RETRACTED ARTICLE: A mechanism for the suppression of homologous recombination in G1 cells

Genome engineering using the CRISPR-Cas9 system

Ran, F. A., Hsu, P. D., Wright, J., Agarwala, V., Scott, D. A., & Zhang, F. (2013) · Nature Protocols · doi:10.1038/nprot.2013.143 · Cited by 11,133

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

BRCA1 and BRCA2: different roles in a common pathway of genome protection

Roy, R., Chun, J., & Powell, S. N. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3181 · Cited by 1,555

Defining the Human Deubiquitinating Enzyme Interaction Landscape

Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,523

Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution

Taguchi, K., Motohashi, H., & Yamamoto, M. (2011) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01473.x · Cited by 1,478

Pathways of DNA Double-Strand Break Repair during the Mammalian Cell Cycle

Rothkamm, K., Krüger, I., Thompson, L. H., & Lübrich, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5706-5715.2003 · Cited by 1,187

Repair of Strand Breaks by Homologous RecombinationPreprint

Jasin, M., & Rothstein, R. J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012740 · Cited by 929

A Cell Cycle-Dependent Regulatory Circuit Composed of 53BP1-RIF1 and BRCA1-CtIP Controls DNA Repair Pathway Choice

Escribano‐Diaz, C., Orthwein, A., Fradet‐Turcotte, A., Xing, M., Young, J. T. F., Tkáč, J., Cook, M. A., Rosebrock, A. P., Munro, M., Canny, M. D., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.001 · Cited by 903

Control of BRCA2 Cellular and Clinical Functions by a Nuclear Partner, PALB2

Xia, B., Sheng, Q., Nakanishi, K., Ohashi, A., Wu, J., Christ, N., Liu, X., Jasin, M., Couch, F. J., & Livingston, D. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.022 · Cited by 861

Factors forming the BRCA1-A complex orchestrate BRCA1 recruitment to the sites of DNA damage

Her, J., Lee, N. S., Kim, Y., & Kim, H. (2016) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmw047 · Cited by 43

A lysosome independent role for TFEB in activating DNA repair and inhibiting apoptosis in breast cancer cells

Slade, L., Biswas, D., Ihionu, F., Hiani, Y. E., Kienesberger, P. C., & Pulinilkunnil, T. (2019) · Biochemical Journal · doi:10.1042/bcj20190596 · Cited by 40

PRMT1-dependent methylation of BRCA1 contributes to the epigenetic defense of breast cancer cells against ionizing radiation

Montenegro, M. F., González-Guerrero, R., Sánchez‐del‐Campo, L., Piñero, A., Cabezas‐Herrera, J., & Rodríguez‐López, J. N. (2020) · Scientific Reports · doi:10.1038/s41598-020-70289-3 · Cited by 40

Cancer-causing mutations in the tumor suppressor PALB2 reveal a novel cancer mechanism using a hidden nuclear export signal in the WD40 repeat motif

Pauty, J., Couturier, A. M., Rodrigue, A., Caron, M., Coulombe, Y., Dellaire, G., & Masson, J. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx011 · Cited by 39

BAP1 is a haploinsufficient tumor suppressor linking chronic pancreatitis to pancreatic cancer in mice

Perkail, S., Andricovich, J., Yan, K., & Tzatsos, A. (2020) · Nature Communications · doi:10.1038/s41467-020-16589-8 · Cited by 41

A Functional Genomic Screen Identifies the Deubiquitinase USP11 as a Novel Transcriptional Regulator of ERα in Breast Cancer

Dwane, L., O’Connor, A. E., Das, S., Moran, B., Mulrane, L., Pinto-Fernández, A., Ward, E., Blümel, A. M., Cavanagh, B., Mooney, B., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-0214 · Cited by 39

Adenine base editing reduces misfolded protein accumulation and toxicity in alpha-1 antitrypsin deficient patient iPSC-hepatocytes

Werder, R. B., Kaserman, J. E., Packer, M. S., Lindstrom-Vautrin, J., Villacorta-Martín, C., Young, L. E., Aratyn-Schaus, Y., Gregoire, F. M., & Wilson, A. A. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.06.021 · Cited by 38

