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Artículos de revistas sobre el tema "Cyclin-dependent kinases"

Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 30 de julio de 2024

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1

Sclafani, Robert A. "Cyclin dependent kinase activating kinases." Current Opinion in Cell Biology 8, no. 6 (December 1996): 788–94. http://dx.doi.org/10.1016/s0955-0674(96)80079-2.

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2

Gitig, Diana M., and Andrew Koff. "Cdk Pathway: Cyclin-Dependent Kinases and Cyclin-Dependent Kinase Inhibitors." Molecular Biotechnology 19, no. 2 (2001): 179–88. http://dx.doi.org/10.1385/mb:19:2:179.

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3

Malumbres, Marcos. "Cyclin-dependent kinases." Genome Biology 15, no. 6 (2014): 122. http://dx.doi.org/10.1186/gb4184.

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4

Harper, J. W., and P. D. Adams. "Cyclin-Dependent Kinases." Chemical Reviews 101, no. 8 (August 2001): 2511–26. http://dx.doi.org/10.1021/cr0001030.

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5

Dynlacht, B. D., K. Moberg, J. A. Lees, E. Harlow, and L. Zhu. "Specific regulation of E2F family members by cyclin-dependent kinases." Molecular and Cellular Biology 17, no. 7 (July 1997): 3867–75. http://dx.doi.org/10.1128/mcb.17.7.3867.

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The transcription factor E2F-1 interacts stably with cyclin A via a small domain near its amino terminus and is negatively regulated by the cyclin A-dependent kinases. Thus, the activities of E2F, a family of transcription factors involved in cell proliferation, are regulated by at least two types of cell growth regulators: the retinoblastoma protein family and the cyclin-dependent kinase family. To investigate further the regulation of E2F by cyclin-dependent kinases, we have extended our studies to include additional cyclins and E2F family members. Using purified components in an in vitro sy
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6

Malumbres, Marcos, and Mariano Barbacid. "Mammalian cyclin-dependent kinases." Trends in Biochemical Sciences 30, no. 11 (November 2005): 630–41. http://dx.doi.org/10.1016/j.tibs.2005.09.005.

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7

Clarke, Paul R. "Cyclin-Dependent Kinases: CAK-handed kinase activation." Current Biology 5, no. 1 (January 1995): 40–42. http://dx.doi.org/10.1016/s0960-9822(95)00013-3.

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8

Feroche, Alemu Tadesse, and Frehiwot Beyene Woselassie. "A review on macrocyclic kinase inhibitors in clinical trials." International Journal of Pharmaceutical Chemistry and Analysis 11, no. 2 (July 15, 2024): 147–52. http://dx.doi.org/10.18231/j.ijpca.2024.020.

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Macrocyclic kinase inhibitors have high binding affinity and selectivity towards a variety of kinases including mammalian target of rapamycin complex 1/2, janus kinases/ Fms like tyrosine kinase, cyclin-dependent kinases and anaplastic lymphoma kinase1. Recently, few macrocyclic kinase inhibitors have entered clinical trial for treatment different types of cancers including leukemia, non-small cell lung cancer, myelofibrosis, breast cancer, glioblastoma and lymphoma. Of them, ridaforomilus has completed Phase III clinical trial and is waiting to be approved for treatment of breast cancer and a
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9

Wang, Fuhu, Dale Corbett, Hitoshi Osuga, Sachiko Osuga, Joh-E. Ikeda, Ruth S. Slack, Matthew J. Hogan, Antoine M. Hakim, and David S. Park. "Inhibition of Cyclin-Dependent Kinases Improves CA1 Neuronal Survival and Behavioral Performance after Global Ischemia in the Rat." Journal of Cerebral Blood Flow & Metabolism 22, no. 2 (February 2002): 171–82. http://dx.doi.org/10.1097/00004647-200202000-00005.

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Increasing evidence suggests that cyclin-dependent kinases participate in neuronal death induced by multiple stresses in vitro. However, their role in cell death paradigms in vivo is not well characterized. Accordingly, the authors examined whether cyclin-dependent kinase inhibition resulted in functionally relevant and sustained neuroprotection in a model of global ischemia. Intracerebroventricular administration of the cyclin-dependent kinase inhibitor flavopiridol, immediately or at 4 hours postreperfusion after a global insult, reduced injury in the CA1 of the hippocampus when examined 7 d
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10

Canavese, Miriam, Loredana Santo, and Noopur Raje. "Cyclin dependent kinases in cancer." Cancer Biology & Therapy 13, no. 7 (May 2012): 451–57. http://dx.doi.org/10.4161/cbt.19589.

