Regulation of DNA Damage Responses by Ubiquitin and SUMO

Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy

Farmer, H., McCabe, N., Lord, C. J., Tutt, A. N. J., Johnson, D. A., Richardson, T. B., Santarosa, M., Dillon, K. J., Hickson, I., Knights, C., et al. (2005) · Nature · doi:10.1038/nature03445 · Cited by 6,683 · see citing works

The DNA-damage response in human biology and disease

Jackson, S. P., & Bartek, J. (2009) · Nature · doi:10.1038/nature08467 · Cited by 6,092 · see citing works

Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase

Bryant, H. E., Schultz, N., Thomas, H. D., Parker, K. M., Flower, D., Lopez, E., Kyle, S., Meuth, M., Curtin, N. J., & Helleday, T. (2005) · Nature · doi:10.1038/nature03443 · Cited by 5,198 · see citing works

The ubiquitin code

Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679 · see citing works

DNA damage, aging, and Cancer

Hoeijmakers, J. H. J. (2009) · New England Journal of Medicine · doi:10.1056/nejmra0804615 · Cited by 2,239 · see citing works

RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO

Hoege, C., Pfander, B., Moldovan, G., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,202 · see citing works

A genomic and functional inventory of deubiquitinating enzymes.

Nijman, S. M. B., Luna-Vargas, M. P. A., Velds, A., Brummelkamp, T. R., Dirac, A. M. G., Sixma, T. K., & Bernards, R. (2005) · Cell · doi:10.1016/j.cell.2005.11.007 · Cited by 1,854 · see citing works

53BP1 Inhibits Homologous Recombination in Brca1-Deficient Cells by Blocking Resection of DNA Breaks

Bunting, S. F., Callén, E., Wong, N., Chen, H.-T., Polato, F., Gunn, A., Bothmer, A., Feldhahn, N., Fernandez-Capetillo, O., Cao, L., et al. (2010) · Cell · doi:10.1016/j.cell.2010.03.012 · Cited by 1,671 · see citing works

DNA repair pathways as targets for cancer therapy

Helleday, T., Petermann, E., Lundin, C., Hodgson, B., & Sharma, R. A. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2342 · Cited by 1,666 · see citing works

Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome

Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A. P., Sowa, M. E., Rad, R., Rush, A. J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,614 · see citing works

RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins

Mailand, N., Bekker‐Jensen, S., Kildegaard, H. F., Melander, F., Bártek, J., Lukas, C., & Lukas, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.040 · Cited by 1,151 · see citing works

MDC1 Directly Binds Phosphorylated Histone H2AX to Regulate Cellular Responses to DNA Double-Strand Breaks

Stucki, M., Clapperton, J. A., Mohammad, D. H., Yaffe, M. B., Smerdon, S. J., & Jackson, S. P. (2005) · Cell · doi:10.1016/j.cell.2005.09.038 · Cited by 1,103 · see citing works

RNF8 Transduces the DNA-Damage Signal via Histone Ubiquitylation and Checkpoint Protein Assembly

Huen, M. S. Y., Grant, R. A., Manke, I. A., Minn, K. T., Yu, X., Yaffe, M. B., & Chen, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.041 · Cited by 1,027 · see citing works

53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers

Bouwman, P., Aly, A., Escandell, J. M., Pieterse, M., Bartkova, J., van der Gulden, H., Hiddingh, S., Thanasoula, M., Kulkarni, A., Yang, Q., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1831 · Cited by 1,001 · see citing works

Structural Basis for the Methylation State-Specific Recognition of Histone H4-K20 by 53BP1 and Crb2 in DNA Repair

Botuyan, M. V., Lee, J., Ward, I. M., Kim, J., Thompson, J. R., Chen, J., & Mer, G. (2006) · Cell · doi:10.1016/j.cell.2006.10.043 · Cited by 973 · see citing works

RNF168 Binds and Amplifies Ubiquitin Conjugates on Damaged Chromosomes to Allow Accumulation of Repair Proteins

Doil, C., Mailand, N., Bekker‐Jensen, S., Ménard, P., Larsen, D. H., Pepperkok, R., Ellenberg, J., Panier, S., Durocher, D., Bártek, J., et al. (2009) · Cell · doi:10.1016/j.cell.2008.12.041 · Cited by 938 · see citing works

