Signalling through Class I PI3Ks in mammalian cells

TOR signaling in growth and metabolism

Wullschleger, S., Loewith, R., & Hall, M. N. (2006) · Cell · doi:10.1016/j.cell.2006.01.016 · Cited by 5,787

The phosphoinositide 3-kinase pathway

Cantley, L. C. (2002) · Science · doi:10.1126/science.296.5573.1655 · Cited by 5,621

Cell Migration: Integrating Signals from Front to Back

Ridley, A. J., Schwartz, M. A., Burridge, K., Firtel, R., Ginsberg, M. H., Borisy, G. G., Parsons, J. T., & Horwitz, A. R. (2003) · Science · doi:10.1126/science.1092053 · Cited by 5,109

High Frequency of Mutations of the PIK3CA Gene in Human Cancers

Samuels, Y., Wang, Z., Bardelli, A., Silliman, N., Ptak, J., Szabo, S., Yan, H., Gazdar, A. F., Powell, S. M., Riggins, G. J., et al. (2004) · Science · doi:10.1126/science.1096502 · Cited by 3,448

Targeting RAS signalling pathways in cancer therapy

Downward, J. (2003) · Nature reviews. Cancer · doi:10.1038/nrc969 · Cited by 3,354

The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism

Engelman, J. A., Luo, J., & Cantley, L. C. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1879 · Cited by 3,330

Ras, PI(3)K and mTOR signalling controls tumour cell growth

Shaw, R. J., & Cantley, L. C. (2006) · Nature · doi:10.1038/nature04869 · Cited by 2,019

Phosphatidylinositol-3-OH kinase direct target of Ras

Rodriguez-Viciana, P., Warne, P. H., Dhand, R., Vanhaesebroeck, B., Gout, I., Fry, M. J., Waterfield, M. D., & Downward, J. (1994) · Nature · doi:10.1038/370527a0 · Cited by 1,954

Synthesis and Function of 3-Phosphorylated Inositol Lipids

Vanhaesebroeck, B., Leevers, S. J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P. C., Woscholski, R., Parker, P. J., & Waterfield, M. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.535 · Cited by 1,535

Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis

Cully, M., You, H., Levine, A. J., & Mak, T. W. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1819 · Cited by 1,267

Discovery of 5-(2-amino-[1,2,4]triazolo[1,5-a]pyridin-7-yl)-N-(tert-butyl)pyridine-3-sulfonamide (CZC24758), as a potent, orally bioavailable and selective inhibitor of PI3K for the treatment of inflammatory disease.

Sunose, M., Bell, K., Ellard, K., Bergamini, G., Neubauer, G., Werner, T., & Ramsden, N. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.05.090 · Cited by 23

Gq-coupled Purinergic Receptors Inhibit Insulin-like Growth Factor-I/Phosphoinositide 3-Kinase Pathway-dependent Keratinocyte Migration

Taboubi, S., Garrouste, F. L., Parat, F., Pommier, G. J., Faure, E., Monferran, S., Kovacic, H., & Lehmann, M. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-06-0497 · Cited by 24

Downregulation of eEF1A/EFT3-4 Enhances Dopaminergic Neurodegeneration After 6-OHDA Exposure in C. elegans Model

Chalorak, P., Dharmasaroja, P., & Meemon, K. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00303 · Cited by 24

Direct stimulation of the transcellular and paracellular calcium transport in the rat cecum by prolactin

Kraidith, K., Jantarajit, W., Teerapornpuntakit, J., Nakkrasae, L.-I., Krishnamra, N., & Charoenphandhu, N. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0679-6 · Cited by 24

Ablation of phosphoinositide-3-kinase class II alpha suppresses hepatoma cell proliferation

Ng, S. K.-L., Neo, S.-Y., Yap, Y. W., Karuturi, R. K. M., Loh, E., Liau, K., & Ren, E.-C. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.07.013 · Cited by 24

Discovery of Novel Indazoles as Potent and Selective PI3Kδ Inhibitors with High Efficacy for Treatment of Hepatocellular Carcinoma

Qi, J., Wang, W., Tang, Y., Lou, S., Wang, J., Yuan, T., He, Q., Yang, B., Zhu, H., & Cui, S. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01520 · Cited by 23

