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The cBio Cancer Genomics Portal: An Open Platform for Exploring Multidimensional Cancer Genomics Data
Open accessAbstract
The cBio Cancer Genomics Portal (http://cbioportal.org) is an open-access resource for interactive exploration of multidimensional cancer genomics data sets, currently providing access to data from more than 5,000 tumor samples from 20 cancer studies. The cBio Cancer Genomics Portal significantly lowers the barriers between complex genomic data and cancer researchers who want rapid, intuitive, and high-quality access to molecular profiles and clinical attributes from large-scale cancer genomics projects and empowers researchers to translate these rich data sets into biologic insights and clinical applications. Cancer Discov; 2(5); 401–4. ©2012 AACR.
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“Second, cBioPortal and COSMIC are primarily focused on patient tumour genomic data.”
From Cell Model Passports-a hub for clinical, genetic and functional datasets of preclinical cancer models (2019) · cites this paper as [36]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Publicly available gene expression data from a matched cohort established previously59 or mCRPC was downloaded from cBioportal (20 May 2021)94–96.”
From Genome-scale CRISPR screens identify PTGES3 as a direct modulator of androgen receptor function in advanced prostate cancer (2025) · cites this paper as [95]
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“IMP2 is genomically altered in over 2% of all cancers, which is above the baseline of random alterations in the average passenger genes (Figure 5A) [77,78,79].”
From IMPlications of IMP2 in RNA Biology and Disease (2025) · cites this paper as [77]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Genomic amplifications creating extra copies of IGF2BP2 occur in 9% of lung cancers (Figure 5A) [77,78,79].”
From IMPlications of IMP2 in RNA Biology and Disease (2025) · cites this paper as [77]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“KRAS mutations are implicated in 25–30% of all human cancers, about 19% of non-small cell lung cancers (NSCLCs), about 40% of colorectal cancers (CRCs), and about 73% of pancreatic ductal adenocarcinoma (PDAC) cases (Figure 1) [1,2].”
From KRAS: Biology, Inhibition, and Mechanisms of Inhibitor Resistance (2024) · cites this paper as [1]
Experimental — accuracy not yet measured
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In the citing paper
“TP53 is deregulated in 22% of GBMs, while ARF, MDM2, and MDM4 are deregulated in 61%, 10%, and 10% of GBMs, respectively (Figure 1) [22,23].”
From The p53 Pathway in Glioblastoma (2018) · cites this paper as [22]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“The most frequently deregulated component of the p53 pathway is a homozygous deletion of the CDKN2A/ARF locus, which occurs in ~60% of all GBM cases (Figure 1) [22,23].”
From The p53 Pathway in Glioblastoma (2018) · cites this paper as [22]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“in patients with HCC, high PROX1 expression or chromosomal amplifications including PROX1 were both associated with increased survival25–32”
From Active repression of cell fate plasticity by PROX1 safeguards hepatocyte identity and prevents liver tumorigenesis (2025) · cites this paper as [26]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“in patients with HCC, high PROX1 expression or chromosomal amplifications including PROX1 were both associated with increased survival25–32”
From Active repression of cell fate plasticity by PROX1 safeguards hepatocyte identity and prevents liver tumorigenesis (2025) · cites this paper as [26]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“The prevalence of STAT3 overactivation in cancer cannot be explained by mutational activation of STAT3 because somatic mutation of the STAT3 gene in cancer is rare (1.08%; 54/4980 tumors analyzed to date by whole exome sequencing by The Cancer Genome Atlas).38”
From Critical analysis of the potential for targeting STAT3 in human malignancy (2013) · cites this paper as [38]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“It is an important tumour suppressor gene mutated in 6% of colorectal cancers (CRCs), and germline variants in PTEN are causative of PTEN hamartoma tumour syndrome (Hobert and Eng, 2009; Cerami et al., 2012).”
From Efficient genetic editing of human intestinal organoids using ribonucleoprotein-based CRISPR (2023) · cites this paper as Cerami et al., 2012
Experimental — accuracy not yet measuredIn the citing paper
“We note that the region of BRCA1 (amino acid residues 758-1064) that harbors the RAD51 interaction domain17 is frequently mutated in cancer (cBioPortal for Cancer Genomic)44,45”
From BRCA1–BARD1 promotes RAD51-mediated homologous DNA pairing (2017) · cites this paper as [44]
In the citing paper
“Despite being the most frequently altered oncogenic protein in solid tumours, KRAS has historically been considered ‘undruggable’”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [17]
In the citing paper
“each dataset indicates that ~20% of all malignancies have a RAS abnormality. Overall, ~17% of solid tumours have KRAS mutations, including ~90% of pancreatic, ~50% of colon and ~25% of lung adenocarcinomas16,17”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [17]
In the citing paper
“KRAS mutations predominate in NSCLCs, accounting for ~78% of all RAS mutations found in such tumours17. The activating missense KRAS mutations that occur in ~25% of NSCLCs19–23 are typically mutually exclusive with other clinically actionable driver mutations, such as those in EGFR, BRAF and ALK24.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [17]
In the citing paper
“approximately one in seven of all human cancers harbor KRAS (Kirsten rat sarcoma virus) alterations”
From Expanding the Reach of Precision Oncology by Drugging All KRAS Mutants (2022) · cites this paper as [4]
In the citing paper
“KRAS is the most frequently mutated oncogene”
From Expanding the Reach of Precision Oncology by Drugging All KRAS Mutants (2022) · cites this paper as [4]
In the citing paper
“Based on non-small cell lung cancer datasets within cBioPortal, the landscape of KRAS G12C mutated tumors includes a complex landscape of co-altered genes (Fig. 3)25,26.”
