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Assistant Professor at the University of Virginia, Biochemist, Molecular and Structural Biologist, Husband, Father, Traveller #cryoem #ribosome #rna med.virginia.edu/jomaa-lab/
Ahmad Jomaa








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www.nature.com/articles/s41...
Excited to share our work uncovering SNOR, a ribosome-associated factor that promotes translation restart after dormancy published in Nature!! This was, as usual, a wonderful collaborative effort between our group and the Mattei Lab @simonemattei.bsky.social @embl.org www.nature.com/articles/s41...
Disrupting phage liquid crystalline droplets restores antibiotic susceptibility in Pseudomonas aeruginosa biofilms out in @plosbiology.org by @abultarafder.bsky.social and team. Exciting collaboration with @geiselbiofilm.bsky.social @pearce-maths.bsky.social and others
🛠️💉It's time for engineering contractile injection systems! @chipericson.bsky.social & @davidschaumann.bsky.social introduce programmable CIS - PROCIS, combining tail length control, non-native cargo loading, and cell retargeting all in one system! www.biorxiv.org/content/10.6... 🧵 1/5
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For years, the #cryoEM community viewed ~50 kDa as the practical lower size limit for SPA. This was challenged by Kim et al., who introduced the HR-HAIR method and demonstrated structure determination of proteins below 30 kDa using #CryoSPARC. Read more 👉 bit.ly/3RHMxAt
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Our findings enabled through an integration across scales from cellular in situ structural biology to mechanistic biochemistry and physiology, reveal that translation restart is a regulated process rather than simply a passive recovery from dormancy.
This work is made possible through wonderful collaborations with the Gould Lab @gouldlab.bsky.social at Vanderbilt and the Feaga Lab @heatherfeaga.bsky.social at Cornell. Big congratulations to co-first authors Maciej and Higor, and to the entire team for the immense effort!!
Improved fractionation strategies can identify antibiotics with previously unseen scaffolds and mechanisms, exemplified by manikomycin from Streptomyces rimosus, which acts by targeting the E-site of ...
www.nature.com
A natural depsipeptide antibiotic binds the E-site of the bacterial ribosome - Nature
www.nature.com/articles/s41...
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Ahmad Jomaa
Wilson Lab
Tanmay Bharat
Pilhofer Lab 🦠❄️🔬
In this work authors show how minimal mutations in proline-rich antimicrobial peptides can flip their orientation in the ribosome exit tunnel, switching their mechanism from stalling translation termi...
www.nature.com
Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome - Nature Communications
Ahmad Jomaa
Ahmad Jomaa
#Biofilm matrices containing filamentous phages help #Pseudomonas aeruginosa tolerate antibiotics. @abultarafder.bsky.social @tbharat-lab.bsky.social &co show that #nanobody disruption of #phage Pf4 #LiquidCrystalline droplets restores #antibiotic susceptibility @plosbiology.org 🧪 plos.io/4xkd6Mw
Structura Biotechnology