Bibliographies thématiques / CDC25Mm

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Littérature scientifique sur le sujet « CDC25Mm »

Auteur : Grafiati
Publié le 9 mars 2023
Mis à jour le 31 juillet 2025

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Articles de revues sur le sujet "CDC25Mm"

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Ferguson, Angela M., Lynn S. White, Peter J. Donovan, and Helen Piwnica-Worms. "Normal Cell Cycle and Checkpoint Responses in Mice and Cells Lacking Cdc25B and Cdc25C Protein Phosphatases." Molecular and Cellular Biology 25, no. 7 (2005): 2853–60. http://dx.doi.org/10.1128/mcb.25.7.2853-2860.2005.

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ABSTRACT The Cdc25 family of protein phosphatases positively regulates cell division by activating cyclin-dependent protein kinases (CDKs). In humans and rodents, there are three Cdc25 family members—denoted Cdc25A, Cdc25B, and Cdc25C—that can be distinguished based on their subcellular compartmentalizations, their abundances and/or activities throughout the cell cycle, the CDKs that they target for activation, and whether they are overexpressed in human cancers. In addition, murine forms of Cdc25 exhibit distinct patterns of expression throughout development and in adult tissues. These proper
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Lammer, C., S. Wagerer, R. Saffrich, D. Mertens, W. Ansorge, and I. Hoffmann. "The cdc25B phosphatase is essential for the G2/M phase transition in human cells." Journal of Cell Science 111, no. 16 (1998): 2445–53. http://dx.doi.org/10.1242/jcs.111.16.2445.

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Cdc25 phosphatases play key roles in cell cycle progression by activating cyclin-dependent kinases. In human cells, cdc25 proteins are encoded by a multigene family, consisting of cdc25A, cdc25B and cdc25C. While cdc25A plays a crucial role at the G1/S phase transition, cdc25C is involved in the dephosphorylation and activation of the mitotic kinase, cdc2/cyclinB. In addition, cdc25C itself is regulated by cdc2/cyclinB which then creates a positive feedback loop that controls entry into mitosis. In this study we show that the activity of cdc25B appears during late S phase and peaks during G2 p
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Cen, H., A. G. Papageorge, W. C. Vass, K. E. Zhang, and D. R. Lowy. "Regulated and constitutive activity by CDC25Mm (GRF), a Ras-specific exchange factor." Molecular and Cellular Biology 13, no. 12 (1993): 7718–24. http://dx.doi.org/10.1128/mcb.13.12.7718-7724.1993.

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Serum stimulates cells to increase their proportion of Ras protein in the active GTP-bound state. We have recently identified four types (I to IV) of apparently full-length cDNAs from a single mammalian gene, called CDC25Mm or GRF, which is homologous to the Ras-specific exchange factor CDC25 of S. cerevisiae. The largest cDNA (type IV) is brain specific, with the other three classes, although they have distinct 5' ends, essentially representing progressive N-terminal deletions of this cDNA. When placed in a retroviral expression vector, all four types of cDNAs induced morphologic transformati
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Cen, H., A. G. Papageorge, W. C. Vass, K. E. Zhang, and D. R. Lowy. "Regulated and constitutive activity by CDC25Mm (GRF), a Ras-specific exchange factor." Molecular and Cellular Biology 13, no. 12 (1993): 7718–24. http://dx.doi.org/10.1128/mcb.13.12.7718.

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Serum stimulates cells to increase their proportion of Ras protein in the active GTP-bound state. We have recently identified four types (I to IV) of apparently full-length cDNAs from a single mammalian gene, called CDC25Mm or GRF, which is homologous to the Ras-specific exchange factor CDC25 of S. cerevisiae. The largest cDNA (type IV) is brain specific, with the other three classes, although they have distinct 5' ends, essentially representing progressive N-terminal deletions of this cDNA. When placed in a retroviral expression vector, all four types of cDNAs induced morphologic transformati
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Lindqvist, Arne, Helena Källström, Andreas Lundgren, Emad Barsoum, and Christina Karlsson Rosenthal. "Cdc25B cooperates with Cdc25A to induce mitosis but has a unique role in activating cyclin B1–Cdk1 at the centrosome." Journal of Cell Biology 171, no. 1 (2005): 35–45. http://dx.doi.org/10.1083/jcb.200503066.

