The ESCRT machinery: new roles at new holes

Syndecan–syntenin–ALIX regulates the biogenesis of exosomes

Baietti, M. F., Zhang, Z., Mortier, E., Melchior, A., Degeest, G., Geeraerts, A., Ivarsson, Y., Depoortere, F., Coomans, C., Vermeiren, E., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2502 · Cited by 1,899 · see citing works

The ESCRT Pathway

Henne, W. M., Buchkovich, N. J., & Emr, S. D. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.05.015 · Cited by 1,500 · see citing works

Analysis of ESCRT functions in exosome biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles

Colombo, M., Moita, C. F., van Niel, G., Kowal, J., Vigneron, J., Benaroch, P., Manel, N., Moita, L. F., Théry, C., & Raposo, G. (2013) · Journal of Cell Science · doi:10.1242/jcs.128868 · Cited by 1,472 · see citing works

Ubiquitin-Dependent Sorting into the Multivesicular Body Pathway Requires the Function of a Conserved Endosomal Protein Sorting Complex, ESCRT-I

Katzmann, D. J., Babst, M., & Emr, S. D. (2001) · Cell · doi:10.1016/s0092-8674(01)00434-2 · Cited by 1,430 · see citing works

Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding

Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Côté, M., Rich, R. L., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00506-2 · Cited by 1,369 · see citing works

Escrt-III

Babst, M., Katzmann, D. J., Estepa, E. J., Meerloo, T., & Emr, S. D. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00220-4 · Cited by 875 · see citing works

AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding

Strack, B., Calistri, A., Craig, S., Popova, E., & Göttlinger, H. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00653-6 · Cited by 825 · see citing works

Molecular mechanism of multivesicular body biogenesis by ESCRT complexes

Wollert, T., & Hurley, J. H. (2010) · Nature · doi:10.1038/nature08849 · Cited by 804 · see citing works

Parallels Between Cytokinesis and Retroviral Budding: A Role for the ESCRT Machinery

Carlton, J. G., & Martin-Serrano, J. (2007) · Science · doi:10.1126/science.1143422 · Cited by 764 · see citing works

Membrane budding and scission by the ESCRT machinery: it's all in the neck

Hurley, J. H., & Hanson, P. I. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2937 · Cited by 757 · see citing works

Catastrophic nuclear envelope collapse in cancer cell micronuclei

Hatch, E. M., Fischer, A. H., Deerinck, T. J., & Hetzer, M. W. (2013) · Cell · doi:10.1016/j.cell.2013.06.007 · Cited by 741 · see citing works

Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis

Morita, E., Sandrin, V., Chung, H., Morham, S. G., Gygi, S. P., Rodesch, C. K., & Sundquist, W. I. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601850 · Cited by 724 · see citing works

HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress

Martin-Serrano, J., Zang, T., & Bieniasz, P. D. (2001) · Nature Medicine · doi:10.1038/nm1201-1313 · Cited by 710 · see citing works

ESCRTs are everywhere

Hurley, J. H. (2015) · The EMBO Journal · doi:10.15252/embj.201592484 · Cited by 668 · see citing works

Endosome-Associated Complex, ESCRT-II, Recruits Transport Machinery for Protein Sorting at the Multivesicular Body

Babst, M., Katzmann, D. J., Snyder, W. B., Wendland, B., & Emr, S. D. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00219-8 · Cited by 662 · see citing works

ESCRT Machinery Is Required for Plasma Membrane Repair

Jiménez, A. J., Maiuri, P., Lafaurie-Janvore, J., Divoux, S., Piel, M., & Perez, F. (2014) · Science · doi:10.1126/science.1247136 · Cited by 656 · see citing works

Membrane scission by the ESCRT-III complex

Wollert, T., Wunder, C., Lippincott‐Schwartz, J., & Hurley, J. H. (2009) · Nature · doi:10.1038/nature07836 · Cited by 634 · see citing works

Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease

Filimonenko, M., Stuffers, S., Raiborg, C., Yamamoto, A., Malerød, L., Fisher, E. M. C., Isaacs, A., Brech, A., Stenmark, H., & Simonsen, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702115 · Cited by 626 · see citing works

Aurora B-Mediated Abscission Checkpoint Protects against Tetraploidization

Steigemann, P., Wurzenberger, C., Schmitz, M. H. A., Held, M., Guizetti, J., Maar, S., & Gerlich, D. W. (2009) · Cell · doi:10.1016/j.cell.2008.12.020 · Cited by 610 · see citing works

Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55 ^Gag

VerPlank, L., Bouamr, F., LaGrassa, T. J., Agresta, B., Kikonyogo, A., Leis, J., & Carter, C. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.131059198 · Cited by 584 · see citing works

Cortical Constriction During Abscission Involves Helices of ESCRT-III–Dependent Filaments

Guizetti, J., Schermelleh, L., Mäntler, J., Maar, S., Poser, I., Leonhardt, H., Müller-Reichert, T., & Gerlich, D. (2011) · Science · doi:10.1126/science.1201847 · Cited by 496 · see citing works

Orchestrating nuclear envelope disassembly and reassembly during mitosis

Güttinger, S., Laurell, E., & Kutay, U. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2641 · Cited by 465 · see citing works

Polarized release of T-cell-receptor-enriched microvesicles at the immunological synapse

Choudhuri, K., Llodrá, J., Roth, E. W., Tsai, J., Gordo, S., Wucherpfennig, K. W., Kam, L. C., Stokes, D. L., & Dustin, M. L. (2014) · Nature · doi:10.1038/nature12951 · Cited by 397 · see citing works

Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins

Martin‐Serrano, J., Yaravoy, A., Pérez-Caballero, D., & Bieniasz, P. D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2133846100 · Cited by 391 · see citing works

Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission

Elia, N., Sougrat, R., Spurlin, T. A., Hurley, J. H., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102714108 · Cited by 389 · see citing works

Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing

Vietri, M., Schink, K. O., Campsteijn, C., Wegner, C. S., Schultz, S. W., Christ, L., Thoresen, S. B., Brech, A., Raiborg, C., & Stenmark, H. (2015) · Nature · doi:10.1038/nature14408 · Cited by 378 · see citing works

