Academic literature on the topic 'ABCB1 inhibitors'
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Journal articles on the topic "ABCB1 inhibitors"
Michaelis, Martin, Florian Rothweiler, Thomas Nerreter, Marijke Van Rikxoort, Mohsen Sharifi, Michael Wiese, Taravat Ghafourian, and Jindrich Cinatl. "Differential Effects of the Oncogenic BRAF Inhibitor PLX4032 (Vemurafenib) and its Progenitor PLX4720 on ABCB1 Function." Journal of Pharmacy & Pharmaceutical Sciences 17, no. 1 (April 6, 2014): 154. http://dx.doi.org/10.18433/j3tw24.
Full textMichaelis, Martin, Yvonne Voges, Florian Rothweiler, Fabian Weipert, Amara Zia-Ahmad, Jaroslav Cinatl, Andreas von Deimling, et al. "Testing of the Survivin Suppressant YM155 in a Large Panel of Drug-Resistant Neuroblastoma Cell Lines." Cancers 12, no. 3 (March 2, 2020): 577. http://dx.doi.org/10.3390/cancers12030577.
Full textMichaelis, Martin, Florian Rothweiler, Thomas Nerreter, Mohsen Sharifi, Taravat Ghafourian, and Jindrich Cinatl. "Karanjin interferes with ABCB1, ABCC1, and ABCG2." Journal of Pharmacy & Pharmaceutical Sciences 17, no. 1 (March 10, 2014): 92. http://dx.doi.org/10.18433/j3bw2s.
Full textYin, Wei, Jianfeng Xu, and Yanjiao Mao. "Synergistic effects of autophagy inhibitors combined with cisplatin against cisplatin-resistant nasopharyngeal cancer cells." Biochemistry and Cell Biology 99, no. 3 (June 2021): 322–29. http://dx.doi.org/10.1139/bcb-2020-0283.
Full textIbrahim, Mahmoud A. A., Khlood A. A. Abdeljawaad, Alaa H. M. Abdelrahman, Laila A. Jaragh-Alhadad, Hesham Farouk Oraby, Eslam B. Elkaeed, Gamal A. H. Mekhemer, et al. "Exploring Natural Product Activity and Species Source Candidates for Hunting ABCB1 Transporter Inhibitors: An In Silico Drug Discovery Study." Molecules 27, no. 10 (May 12, 2022): 3104. http://dx.doi.org/10.3390/molecules27103104.
Full textNatarajan, Karthika, Jasjeet Bhullar, Suneet Shukla, Mehmet Burcu, Suresh V. Ambudkar, and Maria R. Baer. "The Pim Kinase Inhibitor SGI-1776 Chemosensitizes Multidrug Resistant Cells by Both Inhibiting Drug Transport by ABCB1 and ABCG2 and Decreasing ABCB1 and ABCG2 Surface Expression On Cells That Overexpress Pim-1." Blood 120, no. 21 (November 16, 2012): 2462. http://dx.doi.org/10.1182/blood.v120.21.2462.2462.
Full textNosol, Kamil, Ksenija Romane, Rossitza N. Irobalieva, Amer Alam, Julia Kowal, Naoya Fujita, and Kaspar P. Locher. "Cryo-EM structures reveal distinct mechanisms of inhibition of the human multidrug transporter ABCB1." Proceedings of the National Academy of Sciences 117, no. 42 (October 5, 2020): 26245–53. http://dx.doi.org/10.1073/pnas.2010264117.
Full textWinter, Stuart S., Debbie M. Lovato, Hadya M. Khawaja, Bruce S. Edwards, Irena D. Steele, Susan M. Young, Tudor I. Oprea, Larry A. Sklar, and Richard S. Larson. "Identification of Off-Patent Drugs That Reverse Daunorubicin Efflux Mediated by ABCB1 in T-ALL Cells." Blood 108, no. 11 (November 16, 2006): 2603. http://dx.doi.org/10.1182/blood.v108.11.2603.2603.