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11

Park, David S., Fuhu Wang, and Michael J. O’Hare. "Cyclin-dependent kinases and stroke." Expert Opinion on Therapeutic Targets 5, no. 5 (October 2001): 557–67. http://dx.doi.org/10.1517/14728222.5.5.557.

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12

Harper, J. W., and P. D. Adams. "ChemInform Abstract: Cyclin-Dependent Kinases." ChemInform 32, no. 41 (May 24, 2010): no. http://dx.doi.org/10.1002/chin.200141284.

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13

Grison, Alice, and Suzana Atanasoski. "Cyclins, Cyclin-Dependent Kinases, and Cyclin-Dependent Kinase Inhibitors in the Mouse Nervous System." Molecular Neurobiology 57, no. 7 (June 6, 2020): 3206–18. http://dx.doi.org/10.1007/s12035-020-01958-7.

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14

Jiang, Hong, Hubert S. Chou, and Liang Zhu. "Requirement of Cyclin E-Cdk2 Inhibition in p16INK4a-Mediated Growth Suppression." Molecular and Cellular Biology 18, no. 9 (September 1, 1998): 5284–90. http://dx.doi.org/10.1128/mcb.18.9.5284.

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ABSTRACT Loss-of-function mutations of p16 INK4a have been identified in a large number of human tumors. An established biochemical function of p16 is its ability to specifically inhibit cyclin D-dependent kinases in vitro, and this inhibition is believed to be the cause of the p16-mediated G1 cell cycle arrest after reintroduction of p16 into p16-deficient tumor cells. However, a mutant of Cdk4, Cdk4N158, designed to specifically inhibit cyclin D-dependent kinases through dominant negative interference, was unable to arrest the cell cycle of the same cells (S. van den Heuvel and E. Harlow, Sc
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15

Harper, J. W., S. J. Elledge, K. Keyomarsi, B. Dynlacht, L. H. Tsai, P. Zhang, S. Dobrowolski, C. Bai, L. Connell-Crowley, and E. Swindell. "Inhibition of cyclin-dependent kinases by p21." Molecular Biology of the Cell 6, no. 4 (April 1995): 387–400. http://dx.doi.org/10.1091/mbc.6.4.387.

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p21Cip1 is a cyclin-dependent kinase (Cdk) inhibitor that is transcriptionally activated by p53 in response to DNA damage. We have explored the interaction of p21 with the currently known Cdks. p21 effectively inhibits Cdk2, Cdk3, Cdk4, and Cdk6 kinases (Ki 0.5-15 nM) but is much less effective toward Cdc2/cyclin B (Ki approximately 400 nM) and Cdk5/p35 (Ki > 2 microM), and does not associate with Cdk7/cyclin H. Overexpression of P21 arrests cells in G1. Thus, p21 is not a universal inhibitor of Cdks but displays selectivity for G1/S Cdk/cyclin complexes. Association of p21 with Cdks is gre
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16

Egan, Elizabeth A., and Mark J. Solomon. "Cyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases." Molecular and Cellular Biology 18, no. 7 (July 1, 1998): 3659–67. http://dx.doi.org/10.1128/mcb.18.7.3659.

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ABSTRACT Although Cks proteins were the first identified binding partners of cyclin-dependent protein kinases (cdks), their cell cycle functions have remained unclear. To help elucidate the function of Cks proteins, we examined whether their binding to p34 cdc2 (the mitotic cdk) varies during the cell cycle in Xenopusegg extracts. We observed that binding of human CksHs2 to p34 cdc2 was stimulated by cyclin B. This stimulation was dependent on the activating phosphorylation of p34 cdc2 on Thr-161, which follows cyclin binding and is mediated by the cdk-activating kinase. Neither the inhibitory
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17

Verde, F., M. Dogterom, E. Stelzer, E. Karsenti, and S. Leibler. "Control of microtubule dynamics and length by cyclin A- and cyclin B-dependent kinases in Xenopus egg extracts." Journal of Cell Biology 118, no. 5 (September 1, 1992): 1097–108. http://dx.doi.org/10.1083/jcb.118.5.1097.

