Enhanced serine production by bone metastatic breast cancer cells stimulates osteoclastogenesis

R: A Language and Environment for Statistical Computing

R Core Team (2000) · doi:10.32614/r.manuals · Cited by 355,893

Bioconductor: open software development for computational biology and bioinformatics

Gentleman, R. C., Carey, V. J., Bates, D. M., Bolstad, B., Dettling, M., Dudoit, S., Ellis, B., Gautier, L., Ge, Y., Gentry, J., et al. (2004) · Genome biology · doi:10.1186/gb-2004-5-10-r80 · Cited by 12,082

DAVID: Database for Annotation, Visualization, and Integrated Discovery

Dennis, G., Sherman, B. T., Hosack, D. A., Yang, J., Gao, W., Lane, H. C., & Lempicki, R. A. (2003) · Genome Biology · doi:10.1186/gb-2003-4-5-p3 · Cited by 9,327

Repeated observation of breast tumor subtypes in independent gene expression data sets

Sørlie, T., Tibshirani, R. J., Parker, J. S., Hastie, T. J., Marron, J. S., Nobel, A. B., Deng, S., Johnsen, H., Pesich, R., Geisler, S. B., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0932692100 · Cited by 5,508

Summaries of Affymetrix GeneChip probe level data

Irizarry, R. A. (2003) · Nucleic Acids Research · doi:10.1093/nar/gng015 · Cited by 4,837

A multigenic program mediating breast cancer metastasis to bone

Kang, Y., Siegel, P. M., Shu, W., Drobnjak, M., Käkönen, S.-M., Cordon‐Cardo, C., Guise, T. A., & Massagué, J. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00132-6 · Cited by 2,605

Evolving gene/transcript definitions significantly alter the interpretation of GeneChip data

Dai, M. (2005) · Nucleic Acids Research · doi:10.1093/nar/gni179 · Cited by 1,807

WebGestalt: an integrated system for exploring gene sets in various biological contexts

Zhang, B., Kirov, S. A., & Snoddy, J. R. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki475 · Cited by 1,803

An expression signature for p53 status in human breast cancer predicts mutation status, transcriptional effects, and patient survival

Miller, L. D., Smeds, J., George, J., Vega, V. B., Vergara, L. A., Ploner, A., Yudi Pawitan, Y., Hall, P. N., Klaar, S., Liu, E. T., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506230102 · Cited by 1,256

TGF-β signaling blockade inhibits PTHrP secretion by breast cancer cells and bone metastases development

Yin, J. J., Selander, K. S., Chirgwin, J. M., Dallas, M., Grubbs, B. G., Wieser, R., Massagué, J., Mundy, G. R., & Guise, T. A. (1999) · Journal of Clinical Investigation · doi:10.1172/jci3523 · Cited by 988

Functional genomics reveal that the serine synthesis pathway is essential in breast cancer

Possemato, R., Marks, K. M., Shaul, Y. D., Pacold, M. E., Kim, D., Birsoy, K., Sethumadhavan, S., Woo, H.-K., Jang, H. G., Jha, A. K., et al. (2011) · Nature · doi:10.1038/nature10350 · Cited by 1,683

Serine, glycine and one-carbon units: cancer metabolism in full circle

Locasale, J. W. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3557 · Cited by 1,727

Phosphoglycerate dehydrogenase diverts glycolytic flux and contributes to oncogenesis

Locasale, J. W., Grassian, A. R., Melman, T., Lyssiotis, C. A., Mattaini, K. R., Bass, A. J., Heffron, G., Metallo, C. M., Muranen, T., Sharfi, H., et al. (2011) · Nature Genetics · doi:10.1038/ng.890 · Cited by 1,120

Serine starvation induces stress and p53-dependent metabolic remodelling in cancer cells

Maddocks, O. D. K., Berkers, C. R., Mason, S. M., Zheng, L., Blyth, K., Gottlieb, E., & Vousden, K. H. (2013) · Nature · doi:10.1038/nature11743 · Cited by 1,007

Serine and one-carbon metabolism in cancer

Yang, M., & Vousden, K. H. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.81 · Cited by 992

The metabolism of cancer cells during metastasis

Bergers, G., & Fendt, S. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-020-00320-2 · Cited by 974

Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us?

