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

Systematic functional analysis of the Caenorhabditis elegans genome using RNAi

Kamath, R. S., Fraser, A. G., Yan, D., Poulin, G. B., Durbin, R. M., Gotta, M., Kanapin, A. A., Bot, N. L., Moreno, S., Sohrmann, M., et al. (2003) · Nature · doi:10.1038/nature01278 · Cited by 3,629

ERAD: the long road to destruction

Meusser, B., Hirsch, C., Jarosch, E., & Sommer, T. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-766 · Cited by 1,221

The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore–microtubule attachment and in maintaining the spindle assembly checkpoint

Hauf, S., Cole, R. W., Terra, S. L., Zimmer, C., Schnapp, G., Walter, R., Heckel, A., Meel, J. C. A. V., Rieder, C. L., & Peters, J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200208092 · Cited by 1,169

Regulation of HP1–chromatin binding by histone H3 methylation and phosphorylation

Fischle, W., Tseng, B. S., Dormann, H. L., Ueberheide, B. M., Garcia, B. A., Shabanowitz, J., Hunt, D. F., Funabiki, H., & Allis, C. D. (2005) · Nature · doi:10.1038/nature04219 · Cited by 996

Chapter 30 Cell Cycle Extracts

Murray, A. W. (1991) · Methods in cell biology · doi:10.1016/s0091-679x(08)60298-8 · Cited by 942

Mitotic Phosphorylation of Histone H3 Is Governed by Ipl1/aurora Kinase and Glc7/PP1 Phosphatase in Budding Yeast and Nematodes

Hsu, J.-Y., Sun, Z., Li, X., Reuben, M., Tatchell, K., Bishop, D. K., Grushcow, J. M., Brame, C. J., Caldwell, J., Hunt, D. F., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00034-9 · Cited by 878

Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin

Hirota, T., Lipp, J., Toh, B., & Peters, J. (2005) · Nature · doi:10.1038/nature04254 · Cited by 662

Function of the p97–Ufd1–Npl4 complex in retrotranslocation from the ER to the cytosol

Ye, Y., Meyer, H. H., & Rapoport, T. A. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302169 · Cited by 598

A complex of mammalian Ufd1 and Npl4 links the AAA‐ATPase, p97, to ubiquitin and nuclear transport pathways

Meyer, H. H., Shorter, J., Seemann, J., Pappin, D., & Warren, G. (2000) · The EMBO Journal · doi:10.1093/emboj/19.10.2181 · Cited by 446

p47 is a cofactor for p97-mediated membrane fusion

Kondo, H., Rabouille, C., Newman, R., Levine, T. P., Pappin, D., Freemont, P. S., & Warren, G. (1997) · Nature · doi:10.1038/40411 · Cited by 437

The chromosomal passenger complex (CPC): from easy rider to the godfather of mitosis

Carmena, M., Wheelock, M., Funabiki, H., & Earnshaw, W. C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3474 · Cited by 934

Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system

Meyer, H. H., Bug, M., & Bremer, S. (2012) · Nature Cell Biology · doi:10.1038/ncb2407 · Cited by 832

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

Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy

Lamark, T., & Johansen, T. (2012) · International Journal of Cell Biology · doi:10.1155/2012/736905 · Cited by 514

Survivin Reads Phosphorylated Histone H3 Threonine 3 to Activate the Mitotic Kinase Aurora B

Kelly, A. E., Ghenoiu, C., Xue, J. Z., Zierhut, C., Kimura, H., & Funabiki, H. (2010) · Science · doi:10.1126/science.1189505 · Cited by 466

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 489

VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD

Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T.-P., Dantuma, N. P., & Taylor, J. P. (2010) · Autophagy · doi:10.4161/auto.6.2.11014 · Cited by 437

The VCP/p97 system at a glance: connecting cellular function to disease pathogenesis

Meyer, H. H., & Weihl, C. C. (2014) · Journal of Cell Science · doi:10.1242/jcs.093831 · Cited by 442

The Aurora kinase family in cell division and cancer

Vader, G., & Lens, S. M. A. (2008) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2008.07.003 · Cited by 436