Akt suppresses DLK for maintaining self-renewal of mouse embryonic stem cells

Wu, C.-C., Wu, H., Wang, C.-H., Lin, C., Hsu, S., Chen, Y., Hsiao, M., Schuyler, S. C., Lu, F. L., Ma, N. J.-L., et al. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1014144 · Cited by 21

Involvement of Class II Phosphoinositide 3-Kinase α-Isoform in Antigen-Induced Degranulation in RBL-2H3 Cells

Nigorikawa, K., Hazeki, K., Guo, Y., & Hazeki, O. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111698 · Cited by 23

PI3K signalling in lymphocyte migration

Saudemont, A., & Colucci, F. (2009) · Cell Cycle · doi:10.4161/cc.8.20.9692 · Cited by 23

Signal Protein-Derived Peptides as Functional Probes and Regulators of Intracellular Signaling

Shpakov, A. O. (2011) · Journal of Amino Acids · doi:10.4061/2011/656051 · Cited by 25

Single nucleotide polymorphisms within functional regions of genes implicated in insulin action and association with the insulin resistant phenotype

Małodobra-Mazur, M., Pilecka, A., Gworys, B., & Adamiec, R. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0673-5 · Cited by 25

PI3K signaling in Leishmania infections

Kima, P. E. (2016) · Cellular Immunology · doi:10.1016/j.cellimm.2016.09.004 · Cited by 23

Phosphoinositide 3-Kinases—A Historical Perspective

Toker, A. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-3012-0_4 · Cited by 23

Computational model of mesenchymal migration in 3D under chemotaxis

Ribeiro, F. O., Gómez‐Benito, M. J., Folgado, J., Fernandes, P. R., & García‐Aznar, J. M. (2016) · Computer Methods in Biomechanics & Biomedical Engineering · doi:10.1080/10255842.2016.1198784 · Cited by 22

The Potential of Vitamin D-Regulated Intracellular Signaling Pathways as Targets for Myeloid Leukemia Therapy

Gocek, E., & Studzinski, G. P. (2015) · Journal of Clinical Medicine · doi:10.3390/jcm4040504 · Cited by 22

p85α Regulates Osteoblast Differentiation by Cross-talking with the MAPK Pathway

Wu, X., Shi, C., Orlando, S. A., Yuan, J., Kim, E. T., Munugalavadla, V., Mali, R. S., Kapur, R., & Yang, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.187351 · Cited by 22

INPP4A/INPP4B and P-Rex proteins: Related but different?

Rynkiewicz, N. K., Liu, H.-J., Balamatsias, D., & Mitchell, C. A. (2011) · Advances in Biological Regulation · doi:10.1016/j.advenzreg.2011.09.001 · Cited by 22

The Role of the Pathogen Dose and PI3Kγ in Immunometabolic Reprogramming of Microglia for Innate Immune Memory

Lajqi, T., Marx, C., Hudalla, H., Haas, F., Größe, S., Wang, Z., Heller, R., Bauer, M. W., Wetzker, R., & Bauer, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052578 · Cited by 22

Bacillus anthracis Spore Entry into Epithelial Cells Is an Actin-Dependent Process Requiring c-Src and PI3K

Xue, Q., Jenkins, S. A., Gu, C., Smeds, E., Liu, Q., Vasan, R., Russell, B. H., & Xu, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011665 · Cited by 22

Cardiovascular toxicity of PI3Kα inhibitors

Sadasivan, C., Zhabyeyev, P., Labib, D., White, J. A., Paterson, D. I., & Oudit, G. Y. (2020) · Clinical Science · doi:10.1042/cs20200302 · Cited by 22

Phosphoinositide 3-kinases in platelets, thrombosis and therapeutics

Ribes, A. M., Oprescu, A., Viaud, J., Hnia, K., Chicanne, G., Xuereb, J.-M., Séverin, S., Gratacap, M., & Payrastre, B. (2020) · Biochemical Journal · doi:10.1042/bcj20190402 · Cited by 23

Neuroinflammation regulates the balance between hippocampal neuron death and neurogenesis in an ex vivo model of thiamine deficiency

Cassiano, L. M. G., Oliveira, M. D. S., Pioline, J., Salim, A. C. M., & Coimbra, R. S. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02624-6 · Cited by 21

