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ProteomicsVenomics of the East African green mamba and black mamba, highlights the complexity of their toxin arsenal
Complementary bottom-up MS/MS analyses for the venom phenotype map for the eastern green mamba and black mamba
ORGANISM(S): Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps) Dendroaspis polylepis polylepis (Black mamba) 
2016-06-27 | PXD003876 | Pride
Green mamba Venom Black mamba Venomics 
ProteomicsTop-down venomics of the East African green mamba and the black mamba
Top-down MS analysis of reduced venom from black and green mambas.
ORGANISM(S): Dendroaspis Angusticeps (ncbitaxon:8618) Dendroaspis Polylepis Polylepis (ncbitaxon:8620) 
2016-03-24 | MSV000079607 | MassIVE
UnknownIn vivo neutralization of dendrotoxin-mediated neurotoxicity of black mamba venom by oligoclonal human IgG antibodies.
Not available
S-EPMC6168529 | biostudies-literature
UnknownSelective blockade of Cav1.2 (α1C) versus Cav1.3 (α1D) L-type calcium channels by the black mamba toxin calciseptine.
Not available
S-EPMC10762068 | biostudies-literature
UnknownNeurotoxic Sleight of Fang: Differential Antivenom Efficacy Against Mamba (<i>Dendroaspis</i> spp.) Venom Spastic-Paralysis Presynaptic/Synaptic vs. Flaccid-Paralysis Postsynaptic Effects.
Not available
S-EPMC12568002 | biostudies-literature
UnknownBallistic study on the penetration potential and injury potential of different bullet types in the use of a newly developed bullet shooting stunner for adequate stunning of heavy cattle.
Not available
S-EPMC10014789 | biostudies-literature
UnknownStructural insights into human acid-sensing ion channel 1a inhibition by snake toxin mambalgin1.
Not available
S-EPMC7553779 | biostudies-literature
UnknownAn ecological analysis of snakes captured by C.J.P. Ionides in eastern Africa in the mid-1900s.
Not available
S-EPMC7083826 | biostudies-literature
UnknownStructure and analysis of nanobody binding to the human ASIC1a ion channel.
Not available
S-EPMC8318589 | biostudies-literature
UnknownCryo-EM structure of the ASIC1a-mambalgin-1 complex reveals that the peptide toxin mambalgin-1 inhibits acid-sensing ion channels through an unusual allosteric effect.
Not available
S-EPMC5986765 | biostudies-literature
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