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Volumn 51, Issue 1, 2010, Pages 4-22

Phosphoinositide 3-kinase signaling in the vertebrate retina

Author keywords

[No Author keywords available]

Indexed keywords

CHECKPOINT KINASE RAD3; DIACYLGLYCEROL KINASE; G PROTEIN COUPLED RECEPTOR; GLYCOGEN SYNTHASE KINASE 3; GUANOSINE TRIPHOSPHATASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INSULIN RECEPTOR SUBSTRATE 1; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHATIDYLINOSITOL KINASE; PHOSPHOLIPASE C; PLATELET DERIVED GROWTH FACTOR; PROTEIN CDC42; PROTEIN KINASE B; PROTEIN P50; PROTEIN P85; PROTEIN SH2; PROTEIN TYROSINE PHOSPHATASE 1B; RETINA S ANTIGEN; S6 KINASE; SOMATOMEDIN RECEPTOR; TARGET OF RAPAMYCIN KINASE; TRANSDUCIN;

EID: 73149103927     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.R000232     Document Type: Review
Times cited : (29)

References (291)
  • 1
    • 84960994832 scopus 로고
    • Enzyme secretion and the incorporation of P32 into phospholipides of pancreas slices
    • Hokin, M. R., and L. E. Hokin. 1953. Enzyme secretion and the incorporation of P32 into phospholipides of pancreas slices. J. Biol. Chem. 203: 967-977.
    • (1953) J. Biol. Chem , vol.203 , pp. 967-977
    • Hokin, M.R.1    Hokin, L.E.2
  • 2
    • 0005521383 scopus 로고
    • Effects of acetylcholine on the turnover of phosphoryl units in individual phospholipids of pancreas slices and brain cortex slices
    • Hokin, L. E., and M. R. Hokin. 1955. Effects of acetylcholine on the turnover of phosphoryl units in individual phospholipids of pancreas slices and brain cortex slices. Biochim. Biophys. Acta. 18: 102-110.
    • (1955) Biochim. Biophys. Acta , vol.18 , pp. 102-110
    • Hokin, L.E.1    Hokin, M.R.2
  • 3
    • 0020643801 scopus 로고
    • Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate
    • Streb, H., R. F. Irvine, M. J. Berridge, and I. Schulz. 1983. Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate. Nature. 306: 67-69.
    • (1983) Nature , vol.306 , pp. 67-69
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3    Schulz, I.4
  • 4
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka, Y. 1986. Studies and perspectives of protein kinase C. Science. 233: 305-312.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 5
    • 0025923860 scopus 로고
    • Inositol phospholipids-specific phospholipase C: Interaction of the gamma 1 isoform with tyrosine kinase
    • Rhee, S. G. 1991. Inositol phospholipids-specific phospholipase C: interaction of the gamma 1 isoform with tyrosine kinase. Trends Biochem. Sci. 16: 297-301.
    • (1991) Trends Biochem. Sci , vol.16 , pp. 297-301
    • Rhee, S.G.1
  • 6
    • 0026654469 scopus 로고
    • Regulation of inositol phospholipid-specific phospholipase C isozymes
    • Rhee, S. G., and K. D. Choi. 1992. Regulation of inositol phospholipid-specific phospholipase C isozymes. J. Biol. Chem. 267: 12393-12396.
    • (1992) J. Biol. Chem , vol.267 , pp. 12393-12396
    • Rhee, S.G.1    Choi, K.D.2
  • 7
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge, M. J. 1993.Inositol trisphosphate and calcium signalling. Nature. 361: 315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 8
    • 0024308812 scopus 로고
    • Phosphatidylinositol 3-kinase and its novel product, phosphatidylinositol 3-phosphate, are present in Saccharomyces cerevisiae
    • Auger, K. R., C. L. Carpenter, L. C. Cantley, and L. Varticovski. 1989. Phosphatidylinositol 3-kinase and its novel product, phosphatidylinositol 3-phosphate, are present in Saccharomyces cerevisiae. J. Biol. Chem. 264: 20181-20184.
    • (1989) J. Biol. Chem , vol.264 , pp. 20181-20184
    • Auger, K.R.1    Carpenter, C.L.2    Cantley, L.C.3    Varticovski, L.4
  • 9
    • 0033604577 scopus 로고    scopus 로고
    • Signaling by distinct classes of phosphoinositide 3-kinases
    • Vanhaesebroeck, B., and M. D. Waterfield. 1999. Signaling by distinct classes of phosphoinositide 3-kinases. Exp. Cell Res. 253: 239-254.
    • (1999) Exp. Cell Res , vol.253 , pp. 239-254
    • Vanhaesebroeck, B.1    Waterfield, M.D.2
  • 10
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta, S. R., A. Brunet, and M. E. Greenberg. 1999. Cellular survival: a play in three Akts. Genes Dev. 13: 2905-2927.
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 11
    • 0033605718 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase lipid products in cell function
    • Rameh, L. E., and L. C. Cantley. 1999. The role of phosphoinositide 3-kinase lipid products in cell function. J. Biol. Chem. 274: 8347-8350.
    • (1999) J. Biol. Chem , vol.274 , pp. 8347-8350
    • Rameh, L.E.1    Cantley, L.C.2
  • 12
    • 0028783459 scopus 로고
    • Light adaptation of bovine retinas in situ stimulates phosphatidylinositol synthesis in rod outer segments in vitro
    • Ghalayini, A. J., and R. E. Anderson. 1995. Light adaptation of bovine retinas in situ stimulates phosphatidylinositol synthesis in rod outer segments in vitro. Curr. Eye Res. 14: 1025-1029.
    • (1995) Curr. Eye Res , vol.14 , pp. 1025-1029
    • Ghalayini, A.J.1    Anderson, R.E.2
  • 13
    • 0034131372 scopus 로고    scopus 로고
    • Light-mediated activation of diacylglycerol kinase in rat and bovine rod outer segments
    • Huang, Z., A. Ghalayini, X. X. Guo, K. M. Alvarez, and R. E. Anderson. 2000. Light-mediated activation of diacylglycerol kinase in rat and bovine rod outer segments. J. Neurochem. 75: 355-362.
    • (2000) J. Neurochem , vol.75 , pp. 355-362
    • Huang, Z.1    Ghalayini, A.2    Guo, X.X.3    Alvarez, K.M.4    Anderson, R.E.5
  • 14
    • 0030758287 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase in bovine photoreceptor rod outer segments
    • Guo, X., A. J. Ghalayini, H. Chen, and R. E. Anderson. 1997. Phosphatidylinositol 3-kinase in bovine photoreceptor rod outer segments. Invest. Ophthalmol. Vis. Sci. 38: 1873-1882.
    • (1997) Invest. Ophthalmol. Vis. Sci , vol.38 , pp. 1873-1882
    • Guo, X.1    Ghalayini, A.J.2    Chen, H.3    Anderson, R.E.4
  • 15
    • 0034605626 scopus 로고    scopus 로고
    • Tyrosine phosphorylation is involved in phosphatidylinositol 3-kinase activation in bovine rod outer segments
    • Guo, X. X., Z. Huang, M. W. Bell, H. Chen, and R. E. Anderson. 2000. Tyrosine phosphorylation is involved in phosphatidylinositol 3-kinase activation in bovine rod outer segments. Mol. Vis. 6: 216-221.
    • (2000) Mol. Vis , vol.6 , pp. 216-221
    • Guo, X.X.1    Huang, Z.2    Bell, M.W.3    Chen, H.4    Anderson, R.E.5
  • 16
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking
    • Martin, T. F. 1998. Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking. Annu. Rev. Cell Dev. Biol. 14: 231-264.
    • (1998) Annu. Rev. Cell Dev. Biol , vol.14 , pp. 231-264
    • Martin, T.F.1
  • 17
    • 26544475380 scopus 로고
    • Myo-inositol phosphates from beef brain phosphoinostide
    • Grado, C. and C. E. Ballou. 1960. Myo-inositol phosphates from beef brain phosphoinostide. J. Biol. Chem. 235: C23-C24.
    • (1960) J. Biol. Chem , vol.235
    • Grado, C.1    Ballou, C.E.2
  • 18
    • 0023897684 scopus 로고
    • Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate
    • Whitman, M., C. P. Downes, M. Keeler, T. Keller, and L. Cantley. 1988. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature. 332: 644-646.
    • (1988) Nature , vol.332 , pp. 644-646
    • Whitman, M.1    Downes, C.P.2    Keeler, M.3    Keller, T.4    Cantley, L.5
  • 20
    • 0035916357 scopus 로고    scopus 로고
    • An evolutionarily conserved function of the Drosophila insulin receptor and insulin-like peptides in growth control
    • Brogiolo, W., H. Stocker, T. Ikeya, F. Rintelen, R. Fernandez, and E. Hafen. 2001. An evolutionarily conserved function of the Drosophila insulin receptor and insulin-like peptides in growth control. Curr. Biol. 11: 213-221.