Orchestration of the DNA-Damage Response by the RNF8 Ubiquitin Ligase

Kolas, N. K., Chapman, J. R., Nakada, S., Ylanko, J., Chahwan, R., Sweeney, F. D., Panier, S., Mendez, M., Wildenhain, J., Thomson, T. M., et al. (2007) · Science · doi:10.1126/science.1150034 · Cited by 894 · see citing works

A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles

Wagner, S., Beli, P., Weinert, B. T., Nielsen, M. L., Cox, J., Mann, M., & Choudhary, C. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013284 · Cited by 889 · see citing works

Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation

Stelter, P., & Ulrich, H. D. (2003) · Nature · doi:10.1038/nature01965 · Cited by 849 · see citing works

Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB

Scheuermann, J. C., Alonso, A. G. D. A., Oktaba, K., Ly‐Hartig, N., McGinty, R. K., Fraterman, S., Wilm, M. S., Muir, T. W., & Müller, J. (2010) · Nature · doi:10.1038/nature08966 · Cited by 816 · see citing works

The RIDDLE Syndrome Protein Mediates a Ubiquitin-Dependent Signaling Cascade at Sites of DNA Damage

Stewart, G. S., Panier, S., Townsend, K., Al-Hakim, A., Kolas, N. K., Miller, E. S., Nakada, S., Ylanko, J., Olivarius, S., Mendez, M., et al. (2009) · Cell · doi:10.1016/j.cell.2008.12.042 · Cited by 759 · see citing works

Histone ubiquitination: triggering gene activity.

Weake, V. M., & Workman, J. (2008) · Molecules and Cells · doi:10.1016/j.molcel.2008.02.014 · Cited by 742 · see citing works

ATM-Dependent Chromatin Changes Silence Transcription In cis to DNA Double-Strand Breaks

Shanbhag, N. M., Rafalska-Metcalf, I. U., Balane-Bolivar, C., Janicki, S. M., & Greenberg, R. A. (2010) · Cell · doi:10.1016/j.cell.2010.04.038 · Cited by 737 · see citing works

The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme

Jentsch, S., McGrath, J. P., & Varshavsky, A. J. (1987) · Nature · doi:10.1038/329131a0 · Cited by 736 · see citing works

RAP80 Targets BRCA1 to Specific Ubiquitin Structures at DNA Damage Sites

Sobhian, B., Shao, G., Lilli, D. R., Culhane, A. C., Moreau, L. A., Xia, B., Livingston, D. M., & Greenberg, R. A. (2007) · Science · doi:10.1126/science.1139516 · Cited by 672 · see citing works

RNF168 Ubiquitinates K13-15 on H2A/H2AX to Drive DNA Damage Signaling

Mattiroli, F., Vissers, J. H. A., van Dijk, W. J., Ikpa, P. T., Citterio, E., Vermeulen, W., Marteijn, J. A. F., & Sixma, T. K. (2012) · Cell · doi:10.1016/j.cell.2012.08.005 · Cited by 653 · see citing works

More than just a focus: The chromatin response to DNA damage and its role in genome integrity maintenance

Lukas, J., Lukas, C., & Bartek, J. (2011) · Nature Cell Biology · doi:10.1038/ncb2344 · Cited by 645 · see citing works

SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase

Pfander, B., Moldovan, G., Sacher, M., Hoege, C., & Jentsch, S. (2005) · Nature · doi:10.1038/nature03665 · Cited by 626 · see citing works

DNA helicase Srs2 disrupts the Rad51 presynaptic filament

Krejčí, L., Komen, S. V., Li, Y., Villemain, J. L., Reddy, M. S., Klein, H. L., Ellenberger, T. E., & Sung, P. (2003) · Nature · doi:10.1038/nature01577 · Cited by 624 · see citing works

The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments

Veaute, X., Jeusset, J., Soustelle, C., Kowalczykowski, S. C., Cam, É. L., & Fabre, F. (2003) · Nature · doi:10.1038/nature01585 · Cited by 612 · see citing works

Regulation of monoubiquitinated PCNA by DUB autocleavage

Huang, T. T., Nijman, S. M. B., Mirchandani, K. D., Galardy, P. J., Cohn, M. A., Haas, W., Gygi, S. P., Ploegh, H. L., Bernards, R., & D’Andrea, A. D. (2006) · Nature Cell Biology · doi:10.1038/ncb1378 · Cited by 585 · see citing works

Monoubiquitination of Human Histone H2B: The Factors Involved and Their Roles in HOX Gene Regulation

Zhu, B., Zheng, Y., Pham, A.-D., Mandal, S. S., Erdjument‐Bromage, H., Tempst, P., & Reinberg, D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.025 · Cited by 532 · see citing works

