Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/4473
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dc.contributor.authorMondal, Anish Kumar-
dc.contributor.authorLata, Kusum-
dc.contributor.authorSingh, Mahendra-
dc.contributor.authorChatterjee, Shamaita-
dc.contributor.authorChauhan, Aakanksha-
dc.contributor.authorPuravankara, Sindhoora-
dc.contributor.authorChattopadhyay, Kausik-
dc.date.accessioned2023-08-10T11:28:35Z-
dc.date.available2023-08-10T11:28:35Z-
dc.date.issued2022-
dc.identifier.citationBiochimica et Biophysica Acta - Biomembranes, 1864(11), 184013.en_US
dc.identifier.urihttps://doi.org/10.1016/j.bbamem.2022.184013-
dc.identifier.urihttp://hdl.handle.net/123456789/4473-
dc.descriptionOnly IISERM authors are available in the record.en_US
dc.description.abstractPore-forming toxins (PFTs) rupture plasma membranes and kill target cells. PFTs are secreted as soluble monomers that undergo drastic structural rearrangements upon interacting with the target membrane and generate transmembrane oligomeric pores. A detailed understanding of the molecular mechanisms of the pore-formation process remains unclear due to limited structural insights regarding the transmembrane oligomeric pore states of the PFTs. However, recent advances in the field of cryo-electron microscopy (cryo-EM) have led to the high-resolution structure determination of the oligomeric pore forms of diverse PFTs. Here, we discuss the pore-forming mechanisms of various PFTs, specifically the mechanistic details contributed by the cryo-EM-based structural studies.en_US
dc.language.isoen_USen_US
dc.publisherELSEVIERen_US
dc.subjectCryo-EM elucidates mechanismen_US
dc.subjectbacterial pore-forming toxins Author links open overlay panelen_US
dc.titleCryo-EM elucidates mechanism of action of bacterial pore-forming toxins.en_US
dc.typeArticleen_US
Appears in Collections:Research Articles

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