    • (2001) Curr. Biol , vol.11 , pp. 213-221
    • Brogiolo, W.1    Stocker, H.2    Ikeya, T.3    Rintelen, F.4    Fernandez, R.5    Hafen, E.6
  • 21
    • 0033572644 scopus 로고    scopus 로고
    • Drosophila tumor suppressor PTEN controls cell size and number by antagonizing the Chico/PI3-kinase signaling pathway
    • Goberdhan, D. C., N. Paricio, E. C. Goodman, M. Mlodzik, and C. Wilson. 1999. Drosophila tumor suppressor PTEN controls cell size and number by antagonizing the Chico/PI3-kinase signaling pathway. Genes Dev. 13: 3244-3258.
    • (1999) Genes Dev , vol.13 , pp. 3244-3258
    • Goberdhan, D.C.1    Paricio, N.2    Goodman, E.C.3    Mlodzik, M.4    Wilson, C.5
  • 22
    • 0033258521 scopus 로고    scopus 로고
    • Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/ PKB
    • Verdu, J., M. A. Buratovich, E. L. Wilder, and M. J. Birnbaum. 1999. Cell-autonomous regulation of cell and organ growth in Drosophila by Akt/ PKB. Nat. Cell Biol. 1: 500-506.
    • (1999) Nat. Cell Biol , vol.1 , pp. 500-506
    • Verdu, J.1    Buratovich, M.A.2    Wilder, E.L.3    Birnbaum, M.J.4
  • 23
    • 0030657540 scopus 로고    scopus 로고
    • daf-16: An HNF-3/ forkhead family member that can function to double the life-span of Caenorhabditis elegans
    • Lin, K., J. B. Dorman, A. Rodan, and C. Kenyon. 1997. daf-16: an HNF-3/ forkhead family member that can function to double the life-span of Caenorhabditis elegans. Science. 278: 1319-1322.
    • (1997) Science , vol.278 , pp. 1319-1322
    • Lin, K.1    Dorman, J.B.2    Rodan, A.3    Kenyon, C.4
  • 24
    • 0032238299 scopus 로고    scopus 로고
    • The C. elegans PTEN homolog, DAF-18, acts in the insulin receptor-like metabolic signaling pathway
    • Ogg, S., and G. Ruvkun. 1998. The C. elegans PTEN homolog, DAF-18, acts in the insulin receptor-like metabolic signaling pathway. Mol. Cell. 2: 887-893.
    • (1998) Mol. Cell , vol.2 , pp. 887-893
    • Ogg, S.1    Ruvkun, G.2
  • 25
    • 0033133990 scopus 로고    scopus 로고
    • The PIK-related kinases intercept conventional signaling pathways
    • Kuruvilla, F. G., and S. L. Schreiber. 1999. The PIK-related kinases intercept conventional signaling pathways. Chem. Biol. 6: R129-R136.
    • (1999) Chem. Biol , vol.6
    • Kuruvilla, F.G.1    Schreiber, S.L.2
  • 26
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman, J. A., J. Luo, and L. C. Cantley. 2006. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nat. Rev. Genet. 7: 606-619.
    • (2006) Nat. Rev. Genet , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 28
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein beta gamma subunits
    • Stephens, L., A. Smrcka, F. T. Cooke, T. R. Jackson, P. C. Sternweis, and P. T. Hawkins. 1994. A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein beta gamma subunits. Cell. 77: 83-93.
    • (1994) Cell , vol.77 , pp. 83-93
    • Stephens, L.1    Smrcka, A.2    Cooke, F.T.3    Jackson, T.R.4    Sternweis, P.C.5    Hawkins, P.T.6
  • 30
    • 0042466604 scopus 로고    scopus 로고
    • Insulin induces phosphatidylinositol-3-phosphate formation through TC10 activation
    • Maffucci, T., A. Brancaccio, E. Piccolo, R. C. Stein, and M. Falasca. 2003. Insulin induces phosphatidylinositol-3-phosphate formation through TC10 activation. EMBO J. 22: 4178-4189.
    • (2003) EMBO J , vol.22 , pp. 4178-4189
    • Maffucci, T.1    Brancaccio, A.2    Piccolo, E.3    Stein, R.C.4    Falasca, M.5
  • 31
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by phosphoinositide 3-kinases
    • Lindmo, K., and H. Stenmark. 2006. Regulation of membrane traffic by phosphoinositide 3-kinases. J. Cell Sci. 119: 605-614.
    • (2006) J. Cell Sci , vol.119 , pp. 605-614
    • Lindmo, K.1    Stenmark, H.2
  • 33
    • 51849128358 scopus 로고    scopus 로고
    • Class I PI3K in oncogenic cellular transformation
    • Zhao, L., and P. K. Vogt. 2008. Class I PI3K in oncogenic cellular transformation. Oncogene. 27: 5486-5496.
    • (2008) Oncogene , vol.27 , pp. 5486-5496
    • Zhao, L.1    Vogt, P.K.2
  • 34
    • 33645551286 scopus 로고    scopus 로고
    • Signaling through PI3Kgamma: A common platform for leukocyte, platelet and cardiovascular stress sensing
    • Hirsch, E., G. Lembo, G. Montrucchio, C. Rommel, C. Costa, and L. Barberis. 2006. Signaling through PI3Kgamma: a common platform for leukocyte, platelet and cardiovascular stress sensing. Thromb. Haemost. 95: 29-35.
    • (2006) Thromb. Haemost , vol.95 , pp. 29-35
    • Hirsch, E.1    Lembo, G.2    Montrucchio, G.3    Rommel, C.4    Costa, C.5    Barberis, L.6
  • 35
    • 34547895443 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases as a common platform for multi-hormone signaling
    • Hirsch, E., C. Costa, and E. Ciraolo. 2007. Phosphoinositide 3-kinases as a common platform for multi-hormone signaling. J. Endocrinol. 194: 243-256.
    • (2007) J. Endocrinol , vol.194 , pp. 243-256
    • Hirsch, E.1    Costa, C.2    Ciraolo, E.3
  • 37
    • 0029913340 scopus 로고    scopus 로고
    • Insulin receptor substrate 1 binds two novel splice variants of the regulatory subunit of phosphatidylinositol 3-kinase in muscle and brain
    • Antonetti, D. A., P. Algenstaedt, and C. R. Kahn. 1996. Insulin receptor substrate 1 binds two novel splice variants of the regulatory subunit of phosphatidylinositol 3-kinase in muscle and brain. Mol. Cell. Biol. 16: 2195-2203.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 2195-2203
    • Antonetti, D.A.1    Algenstaedt, P.2    Kahn, C.R.3
  • 38
    • 0029920935 scopus 로고    scopus 로고
    • A novel 55-kDa regulatory subunit for phosphatidylinositol 3-kinase structurally similar to p55PIK Is generated by alternative splicing of the p85alpha gene
    • Inukai, K., M. Anai, E. Van Breda, T. Hosaka, H. Katagiri, M. Funaki, Y. Fukushima, T. Ogihara, Y. Yazaki, Kikuchi, Y. Oka, and T. Asano. 1996. A novel 55-kDa regulatory subunit for phosphatidylinositol 3-kinase structurally similar to p55PIK Is generated by alternative splicing of the p85alpha gene. J. Biol. Chem. 271: 5317-5320.
    • (1996) J. Biol. Chem , vol.271 , pp. 5317-5320
    • Inukai, K.1    Anai, M.2    Van Breda, E.3    Hosaka, T.4    Katagiri, H.5    Funaki, M.6    Fukushima, Y.7    Ogihara, T.8    Yazaki, Y.9    Kikuchi10    Oka, Y.11    Asano, T.12
  • 41
    • 0034697121 scopus 로고    scopus 로고
    • A novel role for phosphatidylinositol 3-kinase beta in signaling from G protein-coupled receptors to Akt
    • Murga, C., S. Fukuhara, and J. S. Gutkind. 2000. A novel role for phosphatidylinositol 3-kinase beta in signaling from G protein-coupled receptors to Akt. J. Biol. Chem. 275: 12069-12073.
    • (2000) J. Biol. Chem , vol.275 , pp. 12069-12073
    • Murga, C.1    Fukuhara, S.2    Gutkind, J.S.3
  • 43
    • 15744363780 scopus 로고    scopus 로고
    • p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma
    • Suire, S., J. Coadwell, G. J. Ferguson, K. Davidson, P. Hawkins, and L. Stephens. 2005. p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma. Curr. Biol. 15: 566-570.
    • (2005) Curr. Biol , vol.15 , pp. 566-570
    • Suire, S.1    Coadwell, J.2    Ferguson, G.J.3    Davidson, K.4    Hawkins, P.5    Stephens, L.6
  • 44
    • 14244266719 scopus 로고    scopus 로고
    • Assigning functional domains within the p101 regulatory subunit of phosphoinositide 3-kinase gamma
    • Voigt, P., C. Brock, B. Nurnberg, and M. Schaefer. 2005. Assigning functional domains within the p101 regulatory subunit of phosphoinositide 3-kinase gamma. J. Biol. Chem. 280: 5121-5127.
    • (2005) J. Biol. Chem , vol.280 , pp. 5121-5127
    • Voigt, P.1    Brock, C.2    Nurnberg, B.3    Schaefer, M.4
  • 46
    • 0032904432 scopus 로고    scopus 로고
    • PTEN: A tumour suppressor that functions as a phospholipid phosphatase
    • Maehama, T., and J. E. Dixon. 1999. PTEN: a tumour suppressor that functions as a phospholipid phosphatase. Trends Cell Biol. 9: 125-128.
