Search Results - "Bende, Niraj S"
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Production of recombinant disulfide-rich venom peptides for structural and functional analysis via expression in the periplasm of E. coli
Published in PloS one (07-05-2013)“…Disulfide-rich peptides are the dominant component of most animal venoms. These peptides have received much attention as leads for the development of novel…”
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Journal Article -
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A distinct sodium channel voltage-sensor locus determines insect selectivity of the spider toxin Dc1a
Published in Nature communications (11-07-2014)“…β-Diguetoxin-Dc1a (Dc1a) is a toxin from the desert bush spider Diguetia canities that incapacitates insects at concentrations that are non-toxic to mammals…”
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insecticidal spider toxin SFI1 is a knottin peptide that blocks the pore of insect voltage‐gated sodium channels via a large β‐hairpin loop
Published in The FEBS journal (01-03-2015)“…Spider venoms contain a plethora of insecticidal peptides that act on neuronal ion channels and receptors. Because of their high specificity, potency and…”
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Journal Article -
4
The insecticidal neurotoxin Aps III is an atypical knottin peptide that potently blocks insect voltage-gated sodium channels
Published in Biochemical pharmacology (15-05-2013)“…One of the most potent insecticidal venom peptides described to date is Aps III from the venom of the trapdoor spider Apomastus schlingeri. Aps III is highly…”
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The insecticidal spider toxin SFI 1 is a knottin peptide that blocks the pore of insect voltage‐gated sodium channels via a large β‐hairpin loop
Published in The FEBS journal (01-03-2015)“…Spider venoms contain a plethora of insecticidal peptides that act on neuronal ion channels and receptors. Because of their high specificity, potency and…”
Get full text
Journal Article -
6
The insecticidal spider toxin SFI1 is a knottin peptide that blocks the pore of insect voltage-gated sodium channels via a large [beta]-hairpin loop
Published in The FEBS journal (01-03-2015)“…Spider venoms contain a plethora of insecticidal peptides that act on neuronal ion channels and receptors. Because of their high specificity, potency and…”
Get full text
Journal Article -
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Production of Recombinant Disulfide-Rich Venom Peptides for Structural and Functional Analysis via Expression in the Periplasm of E. coli. e63865
Published in PloS one (01-05-2013)“…Disulfide-rich peptides are the dominant component of most animal venoms. These peptides have received much attention as leads for the development of novel…”
Get full text
Journal Article