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In eukaryotic cells, the onset of mitosis involves cyclin molecules which interact with proteins of the cdc2 family to produce active kinases. In vertebrate cells, cyclin A dependent kinases become active in S- and pro-phases, whereas a cyclin B-dependent kinase is mostly active in metaphase. It has recently been shown that, when added to Xenopus egg extracts, bacterially produced A- and B-type cyclins associate predominantly with the same kinase catalytic subunit, namely p34cdc2, and induce its histone H1 kinase activity with different kinetics. Here, we show that in the same cell free system
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18

Zhang, H., Y. Xiong, and D. Beach. "Proliferating cell nuclear antigen and p21 are components of multiple cell cycle kinase complexes." Molecular Biology of the Cell 4, no. 9 (September 1993): 897–906. http://dx.doi.org/10.1091/mbc.4.9.897.

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We have recently shown that two proteins, proliferating cell nuclear antigen (PCNA) and p21, are associated with cyclin D. Here we show that PCNA and p21 are common components of a wide variety of cyclin/cyclin-dependent kinase complexes in nontransformed cells. These include kinase complexes containing cyclin A, cyclin B, and cyclin D, associated either with CDC2, CDK2, CDK4, or CDK5. We show that PCNA and p21 form separate quaternary complex with each cyclin/CDK and that these quaternary complexes contain a substantial, if not major, fraction of the cell cycle kinases in asynchronously growi
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19

Desai, D., Y. Gu, and D. O. Morgan. "Activation of human cyclin-dependent kinases in vitro." Molecular Biology of the Cell 3, no. 5 (May 1992): 571–82. http://dx.doi.org/10.1091/mbc.3.5.571.

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We have analyzed the activation of human cyclin-dependent kinases in a cell-free system. Human CDC2, cyclin-dependent kinase 2 (CDK2), cyclin A, and cyclin B1 were produced in insect cells by infection with recombinant baculoviruses. CDC2 or CDK2 monomers in lysates of infected cells could be activated by the addition of lysates containing cyclin A or B1. CDC2 activation by cyclin B1, as well as CDK2 activation by cyclins A and B1, was accompanied by the formation of high molecular weight complexes. In contrast, CDC2 did not bind effectively to cyclin A. CDC2 activation by cyclin B1 was studie
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20

Fiano, Valentina, Chiara Ghimenti, and Davide Schiffer. "Expression of cyclins, cyclin-dependent kinases and cyclin-dependent kinase inhibitors in oligodendrogliomas in humans." Neuroscience Letters 347, no. 2 (August 2003): 111–15. http://dx.doi.org/10.1016/s0304-3940(03)00615-3.

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21

Lukas, J., J. Bartkova, and J. Bartek. "Convergence of mitogenic signalling cascades from diverse classes of receptors at the cyclin D-cyclin-dependent kinase-pRb-controlled G1 checkpoint." Molecular and Cellular Biology 16, no. 12 (December 1996): 6917–25. http://dx.doi.org/10.1128/mcb.16.12.6917.

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The commitment of mammalian cells in late G1 to replicate the genome and divide in response to mitogenic growth factors operating via tyrosine kinase receptors depends on phosphorylation of the retinoblastoma protein (pRb), a process controlled by cyclin D-associated cyclin-dependent kinases (cdks) and their inhibitors. This study addressed the issue of whether also other mitogenic signalling cascades require activation of cyclin D-associated kinases or whether any mitogenic pathway can bypass the cyclin D-pRb checkpoint. We show that mitogenic signal transduction pathways from three classes o
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22

Choi, Y. J., and L. Anders. "Signaling through cyclin D-dependent kinases." Oncogene 33, no. 15 (May 6, 2013): 1890–903. http://dx.doi.org/10.1038/onc.2013.137.

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23

Malumbres, Marcos, Edward Harlow, Tim Hunt, Tony Hunter, Jill M. Lahti, Gerard Manning, David O. Morgan, Li-Huei Tsai, and Debra J. Wolgemuth. "Cyclin-dependent kinases: a family portrait." Nature Cell Biology 11, no. 11 (November 2009): 1275–76. http://dx.doi.org/10.1038/ncb1109-1275.