    • (1999) Trends Cell Biol , vol.9 , pp. 125-128
    • Maehama, T.1    Dixon, J.E.2
  • 47
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama, T., and J. E. Dixon. 1998. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273: 13375-13378.
    • (1998) J. Biol. Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 48
    • 56149108508 scopus 로고    scopus 로고
    • Insulin growth factor 1 receptor/ PI3K/AKT survival pathway in outer segment membranes of rod photoreceptors
    • Dilly, A. K., and R. V. Rajala. 2008. Insulin growth factor 1 receptor/ PI3K/AKT survival pathway in outer segment membranes of rod photoreceptors. Invest. Ophthalmol. Vis. Sci. 49: 4765-4773.
    • (2008) Invest. Ophthalmol. Vis. Sci , vol.49 , pp. 4765-4773
    • Dilly, A.K.1    Rajala, R.V.2
  • 49
    • 34248151108 scopus 로고    scopus 로고
    • G-protein-coupled receptor rhodopsin regulates the phosphorylation of retinal insulin receptor
    • Rajala, A., R. E. Anderson, J. X. Ma, J. Lem, M. R. Al Ubaidi, and R. V. Rajala. 2007. G-protein-coupled receptor rhodopsin regulates the phosphorylation of retinal insulin receptor. J. Biol. Chem. 282: 9865-9873.
    • (2007) J. Biol. Chem , vol.282 , pp. 9865-9873
    • Rajala, A.1    Anderson, R.E.2    Ma, J.X.3    Lem, J.4    Al Ubaidi, M.R.5    Rajala, R.V.6
  • 50
    • 0037044798 scopus 로고    scopus 로고
    • In vivo regulation of phosphoinositide 3-kinase in retina through light-induced tyrosine phosphorylation of the insulin receptor beta-subunit
    • Rajala, R. V., M. E. McClellan, J. D. Ash, and R. E. Anderson. 2002. In vivo regulation of phosphoinositide 3-kinase in retina through light-induced tyrosine phosphorylation of the insulin receptor beta-subunit. J. Biol. Chem. 277: 43319-43326.
    • (2002) J. Biol. Chem , vol.277 , pp. 43319-43326
    • Rajala, R.V.1    McClellan, M.E.2    Ash, J.D.3    Anderson, R.E.4
  • 51
    • 0035656204 scopus 로고    scopus 로고
    • Interaction of the insulin receptor beta-subunit with phosphatidylinositol 3-kinase in bovine ROS
    • Rajala, R. V., and R. E. Anderson. 2001. Interaction of the insulin receptor beta-subunit with phosphatidylinositol 3-kinase in bovine ROS. Invest. Ophthalmol. Vis. Sci. 42: 3110-3117.
    • (2001) Invest. Ophthalmol. Vis. Sci , vol.42 , pp. 3110-3117
    • Rajala, R.V.1    Anderson, R.E.2
  • 53
    • 0029075550 scopus 로고
    • Functional significance of beta gamma-subunit carboxymethylation for the activation of phospholipase C and phosphoinositide 3-kinase
    • Parish, C. A., A. V. Smrcka, and R. R. Rando. 1995. Functional significance of beta gamma-subunit carboxymethylation for the activation of phospholipase C and phosphoinositide 3-kinase. Biochemistry. 34: 7722-7727.
    • (1995) Biochemistry , vol.34 , pp. 7722-7727
    • Parish, C.A.1    Smrcka, A.V.2    Rando, R.R.3
  • 54
    • 34547559208 scopus 로고    scopus 로고
    • SARA-regulated vesicular targeting underlies formation of the light-sensing organelle in mammalian rods
    • Chuang, J. Z., Y. Zhao, and C. H. Sung. 2007. SARA-regulated vesicular targeting underlies formation of the light-sensing organelle in mammalian rods. Cell. 130: 535-547.
    • (2007) Cell , vol.130 , pp. 535-547
    • Chuang, J.Z.1    Zhao, Y.2    Sung, C.H.3
  • 55
    • 0027361002 scopus 로고
    • Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85
    • Hu, P., A. Mondino, E. Y. Skolnik, and J. Schlessinger. 1993. Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol. Cell. Biol. 13: 7677-7688.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 7677-7688
    • Hu, P.1    Mondino, A.2    Skolnik, E.Y.3    Schlessinger, J.4
  • 56
    • 0026603817 scopus 로고
    • The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor
    • Klippel, A., J. A. Escobedo, W. J. Fantl, and L. T. Williams. 1992. The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor. Mol. Cell. Biol. 12: 1451-1459.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 1451-1459
    • Klippel, A.1    Escobedo, J.A.2    Fantl, W.J.3    Williams, L.T.4
  • 57
    • 0028085078 scopus 로고
    • The insulin signaling system
    • White, M. F., and C. R. Kahn. 1994. The insulin signaling system. J. Biol. Chem. 269: 1-4.
    • (1994) J. Biol. Chem , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 59
    • 0028012445 scopus 로고
    • Direct activation of the phosphatidylinositol 3′-kinase by the insulin receptor
    • Van Horn, D. J., M. G. Myers, Jr., and J. M. Backer. 1994. Direct activation of the phosphatidylinositol 3′-kinase by the insulin receptor. J. Biol. Chem. 269: 29-32.
    • (1994) J. Biol. Chem , vol.269 , pp. 29-32
    • Van Horn, D.J.1    Myers Jr., M.G.2    Backer, J.M.3
  • 61
    • 55849129303 scopus 로고    scopus 로고
    • Activation and membrane binding of retinal protein kinase Balpha/ Akt1 is regulated through light-dependent generation of phosphoinositides
    • Li, G., A. Rajala, A. F. Wiechmann, R. E. Anderson, and R. V. Rajala. 2008. Activation and membrane binding of retinal protein kinase Balpha/ Akt1 is regulated through light-dependent generation of phosphoinositides. J. Neurochem. 107: 1382-1397.
    • (2008) J. Neurochem , vol.107 , pp. 1382-1397
    • Li, G.1    Rajala, A.2    Wiechmann, A.F.3    Anderson, R.E.4    Rajala, R.V.5
  • 62
    • 49049110308 scopus 로고    scopus 로고
    • PDGF- and insulin/IGF-1-specific distinct modes of class IA PI 3-kinase activation in normal rat retinas and RGC-5 retinal ganglion cells
    • Biswas, S. K., Y. Zhao, A. Nagalingam, T. W. Gardner, and L. Sandirasegarane. 2008. PDGF- and insulin/IGF-1-specific distinct modes of class IA PI 3-kinase activation in normal rat retinas and RGC-5 retinal ganglion cells. Invest. Ophthalmol. Vis. Sci. 49: 3687-3698.
    • (2008) Invest. Ophthalmol. Vis. Sci , vol.49 , pp. 3687-3698
    • Biswas, S.K.1    Zhao, Y.2    Nagalingam, A.3    Gardner, T.W.4    Sandirasegarane, L.5
  • 64
    • 3042663842 scopus 로고    scopus 로고
    • Characterization of the basic fibroblast growth factor-evoked proliferation of the human Muller cell line, MIO-M1
    • Hollborn, M., K. Jahn, G. A. Limb, L. Kohen, P. Wiedemann, and A. Bringmann. 2004. Characterization of the basic fibroblast growth factor-evoked proliferation of the human Muller cell line, MIO-M1. Graefes Arch. Clin. Exp. Ophthalmol. 242: 414-422.
    • (2004) Graefes Arch. Clin. Exp. Ophthalmol , vol.242 , pp. 414-422
    • Hollborn, M.1    Jahn, K.2    Limb, G.A.3    Kohen, L.4    Wiedemann, P.5    Bringmann, A.6
  • 65
    • 0036786634 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor prevents axotomized retinal ganglion cell death through MAPK and PI3K signaling pathways
    • Nakazawa, T., M. Tamai, and N. Mori. 2002. Brain-derived neurotrophic factor prevents axotomized retinal ganglion cell death through MAPK and PI3K signaling pathways. Invest. Ophthalmol. Vis. Sci. 43: 3319-3326.
    • (2002) Invest. Ophthalmol. Vis. Sci , vol.43 , pp. 3319-3326
    • Nakazawa, T.1    Tamai, M.2    Mori, N.3
  • 66
    • 22144494966 scopus 로고    scopus 로고
    • Erythropoietin promotes regeneration of adult CNS neurons via Jak2/Stat3 and PI3K/AKT pathway activation
    • Kretz, A., C. J. Happold, J. K. Marticke, and S. Isenmann. 2005. Erythropoietin promotes regeneration of adult CNS neurons via Jak2/Stat3 and PI3K/AKT pathway activation. Mol. Cell. Neurosci. 29: 569-579.
    • (2005) Mol. Cell. Neurosci , vol.29 , pp. 569-579
    • Kretz, A.1    Happold, C.J.2    Marticke, J.K.3    Isenmann, S.4
  • 67
    • 11844304348 scopus 로고    scopus 로고
    • Ciliary neurotrophic factor protects rat retina cells in vitro and in vivo via PI3 kinase
    • Ikeda, K., T. Tatsuno, H. Noguchi, and C. Nakayama. 2004. Ciliary neurotrophic factor protects rat retina cells in vitro and in vivo via PI3 kinase. Curr. Eye Res. 29: 349-355.
