Z. Liu, L. D. Lavis, and E. Betzig, Imaging live-cell dynamics and structure at the single-molecule level, Mol. Cell, vol.58, pp.644-659, 2015.

M. Hauser, Correlative super-resolution microscopy: new dimensions and new opportunities, Chem. Rev, vol.117, pp.7428-7456, 2017.

R. Jungmann, Multiplexed 3D cellular super-resolution imaging with DNA-PAINT and Exchange-PAINT, Nat. Methods, vol.11, pp.313-318, 2014.

T. Kiuchi, M. Higuchi, A. Takamura, M. Maruoka, and N. Watanabe, Multitarget super-resolution microscopy with high-density labeling by exchangeable probes, Nat. Methods, vol.12, pp.743-746, 2015.

C. L. Dix, The role of mitotic cell-substrate adhesion re-modeling in animal cell division, Dev. Cell, vol.45, pp.132-145, 2018.

J. Tam, G. A. Cordier, J. S. Borbely, Á. S. Álvarez, and M. Lakadamyali, Crosstalk-free multi-color storm imaging using a single fluorophore, PLoS ONE, vol.9, p.101772, 2014.

C. Schneider, W. S. Rasband, K. W. Eliceiri, and . Nih, Image to ImageJ: 25 years of image analysis, Nat. Methods, vol.9, pp.671-675, 2012.

N. Ramkumar and B. Baum, Coupling changes in cell shape to chromosome segregation, Nat. Rev. Mol. Cell Biol, vol.17, pp.511-521, 2016.

L. T. Vassilev, Selective small-molecule inhibitor reveals critical mitotic functions of human CDK1, Proc. Natl Acad. Sci. USA, vol.103, pp.10660-10665, 2006.

P. Kner, B. B. Chhun, E. R. Griffis, L. Winoto, and M. G. Gustafsson, Superresolution video microscopy of live cells by structured illumination, Nat. Methods, vol.6, pp.339-342, 2009.

M. Hofmann, C. Eggeling, S. Jakobs, and S. W. Hell, Breaking the diffraction barrier in fluorescence microscopy at low light intensities by using reversibly photoswitchable proteins, Proc. Natl Acad. Sci, vol.102, pp.17565-17569, 2005.

N. Gustafsson, Fast live-cell conventional fluorophore nanoscopy with ImageJ through super-resolution radial fluctuations, Nat. Commun, vol.7, pp.1-9, 2016.

M. J. Rust, M. Bates, and X. Zhuang, Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM), Nat. Methods, vol.3, pp.793-795, 2006.

R. Jungmann, Single-molecule kinetics and super-resolution microscopy by fluorescence imaging of transient binding on DNA origami, Nano. Lett, vol.10, pp.4756-4761, 2010.

S. Culley, Quantitative mapping and minimization of super-resolution optical imaging artifacts, Nat. Methods, vol.15, pp.263-266, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01736919

G. T. Dempsey, J. C. Vaughan, K. H. Chen, M. Bates, and X. Zhuang, Evaluation of fluorophores for optimal performance in localization-based super-resolution imaging, Nat. Methods, vol.8, pp.1027-1036, 2011.

S. S. Agasti, DNA-barcoded labeling probes for highly multiplexed Exchange-PAINT imaging, Chem. Sci, vol.8, pp.3080-3091, 2017.

R. F. Laine, NanoJ: a high-performance open-source super-resolution microscopy toolbox, J. Phys. D. Appl. Phys, vol.52, p.163001, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02073339

M. D. Abramoff, P. J. Magalhães, and S. J. Ram, Optical imaging techniques in cell biology, 2006.

J. Schindelin, Fiji: an open-source platform for biological-image analysis, Nat. Methods, vol.9, pp.676-682, 2012.

A. Beghin, Localization-based super-resolution imaging meets highcontent screening, Nat. Methods, vol.14, pp.1184-1190, 2017.

G. Gut, M. D. Herrmann, and L. Pelkmans, Multiplexed protein maps link subcellular organization to cellular states, Science, vol.361, p.7042, 2018.

D. R. Whelan and T. D. Bell, Image artifacts in single molecule localization microscopy: why optimization of sample preparation protocols matters, Sci. Rep, vol.5, p.7924, 2015.

J. Yi, madSTORM: a superresolution technique for large-scale multiplexing at single-molecule accuracy, Mol. Biol. Cell, vol.27, pp.3591-3600, 2016.

C. C. Valley, S. Liu, D. S. Lidke, and . Lidke, Ka Sequential superresolution imaging of multiple targets using a single fluorophore, PLoS ONE, vol.10, p.123941, 2015.

N. Mchedlishvili, Kinetochores accelerate centrosome separation to ensure faithful chromosome segregation, J. Cell. Sci, vol.125, pp.906-918, 2012.

P. Steigemann, Aurora B-mediated abscission checkpoint protects against tetraploidization, Cell, vol.136, pp.473-484, 2009.

B. M. Burkel, G. Von-dassow, and W. M. Bement, Versatile fluorescent probes for actin filaments based on the actin-binding domain of utrophin, Cell Motil. Cytoskelet, vol.64, pp.822-832, 2007.

J. Schnitzbauer, M. T. Strauss, T. Schlichthaerle, F. Schueder, and R. Jungmann, Super-resolution microscopy with DNA-PAINT, Nat. Protocol, vol.12, pp.1198-1228, 2017.

P. M. Pereira, P. Almada, and R. Henriques, High-content 3D multicolor super-resolution localization microscopy, Methods Cell Biol, vol.125, pp.95-117, 2015.

D. Leyton-puig, PFA fixation enables artifact-free super-resolution imaging of the actin cytoskeleton and associated proteins, Biol. Open, vol.5, pp.1001-1009, 2016.

C. Leterrier, Nanoscale architecture of the axon initial segment reveals an organized and robust scaffold, Cell Rep, vol.13, pp.2781-2793, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01474319

M. Ovesný, ThunderSTORM: a comprehensive ImageJ plug-in for PALM and STORM data analysis and super-resolution imaging, Bioinformatics, vol.30, pp.2389-2390, 2014.

R. P. Nieuwenhuizen, Measuring image resolution in optical nanoscopy, Nat. Methods, vol.10, pp.557-562, 2013.

R. D. Gray, VirusMapper: open-source nanoscale mapping of viral architecture through super-resolution microscopy, Sci. Rep, vol.6, p.29132, 2016.