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1 tant for the catalytic activity of bacterial type I signal peptidase.
2 operties of this enzyme were consistent with type I signal peptidase.
3 ion distinguishes Imp1p and Imp2p from other type I signal peptidases.
4 sition protein kinase 8) or Plsp1 (Plastidic type I signal peptidase 1), was replaced with the stop-t
7 signal peptide of 24 amino acids ending in a type I signal peptidase cleavage site of Leu-Ala-Ala.
8 espite partial conservation of motifs of the type I signal peptidase family proteins, SipA lacks the
11 of PhrA, PhrE, and PhrC suggested a role for type I signal peptidases in the processing of the Phr pr
12 ch act via the novel mechanism of inhibiting type I signal peptidase, is broader than previously beli
14 lipoprotein transferase), and lepB (encoding type I signal peptidase), monitored by real-time quantit
15 s study showing that residues comprising the type I signal peptidase signature in the two catalytic s
16 ime, successfully isolated Bacillus subtilis type I signal peptidase (SipS) and a truncated version l
21 well as other bacteria, is dependent on the type I signal peptidase (SPase)-mediated cleavage of the
22 A central event in protein secretion is the type I signal peptidase (SPase)-mediated cleavage of the
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