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Cdc25 phosphatases are essential for the activation of mitotic cyclin–Cdks, but the precise roles of the three mammalian isoforms (A, B, and C) are unclear. Using RNA interference to reduce the expression of each Cdc25 isoform in HeLa and HEK293 cells, we observed that Cdc25A and -B are both needed for mitotic entry, whereas Cdc25C alone cannot induce mitosis. We found that the G2 delay caused by small interfering RNA to Cdc25A or -B was accompanied by reduced activities of both cyclin B1–Cdk1 and cyclin A–Cdk2 complexes and a delayed accumulation of cyclin B1 protein. Further, three-dimension
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Wickramasinghe, D., S. Becker, M. K. Ernst, et al. "Two CDC25 homologues are differentially expressed during mouse development." Development 121, no. 7 (1995): 2047–56. http://dx.doi.org/10.1242/dev.121.7.2047.

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The cdc25 gene product is a tyrosine phosphatase that acts as an initiator of M-phase in eukaryotic cell cycles by activating p34cdc2. Here we describe the cloning and characterization of the developmental expression pattern of two mouse cdc25 homologs. Sequence comparison of the mouse genes with human CDC25 genes reveal that they are most likely the mouse homologs of human CDC25A and CDC25B respectively. Mouse cdc25a, which has not been described previously, shares 84% sequence identity with human CDC25A and has a highly conserved phosphatase domain characteristic of all cdc25 genes. A glutat
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Chen, Mei-Shya, Jonathan Hurov, Lynn S. White, Terry Woodford-Thomas, and Helen Piwnica-Worms. "Absence of Apparent Phenotype in Mice Lacking Cdc25C Protein Phosphatase." Molecular and Cellular Biology 21, no. 12 (2001): 3853–61. http://dx.doi.org/10.1128/mcb.21.12.3853-3861.2001.

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ABSTRACT The Cdc25 family of protein phosphatases positively regulate the cell division cycle by activating cyclin-dependent protein kinases. In humans and rodents, three Cdc25 family members denoted Cdc25A, -B, and -C have been identified. The murine forms of Cdc25 exhibit distinct patterns of expression both during development and in adult mouse tissues. In order to determine unique contributions made by the Cdc25C protein phosphatase to embryonic and adult cell cycles, mice lacking Cdc25C were generated. We report thatCdc25C −/− mice are viable and do not display any obvious abnormalities.
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Zhou, Xiaokun, Danping Lu, Wenxiang Yi, and Dan Xu. "Downregulation of CDC25C in NPCs Disturbed Cortical Neurogenesis." International Journal of Molecular Sciences 24, no. 2 (2023): 1505. http://dx.doi.org/10.3390/ijms24021505.

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Cell division regulators play a vital role in neural progenitor cell (NPC) proliferation and differentiation. Cell division cycle 25C (CDC25C) is a member of the CDC25 family of phosphatases which positively regulate cell division by activating cyclin-dependent protein kinases (CDKs). However, mice with the Cdc25c gene knocked out were shown to be viable and lacked the apparent phenotype due to genetic compensation by Cdc25a and/or Cdc25b. Here, we investigate the function of Cdc25c in developing rat brains by knocking down Cdc25c in NPCs using in utero electroporation. Our results indicate th
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Jacquet, Eric, Soria Baouz, and Andrea Parmeggiani. "Characterization of mammalian C-CDC25Mm exchange factor and kinetic properties of the exchange reaction intermediate p21.cntdot.C-CDC25Mm." Biochemistry 34, no. 38 (1995): 12347–54. http://dx.doi.org/10.1021/bi00038a031.

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Kang, Min, Aera Bang, Ok Choi, and Seung Han. "Comparative analysis of two murine CDC25B isoforms." Archives of Biological Sciences 69, no. 1 (2017): 35–44. http://dx.doi.org/10.2298/abs160315062k.