Full textWang, Jingqiu, Dong-Hua Yang, Yuqi Yang, Jing-Quan Wang, Chao-Yun Cai, Zi-Ning Lei, Qiu-Xu Teng, Zhuo-Xun Wu, Linguo Zhao, and Zhe-Sheng Chen. "Overexpression of ABCB1 Transporter Confers Resistance to mTOR Inhibitor WYE-354 in Cancer Cells." International Journal of Molecular Sciences 21, no. 4 (February 19, 2020): 1387. http://dx.doi.org/10.3390/ijms21041387.
Full textDohse, Marius, Robert W. Robey, Cornelia Brendel, Susan Bates, Andreas Neubauer, and Christian Scharenberg. "Efflux of the Tyrosine Kinase Inhibitors Imatinib and Nilotinib (AMN107) Is Mediated by ABCB1 (MDR1)-Type P-Glycoprotein." Blood 108, no. 11 (November 16, 2006): 1367. http://dx.doi.org/10.1182/blood.v108.11.1367.1367.
Full textDissertations / Theses on the topic "ABCB1 inhibitors"
Ali, Wesam [Verfasser]. "Design and synthesis of novel ligands for Serotonin (5-HT6) receptor and inhibitors of ABCB1 Efflux pump / Wesam Ali." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2020. http://d-nb.info/1229916830/34.
Full textArnaud, Ophélie. "Étude fonctionnelle de la région intracellulaire d’ABCG2 et modulation d’ABCG2 et ABCB1 humains par des petidomimétiques non compétitifs." Thesis, Lyon 1, 2011. http://www.theses.fr/2011LYO10091/document.
Full textResistance to chemotherapy is partly due to efflux pumps expressed in the plasma membrane which prevent the accumulation of anticancer drugs in the tumour cells. Three human ATP-binding Cassette (ABC) transporters are particularly involved in this phenotype: P-gp/ABCB1, MRP1/ABCC1, and the last discovered BCRP/ABCG2. Because of their involvement in chemoresistance, it is critical to understand the mechanism by which those ABC transporters recognize and transport drugs. The mutagenesis study of the intracellular loops, ICL0 and 1 shows that these loops are involved in this mechanism. Two amino acids were particularly remarkable: W379 which act as a substrate filter and H457 which can be involved in substrate recognition and binding. In order to restore the cancer cell sensitivity to chemotherapeutic drugs, we have developed a new class of peptide inhibitors, specific to one transporter. A structure-activity relationship study has been performed and made it possible to develop a second generation of molecules. The most efficient compound inhibiting ABCB1 (CT1347) or ABCG2 (CT1364) have none or limitated cytotoxic effects. These compounds restore the activity of chemotherapeutic drugs and act as non competitive inhibitors. Moreover, CT1364 inhibits the ATP hydrolysis activity and lead to a rapid reduction of ABCG2 expression. Initial in vivo tests that have been carried out with CT1364 associated with irinotecan allow to observe a growth reduction of small mice xenografts
Gassiot, Matthieu. "Rôle du récepteur des xénobiotiques PXR (Pregnane X Receptor) et de ses gènes cibles sur la sensibilité des lignées de cancer de prostate aux inhibiteurs de kinases." Thesis, Montpellier, 2017. http://www.theses.fr/2017MONTT133/document.
