2009
DOI: 10.1016/j.fsi.2009.08.005
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A clip domain serine protease (cSP) from the Chinese mitten crab Eriocheir sinensis: cDNA characterization and mRNA expression

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Cited by 31 publications
(12 citation statements)
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“…They are consistent with the known crustacean clip domain serine proteases or PPAFs [8,21,22]. Unlike commonly encountered substitution of S (Ser) to G (Gly) at the third catalytic site, the second catalytic site D (Asp) is replaced by amino acid A (Ala) for PtcSPH.…”
Section: Discussionsupporting
confidence: 81%
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“…They are consistent with the known crustacean clip domain serine proteases or PPAFs [8,21,22]. Unlike commonly encountered substitution of S (Ser) to G (Gly) at the third catalytic site, the second catalytic site D (Asp) is replaced by amino acid A (Ala) for PtcSPH.…”
Section: Discussionsupporting
confidence: 81%
“…For example, FcSPH was mainly distributed in heart, gill, stomach, intestine and its expression level was lower in haemocytes and hepatopancreas [12]. EscSP mRNA expression was highest in muscle [8]. PtSPH is strongly expressed in eyestalk [9].…”
Section: Discussionmentioning
confidence: 99%
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“…However, in E. sinensis, the temporal response of immune-related gene expression is both gene-and bacteriadependent. The pathogen L. anguillarum, elicited two peaks in EscSP expression at 2 h and 12 h post-injection (4.96 and 9.90 fold, respectively) [57], the other hand, V. anguillarum induced three EsproPO peaks at 2 h (3.68 fold), 12 h (32.1 fold), and 48 h (18.6 fold) post-injection [58]. The collective results indicate that E. sinensis caspase and nm23 are constitutive and inducible acute-phase proteins involved in defense response against bacterial infection.…”
Section: Discussionmentioning
confidence: 99%