Discovery of peptide ligands targeting a specific ubiquitin-like domain–binding site in the deubiquitinase USP11

Spiliotopoulos, A., Ferreras, L. A. B., Densham, R. M., Caulton, S. G., Maddison, B. C., Morris, J. R., Dixon, J. E., Gough, K. C., & Dreveny, I. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004469 · Cited by 39

Nonviral base editing of KCNJ13 mutation preserves vision in a model of inherited retinal channelopathy

Kabra, M., Shahi, P. K., Wang, Y., Sinha, D., Spillane, A., Newby, G. A., Saxena, S., Tong, Y., Chang, Y., Abdeen, A. A., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci171356 · Cited by 36

Nick-initiated homologous recombination: Protecting the genome, one strand at a time

Vriend, L. E. M., & Krawczyk, P. M. (2016) · DNA repair · doi:10.1016/j.dnarep.2016.12.005 · Cited by 37

Directed evolution of hyperactive integrases for site specific insertion of transgenes

Hew, B. E., Gupta, S., Sato, R., Waller, D. F., Stoytchev, I., Short, J. E., Sharek, L., Tran, C. T., Badran, A. H., & Owens, J. B. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae534 · Cited by 35

Roles of Ubiquitination and SUMOylation in DNA Damage Response

Su, S., Zhang, Y., & Liu, P. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.059 · Cited by 37

Functional interrogation of non-coding DNA through CRISPR genome editing

Canver, M. C., Bauer, D. E., & Orkin, S. H. (2017) · Methods · doi:10.1016/j.ymeth.2017.03.008 · Cited by 36

Cullin 3, a cellular scripter of the non-proteolytic ubiquitin code

Jerabkova, K., & Sumara, I. (2019) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2018.12.007 · Cited by 33

Evaluation of Pharmacodynamic Responses to Cancer Therapeutic Agents Using DNA Damage Markers

Wilsker, D. F., Barrett, A. M., Dull, A. B., Lawrence, S. M., Hollingshead, M. G., Chen, A. P., Kummar, S., Parchment, R. E., Doroshow, J. H., & Kinders, R. J. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-2523 · Cited by 33

Pold3is required for genomic stability and telomere integrity in embryonic stem cells and meiosis

Zhou, Z., Wang, L., Ge, F., Gong, P., Wang, H., Wang, F., Chen, L., & Liu, L. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky098 · Cited by 34

Transcription and mRNA export machineries SAGA and TREX-2 maintain monoubiquitinated H2B balance required for DNA repair

Evangelista, F. M., Maglott, A., Stierlé, M., Brino, L., Soutoglou, E., & Tora, L. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201803074 · Cited by 35

Ubiquitin and ubiquitin-like molecules in DNA double strand break repair

Yu, J., Qin, B., & Lou, Z. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-0380-1 · Cited by 35

A genome editing primer for the hematologist

Hoban, M. D., & Bauer, D. E. (2016) · Blood · doi:10.1182/blood-2016-01-678151 · Cited by 32

Keap1–MCM3 interaction is a potential coordinator of molecular machineries of antioxidant response and genomic DNA replication in metazoa

Tamberg, N., Tahk, S., Koit, S., Kristjuhan, K., Kasvandik, S., Kristjuhan, A., & Ilves, I. (2018) · Scientific Reports · doi:10.1038/s41598-018-30562-y · Cited by 32

CSB interacts with BRCA1 in late S/G2 to promote MRN- and CtIP-mediated DNA end resection

Batenburg, N. L., Walker, J. R., Coulombe, Y., Sherker, A., Masson, J., & Zhu, X. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz784 · Cited by 33

Heterochromatic repeat clustering imposes a physical barrier on homologous recombination to prevent chromosomal translocations

Mitrentsi, I., Lou, J., Kerjouan, A., Verigos, J., Reina‐San‐Martin, B., Hinde, E., & Soutoglou, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.033 · Cited by 33

SUMO in the DNA Double-Stranded Break Response: Similarities, Differences, and Cooperation with Ubiquitin

Morris, J. R., & Garvin, A. J. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.012 · Cited by 32