Sizing up the nucleus: nuclear shape, size and nuclear-envelope assembly

Webster, M. T., Witkin, K. L., & Cohen‐Fix, O. (2009) · Journal of Cell Science · doi:10.1242/jcs.037333 · Cited by 402

Mapping the Degradable Kinome Provides a Resource for Expedited Degrader Development

Donovan, K. A., Ferguson, F. M., Bushman, J. W., Eleuteri, N. A., Bhunia, D., Ryu, S., Tan, L., Shi, K., Yue, H., Liu, X., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.038 · Cited by 359

RNF8‐ and RNF168‐dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites

Mallette, F. A., Mattiroli, F., Cui, G., Young, L. C., Hendzel, M. J., Mer, G., Sixma, T. K., & Richard, S. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.47 · Cited by 370

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 370

Mechanisms and functions of nuclear envelope remodelling

Ungricht, R., & Kutay, U. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.153 · Cited by 353

Molecular control of animal cell cytokinesis

Fededa, J. P., & Gerlich, D. W. (2012) · Nature Cell Biology · doi:10.1038/ncb2482 · Cited by 346

Nuclear envelope assembly defects link mitotic errors to chromothripsis

Liu, S., Kwon, M., Mannino, M., Yang, N., Renda, F., Khodjakov, A., & Pellman, D. (2018) · Nature · doi:10.1038/s41586-018-0534-z · Cited by 314

The Nuclear EnvelopePreprint

Hetzer, M. W. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000539 · Cited by 314

Molecular Mechanism of Substrate Processing by the Cdc48 ATPase Complex

Bodnar, N. O., & Rapoport, T. A. (2017) · Cell · doi:10.1016/j.cell.2017.04.020 · Cited by 322

Targeting the endoplasmic reticulum-stress response as an anticancer strategy

Healy, S., Gorman, A. M., Mousavi-Shafaei, P., Gupta, S., & Samali, A. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.06.064 · Cited by 305

Retrotranslocation of a Misfolded Luminal ER Protein by the Ubiquitin-Ligase Hrd1p

Carvalho, P., Stanley, A. M., & Rapoport, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.028 · Cited by 297

Phosphatases: providing safe passage through mitotic exit

Wurzenberger, C., & Gerlich, D. W. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3149 · Cited by 305

The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks

Ács, K., Luijsterburg, M. S., Ackermann, L., Salomons, F. A., Hoppe, T., & Dantuma, N. P. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2188 · Cited by 296

UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97

Schuberth, C. E., & Buchberger, A. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8072-8 · Cited by 277

Polyubiquitin chains: functions, structures, and mechanisms

Li, W., & Ye, Y. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8090-6 · Cited by 287

The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks

Meerang, M., Ritz, D., Paliwal, S., Garajovà, Z., Bosshard, M., Mailand, N., Janščák, P., Hübscher, U., Meyer, H. H., & Ramadan, K. (2011) · Nature Cell Biology · doi:10.1038/ncb2367 · Cited by 277

Valosin-containing protein disease: Inclusion body myopathy with Paget’s disease of the bone and fronto-temporal dementia

Weihl, C. C., Pestronk, A., & Kimonis, V. E. (2009) · Neuromuscular Disorders · doi:10.1016/j.nmd.2009.01.009 · Cited by 243

Cdc48: a power machine in protein degradation

Stolz, A., Hilt, W., Buchberger, A., & Wolf, D. H. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.06.001 · Cited by 235

Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations

Ritz, D., Vuk, M., Kirchner, P., Bug, M., Schütz, S., Hayer, A., Bremer, S., Lusk, C., Baloh, R. H., Lee, H., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2301 · Cited by 224

The Otubain YOD1 Is a Deubiquitinating Enzyme that Associates with p97 to Facilitate Protein Dislocation from the ER

Ernst, R., Mueller, B., Ploegh, H. L., & Schlieker, C. D. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.016 · Cited by 230

Cdc48/p97 mediates UV-dependent turnover of RNA Pol II

Verma, R., Oania, R., Fang, R., Smith, G. T., & Deshaies, R. J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.017 · Cited by 196

Recent advances in p97/VCP/Cdc48 cellular functions

Yamanaka, K., Sasagawa, Y., & Ogura, T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.001 · Cited by 196