From Selective KRAS G12C inhibitors in non-small cell lung cancer: chemistry, concurrent pathway alterations, and clinical outcomes (2021) · cites this paper as [25]
In the citing paper
“Frequently co-altered genes include TP53, STK11, KEAP1, and CDKN2A.”
From Selective KRAS G12C inhibitors in non-small cell lung cancer: chemistry, concurrent pathway alterations, and clinical outcomes (2021) · cites this paper as [25]
In the citing paper
“Within the KRAS mutant subgroup, lower RNA expression of PTK2 (FAK coding gene) correlates with better survival outcomes”
From Focal Adhesion Kinase (FAK) Inhibition Synergizes with KRAS G12C Inhibitors in Treating Cancer through the Regulation of the FAK–YAP Signaling (2021) · cites this paper as [19]
In the citing paper
“while for KRAS wild type subgroup, there is no difference between the PTK2 low and high expression groups (Figure 1A,B)”
From Focal Adhesion Kinase (FAK) Inhibition Synergizes with KRAS G12C Inhibitors in Treating Cancer through the Regulation of the FAK–YAP Signaling (2021) · cites this paper as [19]
In the citing paper
“Analysis of the data in The Cancer Genome Atlas provides further evidence that a certain fraction of multiple cancers have overexpressed MDMX (amplification or mRNA) concurrently with inactivated (mutated or deleted) p53 (Table 1;34,35).”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [34]
In the citing paper
“For example, we evaluated ARF and TP53 status in the data from The Cancer Genome Atlas (TCGA) and determined that malignancies such as squamous cell carcinoma of the lung or head and neck co-inactivate ARF and TP53 in approximately 20% of these tumors (Table 1; (Cerami, et al., 2012; Gao, et al., 2013).”
From The Mdm network and its regulation of p53 activities: a rheostat of cancer risk (2014) · cites this paper as Cerami, et al., 2012
In the citing paper
“However, 5.3% (40 of 760) of breast adenocarcinomas contained amplified USP7 and of those, 75% maintained wild-type TP53 allele status, which implies that USP7 may have other functions related to oncogenesis.”
From The Mdm network and its regulation of p53 activities: a rheostat of cancer risk (2014) · cites this paper as Cerami, et al., 2012
In the citing paper
“Our evaluation of TCGA data revealed that USP7 is rarely amplified in human cancer (Cerami, et al., 2012; Gao, et al., 2013).”
From The Mdm network and its regulation of p53 activities: a rheostat of cancer risk (2014) · cites this paper as Cerami, et al., 2012
In the citing paper
“0.84% (18 of 2148) tumors analyzed had p21 deletions or mutations (Cerami, et al., 2012; Gao, et al., 2013).”
From The Mdm network and its regulation of p53 activities: a rheostat of cancer risk (2014) · cites this paper as Cerami, et al., 2012
In the citing paper
“Our analysis of TCGA data showed that up to 6% of specific human malignancies have amplified MDM2 or MDM4 (and even more have increased MDM2 or MDM4 mRNA expression) with concomitant TP53 mutations”
From The Mdm network and its regulation of p53 activities: a rheostat of cancer risk (2014) · cites this paper as Cerami, et al., 2012
In the citing paper
“even more have increased MDM2 or MDM4 mRNA expression”
From The Mdm network and its regulation of p53 activities: a rheostat of cancer risk (2014) · cites this paper as Cerami, et al., 2012
In the citing paper
“First, Cellosaurus and cBioPortal do not provide cell model functional information, while PharmacoDB does not contain genomic annotation of the cell models and has limited sample/model information.”
From Cell Model Passports-a hub for clinical, genetic and functional datasets of preclinical cancer models (2019) · cites this paper as [36]
In the citing paper
“Third, neither cBioPortal, PharmacoDB nor COSMIC curate samples to map unique identifiers or link samples and models from the same patient, which can be important for identifying mis-identified or cross-contaminated samples.”