Mechanism of Ca2+-triggered ESCRT assembly and regulation of cell membrane repair

Scheffer, L., Sreetama, S. C., Sharma, N., Medikayala, S., Brown, K. J., Defour, A., & Jaiswal, J. K. (2014) · Nature Communications · doi:10.1038/ncomms6646 · Cited by 358 · see citing works

ESCRT-III controls nuclear envelope reformation

Olmos, Y., Hodgson, L. R., Mantell, J., Verkade, P., & Carlton, J. G. (2015) · Nature · doi:10.1038/nature14503 · Cited by 355 · see citing works

Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function

Demirov, D. G., Ono, A., Orenstein, J. M., & Freed, E. O. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032511899 · Cited by 352 · see citing works

ESCRT-III Governs the Aurora B–Mediated Abscission Checkpoint Through CHMP4C

Carlton, J. G., Caballe, A., Agromayor, M., Kloc, M., & Martin‐Serrano, J. (2012) · Science · doi:10.1126/science.1217180 · Cited by 326 · see citing works

Relaxation of Loaded ESCRT-III Spiral Springs Drives Membrane Deformation

Chiaruttini, N., Redondo‐Morata, L., Colom, A., Humbert, F., Lenz, M., Scheuring, S., & Roux, A. (2015) · Cell · doi:10.1016/j.cell.2015.10.017 · Cited by 324 · see citing works

Nuclear Envelope Budding Enables Large Ribonucleoprotein Particle Export during Synaptic Wnt Signaling

Speese, S. D., Ashley, J., Jokhi, V., Nunnari, J. N., Barría, R., Li, Y., Ataman, B., Koon, A. C., Chang, Y., Li, Q., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.032 · Cited by 317 · see citing works

Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly

Hetzer, M. W., Meyer, H. H., Walther, T. C., Bilbao, D., Warren, G., & Mattaj, I. W. (2001) · Nature Cell Biology · doi:10.1038/ncb1201-1086 · Cited by 311 · see citing works

Cytokinetic Abscission: Molecular Mechanisms and Temporal Control

Mierzwa, B. E., & Gerlich, D. W. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.11.006 · Cited by 289 · see citing works

Repetitive disruptions of the nuclear envelope invoke temporary loss of cellular compartmentalization in laminopathies

Vos, W. H. D., Houben, F., Kamps, M. A. F., Malhas, A. N., Verheyen, F., Cox, J., Manders, E. M. M., Verstraeten, V. L. R. M., Steensel, M. A. M. V., Marcelis, C., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr344 · Cited by 271 · see citing works

Structure and membrane remodeling activity of ESCRT-III helical polymers

McCullough, J., Clippinger, A. K., Talledge, N., Skowyra, M. L., Saunders, M. G., Naismith, T. V., Colf, L. A., Afonine, P. V., Arthur, C. P., Sundquist, W. I., et al. (2015) · Science · doi:10.1126/science.aad8305 · Cited by 268 · see citing works

Transient nuclear envelope rupturing during interphase in human cancer cells

Vargas, J. D., Hatch, E. M., Anderson, D. J., & Hetzer, M. W. (2012) · Nucleus · doi:10.4161/nucl.18954 · Cited by 263 · see citing works

Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin

Ramadan, K., Bruderer, R., Spiga, F. M., Popp, O., Baur, T., Gotta, M., & Meyer, H. H. (2007) · Nature · doi:10.1038/nature06388 · Cited by 261 · see citing works

Midbody Targeting of the ESCRT Machinery by a Noncanonical Coiled Coil in CEP55

Lee, H. H., Elia, N., Ghirlando, R., Lippincott‐Schwartz, J., & Hurley, J. H. (2008) · Science · doi:10.1126/science.1162042 · Cited by 260 · see citing works

Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B

Yang, D. J., Rismanchi, N., Renvoisé, B., Lippincott‐Schwartz, J., Blackstone, C. D., & Hurley, J. H. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1512 · Cited by 256 · see citing works

Spastin Couples Microtubule Severing to Membrane Traffic in Completion of Cytokinesis and Secretion

Connell, J. W., Lindon, C., Luzio, J. P., & Reid, E. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00847.x · Cited by 243 · see citing works

Membrane Fission Reactions of the Mammalian ESCRT Pathway

McCullough, J., Colf, L. A., & Sundquist, W. I. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072909-101058 · Cited by 238 · see citing works

Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release

Carlton, J. G., Agromayor, M., & Martin‐Serrano, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802008105 · Cited by 233 · see citing works

Dynamics of ESCRT protein recruitment during retroviral assembly

Jouvenet, N., Zhadina, M., Bieniasz, P. D., & Simon, S. M. (2011) · Nature Cell Biology · doi:10.1038/ncb2207 · Cited by 228 · see citing works

Remodelling the walls of the nucleus

Burke, B. E., & Ellenberg, J. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm860 · Cited by 225 · see citing works

Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4

Webster, B. M., Colombi, P., Jäger, J., & Lusk, C. P. (2014) · Cell · doi:10.1016/j.cell.2014.09.012 · Cited by 219 · see citing works

An inside-out origin for the eukaryotic cell

Baum, D., & Baum, B. (2014) · BMC Biology · doi:10.1186/s12915-014-0076-2 · Cited by 209 · see citing works

Cisternal Organization of the Endoplasmic Reticulum during Mitosis

Lü, L., Ladinsky, M. S., & Kirchhausen, T. L. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-04-0327 · Cited by 207 · see citing works

The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B

Reid, E., Connell, J. W., Edwards, T. L., Duley, S., Brown, S. E., & Sanderson, C. M. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddi003 · Cited by 202 · see citing works

Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum

Anderson, D. J., & Hetzer, M. W. (2007) · Nature Cell Biology · doi:10.1038/ncb1636 · Cited by 201 · see citing works

Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component

Baumgärtel, V., Ivanchenko, S. V., Dupont, A., Sergeev, M., Wiseman, P. W., Kräusslich, H., Bräuchle, C., Müller, B., & Lamb, D. C. (2011) · Nature Cell Biology · doi:10.1038/ncb2215 · Cited by 200 · see citing works

