PPM1D-truncating mutations confer resistance to chemotherapy and sensitivity to PPM1D inhibition in hematopoietic cells

Sensitive detection of somatic point mutations in impure and heterogeneous cancer samples

Cibulskis, K., Lawrence, M. S., Carter, S. L., Sivachenko, A., Jaffe, D. B., Sougnez, C. L., Gabriel, S., Meyerson, M. M., Lander, E. S., & Getz, G. A. (2013) · Nature Biotechnology · doi:10.1038/nbt.2514 · Cited by 4,965

Age-related clonal hematopoiesis associated with adverse outcomes

Jaiswal, S., Fontanillas, P., Flannick, J., Manning, A., Grauman, P. V., Mar, B. G., Lindsley, R. C., Mermel, C. H., Burtt, N., Chavez, A., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1408617 · Cited by 4,841

Optimized sgRNA design to maximize activity and minimize off-target effects of CRISPR-Cas9

Doench, J. G., Fusi, N., Sullender, M., Hegde, M., Vaimberg, E. W., Donovan, K. F., Smith, I., Tothova, Z., Wilen, C., Orchard, R., et al. (2016) · Nature Biotechnology · doi:10.1038/nbt.3437 · Cited by 4,637

Clonal hematopoiesis and blood-cancer risk inferred from blood DNA sequence

Genovese, G., Kähler, A. K., Handsaker, R. E., Lindberg, J., Rose, S. A., Bakhoum, S. F., Chambert, K., Mick, E., Neale, B. M., Fromer, M., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1409405 · Cited by 3,531

CRISPR-Cas9 Knockin Mice for Genome Editing and Cancer Modeling

Platt, R. J., Chen, S., Zhou, Y., Yim, M. J., Swiech, L., Kempton, H. R., Dahlman, J. E., Parnas, O., Eisenhaure, T. M., Jovanovic, M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.09.014 · Cited by 2,001

Clonal hematopoiesis of indeterminate potential and its distinction from myelodysplastic syndromes

Steensma, D. P., Bejar, R., Jaiswal, S., Lindsley, R. C., Sekeres, M. A., Hasserjian, R. P., & Ebert, B. L. (2015) · Blood · doi:10.1182/blood-2015-03-631747 · Cited by 1,971

Age-related mutations associated with clonal hematopoietic expansion and malignancies

Xie, M., Lu, C., Wang, J., McLellan, M. D., Johnson, K. J., Wendl, M. C., McMichael, J. F., Schmidt, H. K., Yellapantula, V., Miller, C. A., et al. (2014) · Nature Medicine · doi:10.1038/nm.3733 · Cited by 1,874

Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members

Certo, M. V., Moore, V. D. G., Nishino, M., Wei, G., Korsmeyer, S. J., Armstrong, S. A., & Letai, A. G. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.03.027 · Cited by 1,278

Role of TP53 mutations in the origin and evolution of therapy-related acute myeloid leukaemia

Wong, T. N., Ramsingh, G., Young, A. L., Miller, C. A., Touma, W., Welch, J. S., Lamprecht, T. L., Shen, D., Hundal, J., Fulton, R. S., et al. (2015) · Nature · doi:10.1038/nature13968 · Cited by 892

Therapy-related clonal hematopoiesis in patients with non-hematologic cancers is common and associated with adverse clinical outcomes

Coombs, C. C., Zehir, A., Devlin, S. M., Kishtagari, A., Syed, A., Jonsson, P., Hyman, D. M., Solit, D. B., Robson, M. E., Baselga, J., et al. (2017) · Cell stem cell · doi:10.1016/j.stem.2017.07.010 · Cited by 866

Prognostic Mutations in Myelodysplastic Syndrome after Stem-Cell Transplantation

Lindsley, R. C., Saber, W., Mar, B. G., Redd, R., Wang, T., Haagenson, M. D., Grauman, P. V., Hu, Z.-H., Spellman, S. R., Lee, S. J., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1611604 · Cited by 776

Integrated proteomic analysis of post-translational modifications by serial enrichment

Mertins, P., Qiao, J., Patel, J., Udeshi, N. D., Clauser, K. R., Mani, D. R., Burgess, M. W., Gillette, M. A., Jaffe, J. D., & Carr, S. A. (2013) · Nature Methods · doi:10.1038/nmeth.2518 · Cited by 619

Generation of mouse models of myeloid malignancy with combinatorial genetic lesions using CRISPR-Cas9 genome editing

Heckl, D., Kowalczyk, M. S., Yudovich, D., Belizaire, R., Puram, R. V., McConkey, M. E., Thielke, A., Aster, J. C., Regev, A., & Ebert, B. L. (2014) · Nature Biotechnology · doi:10.1038/nbt.2951 · Cited by 555