    • (2004) Curr. Eye Res , vol.29 , pp. 349-355
    • Ikeda, K.1    Tatsuno, T.2    Noguchi, H.3    Nakayama, C.4
  • 68
    • 2442448718 scopus 로고    scopus 로고
    • Interaction of the retinal insulin receptor beta-subunit with the P85 subunit of phosphoinositide 3-kinase
    • Rajala, R. V., M. E. McClellan, M. D. Chan, L. Tsiokas, and R. E. Anderson. 2004. Interaction of the retinal insulin receptor beta-subunit with the P85 subunit of phosphoinositide 3-kinase. Biochemistry. 43: 5637-5650.
    • (2004) Biochemistry , vol.43 , pp. 5637-5650
    • Rajala, R.V.1    McClellan, M.E.2    Chan, M.D.3    Tsiokas, L.4    Anderson, R.E.5
  • 70
    • 15644381754 scopus 로고    scopus 로고
    • Andjelkovic, M., D. R. Alessi, R. Meier, A. Fernandez, N. J. Lamb, M. Frech, P. Cron, P. Cohen, J. M. Lucocq, and B. A. Hemmings. 1997. Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272: 31515-31524.
    • Andjelkovic, M., D. R. Alessi, R. Meier, A. Fernandez, N. J. Lamb, M. Frech, P. Cron, P. Cohen, J. M. Lucocq, and B. A. Hemmings. 1997. Role of translocation in the activation and function of protein kinase B. J. Biol. Chem. 272: 31515-31524.
  • 71
    • 0030727172 scopus 로고    scopus 로고
    • Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bbeta
    • Meier, R., D. R. Alessi, P. Cron, M. Andjelkovic, and B. A. Hemmings. 1997. Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bbeta. J. Biol. Chem. 272: 30491-30497.
    • (1997) J. Biol. Chem , vol.272 , pp. 30491-30497
    • Meier, R.1    Alessi, D.R.2    Cron, P.3    Andjelkovic, M.4    Hemmings, B.A.5
  • 73
    • 0030669730 scopus 로고    scopus 로고
    • Growth factor stimulation of hematopoietic cells leads to membrane translocation of AKT1 protein kinase
    • Zhang, X., and T. A. Vik. 1997. Growth factor stimulation of hematopoietic cells leads to membrane translocation of AKT1 protein kinase. Leuk. Res. 21: 849-856.
    • (1997) Leuk. Res , vol.21 , pp. 849-856
    • Zhang, X.1    Vik, T.A.2
  • 74
    • 0032491389 scopus 로고    scopus 로고
    • Sable, C. L., N. Filippa, C. Filloux, B. A. Hemmings, and E. Van Obberghen. 1998. Involvement of the pleckstrin homology domain in the insulin-stimulated activation of protein kinase B. J. Biol. Chem. 273: 29600-29606.
    • Sable, C. L., N. Filippa, C. Filloux, B. A. Hemmings, and E. Van Obberghen. 1998. Involvement of the pleckstrin homology domain in the insulin-stimulated activation of protein kinase B. J. Biol. Chem. 273: 29600-29606.
  • 75
    • 0033084143 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1
    • Currie, R. A., K. S. Walker, A. Gray, M. Deak, A. Casamayor, C. P. Downes, P. Cohen, D. R. Alessi, and J. Lucocq. 1999. Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1. Biochem. J. 337: 575-583.
    • (1999) Biochem. J , vol.337 , pp. 575-583
    • Currie, R.A.1    Walker, K.S.2    Gray, A.3    Deak, M.4    Casamayor, A.5    Downes, C.P.6    Cohen, P.7    Alessi, D.R.8    Lucocq, J.9
  • 76
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning, B. D., and L. C. Cantley. 2007. AKT/PKB signaling: navigating downstream. Cell. 129: 1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 78
    • 0032518467 scopus 로고    scopus 로고
    • 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro
    • Alessi, D. R., M. T. Kozlowski, Q. P. Weng, N. Morrice, and J. Avruch. 1998. 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. Curr. Biol. 8: 69-81.
    • (1998) Curr. Biol , vol.8 , pp. 69-81
    • Alessi, D.R.1    Kozlowski, M.T.2    Weng, Q.P.3    Morrice, N.4    Avruch, J.5
  • 79
    • 28844434558 scopus 로고    scopus 로고
    • mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes
    • Hresko, R. C., and M. Mueckler. 2005. mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes. J. Biol. Chem. 280: 40406-40416.
    • (2005) J. Biol. Chem , vol.280 , pp. 40406-40416
    • Hresko, R.C.1    Mueckler, M.2
  • 80
    • 0033811737 scopus 로고    scopus 로고
    • Impaired phosphorylation and insulin-stimulated translocation to the plasma membrane of protein kinase B/Akt in adipocytes from Type II diabetic subjects
    • Carvalho, E., B. Eliasson, C. Wesslau, and U. Smith. 2000. Impaired phosphorylation and insulin-stimulated translocation to the plasma membrane of protein kinase B/Akt in adipocytes from Type II diabetic subjects. Diabetologia. 43: 1107-1115.
    • (2000) Diabetologia , vol.43 , pp. 1107-1115
    • Carvalho, E.1    Eliasson, B.2    Wesslau, C.3    Smith, U.4
  • 81
    • 0346434149 scopus 로고    scopus 로고
    • Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3-kinase activation
    • Bijur, G. N., and R. S. Jope. 2003. Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3-kinase activation. J. Neurochem. 87: 1427-1435.
    • (2003) J. Neurochem , vol.87 , pp. 1427-1435
    • Bijur, G.N.1    Jope, R.S.2
  • 82
    • 0031469453 scopus 로고    scopus 로고
    • Membrane translocation and activation of the Akt kinase in growth factor-stimulated hematopoietic cells
    • Testa, J. R., and A. Bellacosa. 1997. Membrane translocation and activation of the Akt kinase in growth factor-stimulated hematopoietic cells. Leuk. Res. 21: 1027-1031.
    • (1997) Leuk. Res , vol.21 , pp. 1027-1031
    • Testa, J.R.1    Bellacosa, A.2
  • 83
    • 0034647674 scopus 로고    scopus 로고
    • Translocation of Akt/PKB to the nucleus of osteoblast-like MC3T3-E1 cells exposed to proliferative growth factors
    • Borgatti, P., A. M. Martelli, A. Bellacosa, R. Casto, L. Massari, S. Capitani, and L. M. Neri. 2000. Translocation of Akt/PKB to the nucleus of osteoblast-like MC3T3-E1 cells exposed to proliferative growth factors. FEBS Lett. 477: 27-32.
    • (2000) FEBS Lett , vol.477 , pp. 27-32
    • Borgatti, P.1    Martelli, A.M.2    Bellacosa, A.3    Casto, R.4    Massari, L.5    Capitani, S.6    Neri, L.M.7
  • 84
    • 36248985545 scopus 로고    scopus 로고
    • G protein-coupled receptor-induced Akt activity in cellular proliferation and apoptosis
    • New, D. C., K. Wu, A. W. Kwok, and Y. H. Wong. 2007. G protein-coupled receptor-induced Akt activity in cellular proliferation and apoptosis. FEBS J. 274: 6025-6036.
    • (2007) FEBS J , vol.274 , pp. 6025-6036
    • New, D.C.1    Wu, K.2    Kwok, A.W.3    Wong, Y.H.4
  • 86
    • 0030907987 scopus 로고    scopus 로고
    • PI3K: Downstream AKTion blocks apoptosis
    • Franke, T. F., D. R. Kaplan, and L. C. Cantley. 1997. PI3K: downstream AKTion blocks apoptosis. Cell. 88: 435-437.
    • (1997) Cell , vol.88 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 87
    • 33645990907 scopus 로고    scopus 로고
    • Regulation of protein synthesis by insulin
    • Proud, C. G. 2006. Regulation of protein synthesis by insulin. Biochem. Soc. Trans. 34: 213-216.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 213-216
    • Proud, C.G.1
  • 89
    • 0025029035 scopus 로고
    • Cloning of the mitogen-activated S6 kinase from rat liver reveals an enzyme of the second messenger subfamily
    • Kozma, S. C., S. Ferrari, P. Bassand, M. Siegmann, N. Totty, and G. Thomas. 1990. Cloning of the mitogen-activated S6 kinase from rat liver reveals an enzyme of the second messenger subfamily. Proc. Natl. Acad. Sci. USA. 87: 7365-7369.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7365-7369
    • Kozma, S.C.1    Ferrari, S.2    Bassand, P.3    Siegmann, M.4    Totty, N.5    Thomas, G.6
  • 91
    • 0026504296 scopus 로고
    • A single gene encodes two isoforms of the p70 S6 kinase: Activation upon mitogenic stimulation
    • Reinhard, C., G. Thomas, and S. C. Kozma. 1992. A single gene encodes two isoforms of the p70 S6 kinase: activation upon mitogenic stimulation. Proc. Natl. Acad. Sci. USA. 89: 4052-4056.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4052-4056
    • Reinhard, C.1    Thomas, G.2    Kozma, S.C.3
  • 92
    • 0028175455 scopus 로고
    • Nuclear localization of p85s6k: Functional requirement for entry into S phase
    • Reinhard, C., A. Fernandez, N. J. Lamb, and G. Thomas. 1994. Nuclear localization of p85s6k: functional requirement for entry into S phase. EMBO J. 13: 1557-1565.