DeBerardinis, R. J., & Thompson, C. B. (2012) · Cell · doi:10.1016/j.cell.2012.02.032 · Cited by 858

Serine is a natural ligand and allosteric activator of pyruvate kinase M2

Chaneton, B., Hillmann, P., Zheng, L., Martin, A. C. L., Maddocks, O. D. K., Chokkathukalam, A., Coyle, J. E., Jankevics, A., Holding, F. P., Vousden, K. H., et al. (2012) · Nature · doi:10.1038/nature11540 · Cited by 661

One-carbon metabolism in cancer

Newman, A. C., & Maddocks, O. D. K. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.118 · Cited by 525

Metabolism of Amino Acids in Cancer

Wei, Z. C., Liu, X., Cheng, C., Yu, W., & Yi, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.603837 · Cited by 456

The importance of serine metabolism in cancer

Mattaini, K. R., Sullivan, M. R., & Heiden, M. G. V. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201604085 · Cited by 423

Pyruvate kinase M2 promotes de novo serine synthesis to sustain mTORC1 activity and cell proliferation

Ye, J., Mancuso, A., Tong, X., Ward, P. S., Fan, J., Rabinowitz, J. D., & Thompson, C. B. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204176109 · Cited by 426

Hypoxia‐inducible factors: coupling glucose metabolism and redox regulation with induction of the breast cancer stem cell phenotype

Semenza, G. L. (2016) · The EMBO Journal · doi:10.15252/embj.201695204 · Cited by 380

Identification of a small molecule inhibitor of 3-phosphoglycerate dehydrogenase to target serine biosynthesis in cancers

Mullarky, E., Lucki, N. C., Beheshti Zavareh, R., Anglin, J. L., Gomes, A. P., Nicolay, B. N., Wong, J. C. Y., Christen, S., Takahashi, H., Singh, P. K., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521548113 · Cited by 333

Dysregulated metabolism contributes to oncogenesis

Hirschey, M. D., DeBerardinis, R. J., Diehl, A. M., Drew, J. E., Frezza, C., Green, M. F., Jones, L. W., Ko, Y. H., Le, A., Lea, M. A., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.10.002 · Cited by 316

Resurgence of Serine: An Often Neglected but Indispensable Amino Acid

Kalhan, S. C., & Hanson, R. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.357194 · Cited by 312

Serine in plants: biosynthesis, metabolism, and functions

Ros, R., Muñoz-Bertomeu, J., & Krueger, S. (2014) · Trends in Plant Science · doi:10.1016/j.tplants.2014.06.003 · Cited by 279

Contribution of serine, folate and glycine metabolism to the ATP, NADPH and purine requirements of cancer cells

Tedeschi, P. M., Markert, E. K., Gounder, M. K., Lin, H., Dvorzhinski, D., Dolfi, S. C., Chan, L. L.-Y., Qiu, J., DiPaola, R. S., Hirshfield, K. M., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.393 · Cited by 265

Metabolic reprogramming in triple-negative breast cancer

Wang, Z., Jiang, Q., & Dong, C. (2020) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2019.0210 · Cited by 248

The Histone H3 Methyltransferase G9A Epigenetically Activates the Serine-Glycine Synthesis Pathway to Sustain Cancer Cell Survival and Proliferation

Ding, J., Li, T., Wang, X., Zhao, E., Choi, J.-H., Yang, L., Zha, Y., Dong, Z., Huang, S., Asara, J. M., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.004 · Cited by 246