From Cell Model Passports-a hub for clinical, genetic and functional datasets of preclinical cancer models (2019) · cites this paper as [36]
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Cites
Robinson, J. T., Thorvaldsdóttir, H., Winckler, W., Guttman, M., Lander, E. S., Getz, G., & Mesirov, J. P. (2011) · Nature Biotechnology · doi:10.1038/nbt.1754 · Cited by 15,390
The Pfam Protein Families Database
Bateman, A. G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,075
Integrated genomic analyses of ovarian carcinoma
Perou, C. M. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/hvp3-wg08 · Cited by 7,927
Comprehensive genomic characterization defines human glioblastoma genes and core pathways
The Cancer Genome Atlas Research Network (2008) · Nature · doi:10.1038/nature07385 · Cited by 7,735
The Pfam protein families database
Punta, M., Coggill, P. C., Eberhardt, R. Y., Mistry, J., Tate, J., Boursnell, C., Pang, N., Forslund, K., Ceric, G., Clements, J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr1065 · Cited by 3,719
Integrative Genomic Profiling of Human Prostate Cancer
Taylor, B. S., Schultz, N. D., Hieronymus, H., Gopalan, A., Xiao, Y., Carver, B. S., Arora, V. K., Kaushik, P., Cerami, E. G., Reva, B. A., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.05.026 · Cited by 3,713
Self-citationInternational network of cancer genome projects
The International Cancer Genome Consortium (2010) · Nature · doi:10.1038/nature08987 · Cited by 2,299
Predicting the functional impact of protein mutations: application to cancer genomics
Reva, B. A., Antipin, Y., & Sander, C. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr407 · Cited by 2,046
Self-citationHallmarks of 'BRCAness' in sporadic cancers
Turner, N. C., Tutt, A. N. J., & Ashworth, A. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1457 · Cited by 1,690
Pathway Commons, a web resource for biological pathway data
Cerami, E. G., Gross, B. E., Demir, E., Rodchenkov, I., Babur, O., Anwar, N., Schultz, N., Bader, G. D., & Sander, C. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1039 · Cited by 1,101
Self-citation
Research works printed but not linked: 1
- Cancer Genome Atlas Research Network, 2011, Nature, 474, 609, 10.1038/nature10166 · DOI · Paper page
Cited by
Sorted by citations
Items 301–400 of 1,118
Aparicio, A. M., Shen, L., Tapia, E. L. N., Lu, J., Chen, H.-C., Zhang, J., Wu, G., Wang, X., Troncoso, P., Corn, P. G., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1259 · Cited by 307
ROS1-dependent cancers — biology, diagnostics and therapeutics
Drilon, A. E. D. C., Jenkins, C., Iyer, S. R., Schoenfeld, A. J., Keddy, C., & Davare, M. A. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0408-9 · Cited by 304
Zhang, H., Liu, T., Liu, C., Song, S., Zhang, X., Liu, W., Jia, H., Xue, Y., & Guo, A. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku887 · Cited by 300
Maller, O., Drain, A. P., Barrett, A. S., Borgquist, S., Ruffell, B., Zakharevich, I., Pham, T. T. M., Gruosso, T., Kuasne, H., Lakins, J. N., et al. (2020) · Nature Materials · doi:10.1038/s41563-020-00849-5 · Cited by 307
The Molecular Balancing Act of p16INK4a in Cancer and Aging
LaPak, K. M., & Burd, C. E. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0350 · Cited by 304
The Roles of MDM2 and MDMX in Cancer
Karni-Schmidt, O., Lokshin, M., & Prives, C. L. (2016) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040349 · Cited by 302
Vijayaraghavan, S., Karakaş, C., Doostan, I., Chen, X., Bui, T. N., Yi, M., Raghavendra, A. S., Zhao, Y., Bashour, S. I., Ibrahim, N. K., et al. (2017) · Nature Communications · doi:10.1038/ncomms15916 · Cited by 299
Neurons release serine to support mRNA translation in pancreatic cancer
Banh, R. S., Biancur, D. E., Yamamoto, K., Sohn, A. S. W., Walters, B., Kuljanin, M., Gikandi, A., Wang, H., Mancias, J. D., Schneider, R. J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.016 · Cited by 292
Hoefflin, R., Harlander, S., Schäfer, S., Metzger, P., Kuo, F., Schönenberger, D., Adlesic, M., Peighambari, A., Seidel, P., Chen, C.-Y., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17873-3 · Cited by 292
Transcription-Associated Cyclin-Dependent Kinases as Targets and Biomarkers for Cancer Therapy
Chou, J., Quigley, D. A., Robinson, T. M., Feng, F. Y.-C., & Ashworth, A. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0528 · Cited by 297
