Calmodulin and PI3K Signaling in KRAS Cancers.
暂无分享,去创建一个
Ruth Nussinov | Shaoyong Lu | Jian Zhang | Hyunbum Jang | Chung-Jung Tsai | Avik Banerjee | Guanqiao Wang | R. Nussinov | Shaoyong Lu | Jian Zhang | Chung-Jung Tsai | H. Jang | V. Gaponenko | Vadim Gaponenko | A. Banerjee | Guanqiao Wang | Hyunbum Jang
[1] J. McDonald,et al. The insulin receptor and calmodulin. Calmodulin enhances insulin-mediated receptor kinase activity and insulin stimulates phosphorylation of calmodulin. , 1986, The Journal of biological chemistry.
[2] D. Sacks,et al. Characteristics of calmodulin phosphorylation by the insulin receptor kinase. , 1988, Endocrinology.
[3] D. Sacks,et al. Insulin-stimulated phosphorylation of calmodulin by rat liver insulin receptor preparations. , 1988, The Journal of biological chemistry.
[4] H. Nakano,et al. In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine-like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[5] D. Sacks,et al. Tyrosine-specific phosphorylation of calmodulin by the insulin receptor kinase purified from human placenta. , 1989, The Biochemical journal.
[6] K. Glenn,et al. The carboxyl terminal segment of the c-Ki-ras 2 gene product mediates insulin-stimulated phosphorylation of calmodulin and stimulates insulin-independent autophosphorylation of the insulin receptor. , 1989, Biochemical and biophysical research communications.
[7] D. Sacks,et al. Calmodulin as Substrate for Insulin-Receptor Kinase: Phosphorylation by Receptors From Rat Skeletal Muscle , 1989, Diabetes.
[8] C. Kahn,et al. Expression and function of IRS-1 in insulin signal transmission. , 1992, The Journal of biological chemistry.
[9] B. Margolis,et al. Phosphatidylinositol 3′‐kinase is activated by association with IRS‐1 during insulin stimulation. , 1992, The EMBO journal.
[10] L. Cantley,et al. Phosphoinositide 3-kinase is activated by phosphopeptides that bind to the SH2 domains of the 85-kDa subunit. , 1993, The Journal of biological chemistry.
[11] J. Schlessinger,et al. Specific phosphopeptide binding regulates a conformational change in the PI 3‐kinase SH2 domain associated with enzyme activation. , 1993, The EMBO journal.
[12] R. Sharma,et al. Tyrosine-phosphorylated calmodulin has reduced biological activity. , 1994, Archives of biochemistry and biophysics.
[13] D. Sacks. Alteration of calmodulin-protein interactions by a monoclonal antibody to calmodulin. , 1994, Biochimica et biophysica acta.
[14] A. Benguría,et al. Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase. , 1994, European journal of biochemistry.
[15] Peter J. Parker,et al. The activation of phosphatidylinositol 3-kinase by Ras , 1994, Current Biology.
[16] R. Thoma,et al. Identification of insulin-stimulated phosphorylation sites on calmodulin. , 1996, Biochemistry.
[17] M. White,et al. Calmodulin Activates Phosphatidylinositol 3-Kinase* , 1997, The Journal of Biological Chemistry.
[18] G. Benaim,et al. Comparative phosphorylation of calmodulin from trypanosomatids and bovine brain by calmodulin-binding protein kinases. , 1998, Comparative biochemistry and physiology. Part C, Pharmacology, toxicology & endocrinology.
[19] A. Villalobo,et al. A method for the purification of phospho(Tyr)calmodulin free of nonphosphorylated calmodulin. , 1999, Protein expression and purification.
[20] A. Means,et al. Calmodulin: a prototypical calcium sensor. , 2000, Trends in cell biology.
[21] C. Marshall,et al. Calmodulin Binds to K-Ras, but Not to H- or N-Ras, and Modulates Its Downstream Signaling , 2001, Molecular and Cellular Biology.
