Relevant bibliographies by topics / Phosphatidylinositol 3-Kinases

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Phosphatidylinositol 3-Kinases'

Author: Grafiati
Published: 4 June 2021
Last updated: 8 June 2024

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Journal articles on the topic "Phosphatidylinositol 3-Kinases"

1

Abraham, Robert T. "Phosphatidylinositol 3-kinase related kinases." Current Opinion in Immunology 8, no. 3 (1996): 412–18. http://dx.doi.org/10.1016/s0952-7915(96)80132-4.

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Suzuki, Takahiro, Osamu Hazeki, and Michio Ui. "Phosphatidylinositol 3-Kinases." membrane 21, no. 3 (1996): 158–64. http://dx.doi.org/10.5360/membrane.21.158.

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Muftuoglu, Yagmur, Yi Xue, Xiang Gao, Dianqing Wu, and Ya Ha. "Mechanism of substrate specificity of phosphatidylinositol phosphate kinases." Proceedings of the National Academy of Sciences 113, no. 31 (2016): 8711–16. http://dx.doi.org/10.1073/pnas.1522112113.

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The phosphatidylinositol phosphate kinase (PIPK) family of enzymes is primarily responsible for converting singly phosphorylated phosphatidylinositol derivatives to phosphatidylinositol bisphosphates. As such, these kinases are central to many signaling and membrane trafficking processes in the eukaryotic cell. The three types of phosphatidylinositol phosphate kinases are homologous in sequence but differ in catalytic activities and biological functions. Type I and type II kinases generate phosphatidylinositol 4,5-bisphosphate from phosphatidylinositol 4-phosphate and phosphatidylinositol 5-ph
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Rane, M. J., S. L. Carrithers, J. M. Arthur, J. B. Klein, and K. R. McLeish. "Formyl peptide receptors are coupled to multiple mitogen-activated protein kinase cascades by distinct signal transduction pathways: role in activation of reduced nicotinamide adenine dinucleotide oxidase." Journal of Immunology 159, no. 10 (1997): 5070–78. http://dx.doi.org/10.4049/jimmunol.159.10.5070.

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Abstract Formyl peptide receptor activation of three mitogen-activated protein kinase (MAPK) cascades, extracellular signal-regulated kinases (ERKs), N-terminal kinases (JNKs), and p38 MAPK was examined in differentiated HL-60 granulocytes. FMLP stimulated a concentration- and time-dependent increase in ERK, JNK, and p38 MAPK activities, all of which were dependent on a pertussis toxin-sensitive G protein. Pharmacologic inhibitors were used to examine the roles of tyrosine kinases, phosphatidylinositol 3-kinase, protein kinase C, and phospholipase C. FMLP-stimulated ERK activity was dependent
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Roymans, Dirk, and Herman Slegers. "Phosphatidylinositol 3-kinases in tumor progression." European Journal of Biochemistry 268, no. 3 (2001): 487–98. http://dx.doi.org/10.1046/j.1432-1327.2001.01936.x.

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Imseng, Stefan, Christopher HS Aylett, and Timm Maier. "Architecture and activation of phosphatidylinositol 3-kinase related kinases." Current Opinion in Structural Biology 49 (April 2018): 177–89. http://dx.doi.org/10.1016/j.sbi.2018.03.010.

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Shibasaki, F., Y. Fukui, and T. Takenawa. "Different properties of monomer and heterodimer forms of phosphatidylinositol 3-kinases." Biochemical Journal 289, no. 1 (1993): 227–31. http://dx.doi.org/10.1042/bj2890227.

