RETRACTED ARTICLE: A mechanism for the suppression of homologous recombination in G1 cells

Genome engineering using the CRISPR-Cas9 system

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

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Defining the Human Deubiquitinating Enzyme Interaction Landscape

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

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

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Repair of Strand Breaks by Homologous RecombinationPreprint

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

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53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark

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RIF1 Is Essential for 53BP1-Dependent Nonhomologous End Joining and Suppression of DNA Double-Strand Break Resection

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Protein neddylation: beyond cullin–RING ligases

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PALB2 is an integral component of the BRCA complex required for homologous recombination repair

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53BP1 Regulates DSB Repair Using Rif1 to Control 5′ End Resection

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The Breast Cancer Susceptibility Gene BRCA1 Is Required for Subnuclear Assembly of Rad51 and Survival following Treatment with the DNA Cross-linking Agent Cisplatin

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PALB2 Links BRCA1 and BRCA2 in the DNA-Damage Response

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Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination

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Human CtIP Mediates Cell Cycle Control of DNA End Resection and Double Strand Break Repair

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The emerging family of CULLIN3-RING ubiquitin ligases (CRL3s): cellular functions and disease implications

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Nuclear domain ‘knock-in’ screen for the evaluation and identification of small molecule enhancers of CRISPR-based genome editing

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RIF1 Counteracts BRCA1-mediated End Resection during DNA Repair

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Glutamine Deamidation and Dysfunction of Ubiquitin/NEDD8 Induced by a Bacterial Effector Family

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

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PALB2 Interacts with KEAP1 To Promote NRF2 Nuclear Accumulation and Function

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Push back to respond better: regulatory inhibition of the DNA double-strand break response

Panier, S., & Durocher, D. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3659 · Cited by 168 · see citing works

BRCA2 Is Ubiquitinated In Vivo and Interacts with USP11, a Deubiquitinating Enzyme That Exhibits Prosurvival Function in the Cellular Response to DNA Damage

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Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks.

Panier, S., Ichijima, Y., Fradet-Turcotte, A., Leung, C. C. Y., Kaustov, L., Arrowsmith, C. H., & Durocher, D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.045 · Cited by 152 · see citing works

Sensitivity to Poly(ADP-ribose) Polymerase (PARP) Inhibition Identifies Ubiquitin-specific Peptidase 11 (USP11) as a Regulator of DNA Double-strand Break Repair

Wiltshire, T. D., Lovejoy, C. A., Wang, T., Xia, F., O’Connor, M. J., & Cortez, D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.104745 · Cited by 120 · see citing works

Links between genome integrity and BRCA1 tumor suppression

Covington, M. L., & Greenberg, R. A. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.06.007 · Cited by 116 · see citing works

RPA Accumulation during Class Switch Recombination Represents 5′–3′ DNA-End Resection during the S–G2/M Phase of the Cell Cycle

Yamane, A., Robbiani, D. F., Resch, W., Bothmer, A., Nakahashi, H., Oliveira, T. Y., Rommel, P. C., Brown, E. J., Nussenzweig, A., Nussenzweig, M. C., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2012.12.006 · Cited by 98 · see citing works

Nonhydrolyzable Diubiquitin Analogues Are Inhibitors of Ubiquitin Conjugation and Deconjugation

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PALB2: The hub of a network of tumor suppressors involved in DNA damage responses

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Male Fertility Defect Associated with Disrupted BRCA1-PALB2 Interaction in Mice

Simhadri, S. R., Peterson, S., Patel, D. S., Huo, Y., Cai, H., Bowman-Colin, C., Miller, S., Ludwig, T., Ganesan, S., Bhaumik, M., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.566141 · Cited by 78 · see citing works

Structural Insights into the COP9 Signalosome and Its Common Architecture with the 26S Proteasome Lid and eIF3

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Generation of nonhydrolyzable ubiquitin–histone mimics

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Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4)

