“…For example, the highly resistant HydR3 + isolates were found to contain point mutations leading to amino acid changes at position F412S, F412I or F412V, while similar studies have shown that other changes at L195F, S336C, V309M, A314V, N369C and L400S/F can also lead to fenhexamid resistance (Billard et al., ; Fillinger et al., ; Weber, ). Another study of fenhexamid‐resistant (HydR) isolates in Zhejiang identified seven amino acid changes (S9G, P57A, P269L, V365A, E368D, E375K and A378T) that could be important in fenhexamid resistance (Yin et al., ), and it has been suggested that these mutations and genetic polymorphism in the erg27 genes of fenhexamid‐resistant isolates of B. cinerea could contribute to the unfavourable binding of fenhexamid to its 3‐ketoreductase target (Debieu et al., ; Yin et al., ). The molecular analysis of the resistant isolates (163‐6 and 163‐22) collected from Xinjiang in the current study indicated that they contained three of the four mutations, V365A, E368D and A378T, associated with the type II resistant mutant TZ2‐5 characterized by Yin et al.…”