    • (1994) EMBO J , vol.13 , pp. 1557-1565
    • Reinhard, C.1    Fernandez, A.2    Lamb, N.J.3    Thomas, G.4
  • 94
    • 0029828590 scopus 로고    scopus 로고
    • The principal rapamycin-sensitive p70(s6k) phosphorylation sites, T-229 and T-389, are differentially regulated by rapamycin-insensitive kinase kinases
    • Dennis, P. B., N. Pullen, S. C. Kozma, and G. Thomas. 1996. The principal rapamycin-sensitive p70(s6k) phosphorylation sites, T-229 and T-389, are differentially regulated by rapamycin-insensitive kinase kinases. Mol. Cell. Biol. 16: 6242-6251.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 6242-6251
    • Dennis, P.B.1    Pullen, N.2    Kozma, S.C.3    Thomas, G.4
  • 95
    • 0032973572 scopus 로고    scopus 로고
    • Protein kinase B localization and activation differentially affect S6 kinase 1 activity and eukaryotic translation initiation factor 4E-binding protein 1 phosphorylation
    • Dufner, A., M. Andjelkovic, B. M. Burgering, B. A. Hemmings, and G. Thomas. 1999. Protein kinase B localization and activation differentially affect S6 kinase 1 activity and eukaryotic translation initiation factor 4E-binding protein 1 phosphorylation. Mol. Cell. Biol. 19: 4525-4534.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 4525-4534
    • Dufner, A.1    Andjelkovic, M.2    Burgering, B.M.3    Hemmings, B.A.4    Thomas, G.5
  • 97
    • 0032497842 scopus 로고    scopus 로고
    • The role of PI 3-kinase in insulin action
    • Alessi, D. R., and C. P. Downes. 1998. The role of PI 3-kinase in insulin action. Biochim. Biophys. Acta. 1436: 151-164.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 151-164
    • Alessi, D.R.1    Downes, C.P.2
  • 100
    • 0032932198 scopus 로고    scopus 로고
    • p70 S6 kinase is regulated by protein kinase Czeta and participates in a phosphoinositide 3-kinase-regulated signalling complex
    • Romanelli, A., K. A. Martin, A. Toker, and J. Blenis. 1999. p70 S6 kinase is regulated by protein kinase Czeta and participates in a phosphoinositide 3-kinase-regulated signalling complex. Mol. Cell. Biol. 19: 2921-2928.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 2921-2928
    • Romanelli, A.1    Martin, K.A.2    Toker, A.3    Blenis, J.4
  • 101
    • 0025806666 scopus 로고
    • Inhibition of human T-cell activation by FK 506, rapamycin, and cyclosporine A
    • Sigal, N. H., C. S. Lin, and J. J. Siekierka. 1991. Inhibition of human T-cell activation by FK 506, rapamycin, and cyclosporine A. Transplant. Proc. 23: 1-5.
    • (1991) Transplant. Proc , vol.23 , pp. 1-5
    • Sigal, N.H.1    Lin, C.S.2    Siekierka, J.J.3
  • 102
    • 0026659046 scopus 로고
    • Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases
    • Chung, J., C. J. Kuo, G. R. Crabtree, and J. Blenis. 1992. Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases. Cell. 69: 1227-1236.
    • (1992) Cell , vol.69 , pp. 1227-1236
    • Chung, J.1    Kuo, C.J.2    Crabtree, G.R.3    Blenis, J.4
  • 104
    • 0026759874 scopus 로고
    • Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase
    • Price, D. J., J. R. Grove, V. Calvo, J. Avruch, and B. E. Bierer. 1992. Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase. Science. 257: 973-977.
    • (1992) Science , vol.257 , pp. 973-977
    • Price, D.J.1    Grove, J.R.2    Calvo, V.3    Avruch, J.4    Bierer, B.E.5
  • 107
    • 0034307483 scopus 로고    scopus 로고
    • Internal ribosome initiation of translation and the control of cell death
    • Holcik, M., N. Sonenberg, and R. G. Korneluk. 2000. Internal ribosome initiation of translation and the control of cell death. Trends Genet. 16: 469-473.
    • (2000) Trends Genet , vol.16 , pp. 469-473
    • Holcik, M.1    Sonenberg, N.2    Korneluk, R.G.3
  • 108
    • 0033428811 scopus 로고    scopus 로고
    • Selective sensitivity of early postmitotic retinal cells to apoptosis induced by inhibition of protein synthesis
    • Rehen, S. K., D. D. Neves, L. Fragel-Madeira, L. R. Britto, and R. Linden. 1999. Selective sensitivity of early postmitotic retinal cells to apoptosis induced by inhibition of protein synthesis. Eur. J. Neurosci. 11: 4349-4356.
    • (1999) Eur. J. Neurosci , vol.11 , pp. 4349-4356
    • Rehen, S.K.1    Neves, D.D.2    Fragel-Madeira, L.3    Britto, L.R.4    Linden, R.5
  • 109
    • 58149141478 scopus 로고    scopus 로고
    • Stimulation of the insulin/mTOR pathway delays cone death in a mouse model of retinitis pigmentosa
    • Punzo, C., K. Kornacker, and C. L. Cepko. 2009. Stimulation of the insulin/mTOR pathway delays cone death in a mouse model of retinitis pigmentosa. Nat. Neurosci. 12: 44-52.
    • (2009) Nat. Neurosci , vol.12 , pp. 44-52
    • Punzo, C.1    Kornacker, K.2    Cepko, C.L.3
  • 110
    • 0030840724 scopus 로고    scopus 로고
    • Alterations in skeletal muscle protein-tyrosine phosphatase activity and expression in insulin-resistant human obesity and diabetes
    • Ahmad, F., J. L. Azevedo, R. Cortright, G. L. Dohm, and B. J. Goldstein. 1997. Alterations in skeletal muscle protein-tyrosine phosphatase activity and expression in insulin-resistant human obesity and diabetes. J. Clin. Invest. 100: 449-458.
    • (1997) J. Clin. Invest , vol.100 , pp. 449-458
    • Ahmad, F.1    Azevedo, J.L.2    Cortright, R.3    Dohm, G.L.4    Goldstein, B.J.5
  • 111
    • 0030821972 scopus 로고    scopus 로고
    • Improved sensitivity to insulin in obese subjects following weight loss is accompanied by reduced protein-tyrosine phosphatases in adipose tissue
    • Ahmad, F., R. V. Considine, T. L. Bauer, J. P. Ohannesian, C. C. Marco, and B. J. Goldstein. 1997. Improved sensitivity to insulin in obese subjects following weight loss is accompanied by reduced protein-tyrosine phosphatases in adipose tissue. Metabolism. 46: 1140-1145.
    • (1997) Metabolism , vol.46 , pp. 1140-1145
    • Ahmad, F.1    Considine, R.V.2    Bauer, T.L.3    Ohannesian, J.P.4    Marco, C.C.5    Goldstein, B.J.6
  • 112
    • 0029018196 scopus 로고
    • Increased abundance of the receptor-type protein-tyrosine phosphatase LAR accounts for the elevated insulin receptor dephosphorylating activity in adipose tissue of obese human subjects
    • Ahmad, F., R. V. Considine, and B. J. Goldstein. 1995. Increased abundance of the receptor-type protein-tyrosine phosphatase LAR accounts for the elevated insulin receptor dephosphorylating activity in adipose tissue of obese human subjects. J. Clin. Invest. 95: 2806-2812.
    • (1995) J. Clin. Invest , vol.95 , pp. 2806-2812
    • Ahmad, F.1    Considine, R.V.2    Goldstein, B.J.3
  • 113
    • 0029548985 scopus 로고
    • Increased abundance of specific skeletal muscle protein-tyrosine phosphatases in a genetic model of insulin-resistant obesity an diabetes mellitus
    • Ahmad, F., and B. J. Goldstein. 1995. Increased abundance of specific skeletal muscle protein-tyrosine phosphatases in a genetic model of insulin-resistant obesity an diabetes mellitus. Metabolism. 44: 1175-1184.
    • (1995) Metabolism , vol.44 , pp. 1175-1184
    • Ahmad, F.1    Goldstein, B.J.2
  • 114
    • 0032887199 scopus 로고    scopus 로고
    • Dissociation of PTPase levels from their modulation of insulin receptor signal transduction
    • Bleyle, L. A., Y. Peng, C. Ellis, and R. A. Mooney. 1999. Dissociation of PTPase levels from their modulation of insulin receptor signal transduction. Cell. Signal. 11: 719-725.
    • (1999) Cell. Signal , vol.11 , pp. 719-725
    • Bleyle, L.A.1    Peng, Y.2    Ellis, C.3    Mooney, R.A.4
  • 115
    • 0026643477 scopus 로고
    • Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain
    • Hashimoto, N., E. P. Feener, W. R. Zhang, and B. J. Goldstein. 1992. Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain. J. Biol. Chem. 267: 13811-13814.
