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Thematische Bibliographien / Breas cancer resistance protein

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Auswahl der wissenschaftlichen Literatur zum Thema „Breas cancer resistance protein“

Autor: Grafiati

Veröffentlicht am 28. Juni 2021

Zuletzt aktualisiert am 17. Februar 2022

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Zeitschriftenartikel zum Thema "Breas cancer resistance protein"

1

Horak, I. R., D. S. Gerashchenko und L. B. Drobot. „Adaptor protein Ruk/CIN85 modulates resistance to doxorubicin of murine 4T1 breast cancer cells“. Ukrainian Biochemical Journal 90, Nr. 3 (25.06.2018): 94–100. http://dx.doi.org/10.15407/ubj90.03.094.

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Qadir, Misbah, Kieran L. O’Loughlin, Nicole A. Williamson, Hans Minderman und Maria R. Baer. „Cyclosporine A Modulates the Multidrug Resistance Proteins P-Glycoprotein, Multidrug Resistance Protein, Breast Cancer Resistance Protein and Lung Resistance Protein.“ Blood 104, Nr. 11 (16.11.2004): 1180. http://dx.doi.org/10.1182/blood.v104.11.1180.1180.

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Abstract Multidrug resistance (MDR) mediated by the ATP-binding cassette proteins P-glycoprotein (Pgp), multidrug resistance protein (MRP-1), breast cancer resistance protein (BCRP) and the vault protein lung resistance protein (LRP) is implicated in treatment failure in acute myeloid leukemia (AML). Pgp, MRP-1 and BCRP mediate energy-dependent cellular drug efflux, while LRP blocks cytoplasmic-nuclear drug transport. MDR modulators are non-cytotoxic drugs that block the activity of MDR proteins. In clinical trials, the Pgp modulator cyclosporine A (CsA) improved treatment outcome in AML, while its non-immunosuppressive, non-nephrotoxic analogue PSC-833 has not, despite being a potent Pgp modulator in preclinical models. CsA is known to also modulate MRP-1, and we hypothesized that a broad spectrum of MDR modulation might contribute to its clinical efficacy. We studied the effects of CsA and PSC-833 on in vitro drug uptake, retention and cytotoxicity in drug-selected and transfected resistant cell lines overexpressing Pgp, MRP-1 or BCRP, and on nuclear-cytoplasmic drug distribution and cytotoxicity in cell lines overexpressing LRP. Cellular drug content was measured by flow cytometry, and nuclear-cytoplasmic drug distribution was assessed by confocal microscopy. CsA enhanced uptake and retention of the substrate drug mitoxantrone in cells overexpressing Pgp (HL60/VCR), MRP-1 (HL60/ADR) and BCRP (8226/MR20) and increased cytotoxicity 7-, 4- and 4-fold, respectively. Moreover, CsA increased the nuclear content of doxorubicin in 8226/MR20 cells, which co-express LRP with BCRP, and increased doxorubicin cytotoxicity 12-fold. The effect of CsA on nuclear drug content and cytotoxicity in 8226/MR20 cells occurred without an effect on cellular doxorubicin content, consistent with the fact that 8226/MR20 cells co-express wild type BCRP (BCRPR482), which does not efflux doxorubicin. Moreover the BCRP modulator fumitremorgin C had no effect on 8226/MR20 content, nuclear uptake nor cytotoxicity of doxorubicin. CsA also enhanced nuclear doxorubicin content in a second cell line with LRP-mediated resistance, HT1080/DR4. PSC-833 enhanced mitoxantrone retention and cytotoxicity in cells overexpressing Pgp, but, in contrast to CsA, had no effect on mitoxantrone uptake, retention nor cytotoxicity in cells expressing MRP-1 nor BCRP, and had no effect on doxorubicin nuclear content nor cytotoxicity in cells expressing LRP. Thus CsA is a broad-spectrum MDR modulator, with activity against Pgp, MRP-1, BCRP and LRP, while PSC-833 only modulates Pgp. The broad-spectrum activity of CsA may contribute to its clinical efficacy. These findings support identification and testing of other broad-spectrum MDR modulators.