Principles of ubiquitin and SUMO modifications in DNA repair

Bergink, S., & Jentsch, S. (2009) · Nature · doi:10.1038/nature07963 · Cited by 525 · see citing works

Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks

Galanty, Y., Belotserkovskaya, R., Coates, J., Polo, S. E., Miller, K. M., & Jackson, S. P. (2009) · Nature · doi:10.1038/nature08657 · Cited by 523 · see citing works

The Fanconi Anemia Pathway Promotes Replication-Dependent DNA Interstrand Cross-Link Repair

Knipscheer, P., Räschle, M., Smogorzewska, A., Enoiu, M., Ho, T. V., Schärer, O. D., Elledge, S. J., & Walter, J. C. (2009) · Science · doi:10.1126/science.1182372 · Cited by 515 · see citing works

Regulation of DNA cross-link repair by the Fanconi anemia/BRCA pathwayPreprint

Kim, H., & D’Andrea, A. D. (2012) · Genes & Development · doi:10.1101/gad.195248.112 · Cited by 510 · see citing works

DNA-PK, ATM and ATR as sensors of DNA damage: variations on a theme?

Durocher, D., & Jackson, S. P. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00201-5 · Cited by 506 · see citing works

BRCA1 tumour suppression occurs via heterochromatin-mediated silencing

Zhu, Q., Pao, G. M., Huynh, A. M., Suh, H., Tonnu, N. U., Nederlof, P. M., Gage, F. H., & Verma, I. M. (2011) · Nature · doi:10.1038/nature10371 · Cited by 486 · see citing works

Protein Group Modification and Synergy in the SUMO Pathway as Exemplified in DNA Repair

Psakhye, I., & Jentsch, S. (2012) · Cell · doi:10.1016/j.cell.2012.10.021 · Cited by 484 · see citing works

p53 Research: The Past Thirty Years and the Next Thirty YearsPreprint

Lane, D. P., & Levine, A. J. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000893 · Cited by 455 · see citing works

Deubiquitinases in cancer: new functions and therapeutic options

Fraile, J. M., Quesada, V., Rodrı́guez, D., Freije, J. M. P., & López-Otı́n, C. (2011) · Oncogene · doi:10.1038/onc.2011.443 · Cited by 453 · see citing works

Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage

Wang, B., & Elledge, S. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710061104 · Cited by 446 · see citing works

The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress

Morris, J. R., Boutell, C., Epple, M., Densham, R. M., Weekes, D. B., Alamshah, A., Butler, L. R., Galanty, Y., Pangon, L., Kiuchi, T., et al. (2009) · Nature · doi:10.1038/nature08593 · Cited by 434 · see citing works

Requirement of ATM-Dependent Monoubiquitylation of Histone H2B for Timely Repair of DNA Double-Strand Breaks

Moyal, L., Lerenthal, Y., Gana‐Weisz, M., Mass, G., So, S., Wang, S., Eppink, B., Chung, Y. M., Shalev, G., Shema, E., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.015 · Cited by 402 · see citing works

The Smc5–Smc6 complex and SUMO modification of Rad52 regulates recombinational repair at the ribosomal gene locus

Torres‐Rosell, J., Šunjevarić, I., Piccoli, G. D., Sacher, M., Eckert‐Boulet, N., Reid, R. J. D., Jentsch, S., Rothstein, R. J., Aragón, L., & Lisby, M. (2007) · Nature Cell Biology · doi:10.1038/ncb1619 · Cited by 379 · see citing works

Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1

Nakada, S., Tai, I., Panier, S., Al-Hakim, A., Iemura, S.-I., Juang, Y.-C., O’Donnell, L., Kumakubo, A., Munro, M., Sicheri, F., et al. (2010) · Nature · doi:10.1038/nature09297 · Cited by 357 · see citing works

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 357 · see citing works

Regulation of Homologous Recombination by RNF20-Dependent H2B Ubiquitination

Nakamura, K., Kato, A., Kobayashi, J., Yanagihara, H., Sakamoto, S., Oliveira, D. V. N. P., Shimada, M., Tauchi, H., Suzuki, H., Tashiro, S., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.002 · Cited by 351 · see citing works

TRIP12 and UBR5 Suppress Spreading of Chromatin Ubiquitylation at Damaged Chromosomes

Guðjόnsson, Þ., Altmeyer, M., Savic, V., Toledo, L. I., Dinant, C., Grøfte, M., Bártková, J., Poulsen, M., Oka, Y., Bekker‐Jensen, S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.039 · Cited by 338 · see citing works