    • (1992) J. Biol. Chem , vol.267 , pp. 13811-13814
    • Hashimoto, N.1    Feener, E.P.2    Zhang, W.R.3    Goldstein, B.J.4
  • 116
    • 0027373187 scopus 로고
    • Regulation of protein tyrosine phosphatases by insulin and insulin-like growth factor I
    • Kenner, K. A., D. E. Hill, J. M. Olefsky, and J. Kusari. 1993. Regulation of protein tyrosine phosphatases by insulin and insulin-like growth factor I. J. Biol. Chem. 268: 25455-25462.
    • (1993) J. Biol. Chem , vol.268 , pp. 25455-25462
    • Kenner, K.A.1    Hill, D.E.2    Olefsky, J.M.3    Kusari, J.4
  • 117
    • 0029810614 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling
    • Kenner, K. A., E. Anyanwu, J. M. Olefsky, and J. Kusari. 1996. Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling. J. Biol. Chem. 271: 19810-19816.
    • (1996) J. Biol. Chem , vol.271 , pp. 19810-19816
    • Kenner, K.A.1    Anyanwu, E.2    Olefsky, J.M.3    Kusari, J.4
  • 118
    • 0027158159 scopus 로고
    • The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp
    • Kuhne, M. R., T. Pawson, G. E. Lienhard, and G. S. Feng. 1993. The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J. Biol. Chem. 268: 11479-11481.
    • (1993) J. Biol. Chem , vol.268 , pp. 11479-11481
    • Kuhne, M.R.1    Pawson, T.2    Lienhard, G.E.3    Feng, G.S.4
  • 120
    • 15644368839 scopus 로고    scopus 로고
    • The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling
    • Myers, M. G., Jr., R. Mendez, P. Shi, J. H. Pierce, R. Rhoads, and M. F. White. 1998. The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling. J. Biol. Chem. 273: 26908-26914.
    • (1998) J. Biol. Chem , vol.273 , pp. 26908-26914
    • Myers Jr., M.G.1    Mendez, R.2    Shi, P.3    Pierce, J.H.4    Rhoads, R.5    White, M.F.6
  • 122
    • 0031941815 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase-1B acts as a negative regulator of insulin signal transduction
    • Byon, J. C., A. B. Kusari, and J. Kusari. 1998. Protein-tyrosine phosphatase-1B acts as a negative regulator of insulin signal transduction. Mol. Cell. Biochem. 182: 101-108.
    • (1998) Mol. Cell. Biochem , vol.182 , pp. 101-108
    • Byon, J.C.1    Kusari, A.B.2    Kusari, J.3
  • 123
    • 0031943479 scopus 로고    scopus 로고
    • Regulation of the insulin signalling pathway by cellular protein-tyrosine phosphatases
    • Goldstein, B. J., F. Ahmad, W. Ding, P. M. Li, and W. R. Zhang. 1998. Regulation of the insulin signalling pathway by cellular protein-tyrosine phosphatases. Mol. Cell. Biochem. 182: 91-99.
    • (1998) Mol. Cell. Biochem , vol.182 , pp. 91-99
    • Goldstein, B.J.1    Ahmad, F.2    Ding, W.3    Li, P.M.4    Zhang, W.R.5
  • 124
    • 0026584285 scopus 로고
    • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • Frangioni, J. V., P. H. Beahm, V. Shifrin, C. A. Jost, and B. G. Neel. 1992. The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell. 68: 545-560.
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 125
    • 0026559962 scopus 로고
    • Expression of a protein tyrosine phosphatase in normal and v-src-transformed mouse 3T3 fibroblasts
    • Woodford-Thomas, T. A., J. D. Rhodes, and J. E. Dixon. 1992. Expression of a protein tyrosine phosphatase in normal and v-src-transformed mouse 3T3 fibroblasts. J. Cell Biol. 117: 401-414.
    • (1992) J. Cell Biol , vol.117 , pp. 401-414
    • Woodford-Thomas, T.A.1    Rhodes, J.D.2    Dixon, J.E.3
  • 127
    • 0038199726 scopus 로고    scopus 로고
    • PTP1B: From the sidelines to the front lines!
    • Tonks, N. K. 2003. PTP1B: from the sidelines to the front lines! FEBS Lett. 546: 140-148.
    • (2003) FEBS Lett , vol.546 , pp. 140-148
    • Tonks, N.K.1
  • 128
    • 0030963867 scopus 로고    scopus 로고
    • Regulation of growth factor-induced signaling by protein-tyrosine-phosphatases
    • Byon, J. C., K. A. Kenner, A. B. Kusari, and J. Kusari. 1997. Regulation of growth factor-induced signaling by protein-tyrosine-phosphatases. Proc. Soc. Exp. Biol. Med. 216: 1-20.
    • (1997) Proc. Soc. Exp. Biol. Med , vol.216 , pp. 1-20
    • Byon, J.C.1    Kenner, K.A.2    Kusari, A.B.3    Kusari, J.4
  • 129
    • 0029130199 scopus 로고
    • Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway
    • Ahmad, F., P. M. Li, J. Meyerovitch, and B. J. Goldstein. 1995. Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway. J. Biol. Chem. 270: 20503-20508.
    • (1995) J. Biol. Chem , vol.270 , pp. 20503-20508
    • Ahmad, F.1    Li, P.M.2    Meyerovitch, J.3    Goldstein, B.J.4
  • 130
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • Klaman, L. D., O. Boss, O. D. Peroni, J. K. Kim, J. L. Martino, J. M. Zabolotny, N. Moghal, M. Lubkin, Y. B. Kim, A. H. Sharpe, et al. 2000. Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell. Biol. 20: 5479-5489.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 5479-5489
    • Klaman, L.D.1    Boss, O.2    Peroni, O.D.3    Kim, J.K.4    Martino, J.L.5    Zabolotny, J.M.6    Moghal, N.7    Lubkin, M.8    Kim, Y.B.9    Sharpe, A.H.10
  • 133
    • 62649134313 scopus 로고    scopus 로고
    • Diabetes reduces autophosphorylation of retinal insulin receptor and increases protein-tyrosine phosphatase-1B activity
    • Rajala, R. V., B. Wiskur, M. Tanito, M. Callegan, and A. Rajala. 2009. Diabetes reduces autophosphorylation of retinal insulin receptor and increases protein-tyrosine phosphatase-1B activity. Invest. Ophthalmol. Vis. Sci. 50: 1033-1040.
    • (2009) Invest. Ophthalmol. Vis. Sci , vol.50 , pp. 1033-1040
    • Rajala, R.V.1    Wiskur, B.2    Tanito, M.3    Callegan, M.4    Rajala, A.5
  • 134
    • 85047682027 scopus 로고    scopus 로고
    • Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor
    • Ravichandran, L. V., H. Chen, Y. Li, and M. J. Quon. 2001. Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor. Mol. Endocrinol. 15: 1768-1780.
    • (2001) Mol. Endocrinol , vol.15 , pp. 1768-1780
    • Ravichandran, L.V.1    Chen, H.2    Li, Y.3    Quon, M.J.4
  • 135
    • 33846233063 scopus 로고    scopus 로고
    • Nonredundant role of Akt2 for neuroprotection of rod photoreceptor cells from light-induced cell death
    • Li, G., R. E. Anderson, H. Tomita, R. Adler, X. Liu, D. J. Zack, and R. V. Rajala. 2007. Nonredundant role of Akt2 for neuroprotection of rod photoreceptor cells from light-induced cell death. J. Neurosci. 27: 203-211.
    • (2007) J. Neurosci , vol.27 , pp. 203-211
    • Li, G.1    Anderson, R.E.2    Tomita, H.3    Adler, R.4    Liu, X.5    Zack, D.J.6    Rajala, R.V.7
  • 136
    • 0033018109 scopus 로고    scopus 로고
    • Mechanism of protein kinase B activation by insulin/ insulin-like growth factor-1 revealed by specific inhibitors of phosphoinositide 3-kinase-significance for diabetes and cancer
    • Galetic, I., M. Andjelkovic, R. Meier, D. Brodbeck, J. Park, and B. A. Hemmings. 1999. Mechanism of protein kinase B activation by insulin/ insulin-like growth factor-1 revealed by specific inhibitors of phosphoinositide 3-kinase-significance for diabetes and cancer. Pharmacol. Ther. 82: 409-425.
    • (1999) Pharmacol. Ther , vol.82 , pp. 409-425
    • Galetic, I.1    Andjelkovic, M.2    Meier, R.3    Brodbeck, D.4    Park, J.5    Hemmings, B.A.6
  • 137
    • 0035432971 scopus 로고    scopus 로고
    • Defective insulin-induced GLUT4 translocation in skeletal muscle of high fat-fed rats is associated with alterations in both Akt/protein kinase B and atypical protein kinase C (zeta/lambda) activities
    • Tremblay, F., C. Lavigne, H. Jacques, and A. Marette. 2001. Defective insulin-induced GLUT4 translocation in skeletal muscle of high fat-fed rats is associated with alterations in both Akt/protein kinase B and atypical protein kinase C (zeta/lambda) activities. Diabetes. 50: 1901-1910.
