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Joao Medeiros Silva @JMSism
Joined October 2019
  • Tweets 179
  • Following 362
  • Followers 181
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Joao Medeiros Silva@JMSism
4 Aug 2022
So proud of this team🤩 This is massive: mode of action of the newest antibiotic Teixobactin was just reported at the highest detail, both for receptor-antibiotic and resulting supramolecular assembly. Both kill! This might be game-changing for fighting those pesky Superbugs
Markus Weingarth@MarkusWeingarth
3 Aug 2022
#Teixobactin, isolated from 'unculturable' bacteria, is considered the first new 💊#antibiotic💊 in 30 years. But how does it kill bacteria? We show teixobactin uses a new mechanism that involves a double attack on the cell envelope Out @Nature nature.com/articles/s41586-0… #NMR 1/n
Teixobactin uses a new 'two-pronged' mechanism to kill bacteria

ALT Teixobactin uses a new 'two-pronged' mechanism to kill bacteria

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Joao Medeiros Silva retweeted
Markus Weingarth@MarkusWeingarth
6 Mar 2025
I have 3 PhD and 3 postdoc positions available at Utrecht University, all in the context of ‘solid-state #NMR & drug discovery (#antibiotics: small molecules & peptides)’ Starting date is flexible. Please see here: weingarth-group.net/student-… #Postdoc #PhD

Open Positions & Student Projects | Weingarth Group

weingarth-group.net
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Joao Medeiros Silva retweeted
J. Am. Chem. Soc.@J_A_C_S
29 Dec 2024
Polar Networks Mediate Ion Conduction of the SARS-CoV-2 Envelope Protein | Journal of the American Chemical Society @ChemistryMIT @MIT @nmr900 High Resolution Structure E Transmembrane Domain SARS Cov2 pubs.acs.org/doi/10.1021/jac…

Polar Networks Mediate Ion Conduction of the SARS-CoV-2 Envelope Protein

The SARS-CoV-2 E protein conducts cations across the cell membrane to cause pathogenicity to infected cells. The high-resolution structures of the E transmembrane domain (ETM) in the closed state at...

pubs.acs.org
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Joao Medeiros Silva retweeted
MeiHongLab@MeiHongLab
27 Dec 2024
Check out our new NMR study of how a dynamic polar network in the SARS-CoV-2 E protein mediates proton and calcium ion binding! pubs.acs.org/doi/full/10.102…
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Joao Medeiros Silva retweeted
Markus Weingarth@MarkusWeingarth
23 May 2024
🔥Hot off the press⬇️⬇️⬇️ in @NatureMicrobiol nature.com/articles/s41564-0… Plectasin is a complex peptide 💊 #antibiotic, isolated from funghi. We show that plectasin uses a new Calcium-dependent supramolecular mechanism to ensnare its target on the membrane surface. 1/4 #NMR
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and they were saying I can't see a total solar eclipse from the Azores. 😎
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Such a noble initiative promoted by Native Scientists, thanks for enabling this science class for children in my hometown! School dropout in my region is ~25%, we desperately need initiatives like these that keeps kids interested in school and motivates them to seek knowledge
Native Scientists@NativeScientis1
22 Mar 2024
Da @NYUScience à Figueira da Foz e do @MIT aos Açores! Os cientistas Sílvia Curado e João Silva trouxeram a ciência de volta a casa, inspirando 75 crianças com os maravilhosos mundos da biologia e da química 🙏🏼Muito obrigada pelo apoio @FundlaCaixa e @FLAD_PT
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We distinguish α- from 310-helices using a 3D hCOhNH, a straightforward 1H-detected ssNMR experiment. The obtained CO(i-n)NH(i) signal intensity patterns give a signature of the helix type. pubs.acs.org/doi/10.1021/acs…

Distinguishing Different Hydrogen-Bonded Helices in Proteins by Efficient 1H-Detected Three-Dimen...

