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Bibliografías temáticas / Cyclin-dependent kinases

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

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

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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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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 system, we show that the E2F-1-DP-1 heterodimer, the functionally active form of the E2F activity, is not a substrate for the active cyclin D-dependent kinases but is efficiently phosphorylated by the cyclin B-dependent kinases, which do not form stable complexes with the E2F-1-DP-1 heterodimer. Phosphorylation of the E2F-1-DP-1 heterodimer by cyclin B-dependent kinases, however, did not result in down-regulation of its DNA-binding activity, as is readily seen after phosphorylation by cyclin A-dependent kinases, suggesting that phosphorylation per se is not sufficient to regulate E2F DNA-binding activity. Furthermore, heterodimers containing E2F-4, a family member lacking the cyclin A binding domain found in E2F-1, are not efficiently phosphorylated or functionally down-regulated by cyclin A-dependent kinases. However, addition of the E2F-1 cyclin A binding domain to E2F-4 conferred cyclin A-dependent kinase-mediated down-regulation of the E2F-4-DP-1 heterodimer. Thus, both enzymatic phosphorylation and stable physical interaction are necessary for the specific regulation of E2F family members by cyclin-dependent kinases.

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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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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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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 advanced leukemia. Pacritinib is also currently being tested in phase III clinical trial for treatment of myelofibrosis and, loratinib is being evaluated for advanced ALK gene positive nonsmall cell lung carcinoma. The broad-spectrum cyclin-dependent kinases inhibitor, TGO2, has also entered phase II clinical trial for treatment of glioblastoma and advanced leukemia.

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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 days after reperfusion. No significant protection was observed when flavopiridol was administered 8 hours after reperfusion. The tumor-suppressor retinoblastoma protein, a substrate of cyclin-dependent kinase, was phosphorylated on a cyclin-dependent kinase consensus site after the global insult; this phosphorylation was inhibited by flavopiridol administration. Importantly, flavopiridol had no effect on core body temperature, suggesting that the mechanism of neuroprotection was through cyclin-dependent kinase inhibition but not through hypothermia. Furthermore, inhibition of cyclin-dependent kinases improved spatial learning behavior as assessed by the Morris water maze 7 to 9 days after reperfusion. However, the histologic protection observed at day 7 was absent 28 days after reperfusion. These results indicate that cyclin-dependent kinase inhibition provides an extended period of morphologic and functional neuroprotection that may allow time for other neuroprotective modalities to be introduced.

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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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Tesis sobre el tema "Cyclin-dependent kinases"

1

Kitsios, Georgios. "Characterization of Arabidopsis cyclin dependent kinases." Thesis, University of East Anglia, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.426634.

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Miller, Matthew P. Ph D. (Matthew Paul) Massachusetts Institute of Technology. "Meiotic regulation of cyclin-dependent kinases." Thesis, Massachusetts Institute of Technology, 2013. http://hdl.handle.net/1721.1/79185.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2013.<br>Cataloged from PDF version of thesis.<br>Includes bibliographical references.<br>During meiosis, a single round of DNA replication is followed by two consecutive rounds of nuclear divisions called meiosis I and meiosis II. In meiosis I, homologous chromosomes segregate, while sister chromatids remain together. Determining how this unusual chromosome segregation behavior is established is central to understanding germ cell development. Here we show that preventing microtubule-kinetochore interactions during premeiotic S phase and prophase I is essential for establishing the meiosis I chromosome segregation pattern. Premature interactions of kinetochores with microtubules transform meiosis I into a mitosis-like division by disrupting two key meiosis I events: coorientation of sister kinetochores and protection of centromeric cohesin removal from chromosomes. Furthermore we find that restricting outer kinetochore assembly contributes to preventing premature engagement of microtubules with kinetochores. We propose that inhibition of microtubule-kinetochore interactions during premeiotic S phase and prophase I is central to establishing the unique meiosis I chromosome segregation pattern.<br>by Matthew P. Miller.<br>Ph.D.

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Gomes, Felipe Campelo. "Analysis of cyclin dependent kinases in Leishmania." Thesis, University of Glasgow, 2007. http://theses.gla.ac.uk/32/.