The Fanconi anemia core complex promotes CtIP-dependent end resection to drive homologous recombination at DNA double-strand breaks

van de Kooij, B., van der Wal, F. J., Rother, M. B., Wiegant, W. W., Creixell, P., Stout, M., Joughin, B. A., Vornberger, J., Altmeyer, M., van Vugt, M. A. T. M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51090-6 · Cited by 31

Disruptive Technology: CRISPR/Cas-Based Tools and Approaches

Patsali, P., Kleanthous, M., & Lederer, C. W. (2019) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-019-00391-4 · Cited by 31

To Join or Not to Join: Decision Points Along the Pathway to Double-Strand Break Repair vs. Chromosome End Protection

Ackerson, S. M., Romney, C. V., Schuck, P. L., & Stewart, J. A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.708763 · Cited by 39

POGZ promotes homology‐directed DNA repair in an HP1‐dependent manner

Heath, J., Simo‐Cheyou, E. R., Findlay, S., Luo, V. M., Carpio, E. P., Lee, J., Djerir, B., Chen, X., Morin, T., Lebeau, B., et al. (2021) · EMBO Reports · doi:10.15252/embr.202051041 · Cited by 33

USP11 mediates repair of DNA–protein cross-links by deubiquitinating SPRTN metalloprotease

Perry, M. C., Biegert, M., Kollala, S. S., Mallard, H. J., Su, G., Kodavati, M. M., Kreiling, N. F., Holbrook, A., & Ghosal, G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100396 · Cited by 30

Modulating CRISPR/Cas9 genome-editing activity by small molecules

Chen, S., Chen, D., Liu, B., & Haisma, H. J. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.11.018 · Cited by 32

Impaired 53BP1/RIF1 DSB mediated end-protection stimulates CtIP-dependent end resection and switches the repair to PARP1-dependent end joining in G1

Bakr, A., Köcher, S., Volquardsen, J., Petersen, C., Borgmann, K., Dikomey, E., Rothkamm, K., & Mansour, W. Y. (2016) · Oncotarget · doi:10.18632/oncotarget.11023 · Cited by 35

Defects in homologous recombination repair behind the human diseases: FA and HBOC

Katsuki, Y., & Takata, M. (2016) · Endocrine Related Cancer · doi:10.1530/erc-16-0221 · Cited by 32

Reduced RBX1 expression induces chromosome instability and promotes cellular transformation in high-grade serous ovarian cancer precursor cells

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Triple-Negative Breast Cancer and Emerging Therapeutic Strategies: ATR and CHK1/2 as Promising Targets

Sofianidi, A. A., Dumbrava, E. E. I., Syrigos, K. N., & Nasrazadani, A. (2024) · Cancers · doi:10.3390/cancers16061139 · Cited by 31

CRISPR Craze to Transform Cardiac Biology

van Kampen, S. J., & van Rooij, E. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.06.008 · Cited by 30

USP22 Interacts with PALB2 and Promotes Chemotherapy Resistance via Homologous Recombination of DNA Double-Strand Breaks

Nardi, I. K., Stark, J. M., Larsen, A. B., Salgia, R., & Raz, D. J. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0053 · Cited by 28

Loss of Nrf2 abrogates the protective effect of Keap1 downregulation in a preclinical model of cutaneous squamous cell carcinoma

Knatko, E. V., Higgins, M., Fahey, J. W., & Dinkova‐Kostova, A. T. (2016) · Scientific Reports · doi:10.1038/srep25804 · Cited by 28

Inhibition of RIF1 by SCAI Allows BRCA1-Mediated Repair

Isobe, S.-Y., Nagao, K., Nozaki, N., Kimurâ, H., & Obuse, C. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.056 · Cited by 31

RPA shields inherited DNA lesions for post-mitotic DNA synthesis

Lezaja, A., Παναγόπουλος, Α., Wen, Y., Carvalho, E., Imhof, R., & Altmeyer, M. (2021) · Nature Communications · doi:10.1038/s41467-021-23806-5 · Cited by 32

NUCKS1 is a highly modified, chromatin-associated protein involved in a diverse set of biological and pathophysiological processes

Østvold, A. C., Grundt, K., & Wiese, C. (2022) · Biochemical Journal · doi:10.1042/bcj20220075 · Cited by 28