Protein quality control at the inner nuclear membrane

Khmelinskii, A., Błaszczak, E., Pantazopoulou, M., Fischer, B., Omnus, D. J., Dez, G. L., Brossard, A., Gunnarsson, A., Barry, J. D., Meurer, M., et al. (2014) · Nature · doi:10.1038/nature14096 · Cited by 198 · see citing works

The nuclear pore complex – structure and function at a glance

Kabachinski, G., & Schwartz, T. (2015) · Journal of Cell Science · doi:10.1242/jcs.083246 · Cited by 197 · see citing works

Quality control of inner nuclear membrane proteins by the Asi complex

Foresti, O., Rodríguez-Vaello, V., Funaya, C., & Carvalho, P. (2014) · Science · doi:10.1126/science.1255638 · Cited by 184 · see citing works

Progressive sheet-to-tubule transformation is a general mechanism for endoplasmic reticulum partitioning in dividing mammalian cells

Puhka, M., Joensuu, M., Vihinen, H., Belevich, I. N., & Jokitalo, E. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-12-0950 · Cited by 172 · see citing works

An ESCRT–spastin interaction promotes fission of recycling tubules from the endosome

Allison, R. J., Lumb, J. H., Fassier, C., Connell, J. W., Martín, D. T., Seaman, M. N. J., Hazan, J., & Reid, E. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201211045 · Cited by 164 · see citing works

Computational Model of Membrane Fission Catalyzed by ESCRT-III

Fabrikant, G., Lata, S., Riches, J. D., Briggs, J. A. G., Weissenhorn, W., & Kozlov, M. M. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000575 · Cited by 150 · see citing works

CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins

Howard, T. L., Stauffer, D. R., Degnin, C., & Hollenberg, S. M. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.13.2395 · Cited by 150 · see citing works

Herpes Simplex Virus Type 1 Production Requires a Functional ESCRT-III Complex but Is Independent of TSG101 and ALIX Expression

Pawliczek, T., & Crump, C. M. (2009) · Journal of Virology · doi:10.1128/jvi.00574-09 · Cited by 148 · see citing works

Membrane deformation and scission by the HSV-1 nuclear egress complex

Bigalke, J. M., Heuser, T., Nicastro, D., & Heldwein, E. E. Z. (2014) · Nature Communications · doi:10.1038/ncomms5131 · Cited by 144 · see citing works

SKD1 AAA ATPase-Dependent Endosomal Transport is Involved in Autolysosome Formation.

Nara, A., Mizushima, N., Yamamoto, A., Kabeya, Y., Ohsumi, Y., & Yoshimori, T. (2002) · Cell Structure and Function · doi:10.1247/csf.27.29 · Cited by 144 · see citing works

Torsin Mediates Primary Envelopment of Large Ribonucleoprotein Granules at the Nuclear Envelope

Jokhi, V., Ashley, J., Nunnari, J. N., Noma, A., Ito, N., Wakabayashi-Ito, N., Moore, M. J., & Budnik, V. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.015 · Cited by 138 · see citing works

Essential Role of hIST1 in Cytokinesis

Agromayor, M., Carlton, J. G., Phelan, J. P., Matthews, D. R., Carlin, L. M., Ameer‐Beg, S., Bowers, K., & Martin‐Serrano, J. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0474 · Cited by 138 · see citing works

Biochemical Analyses of Human IST1 and Its Function in Cytokinesis

Bajorek, M., Morita, E., Skalicky, J. J., Morham, S. G., Babst, M., & Sundquist, W. I. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0475 · Cited by 138 · see citing works

Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly

Shen, Q.-T., Schuh, A. L., Zheng, Y., Quinney, K., Wang, L., Hanna, M., Mitchell, J. C., Otegui, M. S., Ahlquist, P., Cui, Q., et al. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201403108 · Cited by 129 · see citing works

ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins

Caballe, A., Wenzel, D. M., Agromayor, M., Alam, S. L., Skalicky, J. J., Kloc, M., Carlton, J. G., Labrador, L., Sundquist, W. I., & Martin‐Serrano, J. (2015) · eLife · doi:10.7554/elife.06547 · Cited by 125 · see citing works

The ESCRT Machinery Is Recruited by the Viral BFRF1 Protein to the Nucleus-Associated Membrane for the Maturation of Epstein-Barr Virus

Lee, C., Liu, P.-T., Kung, H., Su, M.-T., Chua, H., Chang, Y.-H., Chang, C.-W., Tsai, C.-H. A., Liu, F., & Chen, M. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002904 · Cited by 118 · see citing works

Formation of the postmitotic nuclear envelope from extended ER cisternae precedes nuclear pore assembly

Lü, L., Ladinsky, M. S., & Kirchhausen, T. L. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201012063 · Cited by 116 · see citing works

CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression

Stauffer, D. R., Howard, T. L., Nyun, T., & Hollenberg, S. M. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.13.2383 · Cited by 112 · see citing works

Temporal and spatial organization of ESCRT protein recruitment during HIV-1 budding

Bleck, M., Itano, M. S., Johnson, D. S., Thomas, V. K., North, A. J., Bieniasz, P. D., & Simon, S. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321655111 · Cited by 112 · see citing works

An ESCRT module is required for neuron pruning

Loncle, N., Agromayor, M., Martin‐Serrano, J., & Williams, D. W. (2015) · Scientific Reports · doi:10.1038/srep08461 · Cited by 108 · see citing works

Defects in nuclear pore assembly lead to activation of an Aurora B–mediated abscission checkpoint

Mackay, D. R., Makise, M., & Ullman, K. S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201007124 · Cited by 108 · see citing works

Genetic and ultrastructural studies in dilated cardiomyopathy patients: a large deletion in the lamin A/C gene is associated with cardiomyocyte nuclear envelope disruption

Gupta, P., Bilińska, Z. T., Sylvius, N. B., Boudreau, É., Veinot, J. P., Labib, S., Bolongo, P. M., Hamza, A., Jackson, T., Płoski, R., et al. (2010) · Basic Research in Cardiology · doi:10.1007/s00395-010-0085-4 · Cited by 92 · see citing works

The Nucleoporin Nup153 Has Separable Roles in Both Early Mitotic Progression and the Resolution of Mitosis

Mackay, D. R., Elgort, S., & Ullman, K. S. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-08-0883 · Cited by 89 · see citing works

Assembly and disassembly of the ESCRT-III membrane scission complex

Adell, M. A. Y., & Teis, D. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.09.001 · Cited by 86 · see citing works

Building a nuclear envelope at the end of mitosis: coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensation

Schooley, A., Vollmer, B., & Antonin, W. (2012) · Chromosoma · doi:10.1007/s00412-012-0388-3 · Cited by 79 · see citing works

Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene.