Chen, Y., Yang, S., Tavormina, J., Tampe, D., Zeisberg, M., Wang, H., Mahadevan, K. K., Wu, C.-J., Sugimoto, H., Chang, C.-C., et al. (2022) · Cancer Cell · doi:10.1016/j.ccell.2022.06.011 · Cited by 289
Targeted Therapies for Triple-Negative Breast Cancer: Combating a Stubborn Disease
Kalimutho, M., Parsons, K., Mittal, D., López, J. A., Srihari, S., & Khanna, K. K. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.009 · Cited by 298
Transsulfuration Activity Can Support Cell Growth upon Extracellular Cysteine Limitation
Zhu, J., Berisa, M., Schwörer, S., Qin, W., Cross, J. R., & Thompson, C. B. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.009 · Cited by 292
Sattiraju, A., Kang, S., Giotti, B., Chen, Z., Marallano, V. J., Brusco, C., Ramakrishnan, A., Shen, L., Tsankov, A. M., Hambardzumyan, D., et al. (2023) · Immunity · doi:10.1016/j.immuni.2023.06.017 · Cited by 306
Marked for death: Targeting epigenetic changes in cancer
Pfister, S. X., & Ashworth, A. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.256 · Cited by 288
Insulin–PI3K signalling: an evolutionarily insulated metabolic driver of cancer
Hopkins, B. D., Goncalves, M. D., & Cantley, L. C. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0329-9 · Cited by 288
Genomic Characterization of Upper Tract Urothelial Carcinoma
Sfakianos, J. P., Cha, E. K., Iyer, G., Scott, S. N., Zabor, E. C., Shah, R. H., Ren, Q., Bagrodia, A., Kim, P. H., Hakimi, A. A., et al. (2015) · European Urology · doi:10.1016/j.eururo.2015.07.039 · Cited by 288
Self-citationA proteomic landscape of diffuse-type gastric cancer
Ge, S., Xia, X., Ding, C., Zhen, B., Zhou, Q., Feng, J., Yuan, J., Chen, R., Li, Y., Ge, Z., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03121-2 · Cited by 294
Self-citationChakravarty, D., Johnson, A., Sklar, J., Lindeman, N. I., Moore, K. N., Ganesan, S., Lovly, C. M., Perlmutter, J., Gray, S. W., Hwang, J., et al. (2022) · Journal of Clinical Oncology · doi:10.1200/jco.21.02767 · Cited by 301
Carbonic Anhydrases: Role in pH Control and Cancer
Mboge, M. Y., Mahon, B. P., McKENNA, R. V., & Frost, S. C. (2018) · Metabolites · doi:10.3390/metabo8010019 · Cited by 297
RET Aberrations in Diverse Cancers: Next-Generation Sequencing of 4,871 Patients
Kato, S., Subbiah, V., Marchlik, E., Elkin, S. K., Carter, J. L., & Kurzrock, R. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-1679 · Cited by 285
Distinct structural classes of activating FOXA1 alterations in advanced prostate cancer
Parolia, A., Cieslik, M., Chu, S.-C., Xiao, L., Ouchi, T., Zhang, Y., Wang, X., Vats, P., Cao, X., Pitchiaya, S., et al. (2019) · Nature · doi:10.1038/s41586-019-1347-4 · Cited by 284
Next-generation sequencing to guide cancer therapy
Gagan, J., & Allen, E. M. V. (2015) · Genome Medicine · doi:10.1186/s13073-015-0203-x · Cited by 293
Double PIK3CA mutations in cis increase oncogenicity and sensitivity to PI3Kα inhibitors
Vasan, N., Razavi, P., Johnson, J. L., Shao, H., Shah, H., Antoine, A., Ladewig, E., Gorelick, A. N., Lin, T.-Y., Toska, E., et al. (2019) · Science · doi:10.1126/science.aaw9032 · Cited by 296
Oncogenic PI3K and K-Ras stimulate de novo lipid synthesis through mTORC1 and SREBP
Ricoult, S. J. H., Yecies, J. L., Ben‐Sahra, I., & Manning, B. D. (2015) · Oncogene · doi:10.1038/onc.2015.179 · Cited by 288
Fredriksson, N. J., Ny, L., Nilsson, J. A., & Larsson, E. (2014) · Nature Genetics · doi:10.1038/ng.3141 · Cited by 295
Self-citationTherapeutic Targeting of RNA Splicing Catalysis through Inhibition of Protein Arginine Methylation
Fong, J. Y., Pignata, L., Goy, P.-A. V., Kawabata, K. C., Lee, S. C.-W., Koh, C. M., Musiani, D., Massignani, E., Kotini, A. G., Penson, A., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.07.003 · Cited by 294
He, C., Mao, D., Hua, G., Lv, X., Chen, X., Angeletti, P. C., Dong, J., Remmenga, S. W., Rodabaugh, K. J., Zhou, J. R., et al. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201404976 · Cited by 290
ATRX loss promotes tumor growth and impairs nonhomologous end joining DNA repair in glioma
Koschmann, C. J., Calinescu, A., Núñez, F. J., Mackay, A. G., Fazal-Salom, J., Thomas, D., Mendez, F., Kamran, N., Dzaman, M., Mulpuri, L., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aac8228 · Cited by 293
Zhang, Z., Wang, Z., Chen, Y., Wu, H., Yin, L., Zhao, Q., Luo, H., Zeng, Z.-L., Qiu, M., & Xu, R. (2022) · Genome Medicine · doi:10.1186/s13073-022-01050-w · Cited by 282