Full textMore and more kinase inhibitors (KIs) are tested in prostate cancer that represents a major health issue in men with its incidence and mortality rates. Clinical trials to evaluate KIs efficacy in prostate cancer gave disapointing results depsite the presence of KIs pharmacological targets in prostate tumors (VEGF, EGFR, CMET..), suggesting that inefficiency of these drugs would be at least in part linked to the inhibitor itself or its pharmacodynamics/pharmacokinetics parameters. Indeed KIs are metabolized and transported via phase I and II enzymes that are mainly controlled by the xenoreceptor PXR (Pregnane X Receptor, gène NR1I2). It is mainly expressed in liver and gastro-intestinal tract but also in epithelial tumors. PXR is also involved in the resistance to chemotherapies by increasing the catabolism and the efflux of these anticancer agents. To date only one study evaluated PXR expression in prostate cancer without evaluating its impact on treatment efficacy. In collaboration with Pr G. Fromont we analyzed a cohort of 449 prostate tumors and observed that PXR was more frequently detected in castration resistant or metastatic tumors as compared to clinically localized forms in which PXR expression was significantly correlated with TNM and ISUP Score. These results confirmed the interest to study the potential role of PXR and its target genes in the sensitivity to kinase inhibitors in prostate cancer models.We measured the expression of PXR and its target genes in prostate cancer cell lines 22RV1, LnCap, PC3 and DU145. The results showed that enzymes and transporters involved in KI detoxification was significantly expressed in these cells whereasPXR was poorly expressed due to hypermethylation of NR1I2 in our cells. This lead us to develop specific prostate cancer cell models stably overexpressing PXR in which transcriptional activity of PXR can be induced by its known agonist SR12813 further indicating that prostate cancer cells are metabolically competent. Using these models we showed that PXR overexpression modulates the sensitivity of 22RV1 cells to erlotinib, dasatinib, dabrafenib and afatinib, demonstrating that PXR plays a functional role in the sensitivity to KIs. We also demonstrated that several KIs were PXR agonists, including dabrafenib that displayed enhanced agonistic properties as compared to SR12813, a result that was never published before. This original finding led us to engage the cristalization of PXR/dabrafenib complex and to test whether induction of PXR could lead to an alteration of metabolism and transport of other drugs that are co-administered. In this line we have observed that in 22RV1 cells the additive effect of the combination of dabrafenib with trametinib that is already approved in the treatment of melanomas, became antagonistic when PXR was overexpressed in these cells. This result is supporting our hypothesis though we still need to demonstrate that this effect is linked to a change in drugs metabolism, which is currently under investigation by the measurement of the known metabolites of these KIs.Altogether, our data could serve as rational basis for the choice of kinase inhibitors or their potential combinations that could be tested in further clinical trials alone or in association with hormone therapies or with chemotherapies that are currently prescribed in the treatment of advanced prostate cancers, in order to potentiate tumor response
Gomes, Guilherme Wataru. "Expressão gênica dos transportadores de membrana ABCB1,ABCG2, SLC22A1 e SLCO1A2 em linhagens celulares tratadas com inibidor comercial da via JAK-STAT." Universidade de São Paulo, 2015. http://www.teses.usp.br/teses/disponiveis/9/9136/tde-16032016-095918/.
Full textBACKGROUND: JAK-STAT pathway signaling disregulation is a hallmark of myeloproliferative neoplasms (MPN), hematopoietic stem cell clonal diseases, among which is myelofibrosis (MF). Several JAK inhibitors have been developed for MF treatment and are found in different stages of clinical development. Because the recent development of these compounds, the role of drug transporters in their pharmacokinetics is poorly understood. These proteins perform celular influx and effux of endogenous substrates and xenobiotics, and changes in the expression of these drugs transporters may affect the response to these drugs. AIM: To evaluate the effect of a JAK-STAT pathway commercial inhibitor in gene expression of drug transporters ABCB1, ABCG2, SLC22A1 and SLCO1A2 in HepG2, Caco-2 and HEL92.1.7 cells. METHODS: Hepatocellular carcinoma cell line HepG2, colorectal adenocarcinoma cell line Caco-2 and human erythroleukemia homozygous JAK2V617F cell line HEL92.1.7 were grown and treated with the JAK-STAT pathway inhibitor JAK Inhibitor I. In order to determine the optimal concentration for treatment with the inhibitor, cells were treated with several concentrations of JAK inhibitor by 24 hours, and cell viability and DNA fragmentation tests were performed. Once the treatment conditions were standardized, total RNA were obtained from the cells, and cDNA was synthesized in order to evaluate the mRNA expression of ABCB1, ABCG2, SLC22A1 and SLCO1A2 genes, performed by real time PCR. We also evaluate the expression of drug efflux transporters ABCB1 and ABCG2 by flow cytometry, using primary antibodies directed to these proteins. RESULTS: In HepG2 cells, it was observed an increase in ABCB1 mRNA expression in cells treated with 4,00 µM of JAK inhibitor, when compared with controls (cells exposed only to the vehicle) (P=0.041). There was no change in ABCB2 and SLC22A1 mRNA expression with the treatment with JAK inhibitor in this cell line (P>0.05); SLCO1A2 mRNA was not detected in this cell line. In Caco-2 cells, ABCB1, ABCG2, SLC22A1 and SLCO1A2 mRNA expression did not change with treatment with the JAK inhibitor at the concentrations used (0.25 µM to 1.00 µM) by 24 hours (P>0.05). In HEL92.1.7 cells, it was not observed differences in ABCB1, ABCG2 and SLC22A1 mRNA expression with the treatment with 1 µM of JAK inhibitor by 24 hours when compared with controls (P>0.05); in this cell line, SLCO1A2 mRNA was not detected. Protein expression of ABCB1 and ABCG2 drug transporters has not changed with treatment with the JAK inhibitor under the conditions used in the three cell lines studied. CONCLUSIONS: Only HepG2 cells presented an increase in mRNA expression of drug efflux transporter ABCB1 in presence of high levels of JAK inhibitor, suggesting that JAK inhibitors could modulate this transporter gene expression in liver. Treatment with JAK-STAT pathway inhibitor was not associated with changes in ABCB1 and ABCG2 protein expression in all cell lines studied.
