The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling.

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The Biochemical Toxin Arsenal from Ant Venoms Intraspecific variations in the venom peptidome of the ant Odontomachus haematodus (Formicidae: Ponerinae) from French Guiana A comprehensive portrait of the venom of the giant red bull ant, , reveals a hyperdiverse hymenopteran toxin gene family

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P2860

The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling.

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2015 nî lūn-bûn

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The complexity and structural ...... y mass spectrometry profiling.

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The complexity and structural ...... y mass spectrometry profiling.

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The complexity and structural ...... y mass spectrometry profiling.

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The complexity and structural ...... y mass spectrometry profiling.

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Axel Touchard

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Jennifer M S Koh

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Pierre Escoubas

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Samira R Aili

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Disulfide bond contribution to protein stability: positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil.

A comparison of matrix-assisted laser desorption/ionization time-of-flight and liquid chromatography electrospray ionization mass spectrometry methods for the analysis of crude tarantula venoms in the Pterinochilus group.

Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and high-performance liquid chromatography study of quantitative and qualitative variation in tarantula spider venoms.

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385-396

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scholarly article

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10.1002/RCM.7116

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Alain Dejean

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Graham M Nicholson

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2015-03-01T00:00:00Z

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venom

The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling.

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P2860

P2860

The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling.

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