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3

McGrath, Eoghan, Susan Logue, Katarzyna Mnich, Shane Deegan, Richard Jäger, Adrienne Gorman und Afshin Samali. „The Unfolded Protein Response in Breast Cancer“. Cancers 10, Nr. 10 (21.09.2018): 344. http://dx.doi.org/10.3390/cancers10100344.

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In 2018, in the US alone, it is estimated that 268,670 people will be diagnosed with breast cancer, and that 41,400 will die from it. Since breast cancers often become resistant to therapies, and certain breast cancers lack therapeutic targets, new approaches are urgently required. A cell-stress response pathway, the unfolded protein response (UPR), has emerged as a promising target for the development of novel breast cancer treatments. This pathway is activated in response to a disturbance in endoplasmic reticulum (ER) homeostasis but has diverse physiological and disease-specific functions. In breast cancer, UPR signalling promotes a malignant phenotype and can confer tumours with resistance to widely used therapies. Here, we review several roles for UPR signalling in breast cancer, highlighting UPR-mediated therapy resistance and the potential for targeting the UPR alone or in combination with existing therapies.

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4

Staud, Frantisek, und Petr Pavek. „Breast cancer resistance protein (BCRP/ABCG2)“. International Journal of Biochemistry & Cell Biology 37, Nr. 4 (April 2005): 720–25. http://dx.doi.org/10.1016/j.biocel.2004.11.004.

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5

Wang, Ming-Yang, Hsin-Yi Huang, Yao-Lung Kuo, Chiao Lo, Hung-Yu Sun, Yu-Jhen Lyu, Bo-Rong Chen, Jie-Ning Li und Pai-Sheng Chen. „TARBP2-Enhanced Resistance during Tamoxifen Treatment in Breast Cancer“. Cancers 11, Nr. 2 (12.02.2019): 210. http://dx.doi.org/10.3390/cancers11020210.

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Tamoxifen is the most widely used hormone therapy in estrogen receptor-positive (ER+) breast cancer, which accounts for approximately 70% of all breast cancers. Although patients who receive tamoxifen therapy benefit with respect to an improved overall prognosis, resistance and cancer recurrence still occur and remain important clinical challenges. A recent study identified TAR (HIV-1) RNA binding protein 2 (TARBP2) as an oncogene that promotes breast cancer metastasis. In this study, we showed that TARBP2 is overexpressed in hormone therapy-resistant cells and breast cancer tissues, where it enhances tamoxifen resistance. Tamoxifen-induced TARBP2 expression results in the desensitization of ER+ breast cancer cells. Mechanistically, tamoxifen post-transcriptionally stabilizes TARBP2 protein through the downregulation of Merlin, a TARBP2-interacting protein known to enhance its proteasomal degradation. Tamoxifen-induced TARBP2 further stabilizes SOX2 protein to enhance desensitization of breast cancer cells to tamoxifen, while similar to TARBP2, its induction in cancer cells was also observed in metastatic tumor cells. Our results indicate that the TARBP2-SOX2 pathway is upregulated by tamoxifen-mediated Merlin downregulation, which subsequently induces tamoxifen resistance in ER+ breast cancer.

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JIA, P., S. WU, F. LI, Q. XU, M. WU, G. CHEN, G. LIAO et al. „Breast cancer resistance protein-mediated topotecan resistance in ovarian cancer cells“. International Journal of Gynecological Cancer 15, Nr. 6 (November 2005): 1042–48. http://dx.doi.org/10.1111/j.1525-1438.2005.00260.x.

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7

YUAN, Jian-Hui, Jin-Quan CHENG, Long-Yuan JIANG, Wei-Dong JI, Liang-Feng GUO, Jian-Jun LIU, Xing-Yun XU, Jing-Song HE, Xian-Ming WANG und Zhi-Xiong ZHUANG. „Breast Cancer Resistance Protein Expression and 5-Fluorouracil Resistance“. Biomedical and Environmental Sciences 21, Nr. 4 (August 2008): 290–95. http://dx.doi.org/10.1016/s0895-3988(08)60044-6.