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CDC25B phosphatase plays a pivotal role in the cell cycle process by dephosphorylating and activating the CDC2 kinase of maturation-promoting factor (MPF). In mice, two transcripts of Cdc25B are generated by the alternative splicing of one gene. We compared the properties of these two forms of CDC25B. When the expression pattern of Cdc25B was examined using RT-PCR, both forms were detected in almost all mouse tissues tested. The expression of two forms of the CDC25B protein in various mouse tissues was confirmed using Western blotting with generated isoform specific antibodies. CDC25B1 tends t
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Thèses sur le sujet "CDC25Mm"

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BAOUZ, SORIA. "Caracterisation et regulation de cdc25mm, facteur d'echange gdp/gtp de souris des proteines ras." Paris 6, 1998. http://www.theses.fr/1998PA066404.

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La proteine h-ras p21 est un element essentiel au controle de la division et de la differenciation cellulaire. Elle existe sous deux conformations : l'une inactive liee au gdp, l'autre active liee au gtp. Deux types de regulateurs determinent la concentration de la forme biologiquement active : les gaps (gtpase activating proteins) qui accelerent l'hydrolyse du gtp et les gefs (guanine nucleotides exchange factors) qui stimulent l'echange gdp/gtp. La proteine cdc25mm de souris contenant 1262 acides amines est un gef de la p21 qui est exprime essentiellement dans les cellules neuronales. Son ro
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METALLI, DAVID. "Development of Cdc25Mn derivatives as anticancer agents." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2009. http://hdl.handle.net/10281/7476.

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Le proteine Ras sono proteine G monomeriche, a basso peso molecolare e dotate di una bassa attività GTPasica intrinseca che svolgono un ruolo chiave nelle vie di trasduzione del segnale coinvolte in processi di crescita e differenziamento cellulare. Ras può funzionare come un vero e proprio interruttore molecolare, trovandosi alternativamente in due stati: uno attivo (legato a GTP) ed uno inattivo (legato a GDP). I passaggi dallo stato attivo a quello inattivo e viceversa possono avvenire spontaneamente, ma la velocità delle due reazioni in questo caso sarebbe molto bassa. Per questo motivo l’
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Thomas, Yann. "Etude de la régulation de la protéolyse de CDC25B1." Montpellier 2, 2009. http://www.theses.fr/2009MON20127.

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Les phosphatases à double spécificité de la famille CDC25 jouent un rôle prépondérant à différents points du cycle cellulaire en activant les complexes CDK/Cyclines. Afin de restreindre l'activation de ces complexes, les CDC25s, au nombre de trois (A, B et C) dans les cellules de mammifères, sont finement régulées au cours du cycle cellulaire tant au niveau de leur activité, de leur localisation que de leur stabilité. La phosphatase CDC25B, en activant initialement le complexe CDK1/Cycline B au niveau des centrosomes, est considérée comme le starter de la mitose. Bien que dégradée par le proté
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Scrivens, Paul James. "Regulation and chemotherapeutic targeting of human Cdc25A phosphatase." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=103293.

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The Cdc25 phosphatases are highly conserved from yeast through humans and play pivotal roles in regulating the activities of cyclin-dependent kinases (Cdks). Cdc25A is one of three human Cdc25 family members, and has previously been shown to be overexpressed in numerous cancers and to transform rodent fibroblasts. Cdc25A therefore represents a rational target for chemotherapeutic development. Further, a thorough understanding of its biology and regulation in normal and transformed cells may facilitate the development of strategies to specifically interfere with the proliferation of cancerous c
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Sayegh, Raphael Santa Rosa. "Flexibilidade conformacional do domínio catalítico da fosfatase Cdc25B." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/46/46131/tde-22082016-080806/.

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A fosfatase Cdc25B atua na progressão do ciclo celular através da ativação de complexos Cdk/Ciclina. Atualmente, nos modelos estruturais propostos do domínio catalítico da Cdc25B não estão incluídos os últimos 16 resíduos da região C-terminal. Este segmento tem importante papel no reconhecimento do substrato proteico e pode estar envolvido na complexação de pequenas moléculas com a Cdc25B. Assim, o principal objetivo desta tese foi avaliar a flexibilidade conformacional do domínio catalítico completo da Cdc25B em solução através de simulações computacionais e por medidas experimentais de resso
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Theis-Febvre, Nathalie. "REGULATION DE L'ACTIVITE ET DE LA LOCALISATION DES PHOSPHATASES CDC25B." Phd thesis, Université Paul Sabatier - Toulouse III, 2003. http://tel.archives-ouvertes.fr/tel-00010054.