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The results obtained from the experiments presented in this study aimed to further explore the role of cyclin dependent kinases and cyclins in the protozoan parasite Leishmania major. Cdks in kinetoplastids, CRKs, are the key regulators that allow cells to progress through different cell cycle phases and promote parasite proliferation during infection. In chapter 3 of this study, the results presented showed that L. major CYCA is capable of activating CRK3 in an in vitro kinase assay using histone H1 as substrate. The CRK3/CYCA active complex was then used to analyse the effect of the phosphorylation at the CRK3 activation threonine using a kinase activating kinase (yeast CAK or Civ-1). Phosphorylated CRK3 activity was compared to non-phosphorylated CRK3 and it was found that the phosphorylation promotes a 5-fold increase in kinase activity of the complex. The accessory protein Cks1 was assayed in vitro with the active CRK3/CYCA complex and it was shown that Cks1 might have an inhibitory effect when histone H1 substrate is used. The IC50 for two different kinase inhibitors (Flavopiridol and Indirubin) was determined for the in vitro CRK3/CYCA complex and compared with the values found for the in vivo purified CRK3. Similar values were obtained suggesting that the in vivo complex is indeed represented by the recombinant complex. In the following chapter 4, yeast Civ-1 purified from E. coli, was used to try to phosphorylate, in a similar manner, the activation of threonine/serine residues from other L. major CRKs. The kinases assessed were CRK1, CRK2, CRK4, CRK6 and CRK7. None of these were phosphorylated by Civ-1 suggesting that the only CRK under this type of regulation is CRK3. L. major CRK1-4 and CRK6-8 were tested in kinase assays by mixing under described conditions with L. major CYC9 and kinase activities towards three different substrates were assessed. L. major CYC9 was not able to activate the above kinases and the kinase subunit that interacts with this cyclin could not be identified. In chapter 5, the L. major CYCA was used to elucidate the characteristics of this cyclin in vivo. A gene disruption strategy aimed to replace the two genomic alleles of this protein gene by homologous recombination. Plasmids were developed with flanking regions of this gene placed in association with two different drug resistance genes, one for each of the allele’s disruption. These constructs were not able to produce the first allele knock out suggesting that not only this gene might be essential but the levels of expression may also be important. Tagging L. major CYCA was also attempted in vivo using two different strategies (i.e. two different tagging systems). The first tag employed was the TAP tag syste. Although drug resistant transfected cell lines were obtained, no tag detection could be observed by western blot using different tag-specific antibodies (α-protein-A and α-calmodulin antibodies). The second tag employed was HA, the 9-amino acid sequence YPYDVPDYA, derived from the human influenza hemagglutinin (HA) protein. Plasmids that contained C and N-terminal HA tagged L. major CYCA were used to transfect WT cells and cells extracts of resistant cell lines analysed by western blot. Both C and N-terminal HA tagged CYCA were detected by the α-HA antibody. Following the confirmation of the presence of the tagged CYCA in the cell extracts an affinity purification using an HA affinity matrix was attempted and the matrix binding material was used in in vitro kinase assays. The presence of kinase activity towards Histone H1 confirmed that CYCA was being succesfully immunoprecipitated in complex with a kinase partner. The identity of the co-eluted CRK could be confirmed using specific α-CRK3 antibody that detected CRK3 in the eluted material.

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4

Secombe, Julie. "Identification of novel G1 to S phase regulators in Drosophila /." Title page, contents and abstract only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phs4448.pdf.

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Crack, Donna. "Analysis of the function of Drosophila cyclin E isoforms and identification of interactors." Title page, table of contents and abstract only, 2002. http://web4.library.adelaide.edu.au/theses/09PH/09phc8837.pdf.

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"August 2002." Bibliography: p. 157-169. Analysis of the expression of Drosophilia cyclin EII through development show that it was present during larval development and oogenesis, implying a role for DmcycEII outside of early embyogenesis. Ectopic expression analyses using full-length DmcycE proteins as well as N- and C-terminal deletions of DmcycEI, revealed that DmcycEII and N-terminal deletions were able to drive all G1 cells within the morphogenetic furrow of the eye imaginal disc into S phase, while a C-terminal deletion of DmcycEI could not. These results show the DmcycEII is more potent than DmcycEI in driving cells into S phase and that the N-terminal region of DmcycEI contains a negative regulatory domean., suggesting that an inhibitor is present in the posterior morphogenetic furrow that binds to DmcycEI N-terminus and inhibits DmcycEI function. To identify the DmcycEI specific inhibitor, genetic interaction and yeast-2 hybrid screens were undertaken, and an enhancer CG7394, encoding a MAGUK homologue was identified for further study.