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8

Natarajan, Karthika, Yi Xie, Maria R. Baer und Douglas D. Ross. „Role of breast cancer resistance protein (BCRP/ABCG2) in cancer drug resistance“. Biochemical Pharmacology 83, Nr. 8 (April 2012): 1084–103. http://dx.doi.org/10.1016/j.bcp.2012.01.002.

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9

WU, Xin-Gang, Shu-Bin PENG und Qian HUANG. „Transcriptional regulation of breast cancer resistance protein“. Hereditas (Beijing) 34, Nr. 12 (24.12.2012): 1529–36. http://dx.doi.org/10.3724/sp.j.1005.2012.01529.

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10

Nooter, Kees, Guy Brutel de la Riviere, Jan Klijn, Gerrit Stoter und John Foekens. „Multidrug resistance protein in recurrent breast cancer“. Lancet 349, Nr. 9069 (Juni 1997): 1885–86. http://dx.doi.org/10.1016/s0140-6736(05)63876-7.

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Dissertationen zum Thema "Breas cancer resistance protein"

1

Juvale, Kapil [Verfasser]. „Development of New Breast Cancer Resistance Protein Inhibitors / Kapil Juvale“. Bonn : Universitäts- und Landesbibliothek Bonn, 2013. http://d-nb.info/1044971266/34.

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Urfali, Cagri. „Reversal Of Breast Cancer Resistance Protein Mediated Multidrug Resistance In Mcf-7 Breast Adenocarcinoma Cell Line“. Master's thesis, METU, 2012. http://etd.lib.metu.edu.tr/upload/12614062/index.pdf.

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Resistance to various chemotherapeutic agents is a major problem in success of cancer chemotherapy. One of the primary reasons of development of multidrug resistance (MDR) is the overexpression of ATP binding cassette (ABC) transporter proteins. Breast cancer resistance protein (BCRP) belongs to ABC transporter family and encoded by ABCG2 gene. BCRP is mainly expressed in MDR1 (P-glycoprotein) lacking breast cancer cells. Overexpression of BCRP leads to efflux of chemotherapeutic agents at higher rates, therefore, decreased levels of intracellular drug accumulation. Despite the fact that several chemical modulators claim to restore BCRP-mediated increased drug efflux, these modulators were shown to display various side effects, precluding their clinical use. Therefore, to reverse BCRPmediated MDR phenotype by a modulator with minimum cytotoxicity may increase clinical benefits and minimize side effects.

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Mumin, Dk Nuramalina Hafizah Pg Hj. „Acquired resistance to HSP90 inhibition in triple-negative breast cancer“. Thesis, University of Oxford, 2016. https://ora.ox.ac.uk/objects/uuid:d99dfe58-c147-4086-a82d-f10825c3cf87.