Glutamine Metabolism in Cancer

Li, T., & Le, A. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-77736-8_2 · Cited by 242

Targeting amino acid metabolism in cancer growth and anti-tumor immune response

Ananieva, E. A. (2015) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v6.i4.281 · Cited by 203

Small molecule activation of PKM2 in cancer cells induces serine auxotrophy

Kung, C., Hixon, J., Choe, S., Marks, K., Gross, S., Murphy, E., DeLaBarre, B., Cianchetta, G., Sethumadhavan, S., Wang, X., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.07.021 · Cited by 192

Unique Metabolic Adaptations Dictate Distal Organ-Specific Metastatic Colonization

Schild, T., Low, V., Blenis, J., & Gomes, A. P. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.02.001 · Cited by 187

Modeling cancer metabolism on a genome scale

Yizhak, K., Chaneton, B., Gottlieb, E., & Ruppin, E. (2015) · Molecular Systems Biology · doi:10.15252/msb.20145307 · Cited by 187

Bortezomib resistance in multiple myeloma is associated with increased serine synthesis

Zaal, E. A., Wu, W., Jansen, G., Zweegman, S., Cloos, J. J., & Berkers, C. R. (2017) · Cancer & Metabolism · doi:10.1186/s40170-017-0169-9 · Cited by 182

Serine and Functional Metabolites in Cancer

Newman, A. C., & Maddocks, O. D. K. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.05.001 · Cited by 168

Adapt and conquer: Metabolic flexibility in cancer growth, invasion and evasion

Kreuzaler, P. A., Panina, Y., Segal, J., & Yuneva, M. O. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.08.021 · Cited by 170

Targeting cancer metabolism – aiming at a tumour's sweet-spot

Jones, N. P., & Schulze, A. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.12.017 · Cited by 164

PSAT1 is regulated by ATF4 and enhances cell proliferation via the GSK3β/β-catenin/cyclin D1 signaling pathway in ER-negative breast cancer

Gao, S., Ge, A., Xu, S., You, Z., Ning, S., Zhao, Y., & Pang, D. (2017) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-017-0648-4 · Cited by 149

New insights into the correlations between circulating tumor cells and target organ metastasis

Zhan, Q., Liu, B., Situ, X., Luo, Y., Fu, T., Wang, Y., Xie, Z., Ren, L., Zhu, Y. J., He, W., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01725-9 · Cited by 156

Serine deprivation enhances antineoplastic activity of biguanides

Gravel, S.-P., Hulea, L., Toban, N., Birman, E., Blouin, M.-J., Zakikhani, M., Zhao, Y., Topisirovic, I., St-Pierre, J., & Pollak, M. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-2643-t · Cited by 138

Glutamine Metabolism in Cancer

Li, T., Copeland, C., & Le, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-65768-0_2 · Cited by 134

Role of amino acid metabolism in mitochondrial homeostasis

Li, Q., & Hoppe, T. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1127618 · Cited by 129

p73 regulates serine biosynthesis in cancer

Amelio, I., Markert, E. K., Rufini, A., Antonov, A. V., Sayan, B. S., Tucci, P., Agostini, M., Mineo, T. C., Levine, A. J., & Melino, G. (2013) · Oncogene · doi:10.1038/onc.2013.456 · Cited by 126

Pathogenesis and Current Treatment of Osteosarcoma: Perspectives for Future Therapies

Rathore, R., & Tine, B. A. V. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10061182 · Cited by 129

Serine Metabolism: Some Tumors Take the Road Less Traveled

DeBerardinis, R. J. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.004 · Cited by 121

Organ-Specific Cancer Metabolism and Its Potential for Therapy

Elia, I., Schmieder, R., Christen, S., & Fendt, S. (2015) · Handbook of experimental pharmacology · doi:10.1007/164_2015_10 · Cited by 112

In Vivo Evidence for Serine Biosynthesis-Defined Sensitivity of Lung Metastasis, but Not of Primary Breast Tumors, to mTORC1 Inhibition