Cusinato, Diego Alberto Ciscato. "Associação dos polimorfismos do CYP3A5 e da PGP com a farmacocinética do tacrolimus, nefrotoxicidade aguda e rejeição do enxerto após transplante renal." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/17/17133/tde-20082013-151121/.
Full textTacrolimus (TAC) is widely used to prevent acute rejection following solid-organ transplantation. This drug is characterized by a narrow therapeutic index and drug monitoring programs are required both to optimize efficacy and to limit toxicity. TAC is known to be substrate of cytochrome P450 (CYP) 3A5 and P-glycoprotein (PGP/ABCB) and its been suggested that genetic polymorphisms (SNPs) of these proteins are highly associated with variations in TAC pharmacokinetics. We investigated the influence of polymorphisms of CYP3A5 and ABCB1 gene on the pharmacokinetic parameters (PK) of TAC and on the incidence of kidney injuries and allograft rejection (AR) in renal transplant recipients. Patients receiving TAC for at least 12 months (n=108) were genotyped (real-time PCR) for CYP3A5*3 (rs776746) and for ABCB1 1236C>T (rs1128503), 2677G>T/A (rs2032582) and 3435C>T (rs1045642) polymorphisms. TAC predose concentration (Co; ng/mL), TAC daily dose (mg/day per kg body weight) and dose-normalized predose concentrations (Co/dose; ng/mL per mg/day per kg body weight) were retrieved from medical records up to 03 years after transplantation. Clinical outcomes were analyzed evaluating renal function in terms of creatinine clearance ( Cockroft-Gault equation) and allograft survival. Kidney injuries and AR diagnostics were established by clinical suspicion and in presence of histological findings in renal biopsies according to the 2007 Banff classification. ABCB1 gene haplotypes were statistically inferred using PHASE software (version 2.1). No deviation from Hardy-Weinberg equilibrium was observed in our study population for the polymorphic loci examined in CYP3A5 and ABCB1. Allelic frequencies of these polymorphisms (6986G 74%; 1236C 60%; 3435C 60% and 2677G 65%) and haplotypes (49% 2677G-3435C-1236C and 30% 2677T- 3435T-1236T) were consistent with other studies in the Brazilian population. Individuals carrying at least one CYP3A5*1 allele required higher TAC dose to achieve similar TAC blood levels as the homozygous individuals for the *3 allele (0.09 ± 0.03 vs.0.06 ± 0.03, mg/day per kg body weight, p<0.001). The presence of the CYP3A5*1 allele was also associated with lower TAC Co/dose compared to CYP*3 homozygous (84.9 ± 43.2 vs. 144.6 ± 66.7 ng/mL per mg/day per kg body weight, p<0.001). Regarding ABCB1 polymorphisms, individuals homozygous for the variant allele of each individual SNP and for the haplotype (TTT) showed higher Co/dose ratio. No associations were found between SNPs or haplotypes and allograft survival or creatinine clearance. We did find, though, that patients carrying GCC haplotype had a higher incidence of chronic rejection. Our findings confirm the effect of CYP3A5 and, less pronounced of ABCB1 polymorphisms, on the TAC pharmacokinetic. On the other hand, we did not find any association between these polymorphisms and relevant clinical outcomes, suggesting that CYP3A5 and ABCB1 genotyping must not be incorporated as a useful clinical tool on the management of kidney transplantation.