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24

Noble, Martin E. M., and Jane A. Endicott. "Chemical Inhibitors of Cyclin-Dependent Kinases." Pharmacology & Therapeutics 82, no. 2-3 (May 1999): 269–78. http://dx.doi.org/10.1016/s0163-7258(98)00051-5.

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25

Nigg, Erich A. "Targets of cyclin-dependent protein kinases." Current Opinion in Cell Biology 5, no. 2 (April 1993): 187–93. http://dx.doi.org/10.1016/0955-0674(93)90101-u.

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26

Meijer, Laurent. "Chemical inhibitors of cyclin-dependent kinases." Trends in Cell Biology 6, no. 10 (October 1996): 393–97. http://dx.doi.org/10.1016/0962-8924(96)10034-9.

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27

Knockaert, Marie, Paul Greengard, and Laurent Meijer. "Pharmacological inhibitors of cyclin-dependent kinases." Trends in Pharmacological Sciences 23, no. 9 (September 2002): 417–25. http://dx.doi.org/10.1016/s0165-6147(02)02071-0.

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28

Hardcastle, Ian R., Bernard T. Golding, and Roger J. Griffin. "DESIGNING INHIBITORS OF CYCLIN-DEPENDENT KINASES." Annual Review of Pharmacology and Toxicology 42, no. 1 (April 2002): 325–48. http://dx.doi.org/10.1146/annurev.pharmtox.42.090601.125940.

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29

LIU, F. "Smad3 phosphorylation by cyclin-dependent kinases." Cytokine & Growth Factor Reviews 17, no. 1-2 (February 2006): 9–17. http://dx.doi.org/10.1016/j.cytogfr.2005.09.010.

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30

Doonan, John H., and Georgios Kitsios. "Functional Evolution of Cyclin-Dependent Kinases." Molecular Biotechnology 42, no. 1 (January 15, 2009): 14–29. http://dx.doi.org/10.1007/s12033-008-9126-8.

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31

Gao, Chun Y., and Peggy S. Zelenka. "Cyclins, cyclin-dependent kinases and differentiation." BioEssays 19, no. 4 (April 1997): 307–15. http://dx.doi.org/10.1002/bies.950190408.

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32

Tian, Jean Q., and Andrea Quaroni. "Involvement of p21(WAF1/Cip1) and p27(Kip1) in intestinal epithelial cell differentiation." American Journal of Physiology-Cell Physiology 276, no. 6 (June 1, 1999): C1245—C1258. http://dx.doi.org/10.1152/ajpcell.1999.276.6.c1245.

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Using the conditionally immortalized human cell line tsFHI, we have investigated the role of cyclin-dependent kinase inhibitors (CKIs) in intestinal epithelial cell differentiation. Expression of cyclins, cyclin-dependent kinases (Cdk), and CKIs was examined under conditions promoting growth, growth arrest, or expression of differentiated traits. Formation of complexes among cell cycle regulatory proteins and their kinase activities were also investigated. The tsFHI cells express three CKIs: p16, p21, and p27. With differentiation, p21 and p27 were strongly induced, but with different kinetics
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33

Tsakraklides, Vasiliki, and Mark J. Solomon. "Comparison of Cak1p-like Cyclin-dependent Kinase-activating Kinases." Journal of Biological Chemistry 277, no. 36 (June 25, 2002): 33482–89. http://dx.doi.org/10.1074/jbc.m205537200.

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34

Preisinger, Christian, and Francis A. Barr. "Kinases regulating Golgi apparatus structure and function." Biochemical Society Symposia 72 (January 1, 2005): 15–30. http://dx.doi.org/10.1042/bss0720015.

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Protein kinases control Golgi function in both mitotic and interphase cells. In mitosis, phosphorylation of structural proteins by Cdk1 (cyclin-dependent kinase 1)-cyclin B, Polo-like and mitogen-activated protein kinases underlie changes in Golgi reorganization during cell division. While in interphase, signalling pathways that are associated with the Golgi control secretory function through a variety of mechanisms. Some of these, notably those involving protein kinase D and Ste20 family kinases, are also relevant for the establishment and maintenance of cell polarization and migration.
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35

Woo, M. S., I. Sánchez, and B. D. Dynlacht. "p130 and p107 use a conserved domain to inhibit cellular cyclin-dependent kinase activity." Molecular and Cellular Biology 17, no. 7 (July 1997): 3566–79. http://dx.doi.org/10.1128/mcb.17.7.3566.