The Role of DNA Damage and Repair in Idiopathic Pulmonary Fibrosis

Zhu, J., Liu, L., Ma, X., Cao, X., Chen, Y., Qu, X., Ji, M. H., Liu, H., Liu, C., Qin, X., et al. (2022) · Antioxidants · doi:10.3390/antiox11112292 · Cited by 29

Ubiquitin signaling and the proteasome drive human DNA–protein crosslink repair

Essawy, M. M., Chesner, L. N., Alshareef, D., Ji, S., Tretyakova, N. Y., & Campbell, C. J. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad860 · Cited by 27

Regulation of XPC deubiquitination by USP11 in repair of UV-induced DNA damage

Shah, P., Qiang, L., Yang, S., Soltani, K., & He, Y. (2017) · Oncotarget · doi:10.18632/oncotarget.22105 · Cited by 27

Beyond classic editing: innovative CRISPR approaches for functional studies of long non-coding RNA

Awwad, D. A. (2019) · Biology Methods and Protocols · doi:10.1093/biomethods/bpz017 · Cited by 28

Dna2 initiates resection at clean DNA double-strand breaks

Paudyal, S. C., Li, S., Yan, H., Hunter, T. R., & You, Z. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx830 · Cited by 30

HMEJ-mediated efficient site-specific gene integration in chicken cells

Xie, L., Sun, J., Mo, L., Xu, T., Shahzad, Q., Chen, D., Yang, W., Liao, Y., & Lu, Y. (2019) · Journal of Biological Engineering · doi:10.1186/s13036-019-0217-9 · Cited by 26

Therapeutic genome engineering via CRISPR ‐Cas systems

Moreno, A. M., & Mali, P. (2017) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1380 · Cited by 25

RNA-Guided Recombinase-Cas9 Fusion Targets Genomic DNA Deletion and Integration

Standage-Beier, K., Brookhouser, N., Balachandran, P., Zhang, Q., Brafman, D. A., & Wang, X. (2019) · The CRISPR Journal · doi:10.1089/crispr.2019.0013 · Cited by 26

USP15 Deubiquitinase Safeguards Hematopoiesis and Genome Integrity in Hematopoietic Stem Cells and Leukemia Cells

van den Berk, P. C. M., Lancini, C., Serresi, M., Sánchez-Bailón, M. P., Hulsman, D., Pritchard, C., Song, J., Schmitt, M. J., Tanger, E., Popp, O., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108533 · Cited by 25

Function and Evolution of the Loop Extrusion Machinery in Animals

Kabirova, E., Nurislamov, A. R., Shadskiy, A., Smirnov, A. V., Popov, A., Salnikov, P., Баттулин, Н. Р., & Fishman, V. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24055017 · Cited by 27

Gene editing innovations and their applications in cardiomyopathy research

Kyriakopoulou, E., Monnikhof, T., & van Rooij, E. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.050088 · Cited by 26

Oncogene-Stimulated Congestion at the KEAP1 Stress Signaling Hub Allows Bypass of NRF2 and Induction of NRF2-Target Genes that Promote Tumor Survival

Hayes, J. D., & Dinkova‐Kostova, A. T. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.10.009 · Cited by 25

Generation of the Adenovirus Vector-Mediated CRISPR/Cpf1 System and the Application for Primary Human Hepatocytes Prepared from Humanized Mice with Chimeric Liver

Tsukamoto, T., Sakai, E., Iizuka, S., Taracena-Gándara, M., Sakurai, F., & Mizuguchi, H. (2018) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b18-00222 · Cited by 25

Antiparallel Coiled-Coil Interactions Mediate the Homodimerization of the DNA Damage-Repair Protein PALB2

Song, F., Li, M., Liu, G., Swapna, G. V. T., Daigham, N. S., Xia, B., Montelione, G. T., & Bunting, S. F. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00789 · Cited by 25

Evolution of Resistance in Cancer: A Cell Cycle Perspective

Dökümcü, K., & Farahani, R. H. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00376 · Cited by 26

Role of deubiquitinating enzymes in DNA double-strand break repair

Li, Y., & Yuan, J. (2021) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2000309 · Cited by 25