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Heat shock protein 90 (HSP90), a conserved molecular chaperone, has become a potential molecular target for cancer therapeutics. HSP90 inhibition (HSP90i) causes inhibition of several oncogenic pathways simultaneously and leads to anti-cancer activities in multiple cancers including in triple-negative breast cancer (TNBC). TNBC is a subtype of breast cancer with poor prognosis and lack of approved targeted therapies. Although HSP90i has shown promising initial clinical data, resistance to HSP90i can still arise in TNBC patients and its resistance mechanisms are not yet understood. In this study, using an in vitro system, we report for the first time the isolation of TNBC cells with acquired resistance to HSP90i. Proteome and whole transcriptome profiling, and a bioactive small molecule screen were performed to identify the molecular basis of resistance to HSP90i and potential therapeutic approaches to overcome acquired resistance to HSP90i in TNBC cells. Two independent HSP90i-resistant clones were acquired through prolonged exposure of a TNBC cell line (Hs578T) to HSP90i. The clones showed significant resistance to HSP90i, notably to resorcinol-based HSP90i. The HSP90i-resistant clones also shared genomic sequence variants, suggesting a pre-existing population of resistant cells within the parental cells. We demonstrate that upregulated expression of UGT1A9, possibly due to an increased intrinsic oxidative stress, is associated with acquired resistance to resorcinol-based HSP90i in TNBC cells, and sensitivity to HSP90i can be restored with a competitive inhibitor of UGT1A9. The HSP90i-resistant clones also exhibited slower growth and upregulated IL6- mediated JAK2-STAT3 survival signalling pathway, which might contribute to the crossresistance to chemotherapeutics and other targeted therapies seen in the clones. Finally, we demonstrate that inhibition of JAK2-STAT3 signalling pathway is able to increase the cytotoxic effects of HSP90i to TNBC cells. We conclude that by using in vitro assays, we are able to identify potential mechanisms of acquired resistance to HSP90i in TNBC cells. We propose that expression of UGT1A9 or STAT3 might be a potential biomarker of sensitivity to HSP90i in TNBC cells. A combined inhibition of HSP90 and JAK2 might be a potential therapeutic approach for the development of effective targeted therapies in TNBC patients.

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Zhang, Yi. „Potential impact of breast cancer resistance protein on drug disposition during pregnancy /“. Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/7970.

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5

Rainey, Jenna. „The Regulation of Multidrug Resistance Phosphoglycoprotein (MDR1/P-gp) and Breast Cancer Resistance Protein (BCRP) in the Human Placenta“. Thèse, Université d'Ottawa / University of Ottawa, 2011. http://hdl.handle.net/10393/19961.

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Multidrug resistance phosphoglycoprotein (MDR1/P-gp) and breast cancer resistance protein (BCRP) were first isolated in chemoresistant cancer cells and have since been found in a variety of normal tissue, including the placenta. The potential function of MDR1/P-gp and BCRP in the human placenta is to protect the fetus from maternally circulating endogenous steroids and hormones, therapeutic drugs and toxins. The objective of this study was to examine the role of maternal steroids in the regulation of MDR1/P-gp and BCRP in the human placenta. Trophoblast cells were isolated from term placenta tissues and immunohistochemistry, western blot analysis and transport studies were used to determine the effect of maternal steroids on MDR1/P-gp and BCRP regulation. Maternal steroids, present at high concentrations in maternal serum, did not have an effect on BCRP in human syncytiotrophoblast. Estrogen and progesterone did not alter MDR1/P-gp levels in human syncytiotrophoblast, but cortisol significantly decreased MDR1/P-gp levels.

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Pick, Anne-Kathrin [Verfasser]. „Funktionelle Untersuchungen des ABCTransporters Breast Cancer Resistance Protein (BCRP) / Anne-Katrin Pick. Mathematisch-Naturwissenschaftliche Fakultät“. Bonn : Universitäts- und Landesbibliothek Bonn, 2011. http://d-nb.info/1017217661/34.

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Krapf, Michael [Verfasser]. „Investigation of Quinazoline Derivatives as Inhibitors of Breast Cancer Resistance Protein (BCRP/ABCG2) / Michael Krapf“. Bonn : Universitäts- und Landesbibliothek Bonn, 2018. http://d-nb.info/1160594155/34.

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Yeboah, Dorothy. „Expression and regulation of Breast Cancer Resistance Protein in the human placenta and fetal membranes“. Thesis, University of Ottawa (Canada), 2007. http://hdl.handle.net/10393/27942.

