Max Berger on Muck Rack

Max Berger

Los Angeles
As seen in: Medium, HuffPost, Nature, The Guardian, Wiley Online Library, NBC News, POLITICO, Substack, The Daily Beast, The Toronto Star and
EM Medical Education/Simulation Fellow @UCLAEMRes via @BellevueHosp / @nyulangone & @KeckMedUSC| Red Sox Fan | Chiweenie Dad 🐶 | Thoughts Are My Own
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Articles

A natural depsipeptide antibiotic binds the E-site of the bacterial ribosome

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By Manpreet Kaur, Dmitrii Y. Travin, Max Berger, Manoj Jangra, Martino Morici, Haaris A. Safdari, Dorota Klepacki, Wenliang Wang, Michael Cook, Sommer Chou, Allison K. Guitor, Kalinka Koteva, Min Xu, Linda Ejim, Aline A Fiebig, Brian K. Coombes, Lesley T. MacNeil, Nora Vázquez-Laslop, Alexander S. Mankin, Daniel Wilson, Gerard Wright, Yeganeh Yousefi
| Nature
Abstract A key challenge in addressing the antibiotic resistance crisis is identifying new antimicrobial compounds1. Although natural products produced by fungi and bacteria, particularly actinomycetes, have been the source of most antibiotics discovered over the past 80 years, they have fallen out of favour owing to the frequent rediscovery of known drug scaffolds2. The current perception is that antibiotic-producing actinomycetes have been over-mined and possess little novelty left to yield.
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Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome

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By Weiping Huang, Max Berger, Haaris A. Safdari, Dorota Klepacki, Helge Paternoga, Chetana Baliga, Daniel Wilson, Nora Vázquez-Laslop, Alexander S. Mankin
| Nature
Abstract Proline-rich antimicrobial peptides (PrAMPs) kill bacteria by binding in the ribosomal nascent peptide exit tunnel. Type II PrAMPs bind in an orientation matching that of the nascent protein, trap the release factors and arrest ribosomes at stop codons. Conversely, Type I PrAMPs bind in an opposite orientation: their N-terminus invades the peptidyl transferase center arresting translation at start codons.
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Max Berger (@maxberger.bsky.social)

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By Max Berger
| bsky.app
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