Tracing back primed resistance in cancer via sister cells

Dai, J., Zheng, S., Falco, M. M., Bao, J., Eriksson, J., Pikkusaari, S., Forstén, S., Jiang, J., Wang, W., Gao, L., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45478-7 · Cited by 24

Adeno-associated virus-mediated delivery of CRISPR-Cas9 for genome editing in the central nervous system

Fuentes, C., & Schaffer, D. V. (2018) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2018.08.003 · Cited by 27

Controlling DNA-End Resection: An Emerging Task for Ubiquitin and SUMO

Himmels, S.-F., & Sartori, A. A. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00152 · Cited by 24

Suppressor mutations in Mecp2 -null mice implicate the DNA damage response in Rett syndrome pathologyPreprint

Enikanolaiye, A., Ruston, J., Zeng, R., Taylor, C., Schrock, M., Buchovecky, C. M., Shendure, J., Acar, E. F., & Justice, M. J. (2020) · Genome Research · doi:10.1101/gr.258400.119 · Cited by 25

Ubiquitylation in DNA double-strand break repair

Tang, M., Li, S., & Chen, J. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103129 · Cited by 24

Making Connections: Integrative Signaling Mechanisms Coordinate DNA Break Repair in Chromatin

Sanchez, A. R., Lee, D., Kim, D. I., & Miller, K. M. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.747734 · Cited by 25

Future Directions for Adrenal Insufficiency: Cellular Transplantation and Genetic Therapies

Graves, L. E., Torpy, D. J., Coates, P. T., Alexander, I. E., Bornstein, S. R., & Clarke, B. M. (2023) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgac751 · Cited by 23

Role of PRMT1 and PRMT5 in Breast Cancer

Martinez, S., Sentis, S., Poulard, C., Trédan, O., & Romancer, M. L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168854 · Cited by 25

Novel RNA and DNA strand exchange activity of the PALB2 DNA binding domain and its critical role for DNA repair in cells

Deveryshetty, J., Ryzhikov, M., Brahati, N., Peterlini, T., Dellaire, G., Masson, J., & Korolev, S. (2019) · eLife · doi:10.7554/elife.44063 · Cited by 22

Beyond reversal: ubiquitin and ubiquitin-like proteases and the orchestration of the DNA double strand break repair response

Garvin, A. J. (2019) · Biochemical Society Transactions · doi:10.1042/bst20190534 · Cited by 25

RNF8 has both KU-dependent and independent roles in chromosomal break repair

Tsai, L. J., Lopezcolorado, F. W., Bhargava, R., Mendez‐Dorantes, C., Jahanshir, E., & Stark, J. M. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa380 · Cited by 23

CENPO expression regulates gastric cancer cell proliferation and is associated with poor patient prognosis

Cao, Y., Xiong, J., Li, Z., Zhang, G., Tu, Y., Wang, L., & Jie, Z. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10624 · Cited by 21

PML isoform expression and DNA break location relative to PML nuclear bodies impacts the efficiency of homologous recombination

Attwood, K. M., Salsman, J., Chung, D., Mathavarajah, S., Iderstine, C. V., & Dellaire, G. (2019) · Biochemistry and Cell Biology · doi:10.1139/bcb-2019-0115 · Cited by 20

Ubiquitin-Regulated Cell Proliferation and Cancer

Pérez‐Benavente, B., Fathinajafabadi, A., & Farrás, R. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_1 · Cited by 21

KEAP1-NRF2 Interaction in Cancer: Competitive Interactors and Their Role in Carcinogenesis

Oskomić, M., Tomić, A., Barbarić, L., Matić, A., Kindl, D. C., & Matovina, M. (2025) · Cancers · doi:10.3390/cancers17030447 · Cited by 22

Gene editing and CRISPR-dependent homology-mediated end joining

Ruis, B. L., Bielinsky, A., & Hendrickson, E. A. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01442-z · Cited by 20

Regulatory mechanism of cyclins and cyclin-dependent kinases in post-mitotic neuronal cell division

Gupta, R. V., Jha, A., Ambasta, R. K., & Kumar, P. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.120006 · Cited by 19