DeHoratius, C., & Silver, P. A. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.11.1835 · Cited by 72 · see citing works

Ancient ESCRTs and the evolution of binary fission

Samson, R. Y., & Bell, S. D. (2009) · Trends in Microbiology · doi:10.1016/j.tim.2009.08.003 · Cited by 60 · see citing works

Cdc48/p97–Ufd1–Npl4 antagonizes Aurora B during chromosome segregation in HeLa cells

Dobrynin, G., Popp, O., Romer, T., Bremer, S., Schmitz, M. H. A., Gerlich, D. W., & Meyer, H. H. (2011) · Journal of Cell Science · doi:10.1242/jcs.069500 · Cited by 54 · see citing works

Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7

Bauer, I., Brune, T., Preiss, R., & Kölling, R. (2015) · Genetics · doi:10.1534/genetics.115.178939 · Cited by 52 · see citing works

Alternative nuclear transport for cellular protein quality control

Rose, A. E., & Schlieker, C. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.07.003 · Cited by 50 · see citing works

Lumenal interactions in nuclear pore complex assembly and stability

Yewdell, W. T., Colombi, P., Makhnevych, T., & Lusk, C. P. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-06-0554 · Cited by 50 · see citing works

Aurora B–mediated localized delays in nuclear envelope formation facilitate inclusion of late-segregating chromosome fragments

Karg, T., Warecki, B., & Sullivan, W. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-01-0026 · Cited by 46 · see citing works

The nuclear envelope: filling in gaps

Burke, B. E. (2001) · Nature Cell Biology · doi:10.1038/ncb1201-e273 · Cited by 27 · see citing works

ESCRTs breach the nuclear border

Webster, B. M., & Lusk, C. P. (2015) · Nucleus · doi:10.1080/19491034.2015.1035844 · Cited by 18 · see citing works

Reverse-topology membrane scission by the ESCRT proteins

Schöneberg, J., Lee, I., Iwasa, J., & Hurley, J. H. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.121 · Cited by 418 · see citing works

The life cycle of phagosomes: formation, maturation, and resolution

Levin‐Konigsberg, R., Grinstein, S., & Canton, J. (2016) · Immunological Reviews · doi:10.1111/imr.12439 · Cited by 307 · see citing works

Open Sesame: How Transition Fibers and the Transition Zone Control Ciliary Composition

Garcia-Gonzalo, F. R., & Reiter, J. F. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028134 · Cited by 290 · see citing works

ATP-dependent force generation and membrane scission by ESCRT-III and Vps4

Schöneberg, J., Pavlin, M., Yan, S., Righini, M., Lee, I.-H., Carlson, L., Bahrami, A., Goldman, D. H., Ren, X.-F., Hummer, G., et al. (2018) · Science · doi:10.1126/science.aat1839 · Cited by 161 · see citing works

Mechanisms protecting host cells against bacterial pore-forming toxins

Brito, C., Cabanes, D., Mesquita, F. S., & Sousa, S. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2992-8 · Cited by 129 · see citing works

Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing

Webster, B. M., Thaller, D. J., Jäger, J., Ochmann, S. E., Borah, S., & Lusk, C. P. (2016) · The EMBO Journal · doi:10.15252/embj.201694574 · Cited by 129 · see citing works

Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase

Monroe, N., Han, H., Shen, P. S., Sundquist, W. I., & Hill, C. P. (2017) · eLife · doi:10.7554/elife.24487 · Cited by 120 · see citing works

Mechanisms of nuclear pore complex assembly – two different ways of building one molecular machine

Otsuka, S., & Ellenberg, J. (2017) · FEBS Letters · doi:10.1002/1873-3468.12905 · Cited by 109 · see citing works

Interferon Receptor Trafficking and Signaling: Journey to the Cross Roads

Zanin, N., de Lesegno, C. V., Lamaze, C., & Blouin, C. M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.615603 · Cited by 103 · see citing works

ESCRT-dependent control of membrane remodelling during cell division

Stoten, C. L., & Carlton, J. G. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.08.035 · Cited by 101 · see citing works

Exosomal PD‐L1: New Insights Into Tumor Immune Escape Mechanisms and Therapeutic Strategies

Zhou, K., Guo, S., Li, F., Sun, Q., & Liang, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.569219 · Cited by 99 · see citing works

Growing functions of the ESCRT machinery in cell biology and viral replication

Scourfield, E. J., & Martin‐Serrano, J. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160479 · Cited by 92 · see citing works

HIV Genome-Wide Protein Associations: a Review of 30 Years of Research

Li, G., & Clercq, E. D. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00065-15 · Cited by 90 · see citing works

CC2D1B Coordinates ESCRT-III Activity during the Mitotic Reformation of the Nuclear Envelope

Ventimiglia, L. N., Cuesta-Geijo, M. Á., Martinelli, N., Caballe, A., Machebœuf, P., Miguet, N., Parnham, I. M., Olmos, Y., Carlton, J. G., Weissenhorn, W., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.11.012 · Cited by 85 · see citing works

Regulated lipid synthesis and LEM2/CHMP7 jointly control nuclear envelope closure

Penfield, L., Shankar, R., Szentgyörgyi, E., Laffitte, A., Mauro, M. S., Audhya, A., Müller‐Reichert, T., & Bahmanyar, S. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201908179 · Cited by 70 · see citing works

Structural basis of CHMP2A–CHMP3 ESCRT-III polymer assembly and membrane cleavage