Membrane Docking Geometry of GRP1 PH Domain Bound to a Target Lipid Bilayer: An EPR Site-Directed Spin-Labeling and Relaxation Study

Chen, H.-C., Ziemba, B. P., Landgraf, K. E., Corbin, J., & Falke, J. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033640 · Cited by 21

Discovery of N-{5-[3-(3-hydroxypiperidin-1-yl)-1,2,4-oxadiazol-5-yl]-4-methyl-1,3-thiazol-2-yl}acetamide (TASP0415914) as an orally potent phosphoinositide 3-kinase γ inhibitor for the treatment of inflammatory diseases

Oka, Y., Yabuuchi, T., Oi, T., Kuroda, S., Fujii, Y., Ohtake, H., Inoue, T., Wakahara, S., Kimura, K., Fujita, K., et al. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.10.042 · Cited by 21

HIF-1 α may play a role in late pregnancy hypoxia-induced autism-like behaviors in offspring rats

Wang, W., Tang, J., Zhong, M., Chen, J., Li, T., & Dai, Y. (2021) · Behavioural Brain Research · doi:10.1016/j.bbr.2021.113373 · Cited by 20

Small chemicals with inhibitory effects on PtdIns(3,4,5)P3 binding of Btk PH domain

Yoon, Y. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.03.068 · Cited by 20

Extreme Depletion of PIP3 Accompanies the Increased Life Span and Stress Tolerance of PI3K-null C. elegans Mutants

Bharill, P., Ayyadevara, S., Alla, R., & Reis, R. J. S. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00034 · Cited by 20

Integration of in vitro and in silico Models Using Bayesian Optimization With an Application to Stochastic Modeling of Mesenchymal 3D Cell Migration

Merino-Casallo, F., Gómez‐Benito, M. J., Juste-Lanas, Y., Martínez-Cantín, R., & García‐Aznar, J. M. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01246 · Cited by 21

A key role for phosphorylated inositol compounds in pancreatic β-cell stimulus–secretion coupling

Berggren, P., & Barker, C. J. (2008) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2007.11.012 · Cited by 20

Development and application of PI3K assays for novel drug discovery

Yanamandra, M., Mitra, S., & Giri, A. (2014) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2015.997205 · Cited by 20

Correction: Stem Cell Factor SALL4 Represses the Transcriptions of PTEN and SALL1 through an Epigenetic Repressor Complex

Lu, J., Jeong, H., Kong, N. R., Yang, Y., Carroll, J., Luo, H. R., Silberstein, L. E., YupoMa, & Chai, L. (2009) · PLoS ONE · doi:10.1371/annotation/e0bd3a57-1ce4-4eaf-83de-034d39cac787 · Cited by 20

QSAR analysis on a large and diverse set of potent phosphoinositide 3-kinase gamma (PI3Kγ) inhibitors using MLR and ANN methods

Sadeghi, F., Afkhami, A., Madrakian, T., & Ghavami, R. (2022) · Scientific Reports · doi:10.1038/s41598-022-09843-0 · Cited by 20

Increased expression of the PI3K catalytic subunit p110δ underlies elevated S6 phosphorylation and protein synthesis in an individual with autism from a multiplex family

Poopal, A. C., Schroeder, L. M., Horn, P. S., Bassell, G. J., & Groß, C. (2016) · Molecular Autism · doi:10.1186/s13229-015-0066-4 · Cited by 21

Ras Family Small GTPase-Mediated Neuroprotective Signaling in Stroke

Shi, G., Andres, D., & Cai, W. (2011) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/187152411796011349 · Cited by 19

FGD5 Regulates VEGF Receptor-2 Coupling to PI3 Kinase and Receptor Recycling

Farhan, M., Azad, A. K., Touret, N., & Murray, A. G. (2017) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.117.309978 · Cited by 19

Insight into the selective mechanism of phosphoinositide 3‐kinase γ with benzothiazole and thiazolopiperidine γ‐specific inhibitors by in silico approaches

Zhu, J., Li, K., Xu, L., & Jin, J. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13469 · Cited by 19

THE ROLE OF PI3K SIGNALLING IN THE B CELL RESPONSE TO ANTIGEN

Hodson, D. J., & Turner, M. (2008) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-79311-5_5 · Cited by 19