BRCA2 BRC missense variants disrupt RAD51-dependent DNA repair

Jiménez-Sáinz, J., Mathew, J., Moore, G., Lahiri, S., Garbarino, J. M., Eder, J. P., Rothenberg, E., & Jensen, R. B. (2022) · eLife · doi:10.7554/elife.79183 · Cited by 19

A homology independent sequence replacement strategy in human cells using a CRISPR nuclease

Danner, E. W., Lebedin, M. Y., de la Rosa, K., & Kühn, R. (2021) · Open Biology · doi:10.1098/rsob.200283 · Cited by 22

Protein UFMylation regulates early events during ribosomal DNA-damage response

Panichnantakul, P., Aguilar, L. C., Daynard, E., Guest, M., Peters, C., Vogel, J., & Oeffinger, M. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114738 · Cited by 18

Ubiquitylation-Mediated Fine-Tuning of DNA Double-Strand Break Repair

Borsos, B. N., Majoros, H., & Pankotai, T. (2020) · Cancers · doi:10.3390/cancers12061617 · Cited by 18

Elevated APE1 Dysregulates Homologous Recombination and Cell Cycle Driving Genomic Evolution, Tumorigenesis, and Chemoresistance in Esophageal Adenocarcinoma

Kumar, S., Zhao, J., Talluri, S., Buon, L., Mu, S., Potluri, L. B., Liao, C., Shi, J., Chakraborty, C., Gonzalez, G. B., et al. (2023) · Gastroenterology · doi:10.1053/j.gastro.2023.04.035 · Cited by 18

BLM and BRCA1-BARD1 coordinate complementary mechanisms of joint DNA molecule resolution

Tsukada, K., Jones, S. E., Bannister, J. V., Durin, M.-A., Vendrell, I., Fawkes, M., Fischer, R., Kessler, B. M., Chapman, J. R., & Blackford, A. N. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.040 · Cited by 18

Platinum-based chemotherapy: trends in organic nanodelivery systems

Santos, J. A. V., Silva, D., Marques, M. P. M., & de Carvalho, L. A. E. B. (2024) · Nanoscale · doi:10.1039/d4nr01483a · Cited by 20

Regulation of DNA break repair by transcription and RNA

Ouyang, J., Lan, L., & Zou, L. (2017) · Science China Life Sciences · doi:10.1007/s11427-017-9164-1 · Cited by 18

Cathepsin B contributes to radioresistance by enhancing homologous recombination in glioblastoma

Zhang, X., Wang, X., Xu, S., Li, X., & Ma, X. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.08.007 · Cited by 18

The roles of homologous recombination and the immune system in the genomic evolution of cancer

Nandi, B., Talluri, S., Kumar, S., Yenumula, C., Gold, J. S., PRABHALA, R. H., Munshi, N. C., & Shammas, M. A. (2018) · Journal of Translational Science · doi:10.15761/jts.1000282 · Cited by 18

The internal region of CtIP negatively regulates DNA end resection

Howard, S. M., Ceppi, I., Anand, R., Geiger, R., & Ćejka, P. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa273 · Cited by 19

Chromatin Ubiquitination Guides DNA Double Strand Break Signaling and Repair

Kolobynina, K. G., Rapp, A. W., & Cardoso, M. C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.928113 · Cited by 17

Rice OsBRCA2 Is Required for DNA Double-Strand Break Repair in Meiotic Cells

Fu, R., Wang, C., Shen, H., Zhang, J., Higgins, J. D., & Liang, W. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.600820 · Cited by 17

Gene Therapy: The View from NCATS

Brooks, P. J., Yang, N. N., & Austin, C. P. (2016) · Human Gene Therapy · doi:10.1089/hum.2016.29018.pjb · Cited by 16

Scorpins in the DNA Damage Response

Palmieri, D., Tessari, A., & Coppola, V. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061794 · Cited by 16

DNA-dependent protein kinase: Epigenetic alterations and the role in genomic stability of cancer

Vazhappilly, C. G., Ansari, S. A., Chelakkot, V. S., Chelakkot, A. L., Chelakkot, C., Menon, V., Ramadan, W. S. H., Radhakrishnan, E. K., El‐Awady, R., Mantso, T., et al. (2018) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2018.06.001 · Cited by 16