Rinaldi, G., Pranzini, E., Elsen, J. V., Broekaert, D., Funk, C. M., Planque, M., Doglioni, G., Altea‐Manzano, P., Rossi, M., Geldhof, V., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.027 · Cited by 113

Metabolic changes associated with tumor metastasis, part 2: Mitochondria, lipid and amino acid metabolism

Porporato, P. E., Payen, V. L., Baselet, B., & Sonveaux, P. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2100-2 · Cited by 115

High-throughput RNAi screening for novel modulators of vimentin expression identifies MTHFD2 as a regulator of breast cancer cell migration and invasion

Lehtinen, L., Ketola, K., Mäkelä, R., Mpindi, J.-P., Viitala, M., Kallioniemi, O., & Iljin, K. (2012) · Oncotarget · doi:10.18632/oncotarget.756 · Cited by 109

SHMT2-mediated mitochondrial serine metabolism drives 5-FU resistance by fueling nucleotide biosynthesis

Pranzini, E., Pardella, E., Muccillo, L., Leo, A., Nesi, I., Santi, A., Parri, M., Zhang, T., Uribe, A. H., Lottini, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111233 · Cited by 106

Phosphoglycerate dehydrogenase promotes pancreatic cancer development by interacting with eIF4A1 and eIF4E

Ma, X., Li, B., Liu, J., Fu, Y., & Luo, Y. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-019-1053-y · Cited by 97

Serine and one-carbon metabolism, a bridge that links mTOR signaling and DNA methylation in cancer

Zeng, J., Wu, W. K. K., Wang, H., & Li, X. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104352 · Cited by 96

L-serine synthesis via the phosphorylated pathway in humans

Murtas, G., Marcone, G. L., Sacchi, S., & Pollegioni, L. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03574-z · Cited by 89

Genetically-defined metabolic reprogramming in cancer

Mullen, A. R., & DeBerardinis, R. J. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.06.009 · Cited by 90

Serine Biosynthesis with One Carbon Catabolism and the Glycine Cleavage System Represents a Novel Pathway for ATP Generation

Vázquez, A., Markert, E. K., & Oltvai, Z. N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025881 · Cited by 88

Identification of MicroRNAs Inhibiting TGF-β-Induced IL-11 Production in Bone Metastatic Breast Cancer Cells

Pollari, S., Leivonen, S., Perälä, M., Fey, V., Käkönen, S.-M., & Kallioniemi, O. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037361 · Cited by 85

Increased Expression of PHGDH and Prognostic Significance in Colorectal Cancer

Jia, X.-Q., Zhang, S., Zhu, H., Wang, W., Zhu, J., Wang, X., & Qiang, J. (2016) · Translational Oncology · doi:10.1016/j.tranon.2016.03.006 · Cited by 85

Identification of molecular marker associated with ovarian cancer prognosis using bioinformatics analysis and experiments

Zheng, M., Li, X., Hu, Y., Dong, H., Gou, R., Nie, X., Liu, Q., Hao, Y., Liu, J., & Lin, B. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.27926 · Cited by 81

Bioinformatics analysis of the serine and glycine pathway in cancer cells

Antonov, A. V., Agostini, M., Morello, M., Minieri, M., Melino, G., & Amelio, I. (2014) · Oncotarget · doi:10.18632/oncotarget.2668 · Cited by 82

The Phosphorylated Pathway of Serine Biosynthesis Is Essential Both for Male Gametophyte and Embryo Development and for Root Growth in Arabidopsis

Cascales‐Miñana, B., Muñoz‐Bertomeu, J., Flores‐Tornero, M., Anoman, A. D., Pertusa, J., Alaiz, M., Osorio, S., Fernie, A. R., Segura, J., & Ros, R. (2013) · The Plant Cell · doi:10.1105/tpc.113.112359 · Cited by 82