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L'activation séquentielle des Kinases Dépendantes des Cyclines (CDK), associées à leur sous-unité régulatrice la cycline, contrôle la progression des cellules eucaryotes dans le cycle cellulaire. L'activité des complexes CDK/cycline est notamment régulée par une balance entre phosphorylation inhibitrice (Wee, Myt) et déphosphorylation activatrice par les phosphatases CDC25. Dans les cellules humaines, trois phosphatases à double spécificité CDC25A, B et C sont impliquées dans la régulation de ces complexes en différents points du cycle cellulaire. CDC25A agit à la transition G1/S alors que CDC
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Akhtar, Nazia. "Structural & biochemical characterisation of Cdc25C : a dual specificity phosphatase." Thesis, University of Birmingham, 2015. http://etheses.bham.ac.uk//id/eprint/5602/.

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The dual specificity Cdc25 phosphatases regulate mitosis and are expressed in eukaryotes. Cdc25 phosphatases have an active site motif, HCX5R, in common with other phosphatases. However, unlike the classical tyrosine phosphatases, they can dephosphorylate phospho-threonine in addition to phospho-tyrosine and have a much shallower active site. Increased expression of Cdc25 is correlated with poor prognosis in a range of cancers. In particular, increased expression of Cdc25C has been associated with prostate cancer making this protein an attractive target for drug discovery. However, drug discov
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Morris, May Catherine. "Régulation de la phosphatase double spécificité cdc25C humaine par phosphorylation." Montpellier 1, 1997. http://www.theses.fr/1997MON1T021.

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Vidal-Fernandez, Anne. "Rôle et régulations de la phosphatase CDC25A dans les hémopathies malignes." Toulouse 3, 2008. http://thesesups.ups-tlse.fr/412/.

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La phosphatase CDC25A active les complexes CDK/Cycline permettant la progression à travers le cycle cellulaire eucaryote. Cette phosphatase agit lors de la phase G1 et en transition G1/S en activant les complexes CDK2/Cycline E et CDK2/Cycline A, et a aussi été décrite comme un régulateur de la mitose à travers la déphosphorylation du complexe CDK1/Cycline B. De manière importante, CDC25A est retrouvée sur-exprimée dans de nombreux cancers. Cependant, les mécanismes moléculaires conduisant à sa sur-expression ne sont pas encore clairement identifiés. Nous avons recherché l'implication de CDC25
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Manzanedo, Lopez Ana. "Élaboration et caractérisation de peptides inhibiteurs de l'interaction cycline B-cdc25C." Montpellier 2, 2005. http://www.theses.fr/2005MON20196.

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Livres sur le sujet "CDC25Mm"

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Chen, Luping. Murine CDC25-related proteins: Activators of Ras. National Library of Canada, 1993.

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Identification of murine Cdc25 homologues expressed in the mitotic and meiotic cell cyles during gametogenesis and examination of their potential functions. 1996.

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Chapitres de livres sur le sujet "CDC25Mm"

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, et al. "CDC25Mm." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100221.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, et al. "CDC25L." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100220.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, et al. "CDC25." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100219.

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Gabrielli, Brian, and Andrew Burgess. "Cdc25 Family Phosphatases in Cancer." In Protein Tyrosine Phosphatases in Cancer. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3649-6_11.

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Rudolph, Johannes. "Targeting Cdc25 Phosphatases in Cancer Therapy." In Checkpoint Controls and Targets in Cancer Therapy. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-178-3_17.

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Nilsson, Ida, and Ingrid Hoffmann. "Cell cycle regulation by the Cdc25 phosphatase family." In Progress in Cell Cycle Research. Springer US, 2000. http://dx.doi.org/10.1007/978-1-4615-4253-7_10.