Isolation of Mammalian 26S Proteasomes and p97/VCP Complexes Using the Ubiquitin-like Domain from HHR23B Reveals Novel Proteasome-Associated Proteins

Besche, H. C., Haas, W., Gygi, S. P., & Goldberg, A. L. (2009) · Biochemistry · doi:10.1021/bi802198q · Cited by 187

A Mighty “Protein Extractor” of the Cell: Structure and Function of the p97/CDC48 ATPase

Ye, Y., Tang, W. K., Zhang, T., & Xia, D. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00039 · Cited by 189

Deubiquitinases Maintain Protein Homeostasis and Survival of Cancer Cells upon Glutathione Depletion

Harris, I. S., Endress, J. E., Coloff, J. L., Selfors, L. M., McBrayer, S. K., Rosenbluth, J. M., Takahashi, N., Dhakal, S., Koduri, V., Oser, M. G., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.020 · Cited by 171

The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin

Krastev, D. B., Li, S., Sun, Y., Wicks, A. J., Hoslett, G., Weekes, D. B., Badder, L. M., Knight, E. G., Marlow, R., Pardo, M., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-021-00807-6 · Cited by 163

The ERAD Inhibitor Eeyarestatin I Is a Bifunctional Compound with a Membrane-Binding Domain and a p97/VCP Inhibitory Group

Wang, Q., Shinkre, B. A., Lee, J., Weniger, M. A., Liu, Y., Chen, W., Wiestner, A. U., Trenkle, W. C., & Ye, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015479 · Cited by 165

Structure and function of the AAA+ ATPase p97/Cdc48p

Xia, D., Tang, W. K., & Ye, Y. (2016) · Gene · doi:10.1016/j.gene.2016.02.042 · Cited by 168

Ku80 removal from DNA through double strand break–induced ubiquitylation

Postow, L., Ghenoiu, C., Woo, E. M., Krutchinsky, A. N., Chait, B. T., & Funabiki, H. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200802146 · Cited by 172

Chromosome condensation and decondensation during mitosis

Antonin, W., & Neumann, H. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.01.013 · Cited by 149

Golgi Structure and Function in Health, Stress, and Diseases

Li, J., Ahat, E., & Wang, Y. (2019) · Results and problems in cell differentiation · doi:10.1007/978-3-030-23173-6_19 · Cited by 146

Cell division control by the Chromosomal Passenger Complex

van der Waal, M. S., Hengeveld, R. C. C., van der Horst, A., & Lens, S. M. A. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.03.015 · Cited by 159

Proteomic profiling of VCP substrates links VCP to K6‐linked ubiquitylation and c‐Myc function

Heidelberger, J. B., Voigt, A., Borisova, M. E., Petrosino, G., Ruf, S., Wagner, S., & Beli, P. (2018) · EMBO Reports · doi:10.15252/embr.201744754 · Cited by 142

The Cul3–KLHL21 E3 ubiquitin ligase targets Aurora B to midzone microtubules in anaphase and is required for cytokinesis

Maerki, S., Olma, M. H., Staubli, T., Steigemann, P., Gerlich, D. W., Quadroni, M., Sumara, I., & Peter, M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906117 · Cited by 137

Finding the will and the way of ERAD substrate retrotranslocation

Hampton, R. Y., & Sommer, T. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.05.010 · Cited by 133

Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51–Rad52 interaction

Bergink, S., Ammon, T., Kern, M. J., Schermelleh, L., Leonhardt, H., & Jentsch, S. (2013) · Nature Cell Biology · doi:10.1038/ncb2729 · Cited by 134

Chromatin retention of DNA damage sensors DDB2 and XPC through loss of p97 segregase causes genotoxicity

Puumalainen, M.-R., Lessel, D., Rüthemann, P., Kaczmarek, N., Bachmann, K., Ramadan, K., & Naegeli, H. (2014) · Nature Communications · doi:10.1038/ncomms4695 · Cited by 138

RanBP2 and SENP3 Function in a Mitotic SUMO2/3 Conjugation-Deconjugation Cycle on Borealin

Klein, U. R., Haindl, M., Nigg, E. A., & Müller, S. P. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0511 · Cited by 127

Nuclear pore complex assembly through the cell cycle: Regulation and membrane organization

