Mechanics and functional consequences of nuclear deformations

Comparison of the Hi-C, GAM and SPRITE methods using polymer models of chromatin

Fiorillo, L., Musella, F., Conte, M., Kempfer, R., Chiariello, A. M., Bianco, S., Kukalev, A., Irastorza-Azcárate, I., Esposito, A., Abraham, A., et al. (2021) · Nature Methods · doi:10.1038/s41592-021-01135-1 · Cited by 73

Balance of osmotic pressures determines the nuclear-to-cytoplasmic volume ratio of the cell

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The rich inner life of the cell nucleus: dynamic organization, active flows, and emergent rheology

Zidovska, A. (2020) · Biophysical Reviews · doi:10.1007/s12551-020-00761-x · Cited by 72

Nuclear envelope wrinkling predicts mesenchymal progenitor cell mechano-response in 2D and 3D microenvironments

Cosgrove, B. D., Loebel, C., Driscoll, T. P., Tsinman, T. K., Dai, E. N., Heo, S., Dyment, N. A., Burdick, J. A., & Mauck, R. L. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.120662 · Cited by 72

Separate roles for chromatin and lamins in nuclear mechanics

Stephens, A. D., Banigan, E. J., & Marko, J. F. (2017) · Nucleus · doi:10.1080/19491034.2017.1414118 · Cited by 71

Cytoplasmic forces functionally reorganize nuclear condensates in oocytes

Jord, A. A., Letort, G., Chanet, S., Tsai, F., Antoniewski, C., Eichmuller, A., Silva, C. D., Huynh, J., Gov, N. S., Voituriez, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32675-5 · Cited by 71

Mechanically Induced Chromatin Condensation Requires Cellular Contractility in Mesenchymal Stem Cells

Heo, S.-J., Han, W. M., Szczesny, S. E., Cosgrove, B. D., Elliott, D. M., Lee, D. A., Duncan, R. L., & Mauck, R. L. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.07.006 · Cited by 70

Actomyosin contractility scales with myoblast elongation and enhances differentiation through YAP nuclear export

Bruyère, C., Versaevel, M., Mohammed, D., Alaimo, L., Luciano, M., Vercruysse, E., & Gabriele, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-52129-1 · Cited by 69

Nesprin‐2 accumulates at the front of the nucleus during confined cell migration

Davidson, P. M., Battistella, A., Déjardin, T., Betz, T., Plastino, J., Borghi, N., Cadot, B., & Sykes, C. (2020) · EMBO Reports · doi:10.15252/embr.201949910 · Cited by 68

Nuclear Envelopathies—Raising the Nuclear Veil

Somech, R., Shaklai, S., Amariglio, N., Rechavi, G., & Simon, A. J. (2005) · Pediatric Research · doi:10.1203/01.pdr.0000159566.54287.6c · Cited by 67

Microtubule-induced nuclear envelope fluctuations control chromatin dynamics in Drosophila embryos

Hampoelz, B., Azou, Y., Fabre, R., Markova, O., Puech, P., & Lecuit, T. (2011) · Development · doi:10.1242/dev.065706 · Cited by 67

Migration through a small pore disrupts inactive chromatin organization in neutrophil-like cells

Jacobson, E. C., Perry, J. K., Long, D. S., Olins, A. L., Olins, D. E., Wright, B. E., Vickers, M. H., & O'Sullivan, J. M. (2018) · BMC Biology · doi:10.1186/s12915-018-0608-2 · Cited by 67

Nuclear stiffening and chromatin softening with progerin expression leads to an attenuated nuclear response to force

Booth, E. A., Spagnol, S. T., Alcoser, T. A., & Dahl, K. N. (2015) · Soft Matter · doi:10.1039/c5sm00521c · Cited by 66

TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement

Saunders, C. A., Harris, N. J., Willey, P. T., Woolums, B. M., Wang, Y., McQuown, A. J., Schoenhofen, A., Worman, H. J., Dauer, W. T., Gundersen, G. G., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201507113 · Cited by 66

Cell migration through three-dimensional confining pores: speed accelerations by deformation and recoil of the nucleus