Arnaud, Ophélie. "Étude fonctionnelle de la région intracellulaire d'ABCG2 et modulation d'ABCG2 et ABCB1 humains par des petidomimétiques non compétitifs." Phd thesis, Université Claude Bernard - Lyon I, 2011. http://tel.archives-ouvertes.fr/tel-00846207.
Full textTangella, Lokeswari Prathyusha. "An investigation on role of the ATP-binding cassette B5 (ABCB5) transporter as potential mediator of melanoma resistance to BRAF inhibition." Thesis, Edith Cowan University, Research Online, Perth, Western Australia, 2020. https://ro.ecu.edu.au/theses/2369.
Full textRepeľová, Beáta. "Studium vlivu antiretrovirálních léčiv na transmembránový transport tenofoviru disoproxil fumarátu přes monovrstvu MDCKII-ABCB1 buněk." Master's thesis, 2017. http://www.nusl.cz/ntk/nusl-371009.
Full textLI, HAI-CHEN, and 李海辰. "Synthesis of imidazole analogs as ABCB1/ABCG2 inhibitors and the study of their structure-activity relationship." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/18307404638521153952.
Full text東海大學
化學系
104
During the treatment of cancer, multidrug resistance (MDR) is one of the most intractable problems. Multidrug resistance is often caused by the overexpression of ABC transporter (ATP-binding cassette transporter) ABCB1, ABCC1, ABCG2 which result in cancer drug to be exported out of the cell, rendering chemotherapy ineffective. As an effort to counteract this problem, we first took the substructure of tariquidar,2-benzamido-N-phenylbenzamide as the lead compound, and synthesize derivatives with different functional groups. While the synthesis of these derivatives were not as successful, we then synthesized compounds derived from three imidazole inhibitors screened at Professor Chung-Pu Wu’s laboratory, Chang Gung University. The ABC transporter protein inhibitory activity, showed that the nitrile substituting derivative demonstrated the best activity and when carboxyl group was esterified, the activity increased as well. The inhibitory activity of compounds showed that the hydrophobic group was preferred for ABCG2 inhibition. Neither electronic nor structure size of substituents appeared to affect the ABC transporter inhibition.
Luo, Shi Yu, and 羅仕瑜. "Human ABCB1 (P-glycoprotein/MDR1) and ABCG2 (BCRP/MXR) Mediate Resistance to Polo-like kinase 1 inhibitors." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/48402034791397339617.
Full text長庚大學
生物醫學研究所
102
The overexpression of the serine/threonine specific polo-like kinase 1 (Plk1) has been detected in various types of cancer, and thus has fast become an attractive therapeutic target for cancer therapy. Plk1 inhibitors BI 2536, volasertib and GSK461364, were designed to selectively inhibit cancer cell proliferation by promoting G2/M cell cycle arrest at nanomolar concentrations. Unfortunately, alike most chemotherapeutic agents, the development of acquired resistance to Plk1 inhibitors is prone to present a significant therapeutic challenge. One of the most common mechanisms for acquired resistance in cancer chemotherapy is associated with the overexpression of ATP-binding cassette (ABC) transporters ABCB1, ABCC1 and ABCG2. Here, we discovered that in human cancer cells, the overexpression of ABCB1 and/or ABCG2 can lead to acquired resistance to three selective Plk1 inhibitors, BI 2536, volasertib and GSK461364. Moreover, these Plk1 inhibitors stimulate the ATPase activity of ABCB1 and ABCG2, as well as competitively inhibit the drug substrate transport mediated by ABCB1 and ABCG2. More significantly, the reduced chemosensitivity and Plk1 inhibitors-mediated G2/M cell cycle arrest in cancer cells overexpressing either ABCB1 or ABCG2 can be significantly restored in the presence of selective inhibitor of ABCB1 and ABCG2. Taken together, our findings indicate that in order to circumvent ABCB1 or ABCG2-mediated acquired resistance to Plk1 inhibitors, a combined regimen of Plk1 inhibitors and modulators or clinically active drugs that potently inhibit the function of ABC drug transporters, should be considered as a potential treatment strategy in the clinic.
