HSD17B4 methylation enhances glucose dependence of BT-474 breast cancer cells and increases lapatinib sensitivity
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H. Mukai | T. Ushijima | N. Hattori | S. Yamashita | C. Takeuchi | H. Takeshima | Yu-Yu Liu | Nobuaki Arai | S. Fujii | T. Ebata | Haruhiko Kondo | Hideyuki Takeshima
[1] N. Zhou,et al. Characterization of glucose metabolism in breast cancer to guide clinical therapy , 2022, Frontiers in Surgery.
[2] J. Clohessy,et al. PI3K drives the de novo synthesis of coenzyme A from vitamin B5 , 2022, Nature.
[3] Zohreh Hoseinkhani,et al. Cell line-directed breast cancer research based on glucose metabolism status. , 2021, Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie.
[4] A. Otto. Metabolic Constants and Plasticity of Cancer Cells in a Limiting Glucose and Glutamine Microenvironment—A Pyruvate Perspective , 2020, Frontiers in Oncology.
[5] Takeshi Yamaguchi,et al. Multi-omics analyses identify HSD17B4 methylation-silencing as a predictive and response marker of HER2-positive breast cancer to HER2-directed therapy , 2020, Scientific Reports.
[6] T. Shien,et al. Omitting surgery for early breast cancer showing clinical complete response to primary systemic therapy. , 2020, Japanese journal of clinical oncology.
[7] Chuanying Xu,et al. A novel anti-HER2 antibody GB235 reverses Trastuzumab resistance in HER2-expressing tumor cells in vitro and in vivo , 2020, Scientific Reports.
[8] S. McGee,et al. A systematic flux analysis approach to identify metabolic vulnerabilities in human breast cancer cell lines , 2019, Cancer & Metabolism.
[9] G. Hoxhaj,et al. The PI3K–AKT network at the interface of oncogenic signalling and cancer metabolism , 2019, Nature Reviews Cancer.
[10] Zhihui Zhu,et al. Ceramide regulates interaction of Hsd17b4 with Pex5 and function of peroxisomes. , 2019, Biochimica et biophysica acta. Molecular and cell biology of lipids.
[11] Lauren L. Ritterhouse,et al. Seven-Year Follow-Up Analysis of Adjuvant Paclitaxel and Trastuzumab Trial for Node-Negative, Human Epidermal Growth Factor Receptor 2-Positive Breast Cancer. , 2019, Journal of clinical oncology : official journal of the American Society of Clinical Oncology.
[12] Qiao Wu,et al. Nuclear Receptor Nur77 Facilitates Melanoma Cell Survival under Metabolic Stress by Protecting Fatty Acid Oxidation. , 2018, Molecular cell.
[13] F. Filipp,et al. Metabolic profiling of triple-negative breast cancer cells reveals metabolic vulnerabilities , 2017, Cancer & metabolism.
[14] D. Chitale,et al. Bioenergetic Adaptations in Chemoresistant Ovarian Cancer Cells , 2017, Scientific Reports.
[15] H. Kuerer,et al. Nonoperative Management for Invasive Breast Cancer After Neoadjuvant Systemic Therapy: Conceptual Basis and Fundamental International Feasibility Clinical Trials , 2017, Annals of Surgical Oncology.
[16] Takeshi Yamaguchi,et al. Pathological complete response of HER2-positive breast cancer to trastuzumab and chemotherapy can be predicted by HSD17B4 methylation , 2017, Oncotarget.
[17] A. Schneeweiss,et al. Dual HER2-blockade with pertuzumab and trastuzumab in HER2-positive early breast cancer: a subanalysis of data from the randomized phase III GeparSepto trial , 2016, Annals of oncology : official journal of the European Society for Medical Oncology.
[18] Kristine R Broglio,et al. Association of Pathologic Complete Response to Neoadjuvant Therapy in HER2-Positive Breast Cancer With Long-Term Outcomes: A Meta-Analysis. , 2016, JAMA oncology.
[19] L. Thompson,et al. α-linolenic acid and docosahexaenoic acid, alone and combined with trastuzumab, reduce HER2-overexpressing breast cancer cell growth but differentially regulate HER2 signaling pathways , 2015, Lipids in Health and Disease.
[20] A. Kihara,et al. Metabolism of Very Long-Chain Fatty Acids: Genes and Pathophysiology , 2014, Biomolecules & therapeutics.
[21] Pier Paolo Pandolfi,et al. Cancer metabolism: fatty acid oxidation in the limelight , 2013, Nature Reviews Cancer.
[22] A. Kihara. Very long-chain fatty acids: elongation, physiology and related disorders. , 2012, Journal of biochemistry.
[23] Tyler J Moss,et al. The glucose-deprivation network counteracts lapatinib-induced toxicity in resistant ErbB2-positive breast cancer cells , 2012, Molecular systems biology.
[24] Valerie Speirs,et al. Choosing the right cell line for breast cancer research , 2011, Breast Cancer Research.
[25] Wen-Lin Kuo,et al. A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes. , 2006, Cancer cell.
[26] N. Spector,et al. Combining lapatinib (GW572016), a small molecule inhibitor of ErbB1 and ErbB2 tyrosine kinases, with therapeutic anti-ErbB2 antibodies enhances apoptosis of ErbB2-overexpressing breast cancer cells , 2005, Oncogene.
[27] R. Deberardinis,et al. The glucose dependence of Akt-transformed cells can be reversed by pharmacologic activation of fatty acid β-oxidation , 2005, Oncogene.
[28] K. Inoki,et al. TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival , 2003, Cell.
[29] P. Hammerman,et al. Akt-Directed Glucose Metabolism Can Prevent Bax Conformation Change and Promote Growth Factor-Independent Survival , 2003, Molecular and Cellular Biology.
[30] C. J. Lewis,et al. Identification and expression of mammalian long-chain PUFA elongation enzymes , 2002, Lipids.
[31] H. Sprecher,et al. Elongation of long-chain fatty acids. , 2004, Progress in lipid research.