Antonin, W., Ellenberg, J., & Dultz, E. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.02.067 · Cited by 131

Cell division: control of the chromosomal passenger complex in time and space

van der Horst, A., & Lens, S. M. A. (2013) · Chromosoma · doi:10.1007/s00412-013-0437-6 · Cited by 133

Lysine methylation of VCP by a member of a novel human protein methyltransferase family

Kernstock, S., Davydova, E., Jakobsson, M. E., Moen, A. R., Pettersen, S., Mælandsmo, G. M., Egge-Jacobsen, W. M., & Falnes, P. Ø. (2012) · Nature Communications · doi:10.1038/ncomms2041 · Cited by 124

Reorganization of the nuclear envelope during open mitosis

Kutay, U., & Hetzer, M. W. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.09.010 · Cited by 123

Feedback control of chromosome separation by a midzone Aurora B gradient

Afonso, O., Matos, I., Pereira, A. J., Aguiar, P., Lampson, M. A., & Maiato, H. (2014) · Science · doi:10.1126/science.1251121 · Cited by 122

A Conserved Unfoldase Activity for the p97 AAA-ATPase in Proteasomal Degradation

Beskow, A., Grimberg, K. B., Bott, L. C., Salomons, F. A., Dantuma, N. P., & Young, P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.09.050 · Cited by 119

Emerging regulatory mechanisms in ubiquitin-dependent cell cycle control

Mocciaro, A., & Rapé, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.091199 · Cited by 113

Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy

Liu, Y., & Ye, Y. (2011) · Cell Research · doi:10.1038/cr.2011.75 · Cited by 111

A Genome-wide Screen Identifies p97 as an Essential Regulator of DNA Damage-Dependent CDT1 Destruction

Raman, M., Havens, C. G., Walter, J. C., & Harper, J. W. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.036 · Cited by 112

TRIM 21: a cytosolic Fc receptor with broad antibody isotype specificity

Foss, S., Watkinson, R., Sandlie, I., James, L. C., & Andersen, J. T. (2015) · Immunological Reviews · doi:10.1111/imr.12363 · Cited by 108

Nucleosomal regulation of chromatin composition and nuclear assembly revealed by histone depletion

Zierhut, C., Jenness, C., Kimurâ, H., & Funabiki, H. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2845 · Cited by 106

Structure, Dynamics and Function of the 26S Proteasome

Mao, Y. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_1 · Cited by 111

The chromosomal passenger complex (CPC) as a key orchestrator of orderly mitotic exit and cytokinesis

Kitagawa, M., & Lee, S. H. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00014 · Cited by 113

Growing sphere of influence: Cdc48/p97 orchestrates ubiquitin-dependent extraction from chromatin

Dantuma, N. P., & Hoppe, T. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.06.003 · Cited by 101

AAA ATPase p97/VCP is essential for TRIM21-mediated virus neutralization

Hauler, F., Mallery, D. L., McEwan, W. A., Bidgood, S. R., & James, L. C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210659109 · Cited by 104

Critical Role of VCP/p97 in the Pathogenesis and Progression of Non-Small Cell Lung Carcinoma

Valle, C. W., Min, T., Bodas, M., Mazur, S., Begum, S., Tang, D., & Vij, N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029073 · Cited by 101

Altered cofactor regulation with disease-associated p97/VCP mutations

Zhang, X., Gui, L., Zhang, X., Bulfer, S. L., Sanghez, V., Wong, D., Lee, Y., Lehmann, L. W., Lee, J. S., Shih, P.-Y., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1418820112 · Cited by 105

The ESCRT machinery: new roles at new holes

Olmos, Y., & Carlton, J. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.12.001 · Cited by 98

The p97 ATPase associates with EEA1 to regulate the size of early endosomes

Ramanathan, H. N., & Ye, Y. (2011) · Cell Research · doi:10.1038/cr.2011.80 · Cited by 104

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 99

Role of p97/VCP (Cdc48) in genome stability

Vaz, B., Halder, S., & Ramadan, K. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00060 · Cited by 95

Valosin-Containing Protein (VCP)/p97: A Prognostic Biomarker and Therapeutic Target in Cancer

Costantini, S., Capone, F., Polo, A., Bagnara, P., & Budillon, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810177 · Cited by 90