Azad, K., Guilligay, D., Boscheron, C., Maity, S., Franceschi, N. D., Sulbarán, G., Effantin, G., Wang, H., Kleman, J.-P., Bassereau, P. M., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00867-8 · Cited by 65 · see citing works

In vitro methods for testing antiviral drugs

Rumlová, M., & Ruml, T. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.12.016 · Cited by 62 · see citing works

A helical assembly of human ESCRT-I scaffolds reverse-topology membrane scission

Flower, T. G., Takahashi, Y., Hudait, A., Rose, K., Tjahjono, N., Pak, A. J., Yokom, A. L., Liang, X., Wang, H.-G., Bouamr, F., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0426-4 · Cited by 57 · see citing works

Synthetic lethality between VPS4A and VPS4B triggers an inflammatory response in colorectal cancer

Szymańska, E., Nowak, P., Kolmus, K., Cybulska, M., Goryca, K., Derezińska‐Wołek, E., Szumera‐Ciećkiewicz, A., Brewińska‐Olchowik, M., Grochowska, A., Piwocka, K., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.201910812 · Cited by 56 · see citing works

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 55 · see citing works

The ESCRT protein CHMP2B acts as a diffusion barrier on reconstituted membrane necks

Franceschi, N. D., Alqabandi, M., Miguet, N., Caillat, C., Mangenot, S., Weissenhorn, W., & Bassereau, P. M. (2018) · Journal of Cell Science · doi:10.1242/jcs.217968 · Cited by 52 · see citing works

Gasdermins as evolutionarily conserved executors of inflammation and cell death

Chen, K. W., & Brož, P. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01474-z · Cited by 53 · see citing works

Increasing Diversity of Biological Membrane Fission Mechanisms

Renard, H., Johannes, L., & Morsomme, P. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.12.001 · Cited by 52 · see citing works

Lessons learned from CHMP2B, implications for frontotemporal dementia and amyotrophic lateral sclerosis

Ugbode, C., & West, R. J. H. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105144 · Cited by 51 · see citing works

Dynamic and elastic shape transitions in curved ESCRT-III filaments

Chiaruttini, N., & Roux, A. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.07.002 · Cited by 51 · see citing works

Inside job: how the ESCRTs release HIV-1 from infected cells

Hurley, J. H., & Cada, A. K. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180019 · Cited by 48 · see citing works

Eukarya the chimera: eukaryotes, a secondary innovation of the two domains of life?

Nobs, S.-J., MacLeod, F. I., Wong, H. L., & Burns, B. P. (2021) · Trends in Microbiology · doi:10.1016/j.tim.2021.11.003 · Cited by 47 · see citing works

The role of VPS4 in ESCRT-III polymer remodeling

Caillat, C., Maity, S., Miguet, N., Roos, W. H., & Weissenhorn, W. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180026 · Cited by 46 · see citing works

Coevolution of Eukaryote-like Vps4 and ESCRT-III Subunits in the Asgard Archaea

Lu, Z., Fu, T., Li, T., Liu, Y., Zhang, S., Li, J., Dai, J., Koonin, E. V., Li, G., Chu, H., et al. (2020) · mBio · doi:10.1128/mbio.00417-20 · Cited by 42 · see citing works

Advances in HIV-1 Assembly

Lerner, G., Weaver, N. C., Anokhin, B., & Spearman, P. W. (2022) · Viruses · doi:10.3390/v14030478 · Cited by 43 · see citing works

Aquaporins in Urinary Extracellular Vesicles (Exosomes)

Oshikawa, S., Sonoda, H., & Ikeda, M. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17060957 · Cited by 40 · see citing works

Cloaked Viruses and Viral Factors in Cutting Edge Exosome-Based Therapies

Dogrammatzis, C., Waisner, H., & Kalamvoki, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00376 · Cited by 39 · see citing works

The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization

Alqabandi, M., Franceschi, N. D., Miguet, N., Maity, S., Bally, M., Roos, W. H., Weissenhorn, W., Bassereau, P. M., & Mangenot, S. (2021) · BMC Biology · doi:10.1186/s12915-021-00983-9 · Cited by 38 · see citing works

The minimal ESCRT machinery of Giardia lamblia has altered inter-subunit interactions within the ESCRT-II and ESCRT-III complexes

Saha, N., Dutta, S., Datta, S. P., & Sarkar, S. (2017) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2017.11.004 · Cited by 31 · see citing works

ESCRT‐II functions by linking to ESCRT‐I in human immunodeficiency virus‐1 budding

Meng, B., Ip, N. C. Y., Abbink, T. E. M., Kenyon, J. C., & Lever, A. M. L. (2020) · Cellular Microbiology · doi:10.1111/cmi.13161 · Cited by 32 · see citing works

Extracellular vesicles in obesity and its associated inflammation

Kumar, V., Kiran, S., Kumar, S., & Singh, U. P. (2021) · International Reviews of Immunology · doi:10.1080/08830185.2021.1964497 · Cited by 32 · see citing works

The intralumenal fragment pathway mediates ESCRT-independent surface transporter down-regulation

McNally, E. K., & Brett, C. L. (2018) · Nature Communications · doi:10.1038/s41467-018-07734-5 · Cited by 31 · see citing works

NEDD4 family ubiquitin ligases associate with LCMV Z’s PPXY domain and are required for virus budding, but not via direct ubiquitination of Z

Ziegler, C. M., Dang, L., Eisenhauer, P., Kelly, J. A., King, B. R., Klaus, J. P., Manuelyan, I., Mattice, E. B., Shirley, D. J., Weir, M. E., et al. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008100 · Cited by 28 · see citing works

Polygenic Analysis in Absence of Major EffectorATF1Unveils Novel Components in Yeast Flavor Ester Biosynthesis

Holt, S., de Carvalho, B. T., Foulquié-Moreno, M. R., & Thevelein, J. M. (2018) · mBio · doi:10.1128/mbio.01279-18 · Cited by 30 · see citing works

The Role of Phosphatases in Nuclear Envelope Disassembly and Reassembly and Their Relevance to Pathologies

Huguet, F., Flynn, S., & Vagnarelli, P. (2019) · Cells · doi:10.3390/cells8070687 · Cited by 31 · see citing works

Seeking Closure: How Do Herpesviruses Recruit the Cellular ESCRT Apparatus?