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The pRB-related proteins p107 and p130 are thought to suppress growth in part through their associations with two important cell cycle kinases, cyclin A-cdk2 and cyclin E-cdk2, and transcription factor E2F. Although each protein plays a critical role in cell proliferation, the functional consequences of the association among growth suppressor, cyclin-dependent kinase, and transcription factor have remained elusive. In an attempt to understand the biochemical properties of such complexes, we reconstituted each of the p130-cyclin-cdk2 and p107-cyclin-cdk2 complexes found in vivo with purified, r
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36

Jeannon, J. P., and J. A. Wilson. "Cyclins, cyclin-dependent kinases, cyclin-dependent kinase inhibitors and their role in head and neck cancer." Clinical Otolaryngology and Allied Sciences 23, no. 5 (October 1998): 420–24. http://dx.doi.org/10.1046/j.1365-2273.1998.00182.x.

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37

Huang, H.-H., C.-H. Chen, S.-C. Huang, C.-H. Yang, and C.-F. Hwang. "Expression of 14-3-3 sigma, cyclin-dependent kinases 2 and 4, p16, and Epstein–Barr nuclear antigen 1 in nasopharyngeal carcinoma." Journal of Laryngology & Otology 128, no. 2 (January 24, 2014): 134–41. http://dx.doi.org/10.1017/s0022215113003447.

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AbstractObjective:The protein 14-3-3 sigma plays a role in cell cycle arrest by sequestering cyclin-dependent kinase 1 cyclin B1 complexes, as well as cyclin-dependent kinases 2 and 4, hence its definition as a cyclin-dependent kinase inhibitor. However, the nature of the interaction between these biological markers in nasopharyngeal carcinoma is unknown. This study aimed to investigate whether altered expression of these markers contributes to nasopharyngeal carcinogenesis.Methods:The study population consisted of 30 nasopharyngeal carcinoma patients and 10 patients without nasopharyngeal car
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38

Sweeney, C., M. Murphy, M. Kubelka, S. E. Ravnik, C. F. Hawkins, D. J. Wolgemuth, and M. Carrington. "A distinct cyclin A is expressed in germ cells in the mouse." Development 122, no. 1 (January 1, 1996): 53–64. http://dx.doi.org/10.1242/dev.122.1.53.

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In this paper, the existence of two A-type cyclins in the mouse is demonstrated. In the adult mouse, the expression of cyclin A1, which has greatest sequence identity with Xenopus cyclin A1, is restricted to germ cells. In contrast cyclin A2, which has greatest sequence identity with human cyclin A and Xenopus cyclin A2, is expressed in all tissues analysed. In order to explore the function of cyclin A1 in germ cells, its expression during the meiotic cell cycle and its associated kinase subunits have been characterised in the testis. The levels of cyclin A1 mRNA rise dramatically in late pach
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39

Wang, Shixiong, Sachin Singh, Madhumohan Katika, Sandra Lopez-Aviles, and Antoni Hurtado. "High Throughput Chemical Screening Reveals Multiple Regulatory Proteins on FOXA1 in Breast Cancer Cell Lines." International Journal of Molecular Sciences 19, no. 12 (December 19, 2018): 4123. http://dx.doi.org/10.3390/ijms19124123.

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Forkhead box A1 (FOXA1) belongs to the forkhead class transcription factor family, playing pioneering function for hormone receptors in breast and prostate cancers, and mediating activation of linage specific enhancers. Interplay between FOXA1 and breast cancer specific signaling pathways has been reported previously, indicating a regulation network on FOXA1 in breast cancer cells. Here in this study, we aimed to identify which are the proteins that could potentially control FOXA1 function in breast cancer cell lines expressing different molecular markers. We first established a luciferase rep
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40

Hirai, H., and C. J. Sherr. "Interaction of D-type cyclins with a novel myb-like transcription factor, DMP1." Molecular and Cellular Biology 16, no. 11 (November 1996): 6457–67. http://dx.doi.org/10.1128/mcb.16.11.6457.

