@LeaLabTweets

Structural biology lab at NCI-Frederick. Formerly University of Oxford. Studying protein structures at the host-pathogen interface. All views are our own.

 Frederick, MD
Joined February 2013
  • Tweets101
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Thank you to @robinson_julia of Chemistry World (Royal Society of Chemistry) for a lovely write up of our work. Read the article here: chemistryworld.com/news/ultr…. And for the original paper: nature.com/articles/s41564-0…
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Using cryo-electron microscopy two different groups have revealed new insights into how flagellum power bacteria to get where they're going. @robinson_julia reports: chemistryworld.com/news/ultr…
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Replying to @christo71213435 @STCmicrobeblog
Thank you for the kind words. We will look forward to the blog.
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Reducing the complexity of a fascinating molecular motor. Read our Behind the Paper blog, where we detail our journey to deciphering the structural basis for how bacterial flagella shift into reverse gear: communities.springernature.c…
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New meningitis vaccine developed by the @TangLabOxford! The new chimeric protein-based #vaccine to tackle #MenB is the result of a strategic collaboration between @UniofOxford & @SerumInstIndia Find out more: path.ox.ac.uk/news-article/n…
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Also hot off the press! Our latest article on the structural analysis of protein transport by the T9SS is out now 👇nature.com/articles/s41564-0…

Structural insights into the mechanism of protein transport by the Type 9 Secretion System transl...

Nature Microbiology - Cryo-EM analysis of the substrate-bound T9SS from Flavobacterium johnsoniae reveals an extended translocon complex and provides insight into protein secretion.

nature.com
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Thrilled to share that we teamed up across @theNCI and @nih_nhlbi to discover #degraders against #hRpn13 that trigger #apoptosis in #cancer cells in a study led by @xiuxiu_lu with structural data from @Monikachandrav2. 🎉 link.springer.com/10.1038/s4…

A structure-based designed small molecule depletes hRpn13Pru and a select group of KEN box proteins

Nature Communications - Here, the authors identify a small molecule degrader (XL44) for hRpn13 and solve the XL44-hRpn13 structure. XL44 induces apoptosis in myeloma cells with hRpn13 dependency...

link.springer.com
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Lea Lab retweeted
Susan Lea@S_M_Lea8 Mar 2024
Published today @SJohnsonDPhil and @justindeme85 story finally revealing the molecular basis for transmission of uni-directional ion flow into bi-directional rotation of the bacterial flagellum doi.org/10.1038/s41564-024-0… – at Frederick, MD
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Check out our latest paper where we identify a new C-terminal export signal in flagellar Type III secretion substrates which provides further evidence against a subunit capture/chain mechanism for flagellar assembly. doi.org/10.1128/mbio.03067-2…

Identification of a new export signal that targets early subunits to the flagellar type III...

Many bacterial pathogens utilize T3SS to inject virulence proteins (effectors) into host cells or to assemble flagella on the bacterial cell surface. Bacterial flagella present a paradigm for how...

journals.asm.org
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Very happy to share some work from my PhD which is now published in Nature Communications! We have identified a new type of T7SS substrate which has a strange ‘reverse’ secretion signal. doi.org/10.1038/s41467-023-4…

A type VII-secreted lipase toxin with reverse domain arrangement

Nature Communications - Here Garrett et al. describe a toxin, TslA, secreted by type VII secretion system that has a reverse domain arrangement compared to other previously characterised...

nature.com
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Check out our new paper @ nature.com/articles/s41467-0… from my time working in the fantastic Chung lab @TranslatingRNA. Also check out our "Behind the Paper" post go.nature.com/3GCnE09. @ Filip Lastovka, @TranslatingRNA, @CamPathology, @OJ_Bryant. More to come from us soon!
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