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Relevant bibliographies by topics / ATP-competitive

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Journal articles

Academic literature on the topic 'ATP-competitive'

Author: Grafiati

Published: 1 April 2023

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Journal articles on the topic "ATP-competitive"

1

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 (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”). Althou

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2

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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3

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

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4

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 (2011): 1077–79. http://dx.doi.org/10.5012/bkcs.2011.32.3.1077.

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5

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

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6

Lazaro, Glorianne, Eleftherios Kostaras, and Igor Vivanco. "Inhibitors in AKTion: ATP-competitive vs allosteric." Biochemical Society Transactions 48, no. 3 (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 inhibi

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7

Parrish, Cynthia A., Nicholas D. Adams, Kurt R. Auger, et al. "Novel ATP-Competitive Kinesin Spindle Protein Inhibitors." Journal of Medicinal Chemistry 50, no. 20 (2007): 4939–52. http://dx.doi.org/10.1021/jm070435y.

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8

Ito, Masahiro, Misa Iwatani, Yusuke Kamada, et al. "Discovery of selective ATP-competitive eIF4A3 inhibitors." Bioorganic & Medicinal Chemistry 25, no. 7 (2017): 2200–2209. http://dx.doi.org/10.1016/j.bmc.2017.02.035.

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9

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, dur

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10

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 (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 P

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