[22] M. Waterfield,et al. Synthesis and function of 3-phosphorylated inositol lipids. , 2001, Annual review of biochemistry.
[23] G. Benaim,et al. Phosphorylation of calmodulin. Functional implications. , 2002, European journal of biochemistry.
[24] Vojo Deretic,et al. Tuberculosis Toxin Blocking Phagosome Maturation Inhibits a Novel Ca2+/Calmodulin-PI3K hVPS34 Cascade , 2003, The Journal of experimental medicine.
[25] Valéria Szukacsov,et al. Lysophosphatidylcholine is a regulator of tyrosine kinase activity and intracellular Ca(2+) level in Jurkat T cell line. , 2004, Immunology letters.
[26] J. Comella,et al. Glial Cell Line-derived Neurotrophic Factor Increases Intracellular Calcium Concentration , 2004, Journal of Biological Chemistry.
[27] C. Thompson,et al. PKC regulates a farnesyl-electrostatic switch on K-Ras that promotes its association with Bcl-XL on mitochondria and induces apoptosis. , 2006, Molecular cell.
[28] S. Planchon,et al. Growth Factor-dependent AKT Activation and Cell Migration Requires the Function of c-K(B)-Ras Versus Other Cellular Ras Isoforms* , 2006, Journal of Biological Chemistry.
[29] B. Vanhaesebroeck,et al. Class IA phosphoinositide 3-kinases are obligate p85-p110 heterodimers , 2007, Proceedings of the National Academy of Sciences.
[30] K. Kinzler,et al. The Structure of a Human p110a/p85a Complex Elucidates the Effects of Oncogenic PI3Ka Mutations , 2007 .
[31] Bert Vogelstein,et al. The Structure of a Human p110α/p85α Complex Elucidates the Effects of Oncogenic PI3Kα Mutations , 2007, Science.
[32] G. Stamp,et al. Binding of Ras to Phosphoinositide 3-Kinase p110α Is Required for Ras- Driven Tumorigenesis in Mice , 2007, Cell.
[33] Yuval Inbar,et al. Mechanism of Two Classes of Cancer Mutations in the Phosphoinositide 3-Kinase Catalytic Subunit , 2007, Science.
[34] Jing Xu,et al. Subtoxic N‐methyl‐D‐aspartate delayed neuronal death in ischemic brain injury through TrkB receptor‐ and calmodulin‐mediated PI‐3K/Akt pathway activation , 2007, Hippocampus.
[35] R. Copeland,et al. Effects of oncogenic p110alpha subunit mutations on the lipid kinase activity of phosphoinositide 3-kinase. , 2008, The Biochemical journal.
[36] Li Zhao,et al. Helical domain and kinase domain mutations in p110α of phosphatidylinositol 3-kinase induce gain of function by different mechanisms , 2008, Proceedings of the National Academy of Sciences.
[37] L. Zhao,et al. Class I PI3K in oncogenic cellular transformation , 2008, Oncogene.
[38] R. Copeland,et al. Effects of oncogenic p110α subunit mutations on the lipid kinase activity of phosphoinositide 3-kinase , 2008 .
[39] O. Bachs,et al. Identification of Essential Interacting Elements in K-Ras/Calmodulin Binding and Its Role in K-Ras Localization* , 2008, Journal of Biological Chemistry.
[40] L. Anderson,et al. The hypervariable region of K-Ras4B is responsible for its specific interactions with calmodulin. , 2009, Biochemistry.
[41] K. Kinzler,et al. A frequent kinase domain mutation that changes the interaction between PI3Kα and the membrane , 2009, Proceedings of the National Academy of Sciences.
[42] Karim Jellali,et al. Calmodulin‐mediated regulation of the epidermal growth factor receptor , 2010, The FEBS journal.
[43] M. Drosten,et al. K-Ras4B phosphorylation at Ser181 is inhibited by calmodulin and modulates K-Ras activity and function , 2010, Oncogene.