Krause, M., Yang, F. W., Lindert, M. T., Isermann, P., Schepens, J. T. G., Maas, R. J. A., Venkataraman, C., Lammerding, J., Madzvamuse, A., Hendriks, W. J. A. J., et al. (2019) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2018.0225 · Cited by 66

Role of Actin Dependent Nuclear Deformation in Regulating Early Gene Expression

Gupta, S., Marcel, N., Sarin, A., & Shivashankar, G. V. (2012) · PLoS ONE · doi:10.1371/journal.pone.0053031 · Cited by 65

Consequences of a tight squeeze: Nuclear envelope rupture and repair

Isermann, P., & Lammerding, J. (2017) · Nucleus · doi:10.1080/19491034.2017.1292191 · Cited by 65

Laminopathy-causing lamin A mutations reconfigure lamina-associated domains and local spatial chromatin conformation

Briand, N., & Collas, P. (2018) · Nucleus · doi:10.1080/19491034.2018.1449498 · Cited by 65

Local, transient tensile stress on the nuclear membrane causes membrane rupture

Zhang, Q., Tamashunas, A. C., Agrawal, A., Torbati, M., Katiyar, A., Dickinson, R. B., Lammerding, J., & Lele, T. P. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-09-0604 · Cited by 65

Nuclear fragility, blaming the blebs

Srivastava, N., Nader, G. P. F., Williart, A., Rollin, R., Cuvelier, D., Lomakin, A. J., & Piel, M. (2021) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2021.01.007 · Cited by 64

Active Fluctuations of the Nuclear Envelope Shape the Transcriptional Dynamics in Oocytes

Almonacid, M., Jord, A. A., El‐Hayek, S., Othmani, A., Coulpier, F., Lemoine, S., Miyamoto, K., Grosse, R., Klein, C., Piolot, T., et al. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.09.010 · Cited by 63

Samp1 is functionally associated with the LINC complex and A-type lamina networks

Gudise, S., Figueroa, R. A., Lindberg, R., Larsson, V. J., & Hallberg, E. (2011) · Journal of Cell Science · doi:10.1242/jcs.078923 · Cited by 62

Nuclear envelope rupture: Actin fibers are putting the squeeze on the nucleus

Lammerding, J., & Wolf, K. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201609102 · Cited by 62

Disrupted mechanobiology links the molecular and cellular phenotypes in familial dilated cardiomyopathy

Clippinger, S. R., Cloonan, P. E., Greenberg, L., Ernst, M., Stump, W. T., & Greenberg, M. J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1910962116 · Cited by 62

The nucleoporin ELYS regulates nuclear size by controlling NPC number and nuclear import capacity

Jevtić, P., Schibler, A. C., Wesley, C. C., Pegoraro, G., Misteli, T., & Levy, D. L. (2019) · EMBO Reports · doi:10.15252/embr.201847283 · Cited by 61

Dynein pulling forces counteract lamin-mediated nuclear stability during nuclear envelope repair

Penfield, L., Wysolmerski, B., Mauro, M. S., Farhadifar, R., Martinez, M. A. Q., Biggs, R. J., Wu, H., Broberg, C., Needleman, D. J., & Bahmanyar, S. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0374 · Cited by 60

Understanding the Roles of Nuclear A- and B-type Lamins in Brain Development

Young, S. G., Jung, H.-J., Coffinier, C., & Fong, L. G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.354407 · Cited by 59

Myosin IIA suppresses glioblastoma development in a mechanically sensitive manner

Picariello, H. S., Kenchappa, R. S., Rai, V., Crish, J. F., Dovas, A., Pogoda, K., McMahon, M. M., Bell, E. S., Chandrasekharan, U. M., Luu, A., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1902847116 · Cited by 56

The Laminopathies and the Insights They Provide into the Structural and Functional Organization of the Nucleus

Wong, X., & Stewart, C. L. (2020) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-121219-083616 · Cited by 56

Structure and unique mechanical aspects of nuclear lamin filaments

Kronenberg‐Tenga, R., & Medalia, O. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.06.017 · Cited by 56

Nuclear envelope rupture: little holes, big openings

Hatch, E. M. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.02.001 · Cited by 55