Briggs, S., & Tomlinson, I. P. M. (2013) · The Journal of Pathology · doi:10.1002/path.4185 · Cited by 284
Vincent, E. E., Sergushichev, A., Griss, T., Gingras, M., Samborska, B., Ntimbane, T., Coelho, P. P., Blagih, J., Raissi, T. C., Choinière, L., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.013 · Cited by 281
Bao, Y., Zhai, J., Chen, H., Wong, C. C., Liang, C., Ding, Y., Huang, D., Gou, H., Chen, D., Pan, Y., et al. (2023) · Gut · doi:10.1136/gutjnl-2022-328845 · Cited by 282
Cancer-Associated PTEN Mutants Act in a Dominant-Negative Manner to Suppress PTEN Protein Function
Papa, A., Wan, L., Bonora, M., Salmena, L., Song, M. S., Hobbs, R. M., Lunardi, A., Webster, K. A., Ng, C., Newton, R. H., et al. (2014) · Cell · doi:10.1016/j.cell.2014.03.027 · Cited by 286
Rho GTPase signaling in cancer progression and dissemination
Crosas‐Molist, E., Samain, R., Kohlhammer, L., Orgaz, J. L., George, S. L., Maiques, Ó., Barcelo, J., & Sanz‐Moreno, V. (2021) · Physiological Reviews · doi:10.1152/physrev.00045.2020 · Cited by 289
NLRC5/MHC class I transactivator is a target for immune evasion in cancer
Yoshihama, S., Roszik, J., Downs, I., Meissner, T. B., Vijayan, S., Chapuy, B., Sidiq, T., Shipp, M. A., Lizee, G. A., & Kobayashi, K. S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1602069113 · Cited by 276
Targeting signaling pathways in prostate cancer: mechanisms and clinical trials
He, Y., Xu, W., Xiao, Y., Huang, H., Gu, D., & Ren, S. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01042-7 · Cited by 287
KDM5B promotes immune evasion by recruiting SETDB1 to silence retroelements
Zhang, S.-M., Cai, W. L., Liu, X., Thakral, D., Luo, J., Chan, L. H., McGeary, M. K., Song, E., Blenman, K. R. M., Micevic, G., et al. (2021) · Nature · doi:10.1038/s41586-021-03994-2 · Cited by 272
Lipid metabolism and lipophagy in cancer
Maan, M., Peters, J. M., Dutta, M., & Patterson, A. D. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.02.097 · Cited by 282
Konno, H., Yamauchi, S., Berglund, A., Putney, R. M., Mulé, J. J., & Barber, G. N. (2018) · Oncogene · doi:10.1038/s41388-017-0120-0 · Cited by 281
Clinical Implications of Genomic Discoveries in Lung Cancer
Swanton, C., & Govindan, R. (2016) · New England Journal of Medicine · doi:10.1056/nejmra1504688 · Cited by 274
Garg, A. D., Vandenberk, L., Koks, C., Verschuere, T., Boon, L., Van Gool, S. W., & Agostinis, P. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aae0105 · Cited by 270
Direct regulation of GAS6/AXL signaling by HIF promotes renal metastasis through SRC and MET
Rankin, E. B., Fuh, K. C., Castellini, L., Viswanathan, K., Finger, E. C., Diep, A. N., LaGory, E. L., Kariolis, M. S., Chan, A., Lindgren, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404848111 · Cited by 269
Detection of early pancreatic ductal adenocarcinoma with thrombospondin-2 and CA19-9 blood markers
Kim, J., Bamlet, W. R., Oberg, A. L., Chaffee, K. G., Donahue, G., Cao, X.-J., Chari, S., Garcia, B. A., Petersen, G. M., & Zaret, K. S. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aah5583 · Cited by 269
Direct in Vivo RNAi Screen Unveils Myosin IIa as a Tumor Suppressor of Squamous Cell Carcinomas
Schramek, D., Sendoel, A., Segal, J. P., Beronja, S., Heller, E., Oristian, D., Reva, B. A., & Fuchs, E. V. (2014) · Science · doi:10.1126/science.1248627 · Cited by 269
Self-citationDual Chromatin and Cytoskeletal Remodeling by SETD2
Park, I. Y., Powell, R. T., Tripathi, D. N., Dere, R., Ho, T. H., Blasius, T. L., Chiang, Y.-C., Davis, I. J., Fahey, C. C., Hacker, K. E., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.005 · Cited by 285
FOXA1 mutations alter pioneering activity, differentiation and prostate cancer phenotypes
Adams, E., Karthaus, W. R., Hoover, E., Liu, D., Gruet, A., Zhang, Z., Cho, H., DiLoreto, R., Chhangawala, S., Liu, Y., et al. (2019) · Nature · doi:10.1038/s41586-019-1318-9 · Cited by 268
Cell Origins of High-Grade Serous Ovarian Cancer
Kim, J., Park, E. Y., Kim, O., Schilder, J. M., Coffey, D., Cho, C., & Bast, R. C. (2018) · Cancers · doi:10.3390/cancers10110433 · Cited by 267
YTHDF1 Regulates Tumorigenicity and Cancer Stem Cell-Like Activity in Human Colorectal Carcinoma
Bai, Y., Yang, C., Wu, R., Huang, L., Song, S., Li, W., Yan, P., Lin, C., Li, D., & Zhang, Y. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00332 · Cited by 267