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Phosphatidylinositol (PI) 3-kinase plays an important role in the signalling of cell growth. We previously purified two types of PI 3-kinase from bovine thymus, a monomer from (PI 3-kinase I) and a heterodimer form (PI 3-kinase II) [Shibasaki, Homma and Takenawa (1991) J. Biol. Chem. 266, 8108-8114]. Here we examine the properties of these purified PI 3-kinases. Both PI 3-kinases were inhibited strongly by quercetin and isoquercetin. The inhibition of PI 3-kinase I and PI 3-kinase II by quercetin appears to be non-competitive, with apparent Ki values of 4 microM and 2.5 microM respectively. PI
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Yamboliev, Ilia A., Kevin M. Wiesmann, Cherie A. Singer, Jason C. Hedges, and William T. Gerthoffer. "Phosphatidylinositol 3-kinases regulate ERK and p38 MAP kinases in canine colonic smooth muscle." American Journal of Physiology-Cell Physiology 279, no. 2 (2000): C352—C360. http://dx.doi.org/10.1152/ajpcell.2000.279.2.c352.

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In canine colon, M2/M3 muscarinic receptors are coupled to extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein (MAP) kinases. We tested the hypothesis that this coupling is mediated by enzymes of the phosphatidylinositol (PI) 3-kinase family. RT-PCR and Western blotting demonstrated expression of two isoforms, PI 3-kinase-α and PI 3-kinase-γ. Muscarinic stimulation of intact muscle strips (10 μM ACh) activated PI 3-kinase-γ, ERK and p38 MAP kinases, and MAP kinase-activated protein kinase-2, whereas PI 3-kinase-α activation was not detected. Wortmannin (25 μM) abolish
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Choi, Suyong, Xander Houdek, and Richard A. Anderson. "Phosphoinositide 3-kinase pathways and autophagy require phosphatidylinositol phosphate kinases." Advances in Biological Regulation 68 (May 2018): 31–38. http://dx.doi.org/10.1016/j.jbior.2018.02.003.

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Christoforidis, Savvas, Marta Miaczynska, Keith Ashman, et al. "Phosphatidylinositol-3-OH kinases are Rab5 effectors." Nature Cell Biology 1, no. 4 (1999): 249–52. http://dx.doi.org/10.1038/12075.

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Dissertations / Theses on the topic "Phosphatidylinositol 3-Kinases"

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Valet, Colin. "Rôles de la PI3 kinase de classe II alpha et de la PI3K de classe III, vps34, dans la production et les fonctions plaquettaires." Thesis, Toulouse 3, 2017. http://www.theses.fr/2017TOU30032.

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Les mégacaryocytes sont des cellules de la moelle osseuse qui par un processus complexe et encore mal caractérisé, mégacaryopoïèse/thrombopoïèse, donnent naissance, in fine, aux plaquettes sanguines. La différenciation mégacaryocytaire nécessite un intense remodelage nucléaire et cytoplasmique, guidé à la fois par des facteurs intrinsèques mais aussi par des facteurs extrinsèques tel que le microenvironnement médullaire. Les plaquettes sanguines sont des acteurs essentiels du maintien de l'intégrité vasculaire. Elles sont les premiers éléments cellulaires à intervenir dans l'arrêt du saignemen
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Riojas, Ramon Alberto. "Characterization of PDK1 regulation and function in the insulin-stimulated PI3-kinase pathway : a dissertation /." San Antonio : UTHSC, 2007. http://proquest.umi.com/pqdweb?did=1372010131&sid=1&Fmt=2&clientId=70986&RQT=309&VName=PQD.

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Cox, Sian Sarah Eileen. "Characterisation of putative phosphatidylinositol-3 kinases in the parasitic protozoan giardia instestinalis." Thesis, Royal Holloway, University of London, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.498208.

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Fos, Camille. "Etude de la signalisation P 13-kinase induite par le récepteur de costimulation ICOS au cours de l'activation lymphocytaire T." Aix-Marseille 2, 2008. http://theses.univ-amu.fr.lama.univ-amu.fr/2008AIX22012.pdf.