[44] Zoologie. Glial Cell Line-Derived Neurotrophic Factor , 2011 .
[45] John E. Burke,et al. Structural Basis for Activation and Inhibition of Class I Phosphoinositide 3-Kinases , 2011, Science Signaling.
[46] Jie Chen,et al. Both the C-Terminal Polylysine Region and the Farnesylation of K-RasB Are Important for Its Specific Interaction with Calmodulin , 2011, PloS one.
[47] N. Agell,et al. CaM interaction and Ser181 phosphorylation as new K-Ras signaling modulators , 2011, Small GTPases.
[48] Yong Zhou,et al. Nonsteroidal Anti-inflammatory Drugs Alter the Spatiotemporal Organization of Ras Proteins on the Plasma Membrane* , 2012, The Journal of Biological Chemistry.
[49] Carla Mattos,et al. A comprehensive survey of Ras mutations in cancer. , 2012, Cancer research.
[50] Glenn R Masson,et al. Oncogenic mutations mimic and enhance dynamic events in the natural activation of phosphoinositide 3-kinase p110α (PIK3CA) , 2012, Proceedings of the National Academy of Sciences.
[51] P. Bastiaens,et al. The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins , 2011, Nature Cell Biology.
[52] P. Bastiaens,et al. The GDI-like solubilizing factor PDEδ sustains the spatial organization and signalling of Ras family proteins , 2012, Nature Cell Biology.
[53] F. Bermejo-Pareja,et al. Altered calmodulin degradation and signaling in non-neuronal cells from Alzheimer's disease patients. , 2012, Current Alzheimer research.
[54] Activation of PI3Kα by physiological effectors and by oncogenic mutations: structural and dynamic effects , 2014, Biophysical Reviews.
[55] V. Gaponenko,et al. Application of Reductive 13C-Methylation of Lysines to Enhance the Sensitivity of Conventional NMR Methods , 2013, Molecules.
[56] I. Prior,et al. Oncogenic K-ras segregates at spatially distinct plasma membrane signaling platforms according to its phosphorylation status , 2013, Journal of Cell Science.
[57] M. Berchtold,et al. The many faces of calmodulin in cell proliferation, programmed cell death, autophagy, and cancer. , 2014, Biochimica et biophysica acta.
[58] R. Xiang,et al. Emerging roles of the p38 MAPK and PI3K/AKT/mTOR pathways in oncogene-induced senescence. , 2014, Trends in biochemical sciences.
[59] Ozlem Keskin,et al. Plasma membrane regulates Ras signaling networks , 2015, Cellular logistics.
[60] Ozlem Keskin,et al. Principles of K-Ras effector organization and the role of oncogenic K-Ras in cancer initiation through G1 cell cycle deregulation , 2015, Expert review of proteomics.
[61] Ozlem Keskin,et al. The Key Role of Calmodulin in KRAS-Driven Adenocarcinomas , 2015, Molecular Cancer Research.
[62] A. Cox,et al. K-Ras4A splice variant is widely expressed in cancer and uses a hybrid membrane-targeting motif , 2015, Proceedings of the National Academy of Sciences.
[63] A. Balmain,et al. K-Ras Promotes Tumorigenicity through Suppression of Non-canonical Wnt Signaling , 2015, Cell.
[64] M. Menéndez,et al. Characterization of Phospho-(Tyrosine)-Mimetic Calmodulin Mutants , 2015, PloS one.
[65] A. Benguría,et al. The activating role of phospho-(Tyr)-calmodulin on the epidermal growth factor receptor. , 2015, The Biochemical journal.
[66] R. Nussinov,et al. Mechanisms of Membrane Binding of Small GTPase K-Ras4B Farnesylated Hypervariable Region* , 2015, The Journal of Biological Chemistry.
[67] J. Griffiths,et al. Absolute Quantification of Endogenous Ras Isoform Abundance , 2015, PloS one.
