Alpha1 Record ID: FCE58719
16 views
Share this Alpha1 record with your network
Top 1% Selection Manuscript
Loading
Fetching the latest research
Hu, H.; Krah, D.; Ntolkeras, A.; Chanda, S.; Heimbrodt, A.; Mondal, M.; Altendorf, J.; Jing, B.; Berger, B.; Shaib et al.
Biological macromolecules, such as proteins, are made of concatenated building blocks. We hypothesized that individual protein residues could be imaged by anchoring their side chains to a swellable polymer, cleaving backbone amide bonds, and expanding residues away from each other to a degree that enables them to be visualized separately. We introduce thousandfold expansion microscopy (1000ExM), a four-network interpenetrating hydrogel architecture that enables successive expansion from [~]18-fold to >1000-fold (one billion-fold in volume). Protein and peptide structures are maintained across these expansion factors, as verified by analyses of proteins with known structures (nanobodies, GFP) and a well-studied peptide (mCLING). Computational analysis indicates that 1000ExM resolves adjacent amino acid residues, thereby achieving sub-nanometer precision on conventional light microscopes. We anticipate that 1000ExM will find wide utility in protein visualization and identification, potentially even in intact cells and tissues.
In a mind-bending microscopic makeover, scientists crank expansion microscopy to a ridiculous 1,000x (that's billion-fold by volume!), turning tiny cell bits into Olympic-pool-sized wonders so even basic light microscopes can spy on amino-acid distances like nosy neighbors with super binoculars.
Posted by Group Leader Ali H. Shaib (@AliHShaib), it exploded with excitement from neuroscientists and imaging experts praising the democratization of super-res microscopy
View discussionFormal Expert Review in progress...
Read the Kaimen Rigor review above, then add your own assessment.
CD4⁺ T cells confer transplantable rejuvenation via Rivers of telomeres
Lanna, A.; Valvo, S.; Dustin, M.; Rinaldi, F.
Using a GPT-5-driven autonomous lab to optimize the cost and titer of cell-free protein synthesis
Smith, A. A.; Wong, E. L.; Donovan, R. C.; Chapman, B. A.; Harry, R.; Tirandazi, P.; Kanigowska, P.; Gendreau, E. A.; Dahl, R. H.; Jastrzebski, M.; Cortez, J. E.; Bremner, C. J.; Hemuda, J. C. M.; Dooner, J.; Graves, I.; Karandikar, R.; Lionetti, C.; Christopher, K.; Consiglio, A. L.; Tran, A.; McCusker, W.; Nguyen, D. X.; Nunes da Silva, I. B.; Bautista-Ayala, A. R.; McNerney, M. P.; Atkins, S.; McDuffie, M.; Serber, W.; Barber, B. P.; Thanongsinh, T.; Nesson, A.; Lama, B.; Nichols, B.; LaFrance, C.; Nyima, T.; Byrn, A.; Thornhill, R.; Cai, B.; Ayala-Valdez, L.; Wong, A.; Che, A. J.; Thavaraj
A Single-Cell and Spatial 3D Multi-omic Atlas of Developing Human Basal Ganglia and Inhibitory Neurons
Heffel, M. G.; Xu, H.; Pastor-Alonso, O.; Li, X.; Baig, M. S.; Irfan Ghoor, R.; Li, R.; Kern, C.; Kum, J.; Zhang, Y.; Paino, J.; Tsai, M. J.; Tai, C.-Y.; Tucker, G.; Zhao, Z.; Hou, A.; von Behren, Z.; Bhade, M.; Li, S.; Sandoval, K.; Scholes, J.; Codrea, F.; Calimlim, J.; Liao, E. K.; Leung, G.; Kim, J.; Eskin, E.; Flint, J.; Cotter, J. A.; Pasaniuc, B.; Bintu, B.; Zhu, Q.; Mukamel, E. A.; Ernst, J.; Paredes, M. F.; Luo, C.
Prediction of transformative breakthroughs in biomedical research
Davis, M. T.; Busse, B. L.; Arabi, S.; Meyer, P.; Hoppe, T. A.; Meseroll, R. A.; Hutchins, B. I.; Willis, K. A.; Santangelo, G. M.