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Il est maintenant communément admis qu’une activation lymphocytaire T efficace requiert deux signaux indépendants. Le premier, qui détermine la spécificité de la réponse immunitaire, est délivré au travers de l’interaction du récepteur à l’antigène sur la cellule T (TcR) avec le complexe CMH-peptide antigénique à la surface des cellules présentatrices d’antigène. Un signal additionnel (ou signal 2) aussi appelé costimulateur, est critique pour la régulation de l’activation lymphocytaire T. La signalisation induite par le couple ICOS/ICOS-L fournit à la cellule un second signal positif qui cont
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Pomerance, Martine. "Etapes précoces de la transmission du signal des facteurs de croissance : phosphatidylinositol-3 kinase et protéines serine/threonine kinases." Paris 11, 1994. http://www.theses.fr/1994PA11T008.

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Bardet, Valérie. "Anomalies de la signalisation dans les leucémies aiguës myéloïdes." Paris 7, 2006. http://www.theses.fr/2006PA077070.

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Les leucémies aiguës myéloïdes (LAM) sont des maladies clonales qui atteignent des progéniteurs de la lignée myéloïde. Elles résultent de la coexistence d'au moins deux anomalies : un blocage de la différenciation et une prolifération cellulaire anormale. Des activations anormales de voies de signalisation, en particulier des voies PI3K/Akt/mTOR, Ras/MAPK et JAK/STAT ont été mises en évidence dans ces hémopathies. Nous nous sommes intéressés dans ce travail à l'étude des anomalies de la voie PI3K/Akt. Nous avons retrouvé une activation constitutive de cette voie de signalisation dans 50% des é
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Mujalli, Abdulrahman. "Phosphoinositides in blood platelet : mapping of molecular species and evidence for a new localization and role of PI3P." Thesis, Toulouse 3, 2018. http://www.theses.fr/2018TOU30110.

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Les phosphoinositides (PIs) sont des phospholipides membranaires qui jouent un rôle crucial dans le contrôle de l'organisation spatio-temporelle de nombreuses voies de signalisation intracellulaire, du réarrangement du cytosquelette d'actine et du trafic de vésicules. Dans la plaquette, le métabolisme des PIs est particulièrement actif et génère, par le jeu de kinases, phosphatases et phospholipases spécifiques, des seconds messagers indispensables à l'activation plaquettaire, notamment le phosphatidylinositol 3,4,5-trisphosphate (PIP3). La première partie de la thèse concerne l'étude des diff
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Gobin, Bérengère. "Approches thérapeutiques des ostéosarcomes par ciblage des activités kinases." Nantes, 2013. http://archive.bu.univ-nantes.fr/pollux/show.action?id=38b2d404-a1cc-40e0-b8c7-038cf56a7994.

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L'ostéosarcome est la plus fréquente des tumeurs osseuses primitives malignes et est caractérisé par la production de tissu ostéoide tumoral avec ou sans lésions ostéolytiques. Malgré des avancées en termes de chimiothérapie et de chirurgie, le taux de survie des patients reste inchangé depuis plusieurs années. L'absence de réponse aux drogues et l'établissement de résistance montre l'urgence d'explorer de nouvelles voies thérapeutiques. Durant la dernière décade, les avancées biologiques et technologiques ont permis l'émergence de nouvelles thérapies ciblées. Ces drogues inhibitrices sont reg
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Chen, Xi. "The role of PI3K and ERK/MAPK signal transduction cascades in long-term memory formation /." Thesis, Connect to this title online; UW restricted, 2004. http://hdl.handle.net/1773/6248.

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Rojnuckarin, Ponlapat. "Mitogen-activated protein kinase pathways in megakaryocyte development /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/9200.

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Books on the topic "Phosphatidylinositol 3-Kinases"

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Devereaux, Kelly Anne. The role of phosphatidylinositol 3-kinases in autophagy regulation. [publisher not identified], 2014.

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Falcioni, Lisa. The role of the phosphatidylinositol-3 kinase-Akt pathway in determining radiation sensivity in the breast cancer cell line MDA-MB 231. Laurentian University, School of Graduate Studies, 2005.

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Analysis of Complex Diseases: A Mathematical Perspective. Taylor & Francis Group, 2013.

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Ban, Kiwon. The role of phosphatidylinositol-3 kinase isomers in myocardial ischemic preconditioning. 2005.