Cell migration, intercalation and growth regulate mammalian cochlear extension

Driver, E. C., Northrop, A., & Kelley, M. W. (2017) · Development · doi:10.1242/dev.151761 · Cited by 55

Nuclear Lamins and Neurobiology

Young, S. G., Jung, H.-J., Lee, J. M., & Fong, L. G. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00486-14 · Cited by 54

Nesprins and opposing microtubule motors generate a point force that drives directional nuclear motion in migrating neurons

Wu, Y. K., Umeshima, H., Kurisu, J., & Kengaku, M. (2018) · Development · doi:10.1242/dev.158782 · Cited by 54

Constricted migration is associated with stable 3D genome structure differences in cancer cells

Golloshi, R., Playter, C., Freeman, T. F., Das, P., Raines, T. I., Garretson, J. H., Thurston, D., & McCord, R. P. (2022) · EMBO Reports · doi:10.15252/embr.202052149 · Cited by 53

A Comparative Study of Drosophila and Human A-Type Lamins

Schulze, S. R., Curio-Penny, B., Speese, S. D., Dialynas, G. K., Cryderman, D. E., McDonough, C. W., Nalbant, D., Petersen, M., Budnik, V., Geyer, P., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007564 · Cited by 52

Nuclear pores in genome architecture and enhancer function

Pascual‐García, P., & Capelson, M. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.04.001 · Cited by 50

Nuclear envelope structural proteins facilitate nuclear shape changes accompanying embryonic differentiation and fidelity of gene expression

Smith, E. R., Meng, Y. D., Moore, R. H., Tse, J. D., Xu, A. G., & Xu, X. (2017) · BMC Cell Biology · doi:10.1186/s12860-017-0125-0 · Cited by 48

Getting into Position: Nuclear Movement in Muscle Cells

Azevedo, M., & Baylies, M. K. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.01.002 · Cited by 48

Arachidonic acid induction of Rho-mediated transendothelial migration in prostate cancer

Brown, M. D., Roulson, J. A., Hart, C. A., Tawadros, T., & Clarke, N. W. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.99 · Cited by 47

Cell and tissue morphology determine actin-dependent nuclear migration mechanisms in neuroepithelia

Yanakieva, I., Erzberger, A., Matejčić, M., Modes, C. D., & Norden, C. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201901077 · Cited by 47

Lamin Mutations Cause Increased YAP Nuclear Entry in Muscle Stem Cells

Owens, D. J., Fischer, M., Jabre, S., Moog, S., Mamchaoui, K., Butler-Browne, G. S., & Coirault, C. (2020) · Cells · doi:10.3390/cells9040816 · Cited by 47

Molecular models of LINC complex assembly at the nuclear envelope

Jahed, Z., Domkam, N., Ornowski, J., Yerima, G., & Mofrad, M. R. K. (2021) · Journal of Cell Science · doi:10.1242/jcs.258194 · Cited by 47

Nuclei migrate through constricted spaces using microtubule motors and actin networks in C. elegans hypodermal cells

Bone, C. R., Chang, Y.-T., Cain, N. E., Murphy, S. P., & Starr, D. A. (2016) · Development · doi:10.1242/dev.141192 · Cited by 46

The LINC complex is required for endothelial cell adhesion and adaptation to shear stress and cyclic stretch

Denis, K. B., Cabe, J. I., Danielsson, B. E., Tieu, K. V., Mayer, C. R., & Conway, D. E. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-11-0698 · Cited by 46

Three-dimensional superresolution fluorescence microscopy maps the variable molecular architecture of the nuclear pore complex

Sabinina, V. J., Hossain, M. J., Hèriché, J.-K., Hoess, P., Nijmeijer, B., Mosalaganti, S., Kueblbeck, M., Callegari, A., Szymborska, A., Beck, M., et al. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-11-0728 · Cited by 46

The Emerging Roles of Heterochromatin in Cell Migration

Gerlitz, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00394 · Cited by 45

High-throughput gene screen reveals modulators of nuclear shape

Tamashunas, A. C., Tocco, V. J., Matthews, J., Zhang, Q., Atanasova, K. R., Paschall, L., Pathak, S., Ratnayake, R., Stephens, A. D., Luesch, H., et al. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-09-0520 · Cited by 44