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Alphey, Luke, Helen White-Cooper, and David Glover. "The Meiotic Role of twine, A Drosophila Homologue of cdc25." In The Cell Cycle. Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2421-2_6.

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Sturani, E., R. Zippel, E. Martegani, et al. "Further Characterization of CDC25 Mm , a Mammalian Activator of p21ras." In Molecular Oncology and Clinical Applications. Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-5663-8_17.

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Jessus, Catherine, and René Ozon. "Function and regulation of cdc25 protein phosphatase through mitosis and meiosis." In Progress in Cell Cycle Research. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1809-9_17.

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Girard, Franck, Anne Fernandez, and Ned Lamb. "cdc25 protein phosphatase in mammalian fibroblasts: cell cycle expression and intracellular localization." In Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78247-3_44.

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Actes de conférences sur le sujet "CDC25Mm"

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Shen, Tao, Hongyu Zhou, and Shile Huang. "Abstract 3810: Ciclopirox olamine downregulates Cdc25A expression in tumor 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.am2012-3810.

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Ramadan, Stephanie, and Khaled Machaca. "Optimizing The Expression And Purification Of Eukaryotic Cdc25c In E. Coli." In Qatar Foundation Annual Research Conference Proceedings. Hamad bin Khalifa University Press (HBKU Press), 2014. http://dx.doi.org/10.5339/qfarc.2014.hbpp0065.

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Yoshimi, Akihide, Takashi Toya, Masahito Kawazu, et al. "Abstract 3439: Recurrent CDC25C mutations drive malignant transformation in FPD/AML." 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.am2014-3439.

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Lee, Caleb C., and James Manfredi. "Abstract 5094: Investigating the role of CDC25B in inhibition of cellular proliferation." 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.am2014-5094.

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Lee, Caleb C., and James Manfredi. "Abstract 3774: Investigating the role of CDC25B in inhibition of cellular proliferation." 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.am2015-3774.

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Brunetto, Emanuela, Anna Talarico, Francesca Rampoldi, et al. "Abstract 3147: HER2 gene amplification and CDC25A overexpression in human breast cancer." 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.am2011-3147.

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Lee, Caleb C., and James Manfredi. "Abstract 574: Investigating the role of CDC25B in inhibition of cellular proliferation." 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.am2013-574.

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Wei, Dongping, Leslie A. Parsels, Mary A. Davis, et al. "Abstract 1582: Inhibition of protein phosphatase 2A radiosensitizes pancreatic cancer cells by modulation of CDC25C." 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.am2013-1582.

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Takehito Azuma, Hisao Moriya, Hayato Matsumuro, and Hiroaki Kitano. "A robustness analysis of eukaryotic cell cycle concerning Cdc25 and wee1 proteins." In 2006 IEEE Conference on Computer Aided Control System Design, 2006 IEEE International Conference on Control Applications, 2006 IEEE International Symposium on Intelligent Control. IEEE, 2006. http://dx.doi.org/10.1109/cacsd-cca-isic.2006.4776903.

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Azuma, Takehito, Hisao Moriya, Hayato Matsumuro, and Hiroaki Kitano. "A Robustness Analysis of Eukaryotic Cell Cycle concerning Cdc25 and Wee1 Proteins." In 2006 IEEE International Conference on Control Applications. IEEE, 2006. http://dx.doi.org/10.1109/cca.2006.286135.

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Rapports d'organisations sur le sujet "CDC25Mm"

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Kiyokawa, Hiroaki. Role of CDC25A in Breast Cancer Development. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada415692.

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Manfredi, James J. Role of Cdc25C Phosphatases in Human Breast Cancer. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada472361.

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Manfredi, James J. Role of Cdc25C Phosphatases in Human Breast Cancer. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada474891.

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Galaktionov, Konstantin I. Role of cdc25 Phosphatases in Cellular Immortalization. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada369304.

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Galaktionov, Konstantin. Role of cdc25 Phosphatases in Cellular Immortalization. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada391626.

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Manfredi, James J. Role of cdc25 Phosphatases in Human Breast Cancer. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada484236.

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Manfredi, James J. Role of cdc25 Phosphatases in Human Breast Cancer. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada487929.

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