Metabolomics of gastric cancer metastasis detected by gas chromatography and mass spectrometry

Chen, J. (2010) · World Journal of Gastroenterology · doi:10.3748/wjg.v16.i46.5874 · Cited by 78

IDH3α regulates one-carbon metabolism in glioblastoma

May, J., Kouri, F. M., Hurley, L., Liu, J., Tommasini-Ghelfi, S., Ji, Y., Gao, P., Calvert, A. E., Lee, A., Chandel, N. S., et al. (2019) · Science Advances · doi:10.1126/sciadv.aat0456 · Cited by 76

High Expression of PHGDH Predicts Poor Prognosis in Non–Small Cell Lung Cancer

Zhu, J., Ma, J., Wang, X., Ma, T., Zhang, S., Wang, W., Zhou, X., & Shi, J. (2016) · Translational Oncology · doi:10.1016/j.tranon.2016.08.003 · Cited by 75

Metabolism in cancer metastasis: bioenergetics, biosynthesis, and beyond

Teoh, S. T., & Lunt, S. Y. (2017) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1406 · Cited by 77

Links between cancer metabolism and cisplatin resistance

Cocetta, V., Ragazzi, E., & Montopoli, M. (2020) · International review of cytology · doi:10.1016/bs.ircmb.2020.01.005 · Cited by 77

Serine Synthesis Helps Hypoxic Cancer Stem Cells Regulate Redox

Samanta, D., & Semenza, G. L. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-1730 · Cited by 76

α-Ketothioamide Derivatives: A Promising Tool to Interrogate Phosphoglycerate Dehydrogenase (PHGDH)

Ravez, S., Corbet, C., Spillier, Q., Dutu, A., Robin, A. D., Mullarky, E., Cantley, L. C., Féron, O., & Frédérick, R. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01166 · Cited by 72

Dietary restriction of amino acids for Cancer therapy

Kang, J. (2020) · Nutrition & Metabolism · doi:10.1186/s12986-020-00439-x · Cited by 77

Acetylation stabilizes phosphoglycerate dehydrogenase by disrupting the interaction of E3 ligase RNF5 to promote breast tumorigenesis

Wang, C., Wan, X., Yu, T., Huang, Z., Shen, C., Qi, Q., Xiang, S., Chen, X., Arbely, E., Ling, Z.-Q., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108021 · Cited by 70

Glycine decarboxylase maintains mitochondrial protein lipoylation to support tumor growth

Mukha, D., Fokra, M., Feldman, A., Sarvin, B., Sarvin, N., Nevo-Dinur, K., Besser, E., Hallo, E., Aizenshtein, E., Schug, Z. T., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.04.006 · Cited by 69

Review of metabolic pathways activated in cancer cells as determined through isotopic labeling and network analysis

Dong, W., Keibler, M. A., & Stephanopoulos, G. N. (2017) · Metabolic Engineering · doi:10.1016/j.ymben.2017.02.002 · Cited by 69

Hotspot SF3B1 mutations induce metabolic reprogramming and vulnerability to serine deprivation

Dalton, W. B., Helmenstine, E., Walsh, N., Gondek, L. P., Kelkar, D. S., Read, A., Natrajan, R., Christenson, E. S., Román, B., Das, S., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci125022 · Cited by 70

Synergistic Simvastatin and Metformin Combination Chemotherapy for Osseous Metastatic Castration-Resistant Prostate Cancer

Babcook, M. A., Shukla, S., Fu, P., Vazquez, E. J., Puchowicz, M. A., Molter, J. P., Oak, C. Z., MacLennan, G. T., Flask, C. A., Lindner, D. J., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0451 · Cited by 68

Metabolomic alterations in invasive ductal carcinoma of breast: A comprehensive metabolomic study using tissue and serum samples