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Wang, Guanyu. Analysis of Complex Diseases: A Mathematical Perspective. Taylor & Francis Group, 2013.

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Wang, Guanyu. Analysis of Complex Diseases: A Mathematical Perspective. Taylor & Francis Group, 2013.

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Wang, Guanyu. Analysis of Complex Diseases: A Mathematical Perspective. Taylor & Francis Group, 2013.

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Menon, Deepa U. Autism and Intellectual Disabilities. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0053.

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PTEN (phosphatase and tensin homologue) on chromosome 10q23.3 is a tumor suppressor gene that encodes for a dual specificity phosphatase that regulates the phosphatidylinositol 3- kinase pathway and has an important role in brain development by affecting neuronal survival, neurite outgrowth, synaptic plasticity, and learning memory. Germline mutations of the PTEN gene have been implicated in a group of related tumor syndromes with autosomal dominant inheritance and variable expression and include the Cowden syndrome, Bannayan-Riley-Ruvalcaba syndrome, Proteus syndrome, and Juvenile Polyposis s
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Book chapters on the topic "Phosphatidylinositol 3-Kinases"

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Burke, John E., and Roger L. Williams. "Phosphatidylinositol 3-Kinases." In Encyclopedia of Metalloproteins. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_53.

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, et al. "Phosphatidylinositol 3-Kinase." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101025.

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Robert, Jacques. "Phosphatidylinositol 3-Kinase Pathway." In Textbook of Cell Signalling in Cancer. Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-14340-8_3.

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Lee, Yuree, Teun Munnik, and Youngsook Lee. "Plant Phosphatidylinositol 3-Kinase." In Lipid Signaling in Plants. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-03873-0_6.

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, et al. "Phosphatidylinositol 3-OH Kinase." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101026.

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Schomburg, Dietmar, and Dörte Stephan. "1-Phosphatidylinositol 3-kinase." In Enzyme Handbook. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59025-2_32.

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Vogt, Peter K., Jonathan R. Hart, Marco Gymnopoulos, et al. "Phosphatidylinositol 3-Kinase: The Oncoprotein." In Current Topics in Microbiology and Immunology. Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/82_2010_80.

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Robert, Jacques. "La voie de la phosphatidylinositol-3-kinase." In Signalisation cellulaire et cancer. Springer Paris, 2010. http://dx.doi.org/10.1007/978-2-8178-0028-8_4.

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Salajegheh, Ali. "Phosphatidylinositol-4, 5-Bisphosphate 3-Kinase (PIK3Ca)." In Angiogenesis in Health, Disease and Malignancy. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_37.

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Salajegheh, Ali. "PIK3R2 (p85β) – Phosphatidylinositol 3-Kinase β-Subunit." In Angiogenesis in Health, Disease and Malignancy. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_38.

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Conference papers on the topic "Phosphatidylinositol 3-Kinases"

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Ni, Qiang, Matthew Fosbrink, and Jin Zhang. "Illuminating the phosphatidylinositol 3-kinase/Akt pathway." In Biomedical Optics (BiOS) 2008, edited by Alexander P. Savitsky, Robert E. Campbell, and Robert M. Hoffman. SPIE, 2008. http://dx.doi.org/10.1117/12.765524.

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Suga, K., Y. Uemura, T. Tsuijinaka, M. Sakon, J. Kambayashi, and T. Mori. "PROPERTIES OF PHOSPHATIDYLINOSITOL KINASE IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643807.

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We have reported the specific 32P-labelling in phosphatidyl-inositol-4-monophosphate(PIP) of intact platelets upon addition of the agents which elevate intracellular cAMP (Thrombos.Res.44, 155,1986).This event may be catalyzed by the action of Pl-kinase, the properties of which has not been elucidatedyet.Thereby, attempts were made to assay and to characterize PI-kinase of human platelets.Fresh lysed platelets prelabelled with 32P in cold Tris-HCl buffer containing 2mM EGTA were incubated at 37 C in the presence of MgCl2 for designated times and the phospholipids were extracted and analyzed by
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Trautmann, Marcel, Magdalene Cyra, Christian Bertling, et al. "Abstract 3939: Activation of phosphatidylinositol-3′-kinase/Akt signaling in myxoid liposarcoma." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3939.

