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1 to LexA-like proteases and Escherichia coli signal peptidase I.
2 s identified as a substrate of S. pneumoniae signal peptidase I.
3 yme in the ER contains proteins unrelated to signal peptidase I.
5 (SPase) can change the specificity such that signal peptidase is able to cleave pro-OmpA nuclease A i
6 d R. typhi have been demonstrated to possess signal peptidase I activity in Escherichia coli preprote
8 the evidence suggests that it is cleaved by signal peptidase I and a 19-residue C-terminal domain is
9 ey P3 substrate specificity determinants for signal peptidase I and demonstrates the power of the flu
12 ues serine 38 and lysine 76 of S. pneumoniae signal peptidase I are critical for enzyme activity and
13 erved region, Box E, of the Escherichia coli signal peptidase I are critical for maintaining a functi
14 These data provide the first evidence that a signal peptidase is bifunctional and that SipW has a reg
15 via the novel mechanism of inhibiting type I signal peptidase, is broader than previously believed an
16 was inhibited by a C(16) compound targeting signal peptidase I, but not by a C(1) compound known to
18 imilar to LexA-like proteases, S. pneumoniae signal peptidase I catalyzes an intermolecular self-clea
19 etwork trained to identify the most probable signal peptidase I cleavage site of secreted proteins.
23 roteases including calpain, metacaspase, and signal peptidase I have been implicated to be central me
24 proposed for the catalytic dyad mechanism of signal peptidase I in which the general base Lys-145 is
27 we have cloned, expressed, and purified the signal peptidase I of gram-positive Streptococcus pneumo
31 s (HCV) E2-p7-NS2 precursor mediated by host signal peptidase is relatively inefficient, resulting in
32 of the consensus endoplasmic reticulum (ER) signal peptidase I site within exon 3 (UL37x3) were repl
34 -144 and Ile-86 residues in Escherichia coli signal peptidase I (SPase) can change the specificity su
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