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Relevant bibliographies by topics / ATP-competitive

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Academic literature on the topic 'ATP-competitive'

Author: Grafiati

Published: 1 April 2023

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Journal articles on the topic "ATP-competitive"

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Lebakken, Connie S., Laurie J. Reichling, Jason M. Ellefson, and Steven M. Riddle. "Detection of Allosteric Kinase Inhibitors by Displacement of Active Site Probes." Journal of Biomolecular Screening 17, no. 6 (March 26, 2012): 813–21. http://dx.doi.org/10.1177/1087057112439889.

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Non–adenosine triphosphate (ATP) competitive, allosteric inhibitors provide a promising avenue to develop highly selective small-molecule kinase inhibitors. Although this class of compounds is growing, detection of such inhibitors can be challenging as standard kinase activity assays preferentially detect compounds that bind to active kinases in an ATP competitive manner. We have previously described a time-resolved fluorescence resonance energy transfer (TR-FRET)–based kinase binding assay using the competitive displacement of ATP competitive active site fluorescent probes (“tracers”). Although this format has gained acceptance, published data with this and related formats are almost entirely without examples of non-ATP competitive compounds. Thus, this study addresses whether this format is useful for non-ATP competitive inhibitors. To this end, 15 commercially available non-ATP competitive inhibitors were tested for their ability to displace ATP competitive probes. Despite the diversity of both compound structures and their respective targets, 14 of the 15 compounds displaced the tracers with IC50 values comparable to literature values. We conclude that such binding assays are well suited for the study of non-ATP competitive inhibitors. In addition, we demonstrate that allosteric inhibitors of BCR-Abl and MEK bind preferentially to the nonphosphorylated (i.e., inactive) form of the kinase, indicating that binding assays may be a preferred format in some cases.

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Agius, Michael P., Kristin Ko, Taylor K. Johnson, Sameer Phadke, and Matthew B. Soellner. "Conformation-tunable ATP-competitive kinase inhibitors." Chemical Communications 58, no. 21 (2022): 3541–44. http://dx.doi.org/10.1039/d1cc06893h.

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Garuti, L., M. Roberti, and G. Bottegoni. "Non-ATP Competitive Protein Kinase Inhibitors." Current Medicinal Chemistry 17, no. 25 (September 1, 2010): 2804–21. http://dx.doi.org/10.2174/092986710791859333.

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Lee, Byung-Il, Hyung-Jun Ahn, Ki-Cheol Han, Dae-Ro Ahn, and Dong-Yun Shin. "Pyrogallin, an ATP-Competitive Inhibitor of JAK3." Bulletin of the Korean Chemical Society 32, no. 3 (March 20, 2011): 1077–79. http://dx.doi.org/10.5012/bkcs.2011.32.3.1077.

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Schenone, S., C. Brullo, F. Musumeci, M. Radi, and M. Botta. "ATP-Competitive Inhibitors of mTOR: An Update." Current Medicinal Chemistry 18, no. 20 (July 1, 2011): 2995–3014. http://dx.doi.org/10.2174/092986711796391651.

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Lazaro, Glorianne, Eleftherios Kostaras, and Igor Vivanco. "Inhibitors in AKTion: ATP-competitive vs allosteric." Biochemical Society Transactions 48, no. 3 (May 26, 2020): 933–43. http://dx.doi.org/10.1042/bst20190777.

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Aberrant activation of the PI3K pathway is one of the commonest oncogenic events in human cancer. AKT is a key mediator of PI3K oncogenic function, and thus has been intensely pursued as a therapeutic target. Multiple AKT inhibitors, broadly classified as either ATP-competitive or allosteric, are currently in various stages of clinical development. Herein, we review the evidence for AKT dependence in human tumours and focus on its therapeutic targeting by the two drug classes. We highlight the future prospects for the development and implementation of more effective context-specific AKT inhibitors aided by our increasing knowledge of both its regulation and some previously unrecognised non-canonical functions.

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Parrish, Cynthia A., Nicholas D. Adams, Kurt R. Auger, Joelle L. Burgess, Jeffrey D. Carson, Amita M. Chaudhari, Robert A. Copeland, et al. "Novel ATP-Competitive Kinesin Spindle Protein Inhibitors." Journal of Medicinal Chemistry 50, no. 20 (October 2007): 4939–52. http://dx.doi.org/10.1021/jm070435y.

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Ito, Masahiro, Misa Iwatani, Yusuke Kamada, Satoshi Sogabe, Shoichi Nakao, Toshio Tanaka, Tomohiro Kawamoto, Samuel Aparicio, Atsushi Nakanishi, and Yasuhiro Imaeda. "Discovery of selective ATP-competitive eIF4A3 inhibitors." Bioorganic & Medicinal Chemistry 25, no. 7 (April 2017): 2200–2209. http://dx.doi.org/10.1016/j.bmc.2017.02.035.