Im, A., Sehgal, A. R., Carroll, M. P., Smith, B. D., Tefferi, A., Johnson, D. E., & Boyiadzis, M. M. (2014) · Leukemia · doi:10.1038/leu.2014.124 · Cited by 278
Computational genomics tools for dissecting tumour–immune cell interactions
Hackl, H., Charoentong, P., Finotello, F., & Trajanoski, Z. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.67 · Cited by 272
TERT promoter mutations in primary and secondary glioblastomas
Nonoguchi, N., Ohta, T., Oh, J., Kim, Y.-H., Kleihues, P., & Ohgaki, H. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1163-0 · Cited by 265
Johnson, A., Severson, E. A., Gay, L. M., Vergilio, J., Elvin, J. A., Suh, J. H., Daniel, S., Covert, M., Frampton, G. M., Hsu, S. H., et al. (2017) · The Oncologist · doi:10.1634/theoncologist.2017-0242 · Cited by 270
Role of osteopontin in the pathophysiology of cancer
Shevde, L. A., & Samant, R. S. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.03.001 · Cited by 264
Structural insights into the functional diversity of the CDK–cyclin family
Wood, D. J., & Endicott, J. (2018) · Open Biology · doi:10.1098/rsob.180112 · Cited by 272
Immunomodulatory TGF-β Signaling in Hepatocellular Carcinoma
Chen, J., Gingold, J. A., & Su, X. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.06.007 · Cited by 274
The Role of Aneuploidy in Cancer EvolutionPreprint
Sansregret, L., & Swanton, C. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a028373 · Cited by 272
Lissanu, Y., Sun, Y., Terranova, C. J., Khan, F., Martínez-Ledesma, E., Gay, J. P., Gao, G., Mullinax, R. A., Khor, T. O., Feng, N., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0019-5 · Cited by 268
Tumor mutational burden is a determinant of immune-mediated survival in breast cancer
Thomas, A., Routh, E. D., Pullikuth, A., Jin, G., Su, J., Chou, J. W., Hoadley, K. A., Print, C. G., Knowlton, N. S., Black, M. A., et al. (2018) · OncoImmunology · doi:10.1080/2162402x.2018.1490854 · Cited by 266
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 269
Johnson, R. W., Finger, E. C., Olcina, M. M., Vilalta, M., Aguilera, T. A., Miao, Y. R., Merkel, A. R., Johnson, J., Sterling, J. A. R., Wu, J. Y., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3408 · Cited by 266
Genetic Markers in Triple-Negative Breast Cancer
Sporikova, Z., Koudeláková, V., Trojanec, R., & Hajdúch, M. (2018) · Clinical Breast Cancer · doi:10.1016/j.clbc.2018.07.023 · Cited by 270
Three subtypes of lung cancer fibroblasts define distinct therapeutic paradigms
Hu, H., Piotrowska, Z., Hare, P. J., Chen, H., Mulvey, H. E., Mayfield, A., Noeen, S., Kattermann, K. E., Greenberg, M., Williams, A. F., et al. (2021) · Cancer Cell · doi:10.1016/j.ccell.2021.09.003 · Cited by 269
Actin remodeling confers BRAF inhibitor resistance to melanoma cells through YAP/TAZ activation
Kim, M. H., Kim, J., Hong, H., Lee, J. J.-K., Lee, J., Jung, E., & Kim, J. (2015) · The EMBO Journal · doi:10.15252/embj.201592081 · Cited by 270
Tumor Microenvironment-Derived NRG1 Promotes Antiandrogen Resistance in Prostate Cancer
Zhang, Z., Karthaus, W. R., Lee, Y. S., Gao, V. R., Wu, C., Russo, J. W., Liu, M., Mota, J. M., Abida, W. M., Linton, E. L., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.005 · Cited by 260
Gal-Ben-Ari, S., Barrera, I., Ehrlich, M., & Rosenblum, K. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00480 · Cited by 274
Liu, P., Gan, W., Inuzuka, H., Lazorchak, A. S., Gao, D., Arojo, O., Liu, D., Wan, L., Zhai, B., Yu, Y., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2860 · Cited by 264
Immune Cell–Poor Melanomas Benefit from PD-1 Blockade after Targeted Type I IFN Activation
Bald, T., Landsberg, J., Lopez-Ramos, D., Renn, M., Glodde, N., Jansen, P., Gaffal, E., Steitz, J., Tolba, R. H., Kalinke, U., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0458 · Cited by 261
Inhibition of histone deacetylases in cancer therapy: lessons from leukaemia
Ceccacci, E., & Minucci, S. (2016) · British Journal of Cancer · doi:10.1038/bjc.2016.36 · Cited by 262
Postel, M., Roosen, A., Laurent‐Puig, P., Taly, V., & Renault, S. (2017) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2018.1400384 · Cited by 255
Cyclin-Dependent Kinases (CDK) and Their Role in Diseases Development–Review
Łukasik, P., Załuski, M., & Gutowska, I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22062935 · Cited by 262
Liu, Z., Chen, P., Gao, H., Gu, Y., Yang, J., Peng, H., Xu, X., Wang, H., Yang, M., Liu, X., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.05.015 · Cited by 254
