2015
DOI: 10.1016/j.dci.2014.05.020
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Sequence diversity and evolution of antimicrobial peptides in invertebrates

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Cited by 150 publications
(119 citation statements)
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“…For instance, in P. monodon, a Type IIa crustin is essentially active against Gram-positive bacteria, while Type IIb crustins are active against both Gram-positive and Gramnegative bacteria [69,70]. Interestingly, Type III and IV crustins show antimicrobial and/or antiprotease activity [67], whereas Type III crustins lacking the N-terminal proline/argininedomain and Type IV crustins from shrimp [71,72] only have antiprotease activity [67]. Type IV crustins from crabs exhibit both antimicrobial and antiprotease activities [72,73].…”
Section: (Iii) Crustinsmentioning
confidence: 99%
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“…For instance, in P. monodon, a Type IIa crustin is essentially active against Gram-positive bacteria, while Type IIb crustins are active against both Gram-positive and Gramnegative bacteria [69,70]. Interestingly, Type III and IV crustins show antimicrobial and/or antiprotease activity [67], whereas Type III crustins lacking the N-terminal proline/argininedomain and Type IV crustins from shrimp [71,72] only have antiprotease activity [67]. Type IV crustins from crabs exhibit both antimicrobial and antiprotease activities [72,73].…”
Section: (Iii) Crustinsmentioning
confidence: 99%
“…Crustins are antimicrobial polypeptides (6-22 kDa; pI 4-8) containing a whey acidic protein (WAP) domain [67]. This WAP domain, which is also found in some mammalian proteins, supports different biological functions, including antiprotease activities [68].…”
Section: (Iii) Crustinsmentioning
confidence: 99%
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“…Moreover, AMPs have other functions such as fostering the right conditions for mutualists and acting as modulators of the immune response [9][10][11]. A large number of studies and reviews on AMPs have been published to date, but the majority of studies on arthropod AMPs have focused on their biochemical and molecular properties [12][13][14].…”
Section: Introductionmentioning
confidence: 99%
“…Zhang and Zhu (2012) also classified four types of crustins, including insect crustins containing an extra aromatic amino acidrich region between the cysteine-rich domain and WAP domain. Tassanakajon et al [37] classified all crustins into five groups, namely, type I, type II, type III, type IV, and type V. Type I crustins contain a signal peptide and cysteine-rich region at the N-terminus, and WAP domain at the C-terminus. Type II crustins have an extra glycine-rich domain between the signal peptide and cysteine-rich domain.…”
Section: Discussionmentioning
confidence: 99%