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6

Dixon-Clarke, Sarah. "Structure and inhibition of novel cyclin-dependent kinases." Thesis, University of Oxford, 2015. https://ora.ox.ac.uk/objects/uuid:3c6955c9-469a-4f4b-9577-309ccb57b742.

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Protein phosphorylation by members of the cyclin-dependent kinase (CDK) family determines the cell cycle and regulates gene transcription. CDK12 and CDK16 are relatively poorly characterised family members containing atypical domain extensions and represent novel targets for structural studies, as well as cancer drug discovery. In this thesis, I developed protocols to express and purify the human CDK12 kinase domain in complex with its obligate partner, CycK. I solved three distinct crystal structures of the complex providing insights into the structural mechanisms determining CycK assembly and kinase activation. These structures revealed a C-terminal kinase extension that folded flexibly across the active site of CDK12 to potentially gate the binding of the substrate ATP. My structures also identified Cys1039 in the C-terminal extension as the binding site for the first selective covalent inhibitor of CDK12, which has enormous potential as a pharmacological probe to investigate the functions of CDK12 in the DNA damage response and cancer. I also identified rebastinib and dabrafenib as potent, clinically-relevant inhibitors of CDK16 and solved a co-crystal structure that defined the extended type II binding mode of rebastinib. Preliminary trials using these relatively non-selective compounds to inhibit CDK16 in melanoma and medulloblastoma cancer cell lines revealed rebastinib as the more efficacious drug causing loss of cell proliferation in the 1-2 micromolar range. Use of the co-crystal structure to design more selective derivatives would be advantageous to further explore the specific role of CDK16. Finally, I identified a D-type viral cyclin from Kaposi's sarcoma-associated herpesvirus that could bind to the CDK16 kinase domain and interfere with its functional complex with human CycY causing loss of CDK16 activity. These studies provide novel insights into the structural and regulatory mechanisms of two underexplored CDK family subgroups and establish new opportunities for cancer drug development.

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7

Sallam, Hatem. "Pharmacological and analytical studies of the cyclin dependent kinase inhibitors." Stockholm, 2009. http://diss.kib.ki.se/2009/978-91-7409-706-1/.

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8

Alexiou, Konstantinos G. "Cyclin-dependent kinases and nuclear functions in Arabidopsis thaliana." Thesis, University of East Anglia, 2011. https://ueaeprints.uea.ac.uk/34236/.

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9

Henderson, Andrew. "Isosteres of sulfonamide inhibitors of cyclin-dependent kinases (CDKs)." Thesis, University of Newcastle Upon Tyne, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.512187.

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10

Cheng, Kai. "Identification of Pctaire1 as a p35-interacting protein and a novel substrate for Cdk5 /." View Abstract or Full-Text, 2003. http://library.ust.hk/cgi/db/thesis.pl?BICH%202003%20CHENG.

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Thesis (Ph. D.)--Hong Kong University of Science and Technology, 2003.<br>Includes bibliographical references (leaves 153-177). Also available in electronic version. Access restricted to campus users.

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Libros sobre el tema "Cyclin-dependent kinases"

1

Dyson, Nicholas. Abstracts of papers presented at the 2008 meeting on the cell cycle: May 14-May 18, 2008. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 2008.

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Elledge, Stephen Joseph, and J. Wade Harper. Abstracts of papers presented at the 2002 meeting on the cell cycle, May 15-May 19, 2002. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 2002.

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Biggins, Susan, and Nicholas Dyson. Abstracts of papers presented at the 2010 meeting on the cell cycle: May 18-May 22, 2010. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 2010.

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B, Kastan M., and Imperial Cancer Research Fund (Great Britain), eds. Checkpoint controls and cancer. Plainview, NY: Cold Spring Harbor Laboratory Press, 1997.

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5

Vogt, Peter K., and Steven I. Reed, eds. Cyclin Dependent Kinase (CDK) Inhibitors. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-71941-7.

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Orzáez, Mar, Mónica Sancho Medina, and Enrique Pérez-Payá, eds. Cyclin-Dependent Kinase (CDK) Inhibitors. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-2926-9.

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Ip, Nancy Y., and Li-Huei Tsai, eds. Cyclin Dependent Kinase 5 (Cdk5). Boston, MA: Springer US, 2008. http://dx.doi.org/10.1007/978-0-387-78887-6.