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Zarębska, Ewa A., Krzysztof Kusy, Ewa M. Słomińska, Łukasz Kruszyna, and Jacek Zieliński. "Plasma Nucleotide Dynamics during Exercise and Recovery in Highly Trained Athletes and Recreationally Active Individuals." BioMed Research International 2018 (October 9, 2018): 1–11. http://dx.doi.org/10.1155/2018/4081802.

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Circulating plasma ATP is able to regulate local skeletal muscle blood flow and 02 delivery causing considerable vasodilatation during exercise. We hypothesized that sport specialization and specific long-term training stimuli have an impact on venous plasma [ATP] and other nucleotides concentration. Four athletic groups consisting of sprinters (n=11; age range 21–30 yr), endurance-trained athletes (n=16; age range 18–31 yr), futsal players (n=14; age range 18–30 yr), and recreationally active individuals (n=12; age range 22–33 yr) were studied. Venous blood samples were collected at rest, during an incremental treadmill test, and during recovery. Baseline [ATP] was 759±80 nmol·l−1 in competitive athletes and 680±73 nmol·l−1 in controls and increased during exercise by ~61% in competitive athletes and by ~31% in recreationally active participants. We demonstrated a rapid increase in plasma [ATP] at exercise intensities of 83–87% of VO2max in competitive athletes and 94% in controls. Concentrations reported after 30 minutes of recovery were distinct from those obtained preexercise in competitive athletes (P<0.001) but not in controls (P=0.61). We found a correlation between total-body skeletal muscle mass and resting and maximal plasma [ATP] in competitive athletes (r=0.81 and r=0.75, respectively). In conclusion, sport specialization is significantly related to plasma [ATP] at rest, during exercise, and during maximal effort. Intensified exercise-induced plasma [ATP] increases may contribute to more effective vessel dilatation during exercise in highly trained athletes than in recreational runners. The most rapid increase in ATP concentration was associated with the respiratory compensation point. No differences between groups of competitive athletes were observed during the recovery period suggesting a similar pattern of response after exercise. Total-body skeletal muscle mass is indirectly related to plasma [ATP] in highly trained athletes.

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Lyle, S., D. H. Geller, K. Ng, J. Stanczak, J. Westley, and N. B. Schwartz. "Kinetic mechanism of adenosine 5′-phosphosulphate kinase from rat chondrosarcoma." Biochemical Journal 301, no. 2 (July 15, 1994): 355–59. http://dx.doi.org/10.1042/bj3010355.

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Biosynthesis of the activated sulphate donor adenosine 3′-phosphate 5′-phosphosulphate (PAPS) involves the sequential action of two enzyme activities. ATP-sulphurylase catalyses the formation of APS (adenosine 5′-phosphosulphate) from ATP and free sulphate, and APS is then phosphorylated by APS kinase to produce PAPS. Initial-velocity patterns for rat chondrosarcoma APS kinase indicate a single-displacement formal mechanism with KmAPS 76 nM and KmATP = 24 microM. Inhibition studies using analogues of substrates and products were carried out to determine the reaction mechanism. An analogue of PAPS, adenosine 3′-phosphate 5′-[beta-methylene]phosphosulphate, exhibited competitive inhibition with APS and non-competitive inhibition with ATP. An analogue of APS, adenosine 5′-[beta-methylene]phosphosulphate was also competitive with APS and non-competitive with ATP. Adenosine 5′-[beta gamma-imido]triphosphate showed competitive inhibition with respect to ATP and produced mixed-type inhibition, with a pronounced intercept effect and a small slope effect, with respect to APS. These results are in accord with the formulation of the predominant pathway as a steady-state ordered mechanism with APS as the leading substrate and PAPS as the final product released.

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Dissertations / Theses on the topic "ATP-competitive"

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Morgan, R. M. L. "ATP-competitive inhibitors as antifungals : Targeting the spectoria triticic kinome." Thesis, University of Oxford, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.531991.

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Mazaideh, Ghassab M. A. Al Verfasser], Wolfgang [Akademischer Betreuer] Sippl, Peter [Akademischer Betreuer] [Imming, and Manfred [Akademischer Betreuer] Jung. "Development and synthesis of new potential ATP-Competitive Myt1 Kinase inhibitors / Ghassab M. A. Al-Mazaideh. Betreuer: Wolfgang Sippl ; Peter Imming ; Manfred Jung." Halle, Saale : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2012. http://d-nb.info/1025303652/34.