Challenges in Establishing Pure Lung Cancer Organoids Limit Their Utility for Personalized Medicine
Dijkstra, K. K., Monkhorst, K., Schipper, L. J., Hartemink, K. J., Smit, E. F., Kaing, S., de Groot, R., Wolkers, M. C., Clevers, H., Cuppen, E., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107588 · Cited by 254
Big data in basic and translational cancer research
Jiang, P., Sinha, S., Aldape, K., Hannenhalli, S., Sahinalp, C., & Ruppin, E. (2022) · Nature Reviews Cancer · doi:10.1038/s41568-022-00502-0 · Cited by 254
Functional Role of G9a Histone Methyltransferase in Cancer
Casciello, F., Windloch, K., Gannon, F., & Lee, J. S. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00487 · Cited by 263
Caspase-8: The double-edged sword
Mandal, R., Compte, J., Kostova, I., Becker, S., & Strebhardt, K. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188357 · Cited by 261
Identification of six new susceptibility loci for invasive epithelial ovarian cancer
EMBRACE, Kuchenbaecker, K. B., Collaborators, G. S., Breast Cancer Family Registry, HEBON, KConFab Investigators, Australian Cancer Study (Ovarian Cancer Investigators), Australian Ovarian Cancer Study Group, the Consortium of Investigators of Modifiers of BRCA1 and BRCA2, Ramus, S. J., et al. (2015) · Nature Genetics · doi:10.1038/ng.3185 · Cited by 250
Widespread intronic polyadenylation inactivates tumour suppressor genes in leukaemia
Lee, S., Singh, I., Tisdale, S., Abdel-Wahab, O. I., Leslie, C. S., & Mayr, C. (2018) · Nature · doi:10.1038/s41586-018-0465-8 · Cited by 257
Immune Heterogeneity of Glioblastoma Subtypes: Extrapolation from the Cancer Genome Atlas
Doucette, T. A., Rao, G., Rao, A. U. K., Shen, L., Aldape, K., Wei, J., Dziurzynski, K., Gilbert, M. R., & Heimberger, A. B. (2013) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-13-0028 · Cited by 249
A Positive Feedback Loop of lncRNA- PVT1 and FOXM1 Facilitates Gastric Cancer Growth and Invasion
Xu, M., Wang, Y., Weng, W., Wei, P., Qi, P., Zhang, Q., Tan, C., Ni, S., Dong, L., Yang, Y., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-0742 · Cited by 249
Capturing variation impact on molecular interactions in the IMEx Consortium mutations data set
Khadake, J., Meldal, B., Panni, S., Thorneycroft, D., Roey, K. V., Abbani, S., Salwiński, Ł., Pellegrini, M. A., Iannuccelli, M., Licata, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07709-6 · Cited by 248
Wohlhieter, C. A., Richards, A. L., Uddin, F. Z., Hulton, C. H., Quintanal-Villalonga, À., Martin, A. S., de Stanchina, E., Bhanot, U. K., Asher, M., Shah, N., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108444 · Cited by 253
Cause and Consequence of Cancer/Testis Antigen Activation in Cancer
Whitehurst, A. W. (2013) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011112-140326 · Cited by 255
Tang, T. T., Konradi, A. W., Feng, Y., Peng, X., Ma, M., Li, J., Yu, F.-X., Guan, K.-L., & Post, L. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-20-0717 · Cited by 245
Herbst, R. S., Gandara, D. R., Hirsch, F. R., Redman, M. W., LeBlanc, M. L., Mack, P. C., Schwartz, L. H., Vokes, E. E., Ramalingam, S. S., Bradley, J. D., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-3473 · Cited by 247
Biological functions of casein kinase 1 isoforms and putative roles in tumorigenesis
Schittek, B., & Sinnberg, T. W. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-231 · Cited by 250
Jiménez-Sánchez, A., Cybulska, P., Mager, K. L., Koplev, S., Cast, O. M., Couturier, D., Memon, D., Selenica, P., Nikolovski, I., Mazaheri, Y., et al. (2020) · Nature Genetics · doi:10.1038/s41588-020-0630-5 · Cited by 248
KMT2D Deficiency Impairs Super-Enhancers to Confer a Glycolytic Vulnerability in Lung Cancer
Alam, H., Tang, M., Maitituoheti, M., Dhar, S. S., Kumar, M., Han, C. Y., Ambati, C. R., Amin, S. B., Gu, B., Chen, T.-Y., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.03.005 · Cited by 243
Li, W., Cooper, J. M., Zhou, L., Yang, C., Erdjument‐Bromage, H., Zagzag, D., Snuderl, M., Ladanyi, M., Hanemann, C. O., Zhou, P., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.05.001 · Cited by 252
Tchekmedyian, V., Sherman, E. J., Dunn, L. A., Tran, C., Baxi, S. S., Katabi, N., Antonescu, C. R., Ostrovnaya, I., Haque, S. S., Pfister, D. G., et al. (2019) · Journal of Clinical Oncology · doi:10.1200/jco.18.01859 · Cited by 242