Wip1, a novel human protein phosphatase that is induced in response to ionizing radiation in a p53-dependent manner

Fiscella, M., Zhang, H., Fan, S., Sakaguchi, K., Shen, S., Mercer, W. E., Woude, G. F. V., O'Connor, P. M., & Appella, E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6048 · Cited by 535

Clonal Hematopoiesis Associated With Adverse Outcomes After Autologous Stem-Cell Transplantation for Lymphoma

Gibson, C. J., Lindsley, R. C., Tchekmedyian, V., Mar, B. G., Shi, J., Jaiswal, S., Bosworth, A., Francisco, L., He, J., Bansal, A., et al. (2017) · Journal of Clinical Oncology · doi:10.1200/jco.2016.71.6712 · Cited by 480

Amplification of PPM1D in human tumors abrogates p53 tumor-suppressor activity

Bulavin, D. V., Demidov, O. N., Saito, S., Kauraniemi, P., Dudgeon, C., Amundson, S. A., Ambrosino, C., Sauter, G., Nebreda, Á. R., Anderson, C. W., et al. (2002) · Nature Genetics · doi:10.1038/ng894 · Cited by 437

Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels

Mertins, P., Yang, F., Liu, T., Mani, D. R., Petyuk, V. A., Gillette, M. A., Clauser, K. R., Qiao, J. W., Gritsenko, M. A., Moore, R. J., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.036392 · Cited by 400

Drug-Induced Death Signaling Strategy Rapidly Predicts Cancer Response to Chemotherapy

Montero, J., Sarosiek, K. A., DeAngelo, J. D., Maertens, O., Ryan, J., Ercan, D., Piao, H., Horowitz, N. S., Berkowitz, R. S., Matulonis, U., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.042 · Cited by 378

The type 2C phosphatase Wip1: An oncogenic regulator of tumor suppressor and DNA damage response pathways

Lu, X., Nguyen, T., Moon, S.-H., Darlington, Y. F., Sommer, M., & Donehower, L. A. (2008) · Cancer and Metastasis Reviews · doi:10.1007/s10555-008-9127-x · Cited by 251

Mosaic PPM1D mutations are associated with predisposition to breast and ovarian cancer

Ruark, E., Snape, K. M. G., Humburg, P., Loveday, C., Bajrami, I., Brough, R., Rodrigues, D. N., Renwick, A., Seal, S., Ramsay, E., et al. (2012) · Nature · doi:10.1038/nature11725 · Cited by 250

Allosteric Wip1 phosphatase inhibition through flap-subdomain interaction

Gilmartin, A. G., Faitg, T. H., Richter, M. C., Groy, A., Seefeld, M. A., Darcy, M. G., Peng, X., Federowicz, K., Yang, J., Zhang, S., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1427 · Cited by 207

Cellular stressors contribute to the expansion of hematopoietic clones of varying leukemic potential

Wong, T. N., Miller, C. A., Jotte, M. R. M., Bagegni, N. A., Baty, J., Schmidt, A. P., Cashen, A. F., Duncavage, E. J., Helton, N., Fiala, M. A., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-02858-0 · Cited by 201

Tiling Path Genomic Profiling of Grade 3 Invasive Ductal Breast Cancers

Natrajan, R., Lambros, M. B. K., Rodríguez-Pinilla, S. M., Moreno‐Bueno, G., Tan, D. S. P., Marchiò, C., Vatcheva, R., Rayter, S., Mahler-Araujo, B. M., Fulford, L. G., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1878 · Cited by 171

Gain-of-function mutations of PPM1D/Wip1 impair the p53-dependent G1 checkpoint

Kleiblova, P., Shaltiel, I. A., Benada, J., Ševčík, J., Pecháčková, S., Pohlreich, P., Voest, E. E., Dundr, P., Bartek, J., Kleibl, Z., et al. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201210031 · Cited by 170

PPM1D Is a Potential Therapeutic Target in Ovarian Clear Cell Carcinomas

Tan, D. S. P., Lambros, M. B. K., Rayter, S., Natrajan, R., Vatcheva, R., Gao, Q., Marchiò, C., Geyer, F. C., Savage, K., Parry, S., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2403 · Cited by 165

iBH3: simple, fixable BH3 profiling to determine apoptotic priming in primary tissue by flow cytometry

Ryan, J. A., Montero, J., Rocco, J. W., & Letai, A. G. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0107 · Cited by 129