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Driscoll, Brandon. "Modulation of TGF‐β Receptor 1 signalling in Live Cells." Thesis, 2009. http://hdl.handle.net/1807/17505.

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TGF-β negatively affects the maintenance and expansion of hematopoietic stem cells ex vivo and its inhibition has been widely studied as a treatment for numerous hematopoietic disorders and cancers. Current inhibitory strategies (small molecule ATP competitors and neutralizing antibodies) are compared to a novel cell-permeable peptide-based inhibitor of TGF-β RI. Multiple levels of assay from biochemical to functional are utilized with the aim of applying the most successful inhibitor to hematopoietic stem cell culture. The neutralizing antibody proved ineffective in the short-term biochemical assay but was extremely effective at neutralizing TGF-β signalling in proliferation and hematopoietic colony-forming cell assays with no evidence of toxicity. The small molecule inhibitors (SD-208 and Pyrazole TGF-β RI inhibitor) were equally effective at micromolar levels in all forms of assay, with SD-208 being slightly more potent. The novel peptide inhibitor proved ineffective in all assays, which is likely a result of its rapid degradation in live cells.

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Book chapters on the topic "ATP-competitive"

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Liu, Qingsong, Seong A. Kang, Carson C. Thoreen, Wooyoung Hur, Jinhua Wang, Jae Won Chang, Andrew Markhard, et al. "Development of ATP-Competitive mTOR Inhibitors." In Methods in Molecular Biology, 447–60. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-430-8_29.

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Register, Ames C., Sujata Chakraborty, and Dustin J. Maly. "Allosteric Modulation of Src Family Kinases with ATP-Competitive Inhibitors." In Methods in Molecular Biology, 79–89. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7154-1_6.

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Salomon, Dor, Chao Zhang, Kevan M. Shokat, and Guido Sessa. "Sensitizing Plant Protein Kinases to Specific Inhibition by ATP-Competitive Molecules." In Methods in Molecular Biology, 185–97. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-264-9_10.

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McInnes, Campbell. "REPLACE Strategy for Generating Non-ATP-Competitive Inhibitors of Cell Cycle Protein Kinases." In Protein-Protein Interactions in Drug Discovery, 291–304. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527648207.ch12.

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Clausen, Johannes D., David B. McIntosh, David G. Woolley, and Jens Peter Andersen. "Determination of the ATP Affinity of the Sarcoplasmic Reticulum Ca2+-ATPase by Competitive Inhibition of [γ-32P]TNP-8N3-ATP Photolabeling." In P-Type ATPases, 233–59. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3179-8_22.

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Yu, Ker, and Lourdes Toral-Barza. "Biochemical and Pharmacological Inhibition of mTOR by Rapamycin and an ATP-Competitive mTOR Inhibitor." In Methods in Molecular Biology, 15–28. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-430-8_2.

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Rea, Delphine. "Adverse Events Associated with ATP-Competitive BCR-ABL1 Tyrosine Kinase Inhibitors in Chronic Myeloid Leukemia." In Hematologic Malignancies, 77–91. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-71913-5_6.

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Rea, Delphine. "Management of Adverse Events Associated with ATP-Competitive BCR-ABL1 Tyrosine Kinase Inhibitors in Chronic Myeloid Leukemia." In Hematologic Malignancies, 71–87. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-33198-0_5.

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Sarvagalla, Sailu, and Mohane Selvaraj Coumar. "Protein-Protein Interactions (PPIs) as an Alternative to Targeting the ATP Binding Site of Kinase." In Pharmaceutical Sciences, 1115–43. IGI Global, 2017. http://dx.doi.org/10.4018/978-1-5225-1762-7.ch043.

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Most of the developed kinase inhibitor drugs are ATP competitive and suffer from drawbacks such as off-target kinase activity, development of resistance due to mutation in the ATP binding pocket and unfavorable intellectual property situations. Besides the ATP binding pocket, protein kinases have binding sites that are involved in Protein-Protein Interactions (PPIs); these PPIs directly or indirectly regulate the protein kinase activity. Of recent, small molecule inhibitors of PPIs are emerging as an alternative to ATP competitive agents. Rational design of inhibitors for kinase PPIs could be carried out using molecular modeling techniques. In silico tools available for the prediction of hot spot residues and cavities at the PPI sites and the means to utilize this information for the identification of inhibitors are discussed. Moreover, in silico studies to target the Aurora B-INCENP PPI sites are discussed in context. Overall, this chapter provides detailed in silico strategies that are available to the researchers for carrying out structure-based drug design of PPI inhibitors.