Cell confinement: putting the squeeze on the nucleus

Versaevel, M., Riaz, M., Grevesse, T., & Gabriele, S. (2013) · Soft Matter · doi:10.1039/c3sm00147d · Cited by 43

LINCing lamin B2 to neuronal migration

Coffinier, C., Fong, L. G., & Young, S. G. (2010) · Nucleus · doi:10.4161/nucl.1.5.12830 · Cited by 41

Mechanics of nuclear membranes

Agrawal, A., & Lele, T. P. (2019) · Journal of Cell Science · doi:10.1242/jcs.229245 · Cited by 41

LAP2alpha maintains a mobile and low assembly state of A-type lamins in the nuclear interior

Naetar, N., Georgiou, K., Knapp, C., Bronshtein, I., Zier, E., Fichtinger, P., Dechat, T., Garini, Y., & Foisner, R. (2021) · eLife · doi:10.7554/elife.63476 · Cited by 41

The Nesprin-1/-2 ortholog ANC-1 regulates organelle positioning in C. elegans independently from its KASH or actin-binding domains

Hao, H., Kalra, S., Jameson, L. E., Guerrero, L. A., Cain, N. E., Bolivar, J., & Starr, D. A. (2021) · eLife · doi:10.7554/elife.61069 · Cited by 40

A survey of physical methods for studying nuclear mechanics and mechanobiology

Hobson, C. M., Falvo, M. R., & Superfine, R. (2021) · APL Bioengineering · doi:10.1063/5.0068126 · Cited by 39

Constricted migration modulates stem cell differentiation

Smith, L., Irianto, J., Xia, Y., Pfeifer, C. R., & Discher, D. E. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-02-0090 · Cited by 38

Chromatin and Cytoskeletal Tethering Determine Nuclear Morphology in Progerin-Expressing Cells

Lionetti, M. C., Bonfanti, S., Fumagalli, M. R., Budrikis, Z., Font-Clos, F., Costantini, G., Chepizhko, O., Zapperi, S., & Porta, C. A. M. L. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.04.001 · Cited by 38

Gaussian curvature dilutes the nuclear lamina, favoring nuclear rupture, especially at high strain rate

Pfeifer, C. R., Tobin, M. P., Cho, S., Vashisth, M., Dooling, L. J., Vazquez, L. L., Lucca, E. G. R.-D., Simon, K. T., & Discher, D. E. (2022) · Nucleus · doi:10.1080/19491034.2022.2045726 · Cited by 38

Rupture Dynamics and Chromatin Herniation in Deformed Nuclei

Deviri, D., Discher, D. E., & Safran, S. A. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.07.014 · Cited by 35

Granulocyte heterochromatin: defining the epigenome

Olins, D. E., & Olins, A. L. (2005) · BMC Cell Biology · doi:10.1186/1471-2121-6-39 · Cited by 34

Nuclear failure, DNA damage, and cell cycle disruption after migration through small pores: a brief review

Pfeifer, C. R., Vashisth, M., Xia, Y., & Discher, D. E. (2019) · Essays in Biochemistry · doi:10.1042/ebc20190007 · Cited by 34

A network of nuclear envelope proteins and cytoskeletal force generators mediates movements of and within nuclei throughout Caenorhabditis elegans development

Starr, D. A. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219871965 · Cited by 32

Altered Levels and Isoforms of Tau and Nuclear Membrane Invaginations in Huntington’s Disease

Fernández‐Nogales, M., & Lucas, J. J. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00574 · Cited by 32

Structural Analysis of Different LINC Complexes Reveals Distinct Binding Modes

Cruz, V. E., Demircioglu, F. E., & Schwartz, T. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.09.019 · Cited by 32

Mechanobiology of Protein Droplets: Force Arises from Disorder

Welsh, T. J., Shen, Y., Levin, A., & Knowles, T. P. J. (2018) · Cell · doi:10.1016/j.cell.2018.11.020 · Cited by 31