Helical structures in proteins include not only α-helices but also 310 and π helices. These secondary structures differ in the registry of the C═O···H–N hydrogen bonds, which are i to i 4 for...

pubs.acs.org
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Although we didn't get a chance to test β-sheets, the hCOhNH inter-residue signal profile should also distinguish the parallel vs anti-parallel motifs
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by the @MeiHongLab :)
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Subtle but important difference: α-/310-helix are not the same! 310-helices are often hard to distinguish due to higher dynamics, hence lower resolution. This is why 310- may grant functional properties; they're plastic. Here's an NMR approach to distinguish α-, 310- and π, helix
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Here's what the open E viroporin from SARS-CoV-2 looks like! A cone-shaped barrel with a wide N-opening, narrow C-opening, a phenylalanine belt, and a hydrophobic gate. The structure elucidates how this viroporin work and sets a drug target for the potential treatment of COVID-19
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This viroporin is intriguing: the pore is narrow and mostly hydrophobic, impeding the passage of ions. The polar sidechains at the C-term opening may lower the energy barrier for water to cross the gate. Hence, this channel's C-term is wide when closed but narrow when open!
Courtesy of the researchers, MIT News, and iStock

ALT Courtesy of the researchers, MIT News, and iStock

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Image credit to @MIT @ChemistryMIT
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Joao Medeiros Silva retweeted
Markus Weingarth@MarkusWeingarth
22 Aug 2023
We report the discovery & mechanism of #Clovibactin, an #antibiotic from unculturable bacteria! ⬇️⬇️ @CellCellPress ⬇️⬇️ 💊 doi.org/10.1016/j.cell.2023.… Clovibactin uses a 'hydrophobic cage' motif to target the cell wall and kill without detectable resistance @UniUtrecht 1/n
The newly discovered antibiotic Clovibactin from unculturable bacteria, also known as 'microbial dark matter. Clovibactin uses an unusual cage-like binding motif to tightly wrap around immutable pyrophosphate of cell wall precursors, but ignores the variable sugar-peptide part. This enables Clovibactin to target different, indispensable cell wall precursors (Lipid II, Lipid III, C55PP) in bacterial cell membranes, and it makes the drug extremely robust to the development of antimicrobial resistance. Clovibactin does even more: Upon target binding, it assembles to fibrils on the membrane surface. These fibrils help to stably binds the target as long as it takes. Altogether, Clovibactin is a promising lead for the development of next-generation therapeutics with a long clinical lifetime. PS: The name comes from the binding motif - 'Klouvi' means cage in Greek. Illustration by Gloria Fuentes from 'The Visual Thinker'

ALT The newly discovered antibiotic Clovibactin from unculturable bacteria, also known as 'microbial dark matter. Clovibactin uses an unusual cage-like binding motif to tightly wrap around immutable pyrophosphate of cell wall precursors, but ignores the variable sugar-peptide part. This enables Clovibactin to target different, indispensable cell wall precursors (Lipid II, Lipid III, C55PP) in bacterial cell membranes, and it makes the drug extremely robust to the development of antimicrobial resistance. Clovibactin does even more: Upon target binding, it assembles to fibrils on the membrane surface. These fibrils help to stably binds the target as long as it takes. Altogether, Clovibactin is a promising lead for the development of next-generation therapeutics with a long clinical lifetime. PS: The name comes from the binding motif - 'Klouvi' means cage in Greek. Illustration by Gloria Fuentes from 'The Visual Thinker'

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Joao Medeiros Silva retweeted
Mohammed Kaplan@MMMKaplan_
18 Aug 2023
A postdoc position is available in my lab at UChicago to work on various aspects of (bacterial) cell biology using cryo-ET. Please feel free to contact me directly at mohammedk@uchicago.edu. Re-tweeting and spreading the word is highly appreciated. Thank you!
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Thinking why the heck US academic conferences tend to take place during weekends... it's ridiculus imo
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Never imagined mammalian cell line cross-contamination was such a big deal, thanks @SciShow youtu.be/ANK-DG9EkLU

Biology's Huge, Microscopic Problem

Head to https://linode.com/scishow to get a $100 60-day credit on a...

youtube.com
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Joao Medeiros Silva retweeted
Chris Toseland@ChrisToseland
20 Mar 2023
I don’t usually post personal news but Clinicians have told us to pull every lever. Our daughter has with #dipg Brain cancer. There is no cure and typically 9m life expectancy. If anyone knows of trials then please get in contact! #braincancer #childrenscancer @CR_UK
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Joao Medeiros Silva retweeted
Massachusetts Institute of Technology (MIT)
@MIT
14 Mar 2023
The wait is over! Get ready for the adventure of a lifetime, #MIT2027. Written, directed, and animated by Isabella Y. ’24, Jenny B. '25, Jenny Z. '23, & Kai VB. '25.
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