SUMO‐targeted ubiquitin ligases in genome stability

Prudden, J., Kaeser-Pebernard, S., Raffa, G. D., Slavin, D. A., Perry, J. J. P., Tainer, J. A., McGowan, C. H., & Boddy, M. N. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601838 · Cited by 334 · see citing works

BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies temporal control of DNA repair

Chapman, J. R., Sossick, A. J., Boulton, S. J., & Jackson, S. P. (2012) · Journal of Cell Science · doi:10.1242/jcs.105353 · Cited by 327 · see citing works

DNA damage signaling in response to double-strand breaks during mitosis

Giunta, S., Belotserkovskaya, R., & Jackson, S. P. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911156 · Cited by 321 · see citing works

RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair

Galanty, Y., Belotserkovskaya, R., Coates, J., & Jackson, S. P. (2012) · Genes & Development · doi:10.1101/gad.188284.112 · Cited by 314 · see citing works

Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks.

Motegi, A., Liaw, H.-J., Lee, K.-Y., Roest, H. P., Maas, A., Wu, X., Moinova, H., Markowitz, S. D., Ding, H., Hoeijmakers, J. H. J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805685105 · Cited by 304 · see citing works

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 279 · see citing works

HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes

Bekker‐Jensen, S., Danielsen, J. M. R., Fugger, K., Gromova, I., Nerstedt, A., Lukas, C., Bártek, J., Lukas, J., & Mailand, N. (2009) · Nature Cell Biology · doi:10.1038/ncb2008 · Cited by 277 · see citing works

Regulation of BRCC, a Holoenzyme Complex Containing BRCA1 and BRCA2, by a Signalosome-like Subunit and Its Role in DNA Repair

Dong, Y., Hakimi, M., Chen, X., Kumaraswamy, E., Cooch, N. S., Godwin, A. K., & Shiekhattar, R. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00424-6 · Cited by 274 · see citing works

In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product

Fitch, M. E., Nakajima, S., Yasui, A., & Ford, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307254200 · Cited by 260 · see citing works

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 254 · see citing works

The mechanism of OTUB1-mediated inhibition of ubiquitination

Wiener, R., Zhang, X., Wang, T., & Wolberger, C. (2012) · Nature · doi:10.1038/nature10911 · Cited by 248 · see citing works

BRCA1 tumor suppression depends on BRCT phosphoprotein binding, but not its E3 ligase activity

Shakya, R., Reid, L. J., Reczek, C. R., Cole, F., Egli, D., Lin, C.-S., deRooij, D. G., Hirsch, S., Ravi, K., Hicks, J. B., et al. (2011) · Science · doi:10.1126/science.1209909 · Cited by 244 · see citing works

Regulation of DNA End Joining, Resection, and Immunoglobulin Class Switch Recombination by 53BP1

Bothmer, A., Robbiani, D. F., Di Virgilio, M., Bunting, S. F., Klein, I. A., Feldhahn, N., Barlow, J., Chen, H.-T., Bosque, D., Callen, E., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.019 · Cited by 244 · see citing works

SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage

Yin, Y., Seifert, A., Chua, J. S., Maure, J.-F., Golebiowski, F., & Hay, R. T. (2012) · Genes & Development · doi:10.1101/gad.189274.112 · Cited by 237 · see citing works

Crystal structure of thymine DNA glycosylase conjugated to SUMO-1

Baba, D., Maita, N., Jee, J.-G., Uchimura, Y., Saitoh, H., Sugasawa, K., Hanaoka, F., Tochio, H., Hiroaki, H., & Shirakawa, M. (2005) · Nature · doi:10.1038/nature03634 · Cited by 232 · see citing works

RAP80-directed tuning of BRCA1 homologous recombination function at ionizing radiation-induced nuclear fociPreprint

Hu, Y., Scully, R., Sobhian, B., Xie, A., Shestakova, E. A., & Livingston, D. M. (2011) · Genes & Development · doi:10.1101/gad.2011011 · Cited by 232 · see citing works

Inhibition of Homologous Recombination by the PCNA-Interacting Protein PARI

Moldovan, G., Dejsuphong, D., Petalcorin, M. I. R., Hofmann, K., Takeda, S., Boulton, S. J., & D’Andrea, A. D. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.11.010 · Cited by 232 · see citing works

K63‐specific deubiquitination by two JAMM/MPN+ complexes: BRISC‐associated Brcc36 and proteasomal Poh1