Barnes, J., & Wilson, D. W. (2019) · Journal of Virology · doi:10.1128/jvi.00392-19 · Cited by 30 · see citing works

VPS4 is a dynamic component of the centrosome that regulates centrosome localization of γ-tubulin, centriolar satellite stability and ciliogenesis

Ott, C. M., Nachmias, D., Adar-Levor, S., Jarník, M., Sherman, S., Birnbaum, R. Y., Lippincott‐Schwartz, J., & Elia, N. (2018) · Scientific Reports · doi:10.1038/s41598-018-21491-x · Cited by 29 · see citing works

Concurrent depletion of Vps37 proteins evokes ESCRT-I destabilization and profound cellular stress responses

Kolmus, K., Erdenebat, P., Stewig, B. E., Szymańska, E., Goryca, K., Derezińska‐Wołek, E., Szumera‐Ciećkiewicz, A., Brewińska‐Olchowik, M., Piwocka, K., Prochorec‐Sobieszek, M., et al. (2021) · Journal of Cell Science · doi:10.1242/jcs.250951 · Cited by 29 · see citing works

Unexpected organellar locations of ESCRT machinery in Giardia intestinalis and complex evolutionary dynamics spanning the transition to parasitism in the lineage Fornicata

Pipaliya, S. V., Santos, R., Salas-Leiva, D. E., Balmer, E. A., Wirdnam, C. D., Roger, A. J., Hehl, A. B., Faso, C., & Dacks, J. B. (2021) · BMC Biology · doi:10.1186/s12915-021-01077-2 · Cited by 26 · see citing works

Interplay of the nuclear envelope with chromatin in physiology and pathology

Burla, R., Torre, M. L., Maccaroni, K., Vernı̀, F., Giunta, S., & Saggio, I. (2020) · Nucleus · doi:10.1080/19491034.2020.1806661 · Cited by 27 · see citing works

The open architecture of HD-PTP phosphatase provides new insights into the mechanism of regulation of ESCRT function

Gahloth, D., Heaven, G., Jowitt, T. A., Mould, A. P., Bella, J., Baldock, C., Woodman, P. G., & Tabernero, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-09467-9 · Cited by 26 · see citing works

Cdc42 GTPase regulates ESCRTs in nuclear envelope sealing and ER remodeling

Lu, M. S., & Drubin, D. G. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201910119 · Cited by 26 · see citing works

Preparing the lethal hit: interplay between exo- and endocytic pathways in cytotoxic T lymphocytes

Chang, H., Bzeih, H., Chitirala, P., Ravichandran, K., Sleiman, M., Krause, E., Hahn, U., Pattu, V., & Rettig, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2350-7 · Cited by 23 · see citing works

Betaherpesvirus assembly and egress: Recent advances illuminate the path

Wofford, A. S., McCusker, I., Green, J. C., Vensko, T. A., & Pellett, P. E. (2020) · Advances in virus research · doi:10.1016/bs.aivir.2020.09.003 · Cited by 22 · see citing works

Nucleoporins are degraded via upregulation of ESCRT-III/Vps4 complex in Drosophila models of C9-ALS/FTD

Dubey, S. K., Maulding, K., Sung, H., & Lloyd, T. E. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111379 · Cited by 20 · see citing works

Vesicular Nucleo-Cytoplasmic Transport—Herpesviruses as Pioneers in Cell Biology

Mettenleiter, T. C. (2016) · Viruses · doi:10.3390/v8100266 · Cited by 18 · see citing works

The ESCRT-II Subunit EAP20/VPS25 and the Bro1 Domain Proteins HD-PTP and BROX Are Individually Dispensable for Herpes Simplex Virus 1 Replication

Barnes, J., & Wilson, D. W. (2019) · Journal of Virology · doi:10.1128/jvi.01641-19 · Cited by 18 · see citing works

Stem Cell-Derived Exosomes: An Advanced Horizon to Cancer Regenerative Medicine

Ramachandran, A., Dhar, R., & Devi, A. (2024) · ACS Applied Bio Materials · doi:10.1021/acsabm.4c00089 · Cited by 17 · see citing works

Involvement of Human Cellular Proteins and Structures in Realization of the HIV Life Cycle: A Comprehensive Review, 2024

Shchemelev, A. N., Davydenko, V. S., Ostankova, Y. V., Reingardt, D. E., Николаевна, С. Е., Zueva, E. B., & Тотолян, А. А. (2024) · Viruses · doi:10.3390/v16111682 · Cited by 21 · see citing works

Emerging Mechanisms and Roles for Asymmetric Cytokinesis

Thieleke‐Matos, C., Osório, D. S., Carvalho, A. X., & Morais‐de‐Sá, E. (2017) · International review of cytology · doi:10.1016/bs.ircmb.2017.01.004 · Cited by 16 · see citing works

Vascular Smooth Muscle Cell Neutral Sphingomyelinase 2 in the Release of Exosomes and Vascular Calcification

Pavlic, A., Sangani, N. B., Kerins, J., Nicolaes, G. A. F., Schurgers, L. J., & Reutelingsperger, C. P. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169178 · Cited by 17 · see citing works

Mechanochemical Rules for Shape-Shifting Filaments that Remodel Membranes

Meadowcroft, B., Palaia, I., Pfitzner, A.-K., Roux, A., Baum, B., & Šarić, A. (2022) · Physical Review Letters · doi:10.1103/physrevlett.129.268101 · Cited by 16 · see citing works

Structural Basis for Specific Interaction of TGFβ Signaling Regulators SARA/Endofin with HD-PTP

Gahloth, D., Levy, C., Walker, L., Wunderley, L., Mould, A. P., Taylor, S., Woodman, P. G., & Tabernero, L. (2017) · Structure · doi:10.1016/j.str.2017.05.005 · Cited by 16 · see citing works