Xue, X., Ramakrishnan, S. K., Weisz, K. M., Triner, D. A., Xie, L., Attili, D., Pant, A., Győrffy, B., Zhan, M., Carter‐Su, C., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.015 · Cited by 247
Vendetti, F. P., Lau, A., Schamus, S., Conrads, T. P., O’Connor, M. J., & Bakkenist, C. J. (2015) · Oncotarget · doi:10.18632/oncotarget.6247 · Cited by 252
Identification of cancer driver genes based on nucleotide context
Dietlein, F., Weghorn, D., Taylor-Weiner, A. N., Richters, A., Reardon, B. M., Liu, D., Lander, E. S., Allen, E. M. V., & Sunyaev, S. R. (2020) · Nature Genetics · doi:10.1038/s41588-019-0572-y · Cited by 251
The protein histidine phosphatase LHPP is a tumour suppressor
Hindupur, S. K., Colombi, M., Fuhs, S. R., Matter, M. S., Guri, Y., Adam, K., Cornu, M., Piscuoglio, S., Ng, C. K. Y., Betz, C., et al. (2018) · Nature · doi:10.1038/nature26140 · Cited by 240
Therapeutic Targeting of Cancers with Loss of PTEN Function
Dillon, L. M., & Miller, T. W. (2014) · Current Drug Targets · doi:10.2174/1389450114666140106100909 · Cited by 246
YTHDF1 Promotes Gastric Carcinogenesis by Controlling Translation of FZD7
Pi, J., Wang, W., Ji, M. H., Wang, X., Wei, X., Jin, J., Liu, T., Qiang, J., Qi, Z., Li, F., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-0066 · Cited by 239
Falletta, P., Sánchez‐del‐Campo, L., Chauhan, J. S., Effern, M., Kenyon, A., Kershaw, C. J., Siddaway, R., Lisle, R., Freter, R., Daniels, M. J., et al. (2017) · Genes & Development · doi:10.1101/gad.290940.116 · Cited by 260
Phipps, A. I., Buchanan, D. D., Makar, K. W., Win, A. K., Baron, J. A., Lindor, N. M., Potter, J. D., & Newcomb, P. A. (2013) · British Journal of Cancer · doi:10.1038/bjc.2013.118 · Cited by 238
Targeting Rac and Cdc42 GTPases in Cancer
Maldonado, M. D. M., & Dharmawardhane, S. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-0619 · Cited by 242
CD36 mediates palmitate acid-induced metastasis of gastric cancer via AKT/GSK-3β/β-catenin pathway
Pan, J., Fan, Z., Wang, Z., Dai, Q., Xiang, Z., Yuan, F., Yan, M., Zhu, Z., Liu, B., & Li, C. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-019-1049-7 · Cited by 244
Metadata
- Authors
- Cerami, E., Gao, J., Dogrusoz, U., Gross, B. E., Sumer, S. O., Aksoy, B. A., Jacobsen, A., Byrne, C. J., Heuer, M. L., Larsson, E., Antipin, Y., Reva, B., Goldberg, A. P., Sander, C., & Schultz, N.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Authors' Affiliations: 1Computational Biology Center, Memorial Sloan-Kettering Cancer Center, 2Tri-Institutional Training Program in Computational Biology and Medicine, New York, New York; and 3Computer Engineering Department, Bilkent University, Ankara, Turkey
- Corresponding author
- Cerami, Ethan
- ORCID
- Venue
- Cancer Discovery
- Published
- 2012-05-01
- Volume
- 2
- Issue
- 5
- Pages
- 401-404
- ISSN
- 2159-8274 (ISSN-L)
- 2159-8290
- PMC
- PMC3956037
- OpenAlex
- W2149441684
- Semantic Scholar
- b8d2639696825d163188eb5cea5582c350987b70
- Cited by
- 17,455
- References
- 17
- Citations by year
- 2026: 945 · 2025: 1525 · 2024: 1764 · 2023: 2020 · 2022: 2020 · 2021: 2136 · 2020: 1836 · 2019: 1393 · 2018: 1048 · 2017: 906 · 2016: 764 · 2015: 583 · 2014: 324 · 2013: 159 · 2012: 15
- FWCI
- 114.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Cancer Discovery (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Bilkent University Institutional Repository (Bilkent University) (submittedVersion, other-oa)
- Bilkent University Institutional Repository (Bilkent University) (submittedVersion)
- Funders
- Memorial Sloan-Kettering Cancer Center
- University of Toronto
- Bilkent Üniversitesi
- National Institutes of Health
- University of Texas MD Anderson Cancer Center
- Stand Up To Cancer (SU2C‐AACR‐DT0209)
- National Cancer Institute (SU2C-AACR-DT0209, R01CA132744, U24CA143840, NCI-U24CA143840, NCI-R21CA135870, R21CA135870)
- National Institute of General Medical Sciences (GM 103504, P41GM103504)
- National Center for Research Resources (RR031228, P41RR031228)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Genomics and Diagnostics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Keywords
- cancer genomics data, interactive data exploration, tumor molecular profiles, clinical features, cancer research resources
- MeSH terms
- Database Management Systems, Humans, Neoplasms, Databases, Factual, Internet, Genomics
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