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Breast Cancer Resistance Protein, BCRP, is highly expressed in many different tumor tissues conferring multi-drug resistance against many chemotherapy drugs. BCRP has also been reported to be present in normal tissues including the human placenta during pregnancy. It is believed that in the placenta, BCRP controls the levels of toxins, drugs and xenobiotics that may cross maternal circulation into fetal circulation. The expression of BCRP was examined in the human placenta and in placental membranes (amnion and chorion leave) and attached decidua. In addition, the effect of cytokines and hypoxia on BCRP expression in placental cells was examined in vitro. BCRP was found to be highly expressed in the placenta throughout pregnancy as well as in the amnion, chorion laeve and attached decidua. Our data suggest that increased cytokine expression and reduced oxygen levels may not have any effect on BCRP mRNA or protein levels in the placental syncytiotrophoblast cells. This may suggest that BCRP is stably expressed in the placenta, even under adverse conditions, and may imply that activity of this transporter protein is essential for normal placental function.

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KIM, Young-Hak. „Expression of breast cancer resistance protein is associated with a poor clinical outcome in patients with small-cell lung cancer“. Kyoto University, 2011. http://hdl.handle.net/2433/135385.

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10

Cooray, H. C. „Breast cancer resistance protein (BCRP) at the blood-brain barrier and its interactions with steroidal compounds“. Thesis, University of Cambridge, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.597979.

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Five different plant polyphenols (resveratrol, hesperetin, quercetin, daidzein and silymarin) were shown to interact with BCRP expressed in MCF7/MR and K562/BCRP cells, significantly increasing the accumulation of mitoxantrone and bodipy prazosin above control levels. They also stimulated the BCRP-associated ATPase activity in vesicles derived from Lactococcus lactis bacteria transformed with BCRP cDNA. None of these polyphenols had any effects on the long-term expression of BCRP in MCF7/MR cells. Inhaled corticosteroids have revolutionized the treatment of chronic obstructive pulmonary disease but cause long term suppression of the hypothalamic-pituitary-adrenal (HPA) axis, leading to low cortisol levels. It has been suggested that P-gp at the BBB may influence suppression of the HPA by oral corticosteroids. Five inhaled corticosteroids were tested for their ability to modulate P-gp and BCRP function. Beclomethasone dipropionate, mometasone furoate and the newer ciclesonide used at 5 and 10 μM increased the accumulation of mitoxantrone in BCRP-expressing MCF7/MR cells, and the accumulation of calcein in P-gp expressing SW620/R cells, though triamcinolone acetonide and budesonide had no inhibitory effects. Beclomethasone, mometasone and ciclesonide at 5 μM enhanced the cytotoxicity of doxorubicin in SW620/R cells. These three compounds as well as budesonide stimulated the BCRP-associated ATPase activity in L. lactis vesicles expressing BCRP. Both the plant polyphenols and the three corticosteroids examined in this study could either be ‘fast diffusing’ or competitive substrates of BCRP, inhibiting the efflux of another substrate while stimulating the BCRP-associated ATPase activity. These results establish that BCRP is present at the BBB and may modulate the access of both dietary and therapeutic steroidal compounds into the brain.

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Bücher zum Thema "Breas cancer resistance protein"

1

Gannon, Brian R. Dominant inhibition of cyclic AMP - dependent protein kinase in MCF-7 breast cancer cells: Effects on multidrug resistance. Sudbury, Ont: Laurentian University, 1997.

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Gannon, Brian Robert. The role of camp-dependent protein kinase in the expression and function of p-glycoprotein and other molecules implicated in drug resistance in adriamycin-resistant MCF-7 human breast cancer cells. Sudbury, Ont: Laurentian University, Chemistry and Biochemistry Department, 1999.

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Matthews, David J. Targeting protein kinases for cancer therapy. Hoboken, N.J: John Wiley & Sons, 2009.

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E, Gerritsen Mary, Hrsg. Targeting protein kinases for cancer therapy. Hoboken, N.J: John Wiley & Sons, 2010.

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Lee, Gloria. Functional expression of multidrug resistance transporters, P-glycoprotein and the breast cancer resistance protein, in brain cellular compartments. 2006.

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Wang, Bernice. Induction of breast cancer resistance protein (BCRP/ABCG2) by aryl hydrocarbon receptor (AHR) agonists in an AHR-dependent manner. 2005.