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The cyclin D-dependent kinases CDK4 and CDK6 trigger phosphorylation of the retinoblastoma protein (RB) late in G1 phase, helping to cancel its growth-suppressive function and thereby facilitating S-phase entry. Although specific inhibition of cyclin D-dependent kinase activity in vivo can prevent cells from entering S phase, it does not affect S-phase entry in cells lacking functional RB, implying that RB may be the only substrate of CDK4 and CDK6 whose phosphorylation is necessary for G1 exit. Using a yeast two-hybrid interactive screen, we have now isolated a novel cyclin D-interacting myb-
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41

Albrecht, Jeffrey H., Brenda M. Rieland, Christopher J. Nelsen, and Cory L. Ahonen. "Regulation of G1 cyclin-dependent kinases in the liver: role of nuclear localization and p27 sequestration." American Journal of Physiology-Gastrointestinal and Liver Physiology 277, no. 6 (December 1, 1999): G1207—G1216. http://dx.doi.org/10.1152/ajpgi.1999.277.6.g1207.

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Recent studies suggest that cyclin D1 mediates progression of hepatocytes through G1 phase of the cell cycle. The present study further examines the regulation of cyclin D1-dependent kinase activity and the interplay between cyclin D1 and other G1phase regulatory proteins during liver regeneration. After 70% partial hepatectomy in rats, there was upregulation of kinase activity associated with cyclins (A, D1, D3, and E), cyclin-dependent kinases (Cdk2 and Cdk4), and Cdk-inhibitory proteins (p27, p107, and p130). Although cyclin D1/Cdk4 complexes were more abundant in the cytoplasmic fraction a
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42

Kciuk, Mateusz, Adrianna Gielecińska, Somdutt Mujwar, Mariusz Mojzych, and Renata Kontek. "Cyclin-dependent kinases in DNA damage response." Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 1877, no. 3 (May 2022): 188716. http://dx.doi.org/10.1016/j.bbcan.2022.188716.

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43

Morgan, David O. "CYCLIN-DEPENDENT KINASES: Engines, Clocks, and Microprocessors." Annual Review of Cell and Developmental Biology 13, no. 1 (November 1997): 261–91. http://dx.doi.org/10.1146/annurev.cellbio.13.1.261.

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44

Naula, C., R. J. Ford, and J. C. Mottram. "Analysis of Trypanosoma brucei cyclin-dependent kinases." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A482. http://dx.doi.org/10.1042/bst028a482c.

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45

Zhou, Qi. "Targeting Cyclin-Dependent Kinases in Ovarian Cancer." Cancer Investigation 35, no. 6 (April 13, 2017): 367–76. http://dx.doi.org/10.1080/07357907.2017.1283508.

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46

Galbraith, Matthew D., Heather Bender, and Joaquín M. Espinosa. "Therapeutic targeting of transcriptional cyclin-dependent kinases." Transcription 10, no. 2 (November 9, 2018): 118–36. http://dx.doi.org/10.1080/21541264.2018.1539615.

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47

Sherr, C. J., and J. M. Roberts. "Inhibitors of mammalian G1 cyclin-dependent kinases." Genes & Development 9, no. 10 (May 15, 1995): 1149–63. http://dx.doi.org/10.1101/gad.9.10.1149.

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48

Endicott, Jane A., Martin EM Noble, and Julie A. Tucker. "Cyclin-dependent kinases: inhibition and substrate recognition." Current Opinion in Structural Biology 9, no. 6 (December 1999): 738–44. http://dx.doi.org/10.1016/s0959-440x(99)00038-x.

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49

Errico, Alessia, Krupa Deshmukh, Yoshimi Tanaka, Andrei Pozniakovsky, and Tim Hunt. "Identification of substrates for cyclin dependent kinases." Advances in Enzyme Regulation 50, no. 1 (2010): 375–99. http://dx.doi.org/10.1016/j.advenzreg.2009.12.001.

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Jorda, Radek, Eva Schütznerová, Petr Cankař, Veronika Brychtová, Jana Navrátilová, and Vladimír Kryštof. "Novel arylazopyrazole inhibitors of cyclin-dependent kinases." Bioorganic & Medicinal Chemistry 23, no. 9 (May 2015): 1975–81. http://dx.doi.org/10.1016/j.bmc.2015.03.025.

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