Nuclear and nucleolar localization signals and their targeting function in phosphatidylinositol 4-kinase PI4K230

Kakuk, A., FRIEDLANDER, E., VEREBJR, G., LISBOA, D., Bagossi, P., Tóth, G. K., Gergely, P., & Vereb, G. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.05.006 · Cited by 19

Targeting PI3K in cancer treatment: A comprehensive review with insights from clinical outcomes

Hossain, M. T., & Hossain, M. A. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177432 · Cited by 21

The Mechanisms and Therapeutic Implications of PI3K Signaling in Airway Inflammation and Remodeling in Asthma

Song, B., Hu, J., Chen, S., & Zhang, Y. (2025) · Biologics · doi:10.2147/btt.s497622 · Cited by 18

Enhanced catecholamine release in mice expressing PKB/SGK-resistant GSK3

Siraskar, B. D., Voelkl, J. G. J., Ahmed, M. S. E., Hierlmeier, M., Gu, S., Schmid, E., Leibrock, C. B., Föller, M., Lang, U. E., & Lang, F. J. W. (2011) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-011-1006-6 · Cited by 18

The Phosphoinosotide 3-Kinase Catalytic Subunit p110α is Required for Normal Lens Growth

Sellitto, C., Li, L., Vaghefi, E., Donaldson, P. J., Lin, R. Z., & White, T. W. (2016) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.16-19607 · Cited by 18

PI3Kγ Mediates Microglial Proliferation and Cell Viability via ROS

Schmidt, C., Schneble, N., Lajqi, T., Wetzker, R., Müller, J. P., & Bauer, R. (2021) · Cells · doi:10.3390/cells10102534 · Cited by 19

Chemotactic signaling in mesenchymal cells compared to amoeboid cells

Vorotnikov, A. V., & Tyurin‐Kuzmin, P. A. (2014) · Genes & Diseases · doi:10.1016/j.gendis.2014.09.006 · Cited by 18

The Insulin-like Growth Factor-1 Axis and its Potential as a Therapeutic Target in Central Nervous System (CNS) Disorders

Bibollet‐Bahena, O., Cui, Q., & Almazán, G. (2009) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/187152409788452108 · Cited by 18

Inter-cellular adhesion disruption and the RAS/RAF and beta-catenin signalling in lung cancer progression

Götz, R. (2008) · Cancer Cell International · doi:10.1186/1475-2867-8-7 · Cited by 19

The p101 subunit of PI3Kγ restores activation by Gβ mutants deficient in stimulating p110γ

Shymanets, A., Ahmadian, M. R., Koessmeier, K. T., Wetzker, R., Harteneck, C., & Nürnberg, B. (2011) · Biochemical Journal · doi:10.1042/bj20111664 · Cited by 17

Different phosphoinositide 3-kinase isoforms mediate carrageenan nociception and inflammation

Pritchard, R. A., Falk, L., Larsson, M., Leinders, M., & Sorkin, L. S. (2015) · Pain · doi:10.1097/j.pain.0000000000000341 · Cited by 17

T-Cell-Specific Loss of the PI-3-Kinase p110α Catalytic Subunit Results in Enhanced Cytokine Production and Antitumor Response

Aragoneses-Fenoll, L., Ojeda, G., Montes‐Casado, M., Acosta‐Ampudia, Y., Dianzani, U., Portolés, P., & Rojo, J. M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00332 · Cited by 18

Activation of the neutrophil NADPH oxidase by Aspergillus fumigatus

Boyle, K. B., Stephens, L., & Hawkins, P. T. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06821.x · Cited by 17

Activation of PDK-1 maintains mouse embryonic stem cell self-renewal in a PKB-dependent manner

Ling, L. S., Voskas, D., & Woodgett, J. R. (2013) · Oncogene · doi:10.1038/onc.2013.44 · Cited by 18

Exploring the role of two interacting phosphoinositide 3-kinases of Haemonchus contortus

Li, F.-C., Gasser, R. B., Lok, J. B., Korhonen, P. K., Wang, Y.-F., Yin, F., He, L., Zhou, R., Zhao, J., & Hu, M. (2014) · Parasites & Vectors · doi:10.1186/preaccept-5374662301417597 · Cited by 17