More, T. H., RoyChoudhury, S., Christie, J., Taunk, K., Mane, A. D., Santra, M. K., Chaudhury, K., & Rapole, S. (2017) · Oncotarget · doi:10.18632/oncotarget.23626 · Cited by 68

Functional Characterization of the Plastidial 3-Phosphoglycerate Dehydrogenase Family in Arabidopsis

Toujani, W., Muñoz‐Bertomeu, J., Flores‐Tornero, M., Rosa‐Téllez, S., Anoman, A. D., Alseekh, S., Fernie, A. R., & Ros, R. (2013) · PLANT PHYSIOLOGY · doi:10.1104/pp.113.226720 · Cited by 71

Selective loss of phosphoserine aminotransferase 1 (PSAT1) suppresses migration, invasion, and experimental metastasis in triple negative breast cancer

Metcalf, S. A., Dougherty, S. M., Kruer, T. L., Hasan, N., Biyik‐Sit, R., Reynolds, L., & Clem, B. F. (2019) · Clinical & Experimental Metastasis · doi:10.1007/s10585-019-10000-7 · Cited by 66

Inhibition of 3-phosphoglycerate dehydrogenase (PHGDH) by indole amides abrogates de novo serine synthesis in cancer cells

Mullarky, E., Xu, J., Robin, A. D., Huggins, D. J., Jennings, A. J., Noguchi, N., Olland, A. M., Damodharan, L., Miller, M. J., Tomita, D., et al. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2019.07.011 · Cited by 63

Phosphoglycerate dehydrogenase promotes proliferation and bortezomib resistance through increasing reduced glutathione synthesis in multiple myeloma

Wu, X., Xia, J., Zhang, J., Zhu, Y., Wu, Y., Guo, J., Chen, S., Lei, Q., Meng, B., Kuang, C., et al. (2020) · British Journal of Haematology · doi:10.1111/bjh.16503 · Cited by 63

The PHGDH enigma: Do cancer cells only need serine or also a redox modulator?

Li, A. M., & Ye, J. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.01.036 · Cited by 65

Deciphering metabolic rewiring in breast cancer subtypes

Ogrodzinski, M. P., Bernard, J. J., & Lunt, S. Y. (2017) · Translational research · doi:10.1016/j.trsl.2017.07.004 · Cited by 67

Serine and Metabolism Regulation: A Novel Mechanism in Antitumor Immunity and Senescence

Wu, Q., Chen, X., Li, J., & Sun, S. (2020) · Aging and Disease · doi:10.14336/ad.2020.0314 · Cited by 65

Oxidative Stress in Breast Cancer: A Biochemical Map of Reactive Oxygen Species Production

Bel’skaya, L. V., & Dyachenko, E. I. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46050282 · Cited by 71

Alcohol and DNA Methylation: An Epigenome-Wide Association Study in Blood and Normal Breast Tissue

Wilson, L. E., Xu, Z., Harlid, S., White, A. J., Troester, M. A., Sandler, D. P., & Taylor, J. A. (2019) · American Journal of Epidemiology · doi:10.1093/aje/kwz032 · Cited by 62

MicroRNA-340 Inhibits Esophageal Cancer Cell Growth and Invasion by Targeting Phosphoserine Aminotransferase 1

Yan, S., Jiang, H., Fang, S., Yin, F., Wang, Z., Jia, Y., Sun, X., Wu, S., Jiang, T., & Mao, A. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000430361 · Cited by 60

Metabolism and immunity in breast cancer

Zhang, D., Xu, X., & Ye, Q. (2020) · Frontiers of Medicine · doi:10.1007/s11684-020-0793-6 · Cited by 58

Proliferation and tissue remodeling in cancer: the hallmarks revisited

Markert, E. K., Levine, A. J., & Vázquez, A. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.140 · Cited by 57

Overexpression of PSAT1 promotes metastasis of lung adenocarcinoma by suppressing the IRF1-IFNγ axis

