6 Result(s)
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MARIA PELLEGRINI
Science, Humanities and Social Sciences, multidisciplinary
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Article
Open AccessPublisher Correction: A disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
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Article
Open AccessA disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts
ToxR is a transmembrane transcription factor that, together with its integral membrane periplasmic binding partner ToxS, is conserved across the Vibrionaceae family. In some pathogenic Vibrios, including V. parah...
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Article
Open AccessThe IKK-binding domain of NEMO is an irregular coiled coil with a dynamic binding interface
NEMO is an essential component in the activation of the canonical NF-κB pathway and exerts its function by recruiting the IκB kinases (IKK) to the IKK complex. Inhibition of the NEMO/IKKs interaction is an att...
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Open AccessA new class of inhibitors of the AraC family virulence regulator Vibrio cholerae ToxT
Vibrio cholerae is responsible for the diarrheal disease cholera that infects millions of people worldwide. While vaccines protecting against cholera exist, and oral rehydration therapy is an effective treatment ...
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Open AccessA novel caspase 8 selective small molecule potentiates TRAIL-induced cell death
Recombinant soluble TRAIL and agonistic antibodies against TRAIL receptors (DR4 and DR5) are currently being created for clinical cancer therapy, due to their selective killing of cancer cells and high safety ...
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Article
Affinity labelling the acceptor site of the peptidyl transferase centre of the Escherichia coli ribosome
WE have identified two 50S proteins, L2 and L26-L27, in the peptidyl (P) site of the peptidyl transferase centre of E. coli ribosomes1 BrAc-3H-Phe-tRNAphe, a peptidyl-tRNA affinity analogue, was shown to bind spe...