Hendriks, I. A., Schimmel, J., Eifler, K., Olsen, J. V., & Vertegaal, A. C. O. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.618132 · Cited by 46 · see citing works

MDC1 and RNF8 function in a pathway that directs BRCA1-dependent localization of PALB2 required for homologous recombination

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Cell Cycle-Dependent Induction of Homologous Recombination by a Tightly Regulated I-SceI Fusion Protein

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ATM, ATR, and DNA-PK: The Trinity at the Heart of the DNA Damage Response

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DNA double-strand break repair-pathway choice in somatic mammalian cells

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In vivo genome editing via CRISPR/Cas9 mediated homology-independent targeted integration

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Deubiquitylating enzymes and drug discovery: emerging opportunities

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Breaking the chains: deubiquitylating enzyme specificity begets function

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The control of DNA repair by the cell cycle

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Inactivation of DNA repair triggers neoantigen generation and impairs tumour growth

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Nrf2 Activation Promotes Lung Cancer Metastasis by Inhibiting the Degradation of Bach1

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Metabolic regulation of homologous recombination repair by MRE11 lactylation

Chen, Y., Wu, J., Zhai, L., Zhang, T., Yin, H. M., Gao, H., Zhao, F., Wang, Z., Yang, X., Jin, M., et al. (2023) · Cell · doi:10.1016/j.cell.2023.11.022 · Cited by 513 · see citing works

Ubiquitin ligases in oncogenic transformation and cancer therapy

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PARP Inhibitor Resistance: A Tug-of-War in BRCA-Mutated Cells

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Non-viral delivery systems for CRISPR/Cas9-based genome editing: challenges and opportunities

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Advances in genome editing through control of DNA repair pathways

Yeh, C. D., Richardson, C. D., & Corn, J. E. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0425-z · Cited by 405 · see citing works

BRCA1–BARD1 promotes RAD51-mediated homologous DNA pairing

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ATR inhibition disrupts rewired homologous recombination and fork protection pathways in PARP inhibitor-resistant BRCA-deficient cancer cellsPreprint

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Naturally Occurring Off-Switches for CRISPR-Cas9

Pawluk, A., Amrani, N., Zhang, Y., Garcı́a, B., Hidalgo-Reyes, Y., Lee, J., Edraki, A., Shah, M. K., Sontheimer, E. J., Maxwell, K. L., et al. (2016) · Cell · doi:10.1016/j.cell.2016.11.017 · Cited by 384 · see citing works

Mechanism and regulation of DNA end resection in eukaryotes

Symington, L. S. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2016.1172552 · Cited by 368 · see citing works

Hereditary breast and ovarian cancer: new genes in confined pathways

Nielsen, F. C., van Overeem Hansen, T., & Sørensen, C. S. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.72 · Cited by 367 · see citing works

The antitumorigenic roles of BRCA1–BARD1 in DNA repair and replication

Tarsounas, M., & Sung, P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0218-z · Cited by 366 · see citing works

Regulation of DNA double-strand break repair by ubiquitin and ubiquitin-like modifiers

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Methodologies for Improving HDR Efficiency

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Principles of Ubiquitin-Dependent Signaling

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Main steps in DNA double-strand break repair: an introduction to homologous recombination and related processes

Ranjha, L., Howard, S. M., & Ćejka, P. (2018) · Chromosoma · doi:10.1007/s00412-017-0658-1 · Cited by 324 · see citing works

Phosphorylated CtIP Functions as a Co-factor of the MRE11-RAD50-NBS1 Endonuclease in DNA End Resection

Anand, R., Ranjha, L., Cannavò, E., & Ćejka, P. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.10.017 · Cited by 307 · see citing works

How cells ensure correct repair of DNA double-strand breaks

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BRD4 Inhibition Is Synthetic Lethal with PARP Inhibitors through the Induction of Homologous Recombination Deficiency

Sun, C., Yin, J., Fang, Y., Chen, J., Jeong, K. J., Chen, X., Vellano, C. P., Ju, Z., Zhao, W., Zhang, D., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.01.019 · Cited by 302 · see citing works