Scaling laws indicate distinct nucleation mechanisms of holes in the nuclear lamina

Deviri, D., Pfeifer, C. R., Dooling, L. J., Ivanovska, I. L., Discher, D. E., & Safran, S. A. (2019) · Nature Physics · doi:10.1038/s41567-019-0506-8 · Cited by 31

Nuclear Deformation Lets Cells Gauge Their Physical Confinement

Long, J. T., & Lammerding, J. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.01.002 · Cited by 31

Phosphorylation of proliferating cell nuclear antigen promotes cancer progression by activating the ATM/Akt/GSK3β/Snail signaling pathway

Peng, B., Ortega, J., Gu, L., Chang, Z., & Li, G. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007897 · Cited by 30

Regulation of YAP/TAZ Activity by Mechanical Cues: An Experimental Overview

Dupont, S. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8910-2_15 · Cited by 29

Preclinical evaluation of nuclear morphometry and tissue topology for breast carcinoma detection and margin assessment

Nyirenda, N., Farkas, D. L., & Ramanujan, V. K. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-010-0914-z · Cited by 28

Apical and Basal Stress Fibers have Different Roles in Mechanical Regulation of the Nucleus in Smooth Muscle Cells Cultured on a Substrate

NAGAYAMA, K., Yahiro, Y., & MATSUMOTΟ, T. (2013) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-013-0294-7 · Cited by 28

Rapid staining and imaging of subnuclear features to differentiate between malignant and benign breast tissues at a point-of-care setting

Mueller, J. L., Gallagher, J. E., Chitalia, R., Krieger, M., Erkanli, A., Willett, R. M., Geradts, J., & Ramanujam, N. (2016) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-016-2165-9 · Cited by 28

Deregulation of focal adhesion formation and cytoskeletal tension due to loss of A-type lamins

Corne, T., Sieprath, T., Vandenbussche, J., Mohammed, D., Lindert, M. T., Gevaert, K., Gabriele, S., Wolf, K., & Vos, W. H. D. (2016) · Cell Adhesion & Migration · doi:10.1080/19336918.2016.1247144 · Cited by 26

Role of dynamic nuclear deformation on genomic architecture reorganization

Seirin‐Lee, S., Osakada, F., Takeda, J., Tashiro, S., Kobayashi, R., Yamamoto, T., & Ochiai, H. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1007289 · Cited by 26

Lamin A redistribution mediated by nuclear deformation determines dynamic localization of YAPPreprint

Koushki, N., Ghagre, A., Srivastava, L. K., Sitaras, C., Yoshie, H., Molter, C. W., & Ehrlicher, A. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.19.998708 · Cited by 26

The nuclear envelope: LINCing tissue mechanics to genome regulation in cardiac and skeletal muscle

Piccus, R., & Brayson, D. (2020) · Biology Letters · doi:10.1098/rsbl.2020.0302 · Cited by 26

Attach and stretch: Emerging roles for genome–lamina contacts in shaping the 3D genome

Rullens, P. M. J., & Kind, J. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.11.006 · Cited by 26

A synergy between mechanosensitive calcium- and membrane-binding mediates tension-sensing by C2-like domains

Shen, Z., Belcheva, K. T., Jelcic, M., Hui, K. L., Katikaneni, A., & Niethammer, P. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2112390119 · Cited by 25

The Effect of Cell Morphology on the Permeability of the Nuclear Envelope to Diffusive Factors

García‐González, A., Jacchetti, E., Marotta, R., Tunesi, M., Matas, J. F. R., & Raimondi, M. T. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00925 · Cited by 24

The mitotic protein NuMA plays a spindle-independent role in nuclear formation and mechanics

Serra-Marques, A., Houtekamer, R. M., Hintzen, D. C., Canty, J. T., Yıldız, A., & Dumont, S. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202004202 · Cited by 23

Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins

Lim, S. M., Cruz, V. E., Antoku, S., Gundersen, G. G., & Schwartz, T. (2021) · Structure · doi:10.1016/j.str.2020.12.013 · Cited by 22

A cellular sense of space and pressure

Shen, Z., & Niethammer, P. (2020) · Science · doi:10.1126/science.abe3881 · Cited by 18