Dual Recruitment of Cdc48 (p97)-Ufd1-Npl4 Ubiquitin-selective Segregase by Small Ubiquitin-like Modifier Protein (SUMO) and Ubiquitin in SUMO-targeted Ubiquitin Ligase-mediated Genome Stability Functions

Nie, M., Aslanian, A., Prudden, J., Heideker, J., Vashisht, A. A., Wohlschlegel, J. A., Yates, J. R., & Boddy, M. N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.379768 · Cited by 88

Dynamic ubiquitin signaling in cell cycle regulation

Gilberto, S., & Peter, M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201703170 · Cited by 92

The p97/VCP ATPase is critical in muscle atrophy and the accelerated degradation of muscle proteins

Piccirillo, R., & Goldberg, A. L. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.178 · Cited by 85

Ring of Change: CDC48/p97 Drives Protein Dynamics at Chromatin

Franz, A., Ackermann, L., & Hoppe, T. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00073 · Cited by 92

The Abscission Checkpoint: Making It to the Final Cut

Nähse, V., Christ, L., Stenmark, H., & Campsteijn, C. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.10.001 · Cited by 84

The AAA-ATPase molecular chaperone Cdc48/p97 disassembles sumoylated centromeres, decondenses heterochromatin, and activates ribosomal RNA genes

Mérai, Z., Chumak, N., García-Aguilar, M., Hsieh, T., Nishimura, T., Schoft, V. K., Bindics, J., Ślusarz, L., Arnoux, S., Opravil, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1418564111 · Cited by 83

Nuclear Reformation at the End of Mitosis

Schellhaus, A. K., Magistris, P. D., & Antonin, W. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.09.016 · Cited by 83

Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control

Chen, M., Gutierrez, G. J., & Ronai, Z. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100028108 · Cited by 82

Cell cycle progression requires the CDC-48 UFD−1/NPL−4 complex for efficient DNA replication

Mouysset, J., Deichsel, A., Moser, S. C., Hoege, C., Hyman, A. A., Gartner, A., & Hoppe, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805944105 · Cited by 82

Sds22 and Repo-Man stabilize chromosome segregation by counteracting Aurora B on anaphase kinetochores

Wurzenberger, C., Held, M., Lampson, M. A., Poser, I., Hyman, A. A., & Gerlich, D. W. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201112112 · Cited by 87

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

K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle

Yu, Y., Zheng, Q., Erramilli, S. K., Pan, M., Park, S.-J., Xie, Y., Li, J., Fei, J., Kossiakoff, A. A., Liu, L., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00823-5 · Cited by 82

Inhibitors of the ATPase p97/VCP: From basic research to clinical applications

Kilgas, S., & Ramadan, K. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2022.12.007 · Cited by 82

Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways

Dargemont, C., & Ossareh‐Nazari, B. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.011 · Cited by 81

The Nup107-160 Nucleoporin Complex Promotes Mitotic Events via Control of the Localization State of the Chromosome Passenger Complex

Platani, M., Santarella‐Mellwig, R., Posch, M., Walczak, R., Swedlow, J. R., & Mattaj, I. W. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-05-0377 · Cited by 76

Neuronal remodeling and apoptosis require VCP-dependent degradation of the apoptosis inhibitor DIAP1

Rumpf, S., Lee, S. B., Jan, L. Y., & Jan, Y. N. (2011) · Development · doi:10.1242/dev.062703 · Cited by 75

New ATPase regulators—p97 goes to the PUB

Madsen, L., Seeger, M., Semple, C. A. M., & Hartmann‐Petersen, R. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.05.017 · Cited by 73

SUMOylation modulates the function of Aurora-B kinase

Fernández‐Miranda, G., de Castro, I. P., Carmena, M., Aguirre‐Portolés, C., Ruchaud, S., Fant, X., Montoya, G., Earnshaw, W. C., & Malumbres, M. (2010) · Journal of Cell Science · doi:10.1242/jcs.065565 · Cited by 72

Novel ESCRT functions in cell biology: spiraling out of control?

