Extracellular vesicles as a platform to study cell-surface membrane proteins

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Publikováno v: In Methods 1 August 2020 180:35-44

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X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form

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Structure-Function Analysis of Grass Clip Serine Protease Involved in Drosophila Toll Pathway Activation

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Anchoring the T6SS to the Cell Wall: Crystal Structure of the Peptidoglycan Binding Domain of the TagL Accessory Protein

Autor: Nguyen, Van Son, Spinelli, Silvia, Cascales, E., Roussel, Alain, Cambillau, Christian, Leone, Philippe

Publikováno v: PLoS ONE
PLoS ONE, 2021
'PloS One ', vol: 16, pages: e0254232-1-e0254232-10 (2021)
PLoS ONE, Public Library of Science, 2021
PLoS ONE, 2021, 16 (7), pp.e0254232. ⟨10.1371/journal.pone.0254232⟩
PLoS ONE, Public Library of Science, 2021, 16 (7), pp.e0254232. ⟨10.1371/journal.pone.0254232⟩
PLoS ONE, Vol 16, Iss 7, p e0254232 (2021)

International audience; The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, a

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https://hal.science/hal-03358248