Nuclear Acetyl-CoA Production by ACLY Promotes Homologous Recombination

Sivanand, S., Rhoades, S., Jiang, Q., Lee, J. V., Benci, J., Zhang, J., Yuan, S., Viney, I., Zhao, S., Carrer, A., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.008 · Cited by 295 · see citing works

Inhibition of 53BP1 favors homology-dependent DNA repair and increases CRISPR–Cas9 genome-editing efficiency

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Genome-wide mapping of long-range contacts unveils clustering of DNA double-strand breaks at damaged active genes

Aymard, F., Aguirrebengoa, M., Guillou, E., Javierre, B. M., Bugler, B., Arnould, C., Rocher, V., Iacovoni, J. S., Biernacka, A., Skrzypczak, M., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3387 · Cited by 263 · see citing works

Beyond repression of Nrf2: An update on Keap1

Kopacz, A., Klóska, D., Forman, H. J., Józkowicz, A., & Grochot‐Przeczek, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.023 · Cited by 262 · see citing works

Structural basis of CRISPR–SpyCas9 inhibition by an anti-CRISPR protein

Dong, D., Guo, M., Wang, S., Zhu, Y., Wang, S., Xiong, Z., Yang, J., Xu, Z., & Huang, Z. (2017) · Nature · doi:10.1038/nature22377 · Cited by 255 · see citing works

DNA double-strand-break repair in higher eukaryotes and its role in genomic instability and cancer: Cell cycle and proliferation-dependent regulation

Mladenov, E., Magin, S., Soni, A., & Iliakis, G. E. (2016) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2016.03.003 · Cited by 252 · see citing works

Temporal and Spatial Uncoupling of DNA Double Strand Break Repair Pathways within Mammalian Heterochromatin

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CRISPR–Cas9 genome editing in human cells occurs via the Fanconi anemia pathway

Richardson, C. D., Kazane, K. R., Feng, S. J., Zelin, E., Bray, N. L., Schäfer, A. J., Floor, S. N., & Corn, J. E. (2018) · Nature Genetics · doi:10.1038/s41588-018-0174-0 · Cited by 249 · see citing works

Hematopoietic Stem Cell Gene Therapy: Progress and Lessons Learned

Morgan, R. A., Gray, D., Lomova, A., & Kohn, D. B. (2017) · Cell stem cell · doi:10.1016/j.stem.2017.10.010 · Cited by 243 · see citing works

The structural basis of modified nucleosome recognition by 53BP1

Wilson, M. D., Benlekbir, S., Fradet‐Turcotte, A., Sherker, A., Julien, J., McEwan, A., Noordermeer, S. M., Sicheri, F., Rubinstein, J. L., & Durocher, D. (2016) · Nature · doi:10.1038/nature18951 · Cited by 234 · see citing works

53BP1: a DSB escortPreprint

Mirman, Z., & de Lange, T. (2020) · Genes & Development · doi:10.1101/gad.333237.119 · Cited by 231 · see citing works

The democratization of gene editing: Insights from site-specific cleavage and double-strand break repair

Jasin, M., & Haber, J. E. (2016) · DNA repair · doi:10.1016/j.dnarep.2016.05.001 · Cited by 220 · see citing works

CtIP fusion to Cas9 enhances transgene integration by homology-dependent repair

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Virus-Mediated Genome Editing via Homology-Directed Repair in Mitotic and Postmitotic Cells in Mammalian Brain

Nishiyama, J., Mikuni, T., & Yasuda, R. (2017) · Neuron · doi:10.1016/j.neuron.2017.10.004 · Cited by 215 · see citing works

CRISPR-based genome editing through the lens of DNA repair

Nambiar, T. S., Baudrier, L., Billon, P., & Ciccia, A. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.12.026 · Cited by 214 · see citing works

Histone ubiquitination in the DNA damage response

Uckelmann, M., & Sixma, T. K. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.06.011 · Cited by 211 · see citing works

DNA Repair and the Stability of the Plant Mitochondrial Genome

Chevigny, N., Schatz-Daas, D., Weber‐Lotfi, F., & Gualberto, J. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21010328 · Cited by 207 · see citing works

Regulation of Nrf2/ARE Pathway by Dietary Flavonoids: A Friend or Foe for Cancer Management?