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Chen, Zhe-Sheng (Jason), und Dong-Hua Yang. Protein Kinase Inhibitors As Sensitizing Agents for Chemotherapy. Elsevier Science & Technology, 2018.

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Buchteile zum Thema "Breas cancer resistance protein"

1

Saidak, Zuzana, Zakaria Ezzoukhry, Jean-Claude Maziere, Antoine Galmiche, Ken-Ichi Takemaru, Xingwang Chen, Feng-Qian Li et al. „Breast Cancer Antiestrogen Resistance Protein 1 (BCAR1)“. In Encyclopedia of Signaling Molecules, 203. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100135.

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2

Basseville, Agnes, Robert W. Robey, Julian C. Bahr und Susan E. Bates. „Breast Cancer Resistance Protein (BCRP) or ABCG2“. In Drug Transporters, 187–221. Hoboken, NJ: John Wiley & Sons, Inc., 2014. http://dx.doi.org/10.1002/9781118705308.ch11.

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Koehn, Liam M. „ABC Transporters: The Breast Cancer Resistance Protein“. In The ADME Encyclopedia, 1–8. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-51519-5_80-1.

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4

Ross, Douglas D., und Takeo Nakanishi. „Impact of Breast Cancer Resistance Protein on Cancer Treatment Outcomes“. In Methods in Molecular Biology, 251–90. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-416-6_12.

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Natarajan, Karthika, Maria R. Baer und Douglas D. Ross. „Role of Breast Cancer Resistance Protein (BCRP, ABCG2) in Cancer Outcomes and Drug Resistance“. In Resistance to Targeted Anti-Cancer Therapeutics, 53–88. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-09801-2_3.

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6

Bode, Chris, und Li-Bin Li. „In Vitro Characterization of Intestinal Transporter, Breast Cancer Resistance Protein (BCRP)“. In Methods in Pharmacology and Toxicology, 353–67. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-742-6_21.

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Schwabedissen, Henriette E. Meyer zu, und Heyo K. Kroemer. „In Vitro and In Vivo Evidence for the Importance of Breast Cancer Resistance Protein Transporters (BCRP/MXR/ABCP/ABCG2)“. In Handbook of Experimental Pharmacology, 325–71. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-14541-4_9.

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Rumsby, Martin G., Lisa Drew und J. Roger Warr. „Protein kinases and multidrug resistance“. In Multiple Drug Resistance in Cancer 2, 203–24. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-017-2374-9_13.

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Fan, Dominic, Diane R. Bielenberg, Yun-Fang Wang, Robert Radinsky und Pedro J. Beltran. „The Multidrug Resistance-Associated Protein — MRP“. In Alternative Mechanisms of Multidrug Resistance in Cancer, 81–94. Boston, MA: Birkhäuser Boston, 1995. http://dx.doi.org/10.1007/978-1-4615-9852-7_4.

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Basu, Alakananda. „PKC and Resistance to Chemotherapeutic Agents“. In Protein Kinase C in Cancer Signaling and Therapy, 409–29. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-543-9_21.

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Konferenzberichte zum Thema "Breas cancer resistance protein"

1

Thomas, Grandjean,. „Compartmental Modelling of the Pharmacokinetics of a Breast Cancer Resistance Protein“. In Modeling and Control in Biomedical Systems, herausgegeben von Rees, Stephen, chair Andreassen, Steen und Andreassen, Steen. Elsevier, 2009. http://dx.doi.org/10.3182/20090812-3-dk-2006.00020.

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McCartan, DP, M. McIlroy, S. Eary, AD Hill und LS Young. „The developmental protein HOXc11 as a mediator of endocrine resistance in breast cancer.“ In CTRC-AACR San Antonio Breast Cancer Symposium: 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-3034.

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Haluska, P., JM Carboni, YW Asmann, C. Ten Eyck, RM Attar, JD Tibodeau, X. Hou et al. „Drug efflux by breast cancer resistance protein (BCRP) is a mechanism of resistance to the insulin-like growth factor receptor/insulin receptor inhibitor, BMS-536924.“ In CTRC-AACR San Antonio Breast Cancer Symposium: 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-2149.