Cooper, E. M., Cutcliffe, C., Kristiansen, T. Z., Pandey, A., Pickart, C. M., & Cohen, R. E. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.27 · Cited by 223 · see citing works

The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks

Shao, G., Lilli, D. R., Patterson-Fortin, J., Coleman, K. A., Morrissey, D. E., & Greenberg, R. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807485106 · Cited by 218 · see citing works

Damage-Induced Ubiquitylation of Human RNA Polymerase II by the Ubiquitin Ligase Nedd4, but Not Cockayne Syndrome Proteins or BRCA1

Anindya, R., Aygün, O., & Svejstrup, J. Q. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.10.008 · Cited by 215 · see citing works

Regulation of DNA Repair through DeSUMOylation and SUMOylation of Replication Protein A Complex

Dou, H., Huang, C., Singh, M. M., Carpenter, P. B., & Yeh, E. T. H. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.021 · Cited by 212 · see citing works

OTUB1 Co-opts Lys48-Linked Ubiquitin Recognition to Suppress E2 Enzyme Function

Juang, Y.-C. A., Landry, M.-C., Sanches, M., Vittal, V., Leung, C. C. Y., Ceccarelli, D. F. J., Mateo, A.-R. F., Pruneda, J. N., Mao, D. Y. L., Szilard, R. K., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.011 · Cited by 198 · see citing works

Extensive DNA Damage-Induced Sumoylation Contributes to Replication and Repair and Acts in Addition to the Mec1 Checkpoint

Cremona, C. A., Sarangi, P., Yang, Y., Hang, L. E., Rahman, S., & Zhao, X. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.11.028 · Cited by 197 · see citing works

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 · see citing works

Ubiquitylation and degradation of elongating RNA polymerase II: The last resort

Wilson, M. D., Harreman, M. T., & Svejstrup, J. Q. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.08.002 · Cited by 187 · see citing works

p53 regulation by ubiquitin

Brooks, C. L., & Gu, W. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.022 · Cited by 186 · see citing works

SHPRH and HLTF Act in a Damage-Specific Manner to Coordinate Different Forms of Postreplication Repair and Prevent Mutagenesis

Lin, J., Zeman, M. K., Chen, J.-Y., Yee, M., & Cimprich, K. A. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.026 · Cited by 179 · see citing works

A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses

Lilley, C. E., Chaurushiya, M. S., Boutell, C., Landry, S., Suh, J., Panier, S., Everett, R. D., Stewart, G. S., Durocher, D., & Weitzman, M. D. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.400 · Cited by 177 · see citing works

Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation

Harreman, M. T., Taschner, M. J., Sigurðsson, S., Anindya, R., Reid, J., Somesh, B. P., Kong, S. E., Banks, C. A. S., Conaway, R. C., Conaway, J. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907052106 · Cited by 173 · see citing works

A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase

Gatti, M., Pinato, S., Maspero, E., Soffientini, P., Polo, S., & Penengo, L. (2012) · Cell Cycle · doi:10.4161/cc.20919 · Cited by 168 · see citing works

Sumoylation of MDC1 is important for proper DNA damage response

Luo, K., Zhang, H., Wang, L., Yuan, J., & Lou, Z. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.158 · Cited by 166 · see citing works

The proteasomal de‐ubiquitinating enzyme POH1 promotes the double‐strand DNA break response

Butler, L. R., Densham, R. M., Jia, J., Garvin, A. J., Stone, H. R., Shah, V., Weekes, D. B., Festy, F., Beesley, J. F. J., & Morris, J. R. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.232 · Cited by 162 · see citing works

Functionality of Human Thymine DNA Glycosylase Requires SUMO-Regulated Changes in Protein Conformation

Steinacher, R., & Schär, P. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.054 · Cited by 161 · see citing works

Bortezomib-induced “BRCAness” sensitizes multiple myeloma cells to PARP inhibitors

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SUMO playing tag with ubiquitin

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SUMOylation of the α-Kleisin Subunit of Cohesin Is Required for DNA Damage-Induced Cohesion

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Finally, Polyubiquitinated PCNA Gets Recognized

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DNA damage and tissue repair: What we can learn from planaria

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SUMO playing tag with ubiquitin

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A SIM-ultaneous role for SUMO and ubiquitin

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CHFR is negatively regulated by SUMOylation-mediated ubiquitylation

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SUMOylation and ubiquitination reciprocally regulate α-synuclein degradation and pathological aggregation

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