Effects of PI3K and FSH on steroidogenesis, viability and embryo development of the cumulus–oocyte complex after in vitro culture

de Souza, D. K., Salles, L. P., Camargo, R., Gulart, L. V. M., Silva, S. D. C. E., de Lima, B. D., Torres, F. A. G., & Silva, A. A. M. R. E. (2017) · Zygote · doi:10.1017/s0967199417000703 · Cited by 17

PI3Kγ/AKT Signaling in High Molecular Weight Hyaluronan (HMWH)-Induced Anti-Hyperalgesia and Reversal of Nociceptor Sensitization

Bonet, I. J. M., Khomula, E. V., Araldi, D., Green, P. G., & Levine, J. D. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.1189-21.2021 · Cited by 16

Discovery of 7-(3-(piperazin-1-yl)phenyl)pyrrolo[2,1-f][1,2,4]triazin-4-amine derivatives as highly potent and selective PI3Kδ inhibitors

Qin, L.-Y., Ruan, Z., Cherney, R. J., Dhar, T. G. M., Neels, J. F., Weigelt, C. A., Sack, J. S., Srivastava, A., Cornelius, L. A. M., Tino, J. A., et al. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.01.016 · Cited by 16

Biased binding of class IA phosphatidyl inositol 3-kinase subunits to inducible costimulator (CD278)

Acosta‐Ampudia, Y., Zafra, M. P., Ojeda, G., Bernardone, I. S., Dianzani, U., Portolés, P., & Rojo, J. M. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0606-1 · Cited by 16

Thiazolidinedione‐Based PI3Kα Inhibitors: An Analysis of Biochemical and Virtual Screening Methods

Pinson, J., Schmidt‐Kittler, O., Zhu, J., Jennings, I. G., Kinzler, K. W., Vogelstein, B., Chalmers, D. K., & Thompson, P. E. (2011) · ChemMedChem · doi:10.1002/cmdc.201000467 · Cited by 15

Pharmacological profile of phosphatidylinositol 3‐kinases and related phosphatidylinositols mediating endothelinA receptor‐operated native TRPC channels in rabbit coronary artery myocytes

Shi, J., Ju, M., Large, W. A., & Albert, A. P. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.01937.x · Cited by 15

Antagomir Dependent MicroRNA-205 Reduction Enhances Adhesion Ability of Human Corneal Epithelial Keratinocytes

Li, J., Bai, H., Zhu, Y., Wang, X., Wang, F., Zhang, J.-W., Lavker, R. M., & Yu, J. (2010) · Chinese Medical Sciences Journal · doi:10.1016/s1001-9294(10)60024-7 · Cited by 15

Modification of N-(6-(2-methoxy-3-(4-fluorophenylsulfonamido)pyridin-5-yl)-[1,2,4]triazolo[1,5-a]pyridin-2-yl)acetamide as PI3Ks inhibitor by replacement of the acetamide group with alkylurea

Wang, X.-M., Mao, S., Cao, L., Xie, X., Xin, M., Lian, J.-F., Cao, Y.-X., & Zhang, S. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.07.017 · Cited by 15

Multiple protein kinase pathways mediate amplified IL-6 release by human lung fibroblasts co-exposed to nickel and TLR-2 agonist, MALP-2

Gao, F., Brant, K. A., Ward, R. M., Cattley, R. T., Barchowsky, A., & Fabisiak, J. P. (2010) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2010.06.007 · Cited by 14

Distinct Modes of Activation of Phosphatidylinositol 3-Kinase in Response to Cyclic Adenosine 3′, 5′-Monophosphate or Insulin-Like Growth Factor I Play Different Roles in Regulation of Cyclin D1 and p27Kip1 in FRTL-5 Cells

Fukushima, T., Nedachi, T., Akizawa, H., Akahori, M., Hakuno, F., & Takahashi, S. (2008) · Endocrinology · doi:10.1210/en.2007-1443 · Cited by 14

Polar lipid remodeling and increased sulfatide expression are associated with the glioma therapeutic candidates, wild type p53 elevation and the topoisomerase-1 inhibitor, Irinotecan

He, H., Nilsson, C. L., Emmett, M. R., Ji, Y., Marshall, A. G., Kroes, R. A., Moskal, J. R., Colman, H., Lang, F. F., & Conrad, C. A. (2009) · Glycoconjugate Journal · doi:10.1007/s10719-009-9249-6 · Cited by 14