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Chen, Ginny. Analysis of Saccharomyces cerevisiae cyclin dependent kinase inhibitor Far1. Ottawa: National Library of Canada, 2003.

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9

Technologie, Karlsruher Institut für, ed. Phosphorylation and Regulation of the Wnt co-Receptor LRP6 by Cyclin Dependent Kinase 14/Cyclin Y and Tyrosine Kinase Fer. [S.l: s.n.], 2014.

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Logan, Angela Berti. Characterization of new alleles of PHO85, a cyclin-dependent kinase of Saccharomyces cerevisiae. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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Capítulos de libros sobre el tema "Cyclin-dependent kinases"

1

Golsteyn, Roy M. "Cyclin-Dependent Kinases." In Encyclopedia of Cancer, 1–4. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_1429-2.

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Golsteyn, Roy M. "Cyclin-Dependent Kinases." In Encyclopedia of Cancer, 1269–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_1429.

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Malumbres, Marcos. "Cyclins and Cyclin-dependent Kinases." In Encyclopedia of Systems Biology, 509–12. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4419-9863-7_10.

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Meijer, Laurent. "Chemical inhibitors of cyclin-dependent kinases." In Progress in Cell Cycle Research, 351–63. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1809-9_29.

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Law, Mary E., and Brian K. Law. "Cyclin-Dependent Kinases as Therapeutic Targets." In Encyclopedia of Molecular Pharmacology, 505–7. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57401-7_10043.

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Law, Mary E., and Brian K. Law. "Cyclin-dependent kinases as therapeutic targets." In Encyclopedia of Molecular Pharmacology, 1–3. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-21573-6_10043-1.

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Koff, Andrew, and Kornelia Polyak. "p27KIP1, an inhibitor of cyclin-dependent kinases." In Progress in Cell Cycle Research, 141–47. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1809-9_11.

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Li, Yan, Christopher W. Jenkins, Michael A. Nichols, Xiaoyu Wu, Kun-Liang Guan, and Yue Xiong. "p16 Family Inhibitors of Cyclin-Dependent Kinases." In Cancer Genes, 57–82. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5895-8_4.

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Johnson, Neil, and Geoffrey I. Shapiro. "Targeting Cyclin-Dependent Kinases for Cancer Therapy." In Cell Cycle Deregulation in Cancer, 167–85. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-1770-6_11.

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Boutros, Rose. "Regulation of Centrosomes by Cyclin-Dependent Kinases." In The Centrosome, 187–97. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-035-9_11.

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Actas de conferencias sobre el tema "Cyclin-dependent kinases"

1

Surin, Svyatoslav Sergeevich, and G. L. Snigur. "Expression of cyclin-dependent kinases in pancreatic islets during experimental hyperglycemia." In International Research Conference on Technology, Science, Engineering & Management. Seattle: Профессиональная наука, 2021. http://dx.doi.org/10.54092/9781365973192_35.

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Surin, Svyatoslav Sergeevich, and G. L. Snigur. "Expression of cyclin-dependent kinases in pancreatic islets during experimental hyperglycemia." In International Research Conference on Technology, Science, Engineering & Management. Seattle: Профессиональная наука, 2021. http://dx.doi.org/10.54092/9781365973192_35.

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Денисова, Дарья Андреевна. "CYCLIN-DEPENDENT KINASES CDK8 / 19 AND THEIR INFLUENCE ON THE ORIGIN AND DEVELOPMENT OF TUMOR PROCESSES." In Наука. Исследования. Практика: сборник избранных статей по материалам Международной научной конференции (Санкт-Петербург, Апрель 2020). Crossref, 2020. http://dx.doi.org/10.37539/srp290.2020.80.21.015.

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Циклин-зависимая киназа CDK8 и её паралог, CDK19, являются ферментами, задействованными в развитии таких онкологических заболеваний, как рак молочной железы, колоректальный рак, рак простаты, острый миелоидный лейкоз и другие. The cyclin-dependent kinase CDK8 and its paralogue, CDK19, are enzymes involved in the development of oncological diseases such as breast cancer, colorectal cancer, prostate cancer, acute myeloid leukemia and others.

