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000281357 1001_ $$aShaib, Ali H$$b0
000281357 245__ $$aOne-step nanoscale expansion microscopy reveals individual protein shapes.
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000281357 520__ $$aThe 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.
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000281357 650_7 $$2NLM Chemicals$$aCalmodulin
000281357 650_7 $$2NLM Chemicals$$aProteins
000281357 650_7 $$0SY7Q814VUP$$2NLM Chemicals$$aCalcium
000281357 650_2 $$2MeSH$$aHumans
000281357 650_2 $$2MeSH$$aMicroscopy, Fluorescence: methods
000281357 650_2 $$2MeSH$$aCalmodulin: chemistry
000281357 650_2 $$2MeSH$$aParkinson Disease: cerebrospinal fluid
000281357 650_2 $$2MeSH$$aNanotechnology: methods
000281357 650_2 $$2MeSH$$aProteins: chemistry
000281357 650_2 $$2MeSH$$aCalcium: metabolism
000281357 650_2 $$2MeSH$$aProtein Conformation
000281357 7001_ $$aChouaib, Abed Alrahman$$b1
000281357 7001_ $$aChowdhury, Rajdeep$$b2
000281357 7001_ $$00009-0003-2515-8330$$aAltendorf, Jonas$$b3
000281357 7001_ $$aMihaylov, Daniel$$b4
000281357 7001_ $$aZhang, Chi$$b5
000281357 7001_ $$aKrah, Donatus$$b6
000281357 7001_ $$aImani, Vanessa$$b7
000281357 7001_ $$00000-0002-4814-9010$$aSpencer, Russell K W$$b8
000281357 7001_ $$aGeorgiev, Svilen Veselinov$$b9
000281357 7001_ $$aMougios, Nikolaos$$b10
000281357 7001_ $$aMonga, Mehar$$b11
000281357 7001_ $$00000-0003-4847-4144$$aReshetniak, Sofiia$$b12
000281357 7001_ $$aMimoso, Tiago$$b13
000281357 7001_ $$00009-0003-1357-5161$$aChen, Han$$b14
000281357 7001_ $$aFatehbasharzad, Parisa$$b15
000281357 7001_ $$aCrzan, Dagmar$$b16
000281357 7001_ $$aSaal, Kim-Ann$$b17
000281357 7001_ $$aAlawieh, Mohamad Mahdi$$b18
000281357 7001_ $$00000-0002-8591-2513$$aAlawar, Nadia$$b19
000281357 7001_ $$aEilts, Janna$$b20
000281357 7001_ $$aKang, Jinyoung$$b21
000281357 7001_ $$aSoleimani, Alireza$$b22
000281357 7001_ $$00000-0002-7472-973X$$aMüller, Marcus$$b23
000281357 7001_ $$00000-0001-6562-7187$$aPape, Constantin$$b24
000281357 7001_ $$00000-0003-1316-1906$$aAlvarez, Luis$$b25
000281357 7001_ $$aTrenkwalder, Claudia$$b26
000281357 7001_ $$0P:(DE-2719)9001340$$aMollenhauer, Brit$$b27$$udzne
000281357 7001_ $$0P:(DE-2719)2814138$$aOuteiro, Tiago F$$b28
000281357 7001_ $$aKöster, Sarah$$b29
000281357 7001_ $$aPreobraschenski, Julia$$b30
000281357 7001_ $$aBecherer, Ute$$b31
000281357 7001_ $$00000-0001-7145-0533$$aMoser, Tobias$$b32
000281357 7001_ $$00000-0002-0419-3351$$aBoyden, Edward S$$b33
000281357 7001_ $$00000-0003-3783-1388$$aAricescu, A Radu$$b34
000281357 7001_ $$00000-0002-1692-3219$$aSauer, Markus$$b35
000281357 7001_ $$00000-0002-4968-9713$$aOpazo, Felipe$$b36
000281357 7001_ $$00000-0002-1667-7839$$aRizzoli, Silvio O$$b37
000281357 773__ $$0PERI:(DE-600)1494943-X$$a10.1038/s41587-024-02431-9$$gVol. 43, no. 9, p. 1539 - 1547$$n9$$p1539 - 1547$$tNature biotechnology$$v43$$x1087-0156$$y2025
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