Chan, Y.-C., Chang, Y., Chuang, H.-H., Yang, Y., Lin, Y., Huang, M.-S., Hsiao, M., Yang, C., & Hua, K. (2020) · Oncogene · doi:10.1038/s41388-020-1160-4 · Cited by 58

Oncology Therapeutics Targeting the Metabolism of Amino Acids

Muhammad, N., Lee, H. M., & Kim, J. (2020) · Cells · doi:10.3390/cells9081904 · Cited by 59

Metabolomics of Breast Cancer: A Review

Subramani, R., Poudel, S., Smith, K. D., Estrada, A., & Lakshmanaswamy, R. (2022) · Metabolites · doi:10.3390/metabo12070643 · Cited by 59

Quantitative Proteomic Analysis Identifies CPNE3 as a Novel Metastasis-promoting Gene in NSCLC

Lin, H., Zhang, F., Qin, G., Yu, T., Cui, Y., Liu, X., Li, J., Yan, M., Liu, L., He, X., et al. (2013) · Journal of Proteome Research · doi:10.1021/pr400273z · Cited by 56

Amino acid metabolism in skeletal cells

Devignes, C.-S., Carmeliet, G., & Stegen, S. (2022) · Bone Reports · doi:10.1016/j.bonr.2022.101620 · Cited by 55

Metabolic compensation activates pro-survival mTORC1 signaling upon 3-phosphoglycerate dehydrogenase inhibition in osteosarcoma

Rathore, R., Caldwell, K. E., Schutt, C. R., Brashears, C. B., Prudner, B. C., Ehrhardt, W. R., Leung, C. H., Lin, H. Y., Daw, N. C., Beird, H. C., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108678 · Cited by 52

Hypoxia and Metabolism in Cancer

Bensaad, K., & Harris, A. L. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-5915-6_1 · Cited by 49

3-Phosphoglycerate dehydrogenase: a potential target for cancer treatment

Li, M., Wu, C., Yang, Y., Zheng, M., Yu, S., Wang, J., Chen, L., & Li, H. (2021) · Cellular Oncology · doi:10.1007/s13402-021-00599-9 · Cited by 51

Menin regulates the serine biosynthetic pathway in Ewing sarcoma

Svoboda, L. K., Teh, S. S. K., Sud, S., Kerk, S. A., Zebolsky, A. L., Treichel, S., Thomas, D. G., Halbrook, C. J., Lee, H., Kremer, D. M., et al. (2018) · The Journal of Pathology · doi:10.1002/path.5085 · Cited by 52

PHGDH is required for germinal center formation and is a therapeutic target in MYC-driven lymphoma

D’Avola, A., Legrave, N. M., Tajan, M., Chakravarty, P., Shearer, R. L., King, H. W., Kluckova, K., Cheung, E. C., Clear, A. J., Gunawan, A. S., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci153436 · Cited by 47

Mitochondrial functions and melatonin: a tour of the reproductive cancers

Chuffa, L. G. D. A., Seiva, F. R. F., Cucielo, M. S., Silveira, H. S., Reiter, R. J., & Lupi, L. A. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2963-0 · Cited by 52

Mechanisms of Organ-Specific Metastasis of Breast CancerPreprint

Nolan, E., Kang, Y., & Malanchi, I. (2023) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041326 · Cited by 52

PSPH Mediates the Metastasis and Proliferation of Non-small Cell Lung Cancer through MAPK Signaling Pathways

Liao, L., Ge, M., Zhan, Q., Huang, R., Ji, X., Liang, X., & Zhou, X. (2019) · International Journal of Biological Sciences · doi:10.7150/ijbs.29203 · Cited by 48

SHMT2 promotes cell viability and inhibits ROS-dependent, mitochondrial-mediated apoptosis via the intrinsic signaling pathway in bladder cancer cells

