; Thiel, Volker; Baker, Susan C.; Siddell, Stuart G.; Neuman, Benjamin W.
Title: Competitive Fitness in Coronaviruses Is Not Correlated with Size or Number of Double-Membrane Vesicles under Reduced-Temperature Growth Conditions
  • Document date: 2014_4_1
  • ID: tfuupgkg_6
    Snippet: Albts16 has a mutation in a loop within the carboxyl-terminal domain of M pro (23, 31) . Albts22 has a mutation in the predicted thumb domain of the polymerase fold near the carboxyl terminus of nsp12 (23, 32) . Wüts18 has a mutation on the surface of the viral 2=-O-methyltransferase (23, 33) . The last mutant chosen was the previously undescribed Brts105, which contains a single proline to serine substitution (CCA to UCA) at position 19320 in s.....
    Document: Albts16 has a mutation in a loop within the carboxyl-terminal domain of M pro (23, 31) . Albts22 has a mutation in the predicted thumb domain of the polymerase fold near the carboxyl terminus of nsp12 (23, 32) . Wüts18 has a mutation on the surface of the viral 2=-O-methyltransferase (23, 33) . The last mutant chosen was the previously undescribed Brts105, which contains a single proline to serine substitution (CCA to UCA) at position 19320 in sequence AY700211 (Fig. 1) . The Brts105 mutation falls in the viral N7methyltransferase domain of nsp14 (34) , between the previously characterized Wüts38 and Albts17 mutations, both of which map to cistron IV (23) .

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