    • (2001) Diabetes , vol.50 , pp. 1901-1910
    • Tremblay, F.1    Lavigne, C.2    Jacques, H.3    Marette, A.4
  • 138
    • 0035853447 scopus 로고    scopus 로고
    • Akt mediates insulin induction of glucose uptake and up-regulation of GLUT4 gene expression in brown adipocytes
    • Hernandez, R., T. Teruel, and M. Lorenzo. 2001. Akt mediates insulin induction of glucose uptake and up-regulation of GLUT4 gene expression in brown adipocytes. FEBS Lett. 494: 225-231.
    • (2001) FEBS Lett , vol.494 , pp. 225-231
    • Hernandez, R.1    Teruel, T.2    Lorenzo, M.3
  • 139
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes
    • Vosseller, K., L. Wells, M. D. Lane, and G. W. Hart. 2002. Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. Proc. Natl. Acad. Sci. USA. 99: 5313-5318.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 140
    • 0034652392 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase signaling mediates angiogenesis and expression of vascular endothelial growth factor in endothelial cells
    • Jiang, B. H., J. Z. Zheng, M. Aoki, and P. K. Vogt. 2000. Phosphatidylinositol 3-kinase signaling mediates angiogenesis and expression of vascular endothelial growth factor in endothelial cells. Proc. Natl. Acad. Sci. USA. 97: 1749-1753.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1749-1753
    • Jiang, B.H.1    Zheng, J.Z.2    Aoki, M.3    Vogt, P.K.4
  • 141
    • 0035040968 scopus 로고    scopus 로고
    • Early growth response factor-1 mediates insulin-inducible vascular endothelial cell proliferation and regrowth after injury
    • Gousseva, N., K. Kugathasan, C. N. Chesterman, and L. M. Khachigian. 2001. Early growth response factor-1 mediates insulin-inducible vascular endothelial cell proliferation and regrowth after injury. J. Cell. Biochem. 81: 523-534.
    • (2001) J. Cell. Biochem , vol.81 , pp. 523-534
    • Gousseva, N.1    Kugathasan, K.2    Chesterman, C.N.3    Khachigian, L.M.4
  • 142
    • 0034754014 scopus 로고    scopus 로고
    • VEGF increases permeability of the endothelial cell monolayer by activation of PKB/akt, endothelial nitric-oxide synthase, and MAP kinase pathways
    • Lal, B. K., S. Varma, P. J. Pappas, R. W. Hobson, and W. N. Duran. 2001. VEGF increases permeability of the endothelial cell monolayer by activation of PKB/akt, endothelial nitric-oxide synthase, and MAP kinase pathways. Microvasc. Res. 62: 252-262.
    • (2001) Microvasc. Res , vol.62 , pp. 252-262
    • Lal, B.K.1    Varma, S.2    Pappas, P.J.3    Hobson, R.W.4    Duran, W.N.5
  • 144
    • 33646485943 scopus 로고    scopus 로고
    • Loss of class IA PI3K signaling in muscle leads to impaired muscle growth, insulin response, and hyperlipidemia
    • Luo, J., C. L. Sobkiw, M. F. Hirshman, M. N. Logsdon, T. Q. Li, L. J. Goodyear, and L. C. Cantley. 2006. Loss of class IA PI3K signaling in muscle leads to impaired muscle growth, insulin response, and hyperlipidemia. Cell Metab. 3: 355-366.
    • (2006) Cell Metab , vol.3 , pp. 355-366
    • Luo, J.1    Sobkiw, C.L.2    Hirshman, M.F.3    Logsdon, M.N.4    Li, T.Q.5    Goodyear, L.J.6    Cantley, L.C.7
  • 145
    • 0038555740 scopus 로고    scopus 로고
    • Functions of insulin and insulin receptor signaling in retina: Possible implications for diabetic retinopathy
    • Reiter, C. E., and T. W. Gardner. 2003. Functions of insulin and insulin receptor signaling in retina: possible implications for diabetic retinopathy. Prog. Retin. Eye Res. 22: 545-562.
    • (2003) Prog. Retin. Eye Res , vol.22 , pp. 545-562
    • Reiter, C.E.1    Gardner, T.W.2
  • 146
    • 68949199043 scopus 로고    scopus 로고
    • Insulin receptor signaling regulates actin cytoskeletal organization in developing photoreceptors
    • Rajala, R. V., A. Rajala, R. S. Brush, N. P. Rotstein, and L. E. Politi. 2009. Insulin receptor signaling regulates actin cytoskeletal organization in developing photoreceptors. J. Neurochem. 110: 1648-1660.
    • (2009) J. Neurochem , vol.110 , pp. 1648-1660
    • Rajala, R.V.1    Rajala, A.2    Brush, R.S.3    Rotstein, N.P.4    Politi, L.E.5
  • 147
    • 0035980759 scopus 로고    scopus 로고
    • Phosphoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane
    • Takenawa, T., and T. Itoh. 2001. Phosphoinositides, key molecules for regulation of actin cytoskeletal organization and membrane traffic from the plasma membrane. Biochim. Biophys. Acta. 1533: 190-206.
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 190-206
    • Takenawa, T.1    Itoh, T.2
  • 148
    • 50349083511 scopus 로고    scopus 로고
    • Loss of neuroprotective survival signal in mice lacking insulin receptor gene in rod photoreceptor cells
    • Rajala, A., M. Tanito, Y. Z. Le, C. R. Kahn, and R. V. Rajala. 2008. Loss of neuroprotective survival signal in mice lacking insulin receptor gene in rod photoreceptor cells. J. Biol. Chem. 283: 19781-19792.
    • (2008) J. Biol. Chem , vol.283 , pp. 19781-19792
    • Rajala, A.1    Tanito, M.2    Le, Y.Z.3    Kahn, C.R.4    Rajala, R.V.5
  • 149
    • 1842422848 scopus 로고    scopus 로고
    • Association between variation in the actin-binding gene caldesmon and diabetic nephropathy in type 1 diabetes
    • Conway, B. R., A. P. Maxwell, D. A. Savage, C. C. Patterson, P. P. Doran, M. Murphy, H. R. Brady, and D. G. Fogarty. 2004. Association between variation in the actin-binding gene caldesmon and diabetic nephropathy in type 1 diabetes. Diabetes. 53: 1162-1165.
    • (2004) Diabetes , vol.53 , pp. 1162-1165
    • Conway, B.R.1    Maxwell, A.P.2    Savage, D.A.3    Patterson, C.C.4    Doran, P.P.5    Murphy, M.6    Brady, H.R.7    Fogarty, D.G.8
  • 150
    • 0030752545 scopus 로고    scopus 로고
    • The role of axonal cytoskeleton in diabetic neuropathy
    • McLean, W. G. 1997. The role of axonal cytoskeleton in diabetic neuropathy. Neurochem. Res. 22: 951-956.
    • (1997) Neurochem. Res , vol.22 , pp. 951-956
    • McLean, W.G.1
  • 151
    • 0028940097 scopus 로고
    • Post-translational modifications of microtubule- and growth-associated proteins in nerve regeneration and neuropathy
    • McLean, W. G., R. E. Roberts, and F. H. Mullins. 1995. Post-translational modifications of microtubule- and growth-associated proteins in nerve regeneration and neuropathy. Biochem. Soc. Trans. 23: 76-80.
    • (1995) Biochem. Soc. Trans , vol.23 , pp. 76-80
    • McLean, W.G.1    Roberts, R.E.2    Mullins, F.H.3
  • 152
    • 0032076955 scopus 로고    scopus 로고
    • Actin mutations in dilated cardiomyopathy, a heritable form of heart failure
    • Olson, T. M., V. V. Michels, S. N. Thibodeau, Y. S. Tai, and M. T. Keating. 1998. Actin mutations in dilated cardiomyopathy, a heritable form of heart failure. Science. 280: 750-752.
    • (1998) Science , vol.280 , pp. 750-752
    • Olson, T.M.1    Michels, V.V.2    Thibodeau, S.N.3    Tai, Y.S.4    Keating, M.T.5
  • 153
    • 0343820599 scopus 로고
    • Diabetic cardiomyopathy in rats: Mechanical and biochemical response to different insulin doses
    • Fein, F. S., A. Malhotra, B. Miller-Green, J. Scheuer, and E. H. Sonnenblick. 1984. Diabetic cardiomyopathy in rats: mechanical and biochemical response to different insulin doses. Am. J. Physiol. 247: H817-H823.
    • (1984) Am. J. Physiol , vol.247
    • Fein, F.S.1    Malhotra, A.2    Miller-Green, B.3    Scheuer, J.4    Sonnenblick, E.H.5
  • 154
    • 66649095843 scopus 로고    scopus 로고
    • Development of selective axonopathy in adult sensory neurons isolated from diabetic rats: Role of glucose-induced oxidative stress
    • Zherebitskaya, E., E. Akude, D. R. Smith, and P. Fernyhough. 2009. Development of selective axonopathy in adult sensory neurons isolated from diabetic rats: role of glucose-induced oxidative stress. Diabetes. 58: 1356-1364.
