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@ARTICLE{Shaib:281357,
      author       = {Shaib, Ali H and Chouaib, Abed Alrahman and Chowdhury,
                      Rajdeep and Altendorf, Jonas and Mihaylov, Daniel and Zhang,
                      Chi and Krah, Donatus and Imani, Vanessa and Spencer,
                      Russell K W and Georgiev, Svilen Veselinov and Mougios,
                      Nikolaos and Monga, Mehar and Reshetniak, Sofiia and Mimoso,
                      Tiago and Chen, Han and Fatehbasharzad, Parisa and Crzan,
                      Dagmar and Saal, Kim-Ann and Alawieh, Mohamad Mahdi and
                      Alawar, Nadia and Eilts, Janna and Kang, Jinyoung and
                      Soleimani, Alireza and Müller, Marcus and Pape, Constantin
                      and Alvarez, Luis and Trenkwalder, Claudia and Mollenhauer,
                      Brit and Outeiro, Tiago F and Köster, Sarah and
                      Preobraschenski, Julia and Becherer, Ute and Moser, Tobias
                      and Boyden, Edward S and Aricescu, A Radu and Sauer, Markus
                      and Opazo, Felipe and Rizzoli, Silvio O},
      title        = {{O}ne-step nanoscale expansion microscopy reveals
                      individual protein shapes.},
      journal      = {Nature biotechnology},
      volume       = {43},
      number       = {9},
      issn         = {1087-0156},
      address      = {New York, NY},
      publisher    = {Springer Nature},
      reportid     = {DZNE-2025-01104},
      pages        = {1539 - 1547},
      year         = {2025},
      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 Ca2+
                      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.},
      keywords     = {Humans / Microscopy, Fluorescence: methods / Calmodulin:
                      chemistry / Parkinson Disease: cerebrospinal fluid /
                      Nanotechnology: methods / Proteins: chemistry / Calcium:
                      metabolism / Protein Conformation / Calmodulin (NLM
                      Chemicals) / Proteins (NLM Chemicals) / Calcium (NLM
                      Chemicals)},
      cin          = {AG Fischer},
      ddc          = {660},
      cid          = {I:(DE-2719)1410002},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39385007},
      pmc          = {pmc:PMC7616833},
      doi          = {10.1038/s41587-024-02431-9},
      url          = {https://pub.dzne.de/record/281357},
}