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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},
}