Zika Virus-Infected Monocyte Exosomes Mediate Cell-to-Cell Viral Transmission

Martínez-Rojas, P. P., Monroy-Martínez, V., Agredano‐Moreno, L. T., Jiménez‐García, L. F., & Ruíz-Ordaz, B. H. (2024) · Cells · doi:10.3390/cells13020144 · Cited by 15 · see citing works

A Structural View on ESCRT-Mediated Abscission

Horváth, P., & Müller-Reichert, T. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.586880 · Cited by 16 · see citing works

Growth of the fungus Chaetomium aureum in the presence of lead: implications in bioremediation

Júnior, F. M. R. D. S., Volcão, L. M., Honscha, L. C., & Pereira, S. V. (2018) · Environmental Earth Sciences · doi:10.1007/s12665-018-7447-x · Cited by 14 · see citing works

Alix-Mediated Rescue of Feline Immunodeficiency Virus Budding Differs from That Observed with Human Immunodeficiency Virus

Vecchio, C. D., Celestino, M., Celegato, M., Palù, G., Parolin, C., Bouamr, F., & Calistri, A. (2020) · Journal of Virology · doi:10.1128/jvi.02019-19 · Cited by 12 · see citing works

Missing-in-metastasis protein downregulates CXCR4 by promoting ubiquitylation and interaction with small Rab GTPases

Li, L., Baxter, S. S., Gu, N., Ji, M., & Zhan, X. (2017) · Journal of Cell Science · doi:10.1242/jcs.198937 · Cited by 12 · see citing works

Phase Separation in the Nucleus and at the Nuclear Periphery during Post-Mitotic Nuclear Envelope Reformation

Maccaroni, K., Torre, M. L., Burla, R., & Saggio, I. (2022) · Cells · doi:10.3390/cells11111749 · Cited by 11 · see citing works

Intrinsic Disorder in the Host Proteins Entrapped in Rabies Virus Particles

Ashraf, H. N., & Uversky, V. N. (2024) · Viruses · doi:10.3390/v16060916 · Cited by 9 · see citing works

Topography design in model membranes: Where biology meets physics

Chand, S., Beales, P. A., Claeyssens, F., & Ciani, B. (2018) · Experimental Biology and Medicine · doi:10.1177/1535370218809369 · Cited by 9 · see citing works

Vacuolar protein sorting 4 is required for silkworm metamorphosis

Xia, H., Chen, L., Shao, D., Liu, X., Wang, Q., Zhu, F., Guo, Z., Gao, L., & Chen, K. (2019) · Insect Molecular Biology · doi:10.1111/imb.12586 · Cited by 9 · see citing works

The precise function of alphaherpesvirus tegument proteins and their interactions during the viral life cycle

Cui, Y., Wang, M., Cheng, A., Zhang, W., Yang, Q., Tian, B., Ou, X., Huang, J., Wu, Y., Zhang, S., et al. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1431672 · Cited by 6 · see citing works

SH3YL1 cooperates with ESCRT-I in the sorting and degradation of the EGF receptor

Hasegawa, J., Jebri, I., Yamamoto, H., Tsujita, K., Tokuda, E. Y., Shibata, H., Maki, M., & Itoh, T. (2019) · Journal of Cell Science · doi:10.1242/jcs.229179 · Cited by 6 · see citing works

Emerging role and translational potential of small extracellular vesicles in neuroscience

Shanmugam, I., Radhakrishnan, S., Santosh, S., Ramnath, A., Anil, M., Devarajan, Y., Maheswaran, S., Narayanan, V., & Pitchaimani, A. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122987 · Cited by 6 · see citing works

Yeast dynamin interaction with ESCRT proteins at the endosome

Banh, B. T., McDermott, H., Woodman, S. E., Gadila, S. K. G., Saimani, U., Short, J. C. W., & Kim, K. (2017) · Cell Biology International · doi:10.1002/cbin.10738 · Cited by 5 · see citing works

Dictyostelium spastin is involved in nuclear envelope dynamics during semi-closed mitosis

Schweigel, U., Batsios, P., Müller‐Taubenberger, A., Gräf, R., & Grafe, M. (2022) · Nucleus · doi:10.1080/19491034.2022.2047289 · Cited by 5 · see citing works

Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication

Jehad, M. A., Ali, L. M., Pillai, V. N., Prabhu, S. G., Mustafa, F., & Rizvi, T. A. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf066 · Cited by 5 · see citing works

Advances in understanding the mechanisms of repairing damaged nuclear envelop

Kamikawa, Y. F., & Imaizumi, K. (2022) · The Journal of Biochemistry · doi:10.1093/jb/mvac012 · Cited by 4 · see citing works

Familial monophasic acute transverse myelitis due to the pathogenic variant in VPS37A

Mealy, M. A., Nam, T., Pardo, S., Pardo, C. A., Sobreira, N. L. D. M., Avramopoulos, D., Valle, D. L., Burns, K. H., & Levy, M. (2018) · Neurology Genetics · doi:10.1212/nxg.0000000000000213 · Cited by 4 · see citing works

The PMK-3 (p38) Mitochondrial Retrograde Response Functions in Intestinal Cells to Extend Life via the ESCRT MachineryPreprint

Radetskaya, O., Lane, R. K., Friedman, T., Garrett, A., Nguyen, M., Borror, M. B., Russell, J., & Rea, S. L. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/797308 · Cited by 4 · see citing works

Cell entry mechanisms of porcine enteric coronaviruses

Wang, Y., Zhao, F., Zhao, Q., Du, S., Wen, Y., Wu, R. J., Cao, S., Cong, F., & Huang, X.-B. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111250 · Cited by 4 · see citing works

Spatiotemporal control of spindle disassembly in fission yeast

Salas-Pino, S., & Daga, R. R. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03139-9 · Cited by 3 · see citing works

An ESCRT/VPS4 Envelopment Trap To Examine the Mechanism of Alphaherpesvirus Assembly and Transport in Neurons

Barnes, J., Jordan, B. A., & Wilson, D. W. (2022) · Journal of Virology · doi:10.1128/jvi.02178-21 · Cited by 3 · see citing works