PI3K Isoform-Selective Inhibitors in Cancer

Duncan, L., Shay, C., & Teng, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-4494-1_14 · Cited by 14

Differential regulation of cytokine production by PI3Kδ in human monocytes upon acute and chronic inflammatory conditions

Molnarfi, N., Brandt, K. J., Gruaz, L., Dayer, J., & Burger, D. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.04.001 · Cited by 14

PTEN in brain tumors

Haas-Kogan, D. A., & Stokoe, D. (2008) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.8.4.599 · Cited by 14

High mass accuracy and resolution facilitate identification of glycosphingolipids and phospholipids

He, H., Emmett, M. R., Nilsson, C. L., Conrad, C. A., & Marshall, A. G. (2010) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2010.10.014 · Cited by 14

Phosphoinositide 3-kinase at the crossroad between endocytosis and signaling of cytokine receptors

Sauvonnet, N. (2013) · Communicative & Integrative Biology · doi:10.4161/cib.24243 · Cited by 13

Inhibition of the PI 3‐kinase pathway disrupts the unfolded protein response and reduces sensitivity to ER stress‐dependent apoptosis

Winnay, J. N., Solheim, M. H., Sakaguchi, M., Njølstad, P. R., & Kahn, C. R. (2020) · The FASEB Journal · doi:10.1096/fj.202000892r · Cited by 13

Total Synthetic Protoapigenone WYC 02 Inhibits Cervical Cancer Cell Proliferation and Tumour Growth through PIK 3 Signalling Pathway

Chen, Y., Kay, N., Yang, J., Lin, C., Chang, H., Wu, Y., Fu, C., Chang, Y., Lo, S. J., Hou, M., et al. (2013) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12057 · Cited by 13

Molecular Hallmarks of Gliomas

Pojo, M., & Marques, B. (2011) · InTech eBooks · doi:10.5772/21352 · Cited by 14

Targeting the PI3K/AKT/mTOR Pathway in Cancer Cells

Guimarães, I. D. S., Tessarollo, N. G., Junior, P. C. M. L., dos Santos, D. Z., Zampier, R. C., de Oliveira, L. F. R. L., Siqueira, K. V., Silva, I. V., & Rangel, L. B. A. (2015) · InTech eBooks · doi:10.5772/61676 · Cited by 13

Comprehensive circular RNA expression profiling with associated ceRNA network reveals their therapeutic potential in cholesteatoma

Gao, J., Tang, Q., Xue, R., Zhu, X., Wang, S., Zhang, Y., Liu, W., Gao, Z., & Yang, H. (2020) · Oncology Reports · doi:10.3892/or.2020.7501 · Cited by 13

Analysis of cellular phosphatidylinositol (3,4,5)-trisphosphate levels and distribution using confocal fluorescent microscopy

Palmieri, M., Nowell, C. J., Condron, M. M., Gardiner, J., Holmes, A. B., Desai, J., Burgess, A. W., & Catimel, B. (2010) · Analytical Biochemistry · doi:10.1016/j.ab.2010.06.033 · Cited by 12

PIP3-binding proteins promote age-dependent protein aggregation and limit survival in C. elegans

Ayyadevara, S., Balasubramaniam, M., Johnson, J. E., Alla, R., Mackintosh, S. G., & Reis, R. J. S. (2016) · Oncotarget · doi:10.18632/oncotarget.10549 · Cited by 12

Lipids and Secretory Vesicle Exocytosis

Akefe, I. O., Osborne, S. L., Matthews, B., Wallis, T. P., & Meunier, F. A. (2023) · Advances in neurobiology · doi:10.1007/978-3-031-34229-5_14 · Cited by 11

SAF-248, a novel PI3Kδ-selective inhibitor, potently suppresses the growth of diffuse large B-cell lymphoma

Zhang, X., Duan, Y., Wang, Y., Zhao, X., Sun, Y.-M., Lin, D., Chen, Y., Wang, Y., Zhou, Z., Liu, Y.-X., et al. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00644-1 · Cited by 11

Interactions between capsid and viral RNA regulate Chikungunya virus translation in a host-specific manner

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