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Shajahan, Ayesha N., Rebecca B. Riggins, Alan Zwart, F. Edward Hickman und Robert Clarke. „Abstract 2919: XBP1 and the unfolded protein response in antiestrogen resistance in breast cancer“. In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2919.

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Wang, Tingting, Tiannan Guo, Siu Kwan Sze, Mikael Hartman, Shaik Ahmad Buhari, Ching-Wan Chan, Philip Iau et al. „Abstract 2460: Extracellular matrix protein expression is associated with chemotherapy resistance in breast cancer“. In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2460.

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Lee, Min-Ho, Dahae Koh und Mi-Ock Lee. „Abstract 2924: Metastasis-associated protein 1 induces tamoxifen resistance in MCF7 breast cancer cells“. In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-2924.

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Kochel, Tyler, Xinrong Ma, Namita Kundu, Jocelyn Reader, Olga Goloubeva und Amy M. Fulton. „Abstract 4132: Multiple drug resistance-associated protein 4 (MRP4): Role in triple negative breast cancer“. In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4132.

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8

Cakar, B., D. Chan, P. Yan, Z. Zheng, P. Singh, JT Lei, S. Haricharan, M. Ellis und E. Chang. „Abstract P1-08-07: Assessing the impact of loss of NF1 protein on endocrine therapy resistance“. In Abstracts: 2016 San Antonio Breast Cancer Symposium; December 6-10, 2016; San Antonio, Texas. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.sabcs16-p1-08-07.

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9

Natarajan, Karthika, Mehmet Burcu und Maria R. Baer. „Abstract 706: The serine/threonine kinase Pim-1 promotes drug resistance mediated by the ATP-binding cassette multidrug resistance protein breast cancer resistance protein (BCRP, ABCG2) by stabilizing higher-order BCRP multimers“. In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-706.

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Mohammed, Atari,. „Kinetic Modelling of the Role of the Aldehyde Dehydrogenase Enzyme and the Breast Cancer Resistance Protein in Drug Resistance and Transport“. In Modeling and Control in Biomedical Systems, herausgegeben von Rees, Stephen, chair Andreassen, Steen und Andreassen, Steen. Elsevier, 2009. http://dx.doi.org/10.3182/20090812-3-dk-2006.00019.

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Berichte der Organisationen zum Thema "Breas cancer resistance protein"

1

Haynes, Robin L., und Alan J. Townsend. Glutathione Transferases and the Multidrug Resistance - Associated Protein in Prevention of Potentially Carcinogenic Oxidant Stress in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, Juni 2001. http://dx.doi.org/10.21236/ada398035.

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2

Hu, Rong. Role of NF-Kappa B Signaling in X-Box Binding Protein 1 (XBP1)-Mediated Antiestrogen Resistance in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, Oktober 2012. http://dx.doi.org/10.21236/ada569450.

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3

Hu, Rong. Role of NF-Kappa B Signaling in X-Box Binding Protein 1 (XBP1)-Mediated Antiestrogen Resistance in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, Oktober 2011. http://dx.doi.org/10.21236/ada555915.

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4

Hu, Rong. Role of NF-Kappa B Signaling in X-Box Binding Protein 1 (XBP1)-Mediated Antiestrogen Resistance in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, Oktober 2013. http://dx.doi.org/10.21236/ada594159.

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5

Lekostaj, Jacqueline K. The Role of ABC Proteins in Drug Resistant Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, April 2008. http://dx.doi.org/10.21236/ada485613.

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6

Lekostaj, Jacqueline K. The Role of ABC Proteins in Drug-Resistant Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, April 2007. http://dx.doi.org/10.21236/ada470298.

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7

Pleeter, Perri, und Jacqueline K. Lekostaj. The Role of ABC Proteins in Drug Resistant Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, März 2009. http://dx.doi.org/10.21236/ada504701.

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