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Your search keyword '"Monga, Mehar"' showing total 7 results
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7 results on '"Monga, Mehar"'

1. Ca2+ binding to the C2E domain of otoferlin is required for hair cell exocytosis and hearing

Author

Chen, Han, primary, Monga, Mehar, additional, Fang, Qinghua, additional, Slitin, Loujin, additional, Neef, Jakob, additional, Chepurwar, Shashank S, additional, Netto, Regina Célia Mingroni, additional, Lezirovitz, Karina, additional, Tabith, Alfredo, additional, Benseler, Fritz, additional, Brose, Nils, additional, Kusch, Kathrin, additional, Wichmann, Carolin, additional, Strenzke, Nicola, additional, Vona, Barbara, additional, Preobraschenski, Julia, additional, and Moser, Tobias, additional

Published
2023
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4. Visualizing proteins by expansion microscopy

Author

Shaib, Ali H., primary, Chouaib, Abed Alrahman, additional, Chowdhury, Rajdeep, additional, Mihaylov, Daniel, additional, Zhang, Chi, additional, Imani, Vanessa, additional, Georgiev, Svilen Veselinov, additional, Mougios, Nikolaos, additional, Monga, Mehar, additional, Reshetniak, Sofiia, additional, Mimoso, Tiago, additional, Chen, Han, additional, Fatehbasharzad, Parisa, additional, Crzan, Dagmar, additional, Saal, Kim-Ann, additional, Alawar, Nadia, additional, Eilts, Janna, additional, Kang, Jinyoung, additional, Alvarez, Luis, additional, Trenkwalder, Claudia, additional, Mollenhauer, Brit, additional, Outeiro, Tiago F., additional, Köster, Sarah, additional, Preobraschenski, Julia, additional, Becherer, Ute, additional, Moser, Tobias, additional, Boyden, Edward S., additional, Aricescu, A Radu, additional, Sauer, Markus, additional, Opazo, Felipe, additional, and Rizzoli, Silvio O., additional

Published
2022
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5. Expansion microscopy at one nanometer resolution

Author

Shaib, Ali H., Chouaib, Abed Alrahman, Imani, Vanessa, Chowdhury, Rajdeep, Georgiev, Svilen Veselinov, Mougios, Nikolaos, Monga, Mehar, Reshetniak, Sofiia, Mihaylov, Daniel, Chen, Han, Fatehbasharzad, Parisa, Crzan, Dagmar, Saal, Kim-Ann, Trenkwalder, Claudia, Mollenhauer, Brit, Outeiro, Tiago F., Preobraschenski, Julia, Becherer, Ute, Moser, Tobias, Boyden, Edward S., Aricescu, A Radu, Sauer, Markus, Opazo, Felipe, and Rizzoli, Silvio O.

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6. One-step nanoscale expansion microscopy reveals individual protein shapes.

Author

Shaib AH, Chouaib AA, Chowdhury R, Altendorf J, Mihaylov D, Zhang C, Krah D, Imani V, Spencer RKW, Georgiev SV, Mougios N, Monga M, Reshetniak S, Mimoso T, Chen H, Fatehbasharzad P, Crzan D, Saal KA, Alawieh MM, Alawar N, Eilts J, Kang J, Soleimani A, Müller M, Pape C, Alvarez L, Trenkwalder C, Mollenhauer B, Outeiro TF, Köster S, Preobraschenski J, Becherer U, Moser T, Boyden ES, Aricescu AR, Sauer M, Opazo F, and Rizzoli SO

Abstract

The attainable resolution of fluorescence microscopy has reached the subnanometer range, but this technique still fails to image the morphology of single proteins or small molecular complexes. Here, we expand the specimens at least tenfold, label them with conventional fluorophores and image them with conventional light microscopes, acquiring videos in which we analyze fluorescence fluctuations. One-step nanoscale expansion (ONE) microscopy enables the visualization of the shapes of individual membrane and soluble proteins, achieving around 1-nm resolution. We show that conformational changes are readily observable, such as those undergone by the ~17-kDa protein calmodulin upon Ca 2+ binding. ONE is also applied to clinical samples, analyzing the morphology of protein aggregates in cerebrospinal fluid from persons with Parkinson disease, potentially aiding disease diagnosis. This technology bridges the gap between high-resolution structural biology techniques and light microscopy, providing new avenues for discoveries in biology and medicine., (© 2024. The Author(s).)

Published
2024
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