CRISPR/dCas9‐mediated transposition with specificity and efficiency of site‐directed genomic insertions

Goshayeshi, L., Taemeh, S. Y., Dehdilani, N., Nasiri, M., Seno, M. M. G., & Dehghani, H. (2021) · The FASEB Journal · doi:10.1096/fj.202001830rr · Cited by 16

Targeted mutagenesis in plants using Beet curly top virus for efficient delivery of CRISPR/Cas12a components

Eini, O., Schumann, N., Niessen, M., & Varrelmann, M. (2021) · New Biotechnology · doi:10.1016/j.nbt.2021.12.002 · Cited by 16

Oncogenic deubiquitination controls tyrosine kinase signaling and therapy response in acute lymphoblastic leukemia

Jin, Q., Gutierrez-Diaz, B. T., Pieters, T., Zhou, Y., Narang, S., Fijałkowski, I., Borin, C., Laere, J. V., Payton, M. A., Cho, B.-K., et al. (2022) · Science Advances · doi:10.1126/sciadv.abq8437 · Cited by 16

miR4673 improves fitness profile of neoplastic cells by induction of autophagy

Dökümcü, K., Simonian, M. R., & Farahani, R. H. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1088-6 · Cited by 16

Functional Characterization of PALB2 Variants of Uncertain Significance: Toward Cancer Risk and Therapy Response Prediction

Boonen, R. A. C. M., Vreeswijk, M. P. G., & van Attikum, H. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00169 · Cited by 18

CrisPR/CRIS systems are highly effective and useful for genomic manipulation. Despite this, cardiac treatment remains difficult due to existing genome editing and delivery processes.Preprint

Dowaidar, M. (2021) · OSF Preprints (OSF Preprints) · doi:10.31219/osf.io/3nwzd · Cited by 22

Emerging new tools to study and treat muscle pathologies: genetics and molecular mechanisms underlying skeletal muscle development, regeneration, and disease

Crist, C. G. (2016) · The Journal of Pathology · doi:10.1002/path.4830 · Cited by 15

Delivery challenges for CRISPR—Cas9 genome editing for Duchenne muscular dystrophy

Padmaswari, M. H., Agrawal, S., Jia, M. S., Ivy, A., Maxenberger, D. A., Burcham, L. A., & Nelson, C. E. (2023) · Biophysics Reviews · doi:10.1063/5.0131452 · Cited by 18

Keeping homologous recombination in check

Fugger, K., & West, S. C. (2016) · Cell Research · doi:10.1038/cr.2016.25 · Cited by 15

Protein kinase C activator bryostatin‐1 modulates proteasome function

Khan, T. K., & Nelson, T. J. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26887 · Cited by 15

Duplex Labeling and Manipulation of Neuronal Proteins Using Sequential CRISPR/Cas9 Gene Editing

Droogers, W. J., Willems, J., MacGillavry, H. D., & de Jong, A. P. H. (2022) · eNeuro · doi:10.1523/eneuro.0056-22.2022 · Cited by 17

Mitotic cells can repair DNA double-strand breaks via a homology-directed pathway

Sakamoto, Y., Kokuta, T., Teshigahara, A., Iijima, K., Kitao, H., Takata, M., & Tauchi, H. (2020) · Journal of Radiation Research · doi:10.1093/jrr/rraa095 · Cited by 15

Cell-Cycle Regulation of BRCA1 Inhibits Homologous Recombination in G1

(2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-rw2015-237

The cell cycle flavours of repair

Zlotorynski, E. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.24 · Cited by 4

Abstract 2113: Elucidating mechanisms of regulation of homologous recombination utilizing a PALB2 fusion protein that contains the BRCT repeats of BRCA1

Zhang, F., Bick, G., & Andreassen, P. R. (2012) · Cancer Research · doi:10.1158/1538-7445.am2012-2113

Abstract 2471: Role of PALB2-BRCA1 interaction in tumor suppression

Mahdi, A., Huo, Y., & Xia, B. (2017) · Cancer Research · doi:10.1158/1538-7445.am2017-2471

Understanding the role of the PALB2-BRCA1 interaction in tumor suppression

Mahdi, A. (2017) · doi:10.7282/t31g0q4q