Zhang, Y., Liu, Z., Wang, X., Jian, H., Xiao, H., & Wen, T. (2022) · Cancer Gene Therapy · doi:10.1038/s41417-022-00470-5 · Cited by 47

Mitochondria preserve an autarkic one-carbon cycle to confer growth-independent cancer cell migration and metastasis

Kiweler, N., Delbrouck, C., Pozdeev, V. I., Neises, L., Soriano‐Baguet, L., Eiden, K., Xian, F., Benzarti, M., Haase, L., Koncina, E., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30363-y · Cited by 46

Amino Acids in Cancer and Cachexia: An Integrated View

Ragni, M., Fornelli, C., Nisoli, E., & Penna, F. (2022) · Cancers · doi:10.3390/cancers14225691 · Cited by 48

l-3-Phosphoserine phosphatase (PSPH) regulates cutaneous squamous cell carcinoma proliferation independent of l-serine biosynthesis

Bachelor, M. A., Lu, Y., & Owens, D. M. (2011) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2011.06.001 · Cited by 46

Analysis of gene expression during mineralization of cultured human periodontal ligament cells

Choi, H.-D., Noh, W.-C., Park, J., Lee, J.-M., & Suh, J. (2011) · Journal of Periodontal & Implant Science · doi:10.5051/jpis.2011.41.1.30 · Cited by 46

Cause and effect of microenvironmental acidosis on bone metastases

Avnet, S., Pompo, G. D., Lemma, S., & Baldini, N. (2019) · Cancer and Metastasis Reviews · doi:10.1007/s10555-019-09790-9 · Cited by 46

Therapeutic Potential of Tumor Metabolic Reprogramming in Triple-Negative Breast Cancer

Munkácsy, G., Santarpia, L., & Győrffy, B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24086945 · Cited by 46

A world of sphingolipids and glycolipids in the brain —Novel functions of simple lipids modified with glucose—

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Heparin-like Polysaccharides Reduce Osteolytic Bone Destruction and Tumor Growth in a Mouse Model of Breast Cancer Bone Metastasis

Pollari, S., Käkönen, R. S., Mohammad, K. S., Rissanen, J. P., Halleen, J. M., Wärri, A. M., Nissinen, L. M., Pihlavisto, M., Marjamäki, A., Perälä, M., et al. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0482 · Cited by 44

Dissecting the molecular mechanisms of breast cancer bone metastasis for therapeutic targeting

Pollari, S. (2012) · UTUPub (University of Turku)

Abstract 5713: Reprogramming of serine metabolism during breast cancer progression

Li, A. M., Ducker, G. S., Li, Y., Seoane, J. A., Xiao, Y., Melemenidis, S., Zhou, Y., Liu, L., Vanharanta, S., Graves, E. E., et al. (2020) · Cancer Research · doi:10.1158/1538-7445.am2020-5713

Abstract 5712: Nutrient scarcity confers breast cancer brain metastasis sensitivity to serine synthesis pathway inhibition

Ngo, B., Kim, E., Doll, S., Bustraan, S., Luengo, A., Davidson, S. M., Ali, A., Ferraro, G. B., Kang, D. S., Ni, J., et al. (2020) · Cancer Research · doi:10.1158/1538-7445.am2020-5712 · Cited by 1

Metabolic Profiling Reveals a Dependency of Human Metastatic Breast Cancer on Mitochondrial Serine and One-Carbon Unit Metabolism

Li, A. M., Ducker, G. S., Li, Y., Seoane, J. A., Xiao, Y., Melemenidis, S., Zhou, Y., Liu, L., Vanharanta, S., Graves, E. E., et al. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0606 · Cited by 84

Abstract 1435: Investigation of phosphoserine aminotransferase 1: Its role in breast cancer progression

Metcalf, S. A., Kruer, T. L., Wittliff, J. L., Klinge, C. M., & Clem, B. F. (2018) · Cancer Research · doi:10.1158/1538-7445.am2018-1435 · Cited by 1