2019
DOI: 10.1016/j.actatropica.2018.10.008
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Identification, characterization and expression analysis of Anopheles stephensi double peroxidase

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Cited by 5 publications
(8 citation statements)
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“…For colony propagation, 4-to 5-day-old females were fed on anesthetized mice and their eggs were collected in moist conditions. The hatched larvae were floated in water to continue the life cycle and fed on a 1:1 mixture of dog food (Pet Lover's crunch milk biscuit, India) and fish food (Gold Tokyo, India) (Gupta et al, 2017;Choudhury et al, 2019;Kakani et al, 2019).…”
Section: Rearing Of Mosquitoesmentioning
confidence: 99%
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“…For colony propagation, 4-to 5-day-old females were fed on anesthetized mice and their eggs were collected in moist conditions. The hatched larvae were floated in water to continue the life cycle and fed on a 1:1 mixture of dog food (Pet Lover's crunch milk biscuit, India) and fish food (Gold Tokyo, India) (Gupta et al, 2017;Choudhury et al, 2019;Kakani et al, 2019).…”
Section: Rearing Of Mosquitoesmentioning
confidence: 99%
“…The best matching An. stephensi contig 7145 (SuperContig KB664566 and Ensembl identifier ASTE003848) was analyzed using Augustus software to identify the full-length putative AsHPX2 gene as before (Stanke et al, 2008;Choudhury et al, 2019;Kakani et al, 2019). AsHPX2 and AgHPX2 gene sequences were aligned to design gene-specific primers.…”
Section: Retrieval Of Heme Peroxidase Ashpx2mentioning
confidence: 99%
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“…DBLOX is a unique enzyme with two duplicated heme peroxidase domains that is present in insects, but not in vertebrates. The first domain has the predicted substrate binding sites but lacks the functional residues present in catalytically active enzymes and has two integrin-binding motifs, typical of peroxinectins (17). In contrast, the second domain has all the features of a functional heme peroxidase and one integrin-binding motif (17).…”
Section: Antibodies To Recombinant Dblox Detected a Single Band Undermentioning
confidence: 99%
“…The first domain has the predicted substrate binding sites but lacks the functional residues present in catalytically active enzymes and has two integrin-binding motifs, typical of peroxinectins (17). In contrast, the second domain has all the features of a functional heme peroxidase and one integrin-binding motif (17). DBLOX is essential for LXA 4 synthesis, but the biochemical mechanism of lipoxygenase-independent lipoxin synthesis in insects, and the potential involvement of other enzymes besides DBLOX remain to be explored.…”
Section: Antibodies To Recombinant Dblox Detected a Single Band Undermentioning
confidence: 99%