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Troxell, ML, D. Ang, A. Warrick, C. Beadling, and CL Corless. "Abstract P2-08-03: Phosphatidylinositol-3-kinase mutations are common in lobular neoplasia." In Abstracts: Thirty-Fifth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 4‐8, 2012; San Antonio, TX. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/0008-5472.sabcs12-p2-08-03.

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Geletu, Mulu, Samantha Greer, and Leda Raptis. "Abstract 31: Activated phosphatidylinositol-3 kinase: An oncogene that increases gap junctional, intercellular communication." 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.am2012-31.

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Rapp, Judit, Vivien Telek, Tunde Minier, László Czirják, Timea Berki, and Diana Simon. "THU0326 ANALYSIS OF PHOSPHATIDYLINOSITOL 3-KINASE PATHWAY IN B CELL ACTIVATION OF SYSTEMIC SCLEROSIS PATIENTS." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.7499.

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Anders, CK, B. Adamo, AM Deal, et al. "Abstract P1-14-01: Phosphatidylinositol 3-Kinase (PI3K) Pathway Activation in Breast Cancer Brain Metastases." In Abstracts: Thirty-Third Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 8‐12, 2010; San Antonio, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/0008-5472.sabcs10-p1-14-01.

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Troxell, ML, AL Brunner, K. Montgomery, et al. "P2-06-04: Phosphatidylinositol-3-Kinase Pathway Mutations Are Common in Breast Columnar Cell Lesions." In Abstracts: Thirty-Fourth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 6‐10, 2011; San Antonio, TX. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/0008-5472.sabcs11-p2-06-04.

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Choi, Youn Jin, Yoo Yeon Jung, and Jing Jing Liu. "Abstract 338: Inhibition of phosphatidylinositol 3-kinase signaling antagonizes paclitaxel-mediated resistance in cervical 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.am2019-338.

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Choi, Youn Jin, Yoo Yeon Jung, and Jing Jing Liu. "Abstract 338: Inhibition of phosphatidylinositol 3-kinase signaling antagonizes paclitaxel-mediated resistance in cervical 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.sabcs18-338.

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Reports on the topic "Phosphatidylinositol 3-Kinases"

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Balajee, A. S., J. A. Meador, and Y. Su. Cellular response to low dose radiation: Role of phosphatidylinositol-3 kinase like kinases. Office of Scientific and Technical Information (OSTI), 2011. http://dx.doi.org/10.2172/1009811.

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Hutchinson, John N., and William Muller. The Role of Phosphatidylinositol 3' -OH Kinase Signaling in Mammary Tumorigenesis. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada396742.

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Parker, Amanda P., Barbara S. Beckman, and Matthew Burow. Phosphatidylinositol 3-Kinase and Protein Kinase C as Molecular Determinants of Chemoresistance in Breast Cancer. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada409382.

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Parker, Amanda, Barbara Beckman, and Matthew E. Burow. Phosphatidylinositol 3-Kinase and Protein Kinase C as Molecular Determinants of Chemoresistance in Breast Cancer. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada431891.

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Hansen, Peter J., and Amir Arav. Embryo transfer as a tool for improving fertility of heat-stressed dairy cattle. United States Department of Agriculture, 2007. http://dx.doi.org/10.32747/2007.7587730.bard.

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The overall objective of the current proposal is to develop procedures to improve the pregnancy rate achieved following transfer of fresh or cryopreserved embryos produced in the laboratory into heat-stress recipients. The overall hypothesis is that pregnancy rate in heat-stressed lactating cows can be improved by use of embryo transfer and that additional gains in pregnancy rate can be achieved through development of procedures to cryopreserve embryos, select embryos most likely to establish and maintain pregnancy after transfer, and to enhance embryo competence for post-transfer survival thr
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