ESCRT-III assembles around mis-segregated DNA to protect genome stability

Glover, J., Talledge, N., McCullough, J., Alian, A., Sadler, J. B. A., Kamboj, S., Dempsey, N. W. M., Laughlin, T. G., Nguyen, H. C., Wenzel, D. M., et al. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01841-4 · Cited by 2 · see citing works

Tumor Suppressor Gene 101

Carter, C. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811185-7.00009-1 · Cited by 2 · see citing works

How Plasma Membrane and Cytoskeletal Dynamics Influence Single-Cell Wound Healing: Mechanotransduction, Tension and Tensegrity

Boucher, É. L., Kato, T., & Mandato, C. A. (2016) · InTech eBooks · doi:10.5772/63765 · Cited by 1 · see citing works

Causes and Consequences of Nuclear Envelope Rupture and DNA Damage in Micronuclei

Grodsky, A. (2021) · Advances in Bioscience and Clinical Medicine · doi:10.7575/aiac.abcmed.v.9n.4p.12 · Cited by 1 · see citing works

Devising a divisome for synthetic cells

Dommisse, J., Lira, R. B., & Dekker, C. (2026) · Nature Reviews Chemistry · doi:10.1038/s41570-026-00848-1 · Cited by 1 · see citing works

The Cilium- and Centrosome-Associated Protein CCDC11 Is Required for Cytokinesis via Midbody Recruitment of the ESCRT- III Membrane Scission Complex Subunit CHMP2A

Ahmed, A., Lee, J., Parker, J. E., Rizvon, A., Nyayapathi, V., Li, F., Lake, M. W., & Takemaru, K. (2018) · Journal of Emerging Investigators · doi:10.59720/17-013 · Cited by 1 · see citing works

Transport and Communication Across the Nuclear Envelope

Huang, J. (2018) · Springer eBooks · doi:10.1007/978-981-13-0532-0_5

Co-evolution of Eukaryotic-like Vps4 and ESCRT-III Subunits in the Asgard ArchaeaPreprint

Lu, Z., Fu, T., Li, T., Liu, Y., Zhang, S., Li, J., Dai, J., Koonin, E. V., Li, G., Chu, H., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.05.080093

Investigating the Role of the Novel ESCRT-III Recruitment Factor CCDC11 in HIV Budding: A Potential Target for Antiviral Therapy

Takemaru, L., Pandya, P., Lake, M. W., Carter, C. A., & Li, F. (2020) · Journal of Emerging Investigators · doi:10.59720/19-109

Additional file 7 of The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization

Alqabandi, M., Franceschi, N. D., Maity, S., Miguet, N., Bally, M., Roos, W. H., Weissenhorn, W., Bassereau, P. M., & Mangenot, S. (2021) · Figshare · doi:10.6084/m9.figshare.14391213

Additional file 1 of The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization

Alqabandi, M., Franceschi, N. D., Maity, S., Miguet, N., Bally, M., Roos, W. H., Weissenhorn, W., Bassereau, P. M., & Mangenot, S. (2021) · Figshare · doi:10.6084/m9.figshare.14391198

Additional file 6 of The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization

Alqabandi, M., Franceschi, N. D., Maity, S., Miguet, N., Bally, M., Roos, W. H., Weissenhorn, W., Bassereau, P. M., & Mangenot, S. (2021) · Figshare · doi:10.6084/m9.figshare.14391210

Additional file 2 of The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization

Alqabandi, M., Franceschi, N. D., Maity, S., Miguet, N., Bally, M., Roos, W. H., Weissenhorn, W., Bassereau, P. M., & Mangenot, S. (2021) · Figshare · doi:10.6084/m9.figshare.14391201

Additional file 4 of The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization

Alqabandi, M., Franceschi, N. D., Maity, S., Miguet, N., Bally, M., Roos, W. H., Weissenhorn, W., Bassereau, P. M., & Mangenot, S. (2021) · Figshare · doi:10.6084/m9.figshare.14391207

Additional file 3 of The ESCRT-III isoforms CHMP2A and CHMP2B display different effects on membranes upon polymerization

Alqabandi, M., Franceschi, N. D., Maity, S., Miguet, N., Bally, M., Roos, W. H., Weissenhorn, W., Bassereau, P. M., & Mangenot, S. (2021) · Figshare · doi:10.6084/m9.figshare.14391204

Inhibition of ESCRT-III activates alternative pathways for protein degradation and secretion

Fujiwara, M., Sakai, R., Takahashi, M., Matsumoto, G., Hashimoto, T., & Kabuta, T. (2026) · Neurochemistry International · doi:10.1016/j.neuint.2026.106153

Caractérisation fonctionnelle des protéines des appendices du corps basal et de la zone de transition

Augière, C. (2017) · doi:10.70675/e95ed68bz0e3ez4d70za810zd502560026f6

Mechanical properties and function of CHMP2B in the ESCRT membrane remodelling and scission pathway

Alqabandi, M. (2018) · theses.fr (ABES) · doi:10.70675/5a1fed38zfdcez49f8z95d5z9a39d68ac40a

The role of cytonemes in the Hh secretion in Drosophila melanogaster

Novelli, C. (2019) · doi:10.70675/f90edf93z615dz47e2z9744z577831d1496d

La révolution de l’ARN

Scoazec, J. (2006) · Annales de Pathologie · doi:10.1016/s0242-6498(06)70721-0 · Cited by 2 · see citing works

The ESCRT-machinery: closing holes and expanding roles

Gatta, A. T., & Carlton, J. G. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.04.005 · Cited by 126 · see citing works

Cellular Functions and Molecular Mechanisms of the ESCRT Membrane-Scission Machinery

Christ, L., Raiborg, C., Wenzel, E. M., Campsteijn, C., & Stenmark, H. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.016 · Cited by 450 · see citing works

ESCRT-III function in membrane fission and repair

Burigotto, M., & Carlton, J. G. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00909-1 · Cited by 20 · see citing works

ESCRT-III: a versatile membrane remodeling machinery and its implications in cellular processes and diseases

Park, J., Kim, J., Park, H., Kim, T., & Lee, S. (2024) · Animal Cells and Systems · doi:10.1080/19768354.2024.2380294 · Cited by 17 · see citing works