Campsteijn, C., Vietri, M., & Stenmark, H. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.03.008 · Cited by 78

Ubiquitin-Mediated Degradation of Aurora Kinases

Lindon, C., Grant, R., & Min, M. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2015.00307 · Cited by 74

A functional deficiency of TERA/VCP/p97 contributes to impaired DNA repair in multiple polyglutamine diseases

Fujita, K., Nakamura, Y., Oka, T., Ito, H., Tamura, T., Tagawa, K., Sasabe, T., Katsuta, A., Motoki, K., Shiwaku, H., et al. (2013) · Nature Communications · doi:10.1038/ncomms2828 · Cited by 70

Molecular pathogenesis of Spondylocheirodysplastic Ehlers‐Danlos syndrome caused by mutant ZIP13 proteins

Bin, B., Hojyo, S., Hosaka, T., Bhin, J., Kano, H., Miyai, T., Ikeda, M., Kimura‐Someya, T., Shirouzu, M., Cho, E., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201303809 · Cited by 68

Valosin-Containing Protein (VCP/p97) Is Required for Poliovirus Replication and Is Involved in Cellular Protein Secretion Pathway in Poliovirus Infection

Arita, M., Wakita, T., & Shimizu, H. (2012) · Journal of Virology · doi:10.1128/jvi.00114-12 · Cited by 68

The coordination of nuclear envelope assembly and chromosome segregation in metazoans

Liu, S., & Pellman, D. S. (2020) · Nucleus · doi:10.1080/19491034.2020.1742064 · Cited by 68

A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor–promoter DNA complex

Wilcox, A. J., & Laney, J. D. (2009) · Nature Cell Biology · doi:10.1038/ncb1997 · Cited by 67

Importin β Regulates the Seeding of Chromatin with Initiation Sites for Nuclear Pore Assembly

Rotem, A., Gruber, R., Shorer, H., Shaulov, L., Klein, E., & Harel, A. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-02-0150 · Cited by 66

KLHL41 stabilizes skeletal muscle sarcomeres by nonproteolytic ubiquitination

Ramirez-Martinez, A., Cenik, B. K., Bezprozvannaya, S., Chen, B., Bassel‐Duby, R., Liu, N., & Olson, E. N. (2017) · eLife · doi:10.7554/elife.26439 · Cited by 67

Dynamic SUMO modification regulates mitotic chromosome assembly and cell cycle progression in Caenorhabditis elegans

Pelisch, F., Sonneville, R., Pourkarimi, E., Agostinho, A., Blow, J. J., Gartner, A., & Hay, R. T. (2014) · Nature Communications · doi:10.1038/ncomms6485 · Cited by 65

Chromatin-Bound Xenopus Dppa2 Shapes the Nucleus by Locally Inhibiting Microtubule Assembly

Xue, J. Z., Woo, E. M., Postow, L., Chait, B. T., & Funabiki, H. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.08.002 · Cited by 63

The p97–UBXD8 complex destabilizes mRNA by promoting release of ubiquitinated HuR from mRNPPreprint

Zhou, H.-L., Geng, C., Luo, G., & Lou, H. J. (2013) · Genes & Development · doi:10.1101/gad.215681.113 · Cited by 63

Role of autophagy in muscle disease

Franco‐Romero, A., & Sandri, M. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101041 · Cited by 65

Regulation of Aurora B by Cdc48/P97 at the End of Mitosis

Bruderer, R. (2009)

The ubiquitin‐dependent chaperone Cdc48/p97(Ufd1‐Npl4) regulates Aurora‐B kinase on mitotic chromosomes

Meyer, H. H. (2009) · The FASEB Journal · doi:10.1096/fasebj.23.1_supplement.848.1

A role for Cdc48/p97 and Aurora B in controlling chromatin condensation during exit from mitosisThis paper is one of a selection of papers published in this special issue entitled 8th International Conference on AAA Proteins and has undergone the Journal's usual peer review process.

Meyer, H. H., Drozdowska, A. M., & Dobrynin, G. (2010) · Biochemistry and Cell Biology · doi:10.1139/o09-119 · Cited by 18

Characterization of a Novel Chromatin-Induced Mechanism that Couples Microtubule Disassembly and Nuclear Re-Formation

Woo, E. M. (2025) · Digital Commons - RU (Rockefeller University) · doi:10.48496/yhnm-zv47

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