Conference papers on the topic "ABCB1 inhibitors"
Ansbro, Megan R., Suneet Shukla, Suresh V. Ambudkar, Stuart H. Yuspa, and Luowei Li. "Abstract 5635: Development of a high-throughput cell and fluorescent image-based ABCB1-mediated efflux assay for screening inhibitors of ABCB1." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5635.
Full textBarbuti, Anna Maria, Bhargav A. Patel, Tanaji T. Talele, and Zhe-Sheng Chen. "Abstract 2144: Next generation inhibitors to reverse ABCB1 transport mediated multidrug resistance in 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.am2016-2144.
Full textFan, Lin, Mark C. de Gooijer, Levi Buil, Nienke A. de Vries, Jos H. Beijnen, and Olaf van Tellingen. "Abstract LB-301: The impact of Abcb1 and Abcg2 on the brain penetration of PI3K-mTOR inhibitors." 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-lb-301.
Full textSodani, Kamlesh S., Amit K. Tiwari, Satyakam Singh, Atish Patel, Zhijie Xiao, Junjiang Chen, Yueli Sun, Tanaji T. Talele, and Zhe-Sheng Chen. "Abstract 777: GW583340 and GW2974, human EGFR and HER-2 inhibitors, reverse ABCG2- and ABCB1-mediated drug resistance." 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.am2012-777.
Full textWu, Chung-Pu, Hong-May Sim, and Suresh V. Ambudkar. "Abstract 766: Human ABCB1 and ABCG2 confer acquired resistance to Polo-like kinase 1 inhibitors, BI 2536, volasertib and GSK641364." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-766.
Full textKwon, Woo Sun. "Abstract 5458: Identification of functional downstream gene of ABCB1 2677 G>T/A polymorphism, LAMP-1, as a predictor gene to inhibitors of microtubule dynamics using integrative analysis of pharmacogenetics and genomics." 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.am2011-5458.
Full textHe, Ping-Ping, Xin-Ping OuYang, Kai Yin, Wu-Jun Chen, Qian Lu, Zhong-Cheng Mo, Guo-Jun Zhao, Yun-Cheng Lv, and Chao-Ke Tang. "PDE Inhibitor Rolipram Increases Cholesterol Efflux and ABCA1 Expression: Rolipram Increases ABCA1 Expression." In 2012 International Conference on Biomedical Engineering and Biotechnology (iCBEB). IEEE, 2012. http://dx.doi.org/10.1109/icbeb.2012.292.
Full textJi, Ning, Yuqi Yang, Chao-Yun Cai, Zi-Ning Lei, Jing-Quan Wang, Pranav Gupta, Suneet Shukla, Suresh V. Ambudkar, Dexin Kong, and Zhe-Sheng Chen. "Abstract 3796: Selonsertib, an ASK1 inhibitor, antagonizes ABCB1- and ABCG2-mediated chemotherapeutic drug resistance." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3796.
Full textJi, Ning, Yuqi Yang, Chao-Yun Cai, Zi-Ning Lei, Jing-Quan Wang, Pranav Gupta, Suneet Shukla, Suresh V. Ambudkar, Dexin Kong, and Zhe-Sheng Chen. "Abstract 3796: Selonsertib, an ASK1 inhibitor, antagonizes ABCB1- and ABCG2-mediated chemotherapeutic drug resistance." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3796.
Full textPatel, Atish S., Amit Tiwari, Eduardo Chufan, Satyakam Singh, Kamlesh Sodani, Nagaraju Anreddy, Tanaji Talele, Suresh Ambudkar, Ralph Stephani, and Zhe-Sheng Chen. "Abstract 980: PD173074, a selective FGFR inhibitor, reverses ABCB1-mediated drug resistance in cancer cells." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-980.
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