Somatic Mosaic Mutations in PPM1D and TP53 in the Blood of Women With Ovarian Carcinoma

Swisher, E. M., Harrell, M. I., Norquist, B. M., Walsh, T., Brady, M. F., Lee, M. J., Hershberg, R. M., Kalli, K. R., Lankes, H. A., Konnick, E. Q., et al. (2016) · JAMA Oncology · doi:10.1001/jamaoncol.2015.6053 · Cited by 105

WIP1 Phosphatase as a Potential Therapeutic Target in Neuroblastoma

Richter, M. C., Dayaram, T., Gilmartin, A. G., Ganji, G., Pemmasani, S. K., Key, H. V. D., Shohet, J. M., Donehower, L. A., & Kumar, R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0115635 · Cited by 69

Creation of Novel Protein Variants with CRISPR/Cas9-Mediated Mutagenesis: Turning a Screening By-Product into a Discovery Tool

Donovan, K. F., Hegde, M., Sullender, M. E., Vaimberg, E. W., Johannessen, C. M., Root, D. E., & Doench, J. G. (2017) · PLoS ONE · doi:10.1371/journal.pone.0170445 · Cited by 57

PPM1DMosaic Truncating Variants in Ovarian Cancer Cases May Be Treatment-Related Somatic Mutations

Pharoah, P. D. P., Song, H., Dicks, E., Intermaggio, M. P., Harrington, P. A., Baynes, C., Alsop, K., Chenevix‐Trench, G., Bogdanova, N. V., Cicek, M. S., et al. (2016) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djv347 · Cited by 50

Clonal hematopoiesis in human aging and disease

Jaiswal, S., & Ebert, B. L. (2019) · Science · doi:10.1126/science.aan4673 · Cited by 1,156

Bone marrow niches in haematological malignancies

Méndez‐Ferrer, S., Bonnet, D. A., Steensma, D. P., Hasserjian, R. P., Ghobrial, I. M., Gribben, J. G., Andreeff, M., & Krause, D. S. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-0245-2 · Cited by 515

PPM1D Mutations Drive Clonal Hematopoiesis in Response to Cytotoxic Chemotherapy

Hsu, J. I., Dayaram, T., Tovy, A., De Braekeleer, E., Jeong, M., Wang, F., Zhang, J., Heffernan, T. P., Gera, S., Kovacs, J. J., et al. (2018) · Cell stem cell · doi:10.1016/j.stem.2018.10.004 · Cited by 425

Cancer as a disease of old age: changing mutational and microenvironmental landscapes

Laconi, E., Marongiu, F., & DeGregori, J. (2020) · British Journal of Cancer · doi:10.1038/s41416-019-0721-1 · Cited by 348

Chronic infection drives Dnmt3a-loss-of-function clonal hematopoiesis via IFNγ signaling

Hormaechea-Agulla, D., Matatall, K. A., Le, D. T., Kain, B., Long, X., Kus, P., Jaksik, R., Challen, G. A., Kimmel, M., & King, K. Y. (2021) · Cell Stem Cell · doi:10.1016/j.stem.2021.03.002 · Cited by 329

PPM1D Truncating Mutations Confer Chemotherapy Resistance in Hematopoietic Stem Cells, Which Is Reversible By PPM1D Inhibition

Kahn, J. D., Silver, A. J., Mertins, P., Carr, S. A., Jaiswal, S., & Ebert, B. L. (2016) · Blood · doi:10.1182/blood.v128.22.740.740

Somatic mosaic truncating mutations of PPM1D in blood can result from expansion of a mutant clone under selective pressure of chemotherapy

Kim, B., Won, D., Lee, S., & Choi, J. R. (2019) · PLoS ONE · doi:10.1371/journal.pone.0217521 · Cited by 10

High Prevalence of PPM1D Mutations in Therapy-Related AML/MDS Is Due to Context-Specific Clonal Hematopoiesis

Hsu, J. I., Dayaram, T., Tovy, A., Braekeleer, E. D., Jeong, M., Rogers, J. H., Wang, F., Zhang, J., Garcia‐Manero, G., Kantarjian, H. M., et al. (2018) · Blood · doi:10.1182/blood-2018-99-115007

CHIPing out PPM1D-mutant hematopoiesis

Kindler, T. (2018) · Blood · doi:10.1182/blood-2018-07-861716 · Cited by 1

Truncating mutations of PPM1D are found in blood DNA samples of lung cancer patients

Zajkowicz, A., Butkiewicz, D., Drosik, A., Giglok, M., Suwiński, R., & Rusin, M. (2015) · British Journal of Cancer · doi:10.1038/bjc.2015.79 · Cited by 54