Suraweera, T. L., Rupasinghe, H. P. V., Dellaire, G., & Xu, Z. (2020) · Antioxidants · doi:10.3390/antiox9100973 · Cited by 207 · see citing works

Interplay between Fanconi anemia and homologous recombination pathways in genome integrity

Michl, J., Zimmer, J., & Tarsounas, M. (2016) · The EMBO Journal · doi:10.15252/embj.201693860 · Cited by 204 · see citing works

DNA Double-Strand Break Resection Occurs during Non-homologous End Joining in G1 but Is Distinct from Resection during Homologous Recombination

Diemer-Biehs, R., Steinlage, M., Barton, O., Juhász, S., Künzel, J., Spies, J., Shibata, A., Jeggo, P. A., & Löbrich, M. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.12.016 · Cited by 201 · see citing works

CRISPR Cpf1 proteins: structure, function and implications for genome editing

Safari, F., Zare, K., Negahdaripour, M., Barekati‐Mowahed, M., & Ghasemi, Y. (2019) · Cell & Bioscience · doi:10.1186/s13578-019-0298-7 · Cited by 196 · see citing works

H4K20me0 recognition by BRCA1–BARD1 directs homologous recombination to sister chromatids

Nakamura, K., Saredi, G., Becker, J. R., Foster, B. M., Nguyen, N. V., Beyer, T. E., Cesa, L. C., Faull, P. A., Lukauskas, S., Frimurer, T. M., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0282-9 · Cited by 192 · see citing works

Harnessing DNA Double-Strand Break Repair for Cancer Treatment

Trenner, A., & Sartori, A. A. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01388 · Cited by 190 · see citing works

Precision genome editing in the CRISPR era

Salsman, J., & Dellaire, G. (2016) · Biochemistry and Cell Biology · doi:10.1139/bcb-2016-0137 · Cited by 183 · see citing works

NRF2 Activation in Cancer: From DNA to Protein

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Coupling of Homologous Recombination and the Checkpoint by ATR

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CRISPR-Cas: Converting A Bacterial Defence Mechanism into A State-of-the-Art Genetic Manipulation Tool

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53BP1 Enforces Distinct Pre- and Post-resection Blocks on Homologous Recombination

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A Code of Mono-phosphorylation Modulates the Function of RB

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Recent advances of therapeutic targets based on the molecular signature in breast cancer: genetic mutations and implications for current treatment paradigms

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The ubiquitin codes in cellular stress responses

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Sharpening the Molecular Scissors: Advances in Gene-Editing Technology

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The Role of PALB2 in the DNA Damage Response and Cancer Predisposition

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The deubiquitylating enzyme USP15 regulates homologous recombination repair and cancer cell response to PARP inhibitors

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The Tumor Suppressor PALB2: Inside Out

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Priming Human Repopulating Hematopoietic Stem and Progenitor Cells for Cas9/sgRNA Gene Targeting

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BRCA1-Dependent and Independent Recruitment of PALB2–BRCA2–RAD51 in the DNA Damage Response and Cancer

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Inadequate DNA Damage Repair Promotes Mammary Transdifferentiation, Leading to BRCA1 Breast Cancer

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Targeting p38α Increases DNA Damage, Chromosome Instability, and the Anti-tumoral Response to Taxanes in Breast Cancer Cells

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Improving Gene Editing Outcomes in Human Hematopoietic Stem and Progenitor Cells by Temporal Control of DNA Repair

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Genome editing in cardiovascular diseases

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Cell-Cycle Regulation of BRCA1 Inhibits Homologous Recombination in G1

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The cell cycle flavours of repair

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

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

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