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Kholmurodov, Kholmirzo T., Yu E. Penionzhkevich, and E. A. Cherepanov. "Computer Molecular Dynamics Studies on Protein Structures (Visual Pigment Rhodopsin and Cyclin-Dependent Kinases)." In INTERNATIONAL SYMPOSIUM ON EXOTIC NUCLEI. AIP, 2007. http://dx.doi.org/10.1063/1.2746628.

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Kunadharaju, R., A. Saradna, M. Ahmad, and G. Fuhrer. "Palbociclib (Cyclin-Dependent Kinases CDK4 and CDK6 Selective Inhibitor) Induced Grade 3 Interstitial Pneumonitis." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a2118.

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Sankaranarayanan, Ranjini, Rakesh Dachineni, Siddharth Kesharwani, Ramesh Kumar Dhandapani, Hemachand Tummala, and Jayarama B. Gunaje. "Abstract 4411: Identification of novel natural compounds as potential inhibitors of cyclin dependent kinases." 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.sabcs18-4411.

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Sankaranarayanan, Ranjini, Rakesh Dachineni, Siddharth Kesharwani, Ramesh Kumar Dhandapani, Hemachand Tummala, and Jayarama B. Gunaje. "Abstract 4411: Identification of novel natural compounds as potential inhibitors of cyclin dependent kinases." 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.am2019-4411.

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Fu, Wei, Le Ma, Baoky Chu, Xue Wang, Tapan K. Bagui, Marilyn M. Bui, Jennifer Gemmer, Soner Altiok, Douglas G. Letson, and W. Jack Pledger. "Abstract 3596: SCH727965, a cyclin-dependent kinases inhibitor, induces apoptosis in sarcoma cells through caspase 3- dependent pathway." 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.am2011-3596.

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Ramos Rodríguez, J., S. Hernández Rojas, I. González Perera, MM Viña Romero, GJ Nazco Casariego, FJ Merino Alonso, S. García Gil, B. Del Rosario García, L. Cantarelli, and F. Gutiérrez Nicolás. "5PSQ-059 Cyclin dependent kinases 4/6 inhibitors: new options in hr+ her2- breast cancer." In 24th EAHP Congress, 27th–29th March 2019, Barcelona, Spain. British Medical Journal Publishing Group, 2019. http://dx.doi.org/10.1136/ejhpharm-2019-eahpconf.492.

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10

Tien, Amy H., Nasrin R. Mawji, Jun Wang, and Marianne D. Sadar. "Abstract 1000: Targeting androgen receptors and cyclin-dependent kinases 4 and 6 in breast cancer." 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.am2019-1000.

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Informes sobre el tema "Cyclin-dependent kinases"

1

Wohlschlegel, James, and Anindya Dutta. Development of Inhibitors That Selectively Disrupt Substrate Recognition by Cyclin-Dependent Kinases. Fort Belvoir, VA: Defense Technical Information Center, August 2002. http://dx.doi.org/10.21236/ada410428.

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2

Donovan, Joseph. Development and Use of Novel Tools to Directly Screen for Substrates of Cyclin Dependent Kinases. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada376126.

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3

Donovan, Joseph. Development and Use of Novel Tools to Directly Screen for Substrates of Cyclin Dependent Kinases. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada392561.

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4

Williams, Stephen D. Cyclin Dependent Kinase Inhibitors as Targets in Ovarian Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2005. http://dx.doi.org/10.21236/ada446399.

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5

Williams, Stephen D. Cyclin Dependent Kinase Inhibitors as Targets in Ovarian Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2002. http://dx.doi.org/10.21236/ada411751.

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6

Williams, Stephen D. Cyclin Dependent Kinase Inhibitors as Targets in Ovarian Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2003. http://dx.doi.org/10.21236/ada420941.

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7

Harper, J. W. The Role of Cyclin Dependent Kinase Inhibitor, Cip1, in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 1998. http://dx.doi.org/10.21236/ada366917.

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8

Harper, J. W. The Role of Cyclin Dependent Kinase Inhibitor, CIP1, in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 1995. http://dx.doi.org/10.21236/ada302399.

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9

Harper, J. W. The Role of Cyclin Dependent Kinase Inhibitor, CIP1, in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 1997. http://dx.doi.org/10.21236/ada341520.

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10

Harper, J. W. The Role of Cyclin Dependent Kinase Inhibitor, CIP1, in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 1999. http://dx.doi.org/10.21236/ada381538.

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