[68] G. Benaim,et al. Ca2+/Calmodulin and Apo-Calmodulin Both Bind to and Enhance the Tyrosine Kinase Activity of c-Src , 2015, PloS one.
[69] Ruth Nussinov,et al. High-Affinity Interaction of the K-Ras4B Hypervariable Region with the Ras Active Site , 2015, Biophysical journal.
[70] M. Lavin,et al. β-Adducin siRNA disruption of the spectrin-based cytoskeleton in differentiating keratinocytes prevented by calcium acting through calmodulin/epidermal growth factor receptor/cadherin pathway. , 2015, Cellular signalling.
[71] C. Der,et al. Targeting RAS-mutant cancers: is ERK the key? , 2015, Trends in cancer.
[72] C. Der,et al. Targeting RAS Membrane Association: Back to the Future for Anti-RAS Drug Discovery? , 2015, Clinical Cancer Research.
[73] Kendra Marcus,et al. Direct Attack on RAS: Intramolecular Communication and Mutation-Specific Effects , 2015, Clinical Cancer Research.
[74] Ruth Nussinov,et al. A New View of Ras Isoforms in Cancers. , 2016, Cancer research.
[75] T Aittokallio,et al. Cancer stem cell drugs target K-ras signaling in a stemness context , 2016, Oncogene.
[76] Suyong Choi,et al. The Hidden Conundrum of Phosphoinositide Signaling in Cancer. , 2016, Trends in cancer.
[77] Ruth Nussinov,et al. Oncogenic KRAS signaling and YAP1/β-catenin: Similar cell cycle control in tumor initiation. , 2016, Seminars in cell & developmental biology.
[78] L. Birnbaumer,et al. Membrane translocation of TRPC6 channels and endothelial migration are regulated by calmodulin and PI3 kinase activation , 2016, Proceedings of the National Academy of Sciences.
[79] Frank McCormick,et al. K-Ras protein as a drug target , 2016, Journal of Molecular Medicine.
[80] Herbert Waldmann,et al. Regulation of K-Ras4B Membrane Binding by Calmodulin. , 2016, Biophysical journal.
[81] R. Ghirlando,et al. Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ , 2016, Proceedings of the National Academy of Sciences.
[82] D. Calvisi,et al. Comparison of liver oncogenic potential among human RAS isoforms , 2016, Oncotarget.
[83] Wei Zhang,et al. Identification of initial leads directed at the calmodulin-binding region on the Src-SH2 domain that exhibit anti-proliferation activity against pancreatic cancer. , 2016, Bioorganic & medicinal chemistry letters.
[84] Ozlem Keskin,et al. Ras Conformational Ensembles, Allostery, and Signaling. , 2016, Chemical reviews.
[85] M. Hall,et al. mTOR Signaling Confers Resistance to Targeted Cancer Drugs. , 2016, Trends in cancer.
[86] Ozlem Keskin,et al. K-Ras4B/calmodulin/PI3Kα: A promising new adenocarcinoma-specific drug target? , 2016, Expert opinion on therapeutic targets.
[87] Ruth Nussinov,et al. Independent and core pathways in oncogenic KRAS signaling , 2016, Expert review of proteomics.
[88] Ruth Nussinov,et al. The higher level of complexity of K‐Ras4B activation at the membrane , 2016, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[89] Ruth Nussinov,et al. The disordered hypervariable region and the folded catalytic domain of oncogenic K-Ras4B partner in phospholipid binding. , 2016, Current opinion in structural biology.
[90] R. Nussinov,et al. Comparison of the Conformations of KRAS Isoforms, K-Ras4A and K-Ras4B, Points to Similarities and Significant Differences. , 2016, The journal of physical chemistry. B.
[91] Ruth Nussinov,et al. Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view. , 2016, Chemical Society reviews.
[92] Xu Shen,et al. SP6616 as a new Kv2.1 channel inhibitor efficiently promotes β-cell survival involving both PKC/Erk1/2 and CaM/PI3K/Akt signaling pathways , 2016, Cell Death and Disease.