Live imaging and analysis of postnatal mouse retinal development

Nickerson, P. E. B., Ronellenfitch, K., Csuzdi, N., Boyd, J. D., Howard, P. L., Delaney, K. R., & Chow, R. L. (2013) · BMC Developmental Biology · doi:10.1186/1471-213x-13-24 · Cited by 16

Stimulatory effects of arachidonic acid on myosin ATPase activity and contraction of smooth muscle via myosin motor domain

Katayama, T., Watanabe, M., Tanaka, H., Hino, M., Miyakawa, T., Ohki, T., Ye, L.-H., Xie, C., Yoshiyama, S., Nakamura, A., et al. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00577.2009 · Cited by 16

A minimal constraint device for imaging nuclei in live Drosophila contractile larval muscles reveals novel nuclear mechanical dynamics

Lorber, D., Rotkopf, R., & Volk, T. (2020) · Lab on a Chip · doi:10.1039/d0lc00214c · Cited by 16

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Razafsky, D. S., Potter, C., & Hodzic, D. M. (2015) · Journal of Visualized Experiments · doi:10.3791/53318 · Cited by 13

Lamin B2 follows lamin A/C- mediated nuclear mechanics and cancer cell invasion efficacyPreprint

Krause, M., Lindert, M. T., Riet, J. T., Boekhorst, V. T., Marke, R., Perera, R., Isermann, P., van Oorschot, T. G. M., Zwerger, M., Yang, F., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.07.028969 · Cited by 13

Probing cytoskeletal pre-stress and nuclear mechanics in endothelial cells with spatiotemporally controlled (de-)adhesion kinetics on micropatterned substrates

Versaevel, M., Riaz, M., Corne, T., Grevesse, T., Lantoine, J., Mohammed, D., Bruyère, C., Alaimo, L., Vos, W. H. D., & Gabriele, S. (2016) · Cell Adhesion & Migration · doi:10.1080/19336918.2016.1182290 · Cited by 12

Global transcriptional changes caused by an EDMD mutation correlate to tissue specific disease phenotypes inC. elegans

Zuela-Sopilniak, N., Dorfman, J., & Gruenbaum, Y. (2016) · Nucleus · doi:10.1080/19491034.2016.1238999 · Cited by 12

Interleukin 6-triggered ataxia-telangiectasia mutated kinase activation facilitates epithelial-to-mesenchymal transition in lung cancer by upregulating vimentin expression

Jiang, Y., NI, X. Y., Yan, H. Q., Shi, L., Lü, N., Wang, Y. N., Li, Q., & GAO, F. G. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.05.011 · Cited by 12

Push or pull: how cytoskeletal crosstalk facilitates nuclear movement through 3D environments

Chengappa, P., & Petrie, R. J. (2021) · Physical Biology · doi:10.1088/1478-3975/ac45e3 · Cited by 12

Cytoplasmic forces functionally reorganize nuclear condensates in oocytesPreprint

Jord, A. A., Letort, G., Chanet, S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.15.434387 · Cited by 11

Compressive forces driven by lateral actin fibers are a key to the nuclear deformation under uniaxial cell-substrate stretching

Tsukamoto, S., Chiam, K., Asakawa, T., Sawasaki, K., Takesue, N., & Sakamoto, N. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.01.107 · Cited by 11

Constricted migration is associated with stable 3D genome structure differences in cancer cellPreprint

Golloshi, R., Playter, C., Freeman, T. F., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/856583 · Cited by 7

Ensconsin-dependent changes in microtubule organization and LINC complex–dependent changes in nucleus–nucleus interactions result in quantitatively distinct myonuclear positioning defects

Collins, M. A., Coon, L. A., Thomas, R., Mandigo, T. R., Wynn, E., & Folker, E. S. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-06-0324 · Cited by 7

Confined Migration Induces Heterochromatin Formation and Alters Chromatin AccessibilityPreprint

Hsia, C.-R., McAllister, J., Hasan, O., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.22.461293 · Cited by 5

Control of nuclear size by osmotic forces in Schizosaccharomyces pombePreprint

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