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Sarvagalla, Sailu, and Mohane Selvaraj Coumar. "Protein-Protein Interactions (PPIs) as an Alternative to Targeting the ATP Binding Site of Kinase." In Advances in Medical Technologies and Clinical Practice, 249–77. IGI Global, 2016. http://dx.doi.org/10.4018/978-1-5225-0362-0.ch010.

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Most of the developed kinase inhibitor drugs are ATP competitive and suffer from drawbacks such as off-target kinase activity, development of resistance due to mutation in the ATP binding pocket and unfavorable intellectual property situations. Besides the ATP binding pocket, protein kinases have binding sites that are involved in Protein-Protein Interactions (PPIs); these PPIs directly or indirectly regulate the protein kinase activity. Of recent, small molecule inhibitors of PPIs are emerging as an alternative to ATP competitive agents. Rational design of inhibitors for kinase PPIs could be carried out using molecular modeling techniques. In silico tools available for the prediction of hot spot residues and cavities at the PPI sites and the means to utilize this information for the identification of inhibitors are discussed. Moreover, in silico studies to target the Aurora B-INCENP PPI sites are discussed in context. Overall, this chapter provides detailed in silico strategies that are available to the researchers for carrying out structure-based drug design of PPI inhibitors.

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Conference papers on the topic "ATP-competitive"

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Mueller, Daniel, Frank Totzke, Thomas Weber, Carolin Heidemann-Dinger, Constance Ketterer, Diane Krämer, Marcel Pathe, and Michael H. Kubbutat. "Abstract 4186: A biochemical approach to discriminate between ATP-competitive and non-ATP competitive protein kinase inhibitors." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-4186.

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Estes, Kara, Zhengguan Yang, Campbell McInnes, and Michael D. Wyatt. "Abstract 3240: Development of non-ATP competitive, PLK1 selective inhibitors." 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.am2011-3240.

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Rana, Sandeep, Elizabeth Blowers, and Amarnath Natarajan. "Abstract 3645: A non-ATP competitive IKKβ inhibitor for cancer therapy." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-3645.

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Schio, Laurent, Conception Nemecek, Antonio Ugolini, Sylvie Wentzler, Sandrine Grapinet, Jean Khider, Eva Albert, et al. "Abstract 2911: SAR125844: a potent and selective ATP-competitive inhibitor of MET kinase." 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.am2012-2911.

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Lin, Kui. "Abstract DDT02-01: GDC-0068: A novel, selective, ATP-competitive inhibitor of Akt." 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-ddt02-01.

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Zimmerman, Kristin M., Brian Lee, Wei-Jen Chung, Florian Gnad, Eva Lin, Scott Martin, and Kui Lin. "Abstract LB-115: Mechanisms of acquired resistance to allosteric versus ATP-competitive AKT inhibition." 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-lb-115.

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Tandon, Manuj, James Johnson, Elisa Farber, Evan Carder, Peter Wipf, and Qiming J. Wang. "Abstract 2182: Novel ATP-competitive protein kinase D inhibitors: in vitro characterization and SAR analysis." 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.am2013-2182.

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Luke, Richard W., Matthew Addie, Matthew R. Box, David Buttar, Claire Crafter, Gordon S. Currie, Sabina C. Cosulich, et al. "Abstract 4478: Discovery of AZD5363, an orally bioavailable, potent ATP-competitive inhibitor of AKT kinases." 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.am2011-4478.

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Dai, Yao, and Dietmar W. Siemann. "Abstract 3761: Efficacy of the ATP-competitive mTOR inhibitor AZD8055 in PTEN-wild type cancer cells." 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.am2012-3761.

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Sootome, Hiroshi, Suzuko Kato, Masanori Kato, and Hiroshi Hirai. "Abstract 1117: Acquired resistance to ATP-competitive and irreversible FGFR inhibitors (FGFRi's): A library-based approach." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1117.

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Reports on the topic "ATP-competitive"

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Reddy, E. P. A Non-ATP Competitive Inhibitor of BCR-ABL for the Therapy of Imatinib-Resistant Cmls. Fort Belvoir, VA: Defense Technical Information Center, May 2008. http://dx.doi.org/10.21236/ada487510.

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Reddy, E. P. ON012380: A Non-ATP Competitive Inhibitor of BCR-ABL for the Therapy of Imatinib-Resistant CMLs. Fort Belvoir, VA: Defense Technical Information Center, May 2010. http://dx.doi.org/10.21236/ada532978.

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Reddy, E. P. ON012380: A Non-ATP Competitive Inhibitor of BCR-ABL for the Therapy of Imatinib-Resistant CMLs. Fort Belvoir, VA: Defense Technical Information Center, May 2009. http://dx.doi.org/10.21236/ada510718.

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