    • (2009) Diabetes , vol.58 , pp. 1356-1364
    • Zherebitskaya, E.1    Akude, E.2    Smith, D.R.3    Fernyhough, P.4
  • 156
    • 20144374264 scopus 로고    scopus 로고
    • Identification of a NPXY motif in growth factor receptor-bound protein 14 (Grb14) and its interaction with the phosphotyrosine-binding (PTB) domain of IRS-1
    • Rajala, R. V., and M. D. Chan. 2005. Identification of a NPXY motif in growth factor receptor-bound protein 14 (Grb14) and its interaction with the phosphotyrosine-binding (PTB) domain of IRS-1. Biochemistry. 44: 7929-7935.
    • (2005) Biochemistry , vol.44 , pp. 7929-7935
    • Rajala, R.V.1    Chan, M.D.2
  • 157
    • 28244443669 scopus 로고    scopus 로고
    • Lipid-protein interactions of growth factor receptor-bound protein 14 in insulin receptor signaling
    • Rajala, R. V., M. D. Chan, and A. Rajala. 2005. Lipid-protein interactions of growth factor receptor-bound protein 14 in insulin receptor signaling. Biochemistry. 44: 15461-15471.
    • (2005) Biochemistry , vol.44 , pp. 15461-15471
    • Rajala, R.V.1    Chan, M.D.2    Rajala, A.3
  • 158
    • 0032695794 scopus 로고    scopus 로고
    • Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration
    • Jones, N., Z. Master, J. Jones, D. Bouchard, Y. Gunji, H. Sasaki, R. Daly, K. Alitalo, and D. J. Dumont. 1999. Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration. J. Biol. Chem. 274: 30896-30905.
    • (1999) J. Biol. Chem , vol.274 , pp. 30896-30905
    • Jones, N.1    Master, Z.2    Jones, J.3    Bouchard, D.4    Gunji, Y.5    Sasaki, H.6    Daly, R.7    Alitalo, K.8    Dumont, D.J.9
  • 159
    • 17544378927 scopus 로고    scopus 로고
    • Cloning and characterization of GRB14, a novel member of the GRB7 gene family
    • Daly, R. J., G. M. Sanderson, P. W. Janes, and R. L. Sutherland. 1996. Cloning and characterization of GRB14, a novel member of the GRB7 gene family. J. Biol. Chem. 271: 12502-12510.
    • (1996) J. Biol. Chem , vol.271 , pp. 12502-12510
    • Daly, R.J.1    Sanderson, G.M.2    Janes, P.W.3    Sutherland, R.L.4
  • 160
    • 0034677773 scopus 로고    scopus 로고
    • Association of fibroblast growth factor receptor 1 with the adaptor protein Grb14. Characterization of a new receptor binding partner
    • Reilly, J. F., G. Mickey, and P. A. Maher. 2000. Association of fibroblast growth factor receptor 1 with the adaptor protein Grb14. Characterization of a new receptor binding partner. J. Biol. Chem. 275: 7771-7778.
    • (2000) J. Biol. Chem , vol.275 , pp. 7771-7778
    • Reilly, J.F.1    Mickey, G.2    Maher, P.A.3
  • 162
    • 67649197552 scopus 로고    scopus 로고
    • Growth factor receptor-bound protein 14 undergoes light-dependent intracellular translocation in rod photoreceptors: Functional role on retinal insulin receptor activation
    • Rajala, A., R. J. Daly, M. Tanito, D. T. Allen, L. J. Holt, E. Lobanova, V. Y. Arshavsky, and R. V. Rajala. 2009. Growth factor receptor-bound protein 14 undergoes light-dependent intracellular translocation in rod photoreceptors: functional role on retinal insulin receptor activation. Biochemistry. 48: 5563-5572.
    • (2009) Biochemistry , vol.48 , pp. 5563-5572
    • Rajala, A.1    Daly, R.J.2    Tanito, M.3    Allen, D.T.4    Holt, L.J.5    Lobanova, E.6    Arshavsky, V.Y.7    Rajala, R.V.8
  • 164
    • 0032938716 scopus 로고    scopus 로고
    • Regulation of tyrosine kinase cascades by G-protein-coupled receptors
    • Luttrell, L. M., Y. Daaka, and R. J. Lefkowitz. 1999. Regulation of tyrosine kinase cascades by G-protein-coupled receptors. Curr. Opin. Cell Biol. 11: 177-183.
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 177-183
    • Luttrell, L.M.1    Daaka, Y.2    Lefkowitz, R.J.3
  • 165
    • 0032981482 scopus 로고    scopus 로고
    • Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein
    • Lev, S., J. Hernandez, R. Martinez, A. Chen, G. Plowman, and J. Schlessinger. 1999. Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol. Cell. Biol. 19: 2278-2288.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 2278-2288
    • Lev, S.1    Hernandez, J.2    Martinez, R.3    Chen, A.4    Plowman, G.5    Schlessinger, J.6
  • 166
    • 21644486050 scopus 로고    scopus 로고
    • Imaging phosphoinositide dynamics using GFP-tagged protein domains
    • Halet, G. 2005. Imaging phosphoinositide dynamics using GFP-tagged protein domains. Biol. Cell. 97: 501-518.
    • (2005) Biol. Cell , vol.97 , pp. 501-518
    • Halet, G.1
  • 167
    • 19444368038 scopus 로고    scopus 로고
    • Analysis of phosphoinositide binding domain properties within the myotubularin-related protein MTMR3
    • Lorenzo, O., S. Urbe, and M. J. Clague. 2005. Analysis of phosphoinositide binding domain properties within the myotubularin-related protein MTMR3. J. Cell Sci. 118: 2005-2012.
    • (2005) J. Cell Sci , vol.118 , pp. 2005-2012
    • Lorenzo, O.1    Urbe, S.2    Clague, M.J.3
  • 168
    • 13544249968 scopus 로고    scopus 로고
    • In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis
    • Dormann, D., G. Weijer, S. Dowler, and C. J. Weijer. 2004. In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis. J. Cell Sci. 117: 6497-6509.
    • (2004) J. Cell Sci , vol.117 , pp. 6497-6509
    • Dormann, D.1    Weijer, G.2    Dowler, S.3    Weijer, C.J.4
  • 169
    • 0035899829 scopus 로고    scopus 로고
    • A PtdIns(3)P-specific probe cycles on and off host cell membranes during Salmonella invasion of mammalian cells
    • Pattni, K., M. Jepson, H. Stenmark, and G. Banting. 2001. A PtdIns(3)P-specific probe cycles on and off host cell membranes during Salmonella invasion of mammalian cells. Curr. Biol. 11: 1636-1642.
    • (2001) Curr. Biol , vol.11 , pp. 1636-1642
    • Pattni, K.1    Jepson, M.2    Stenmark, H.3    Banting, G.4
  • 170
    • 33645274673 scopus 로고    scopus 로고
    • Analyzing phosphoinositides and their interacting proteins
    • Rusten, T. E., and H. Stenmark. 2006. Analyzing phosphoinositides and their interacting proteins. Nat. Methods. 3: 251-258.
    • (2006) Nat. Methods , vol.3 , pp. 251-258
    • Rusten, T.E.1    Stenmark, H.2
  • 171
    • 0017297774 scopus 로고
    • Photoreceptor shedding is initiated by light in the frog retina
    • Basinger, S., R. Hoffman, and M. Matthes. 1976. Photoreceptor shedding is initiated by light in the frog retina. Science. 194: 1074-1076.
    • (1976) Science , vol.194 , pp. 1074-1076
    • Basinger, S.1    Hoffman, R.2    Matthes, M.3
  • 172
    • 0018427565 scopus 로고
    • Photoreceptor outer segment development: Light and dark regulate the rate of membrane addition and loss
    • Hollyfield, J. G., and M. E. Rayborn. 1979. Photoreceptor outer segment development: light and dark regulate the rate of membrane addition and loss. Invest. Ophthalmol. Vis. Sci. 18: 117-132.
    • (1979) Invest. Ophthalmol. Vis. Sci , vol.18 , pp. 117-132
    • Hollyfield, J.G.1    Rayborn, M.E.2
  • 174
    • 0031054670 scopus 로고    scopus 로고
    • Insulin-like growth factor and potassium depolarization maintain neuronal survival by distinct pathways: Possible involvement of PI 3-kinase in IGF-1 signaling
    • D'Mello, S. R., K. Borodezt, and S. P. Soltoff. 1997. Insulin-like growth factor and potassium depolarization maintain neuronal survival by distinct pathways: possible involvement of PI 3-kinase in IGF-1 signaling. J. Neurosci. 17: 1548-1560.
    • (1997) J. Neurosci , vol.17 , pp. 1548-1560
    • D'Mello, S.R.1    Borodezt, K.2    Soltoff, S.P.3
  • 175
    • 1842370285 scopus 로고    scopus 로고
    • Nerve growth factor protects PC12 cells against peroxynitrite-induced apoptosis via a mechanism dependent on phosphatidylinositol 3-kinase
    • Spear, N., A. G. Estevez, L. Barbeito, J. S. Beckman, and G. V. Johnson. 1997. Nerve growth factor protects PC12 cells against peroxynitrite-induced apoptosis via a mechanism dependent on phosphatidylinositol 3-kinase. J. Neurochem. 69: 53-59.
    • (1997) J. Neurochem , vol.69 , pp. 53-59
    • Spear, N.1    Estevez, A.G.2    Barbeito, L.3    Beckman, J.S.4    Johnson, G.V.5
  • 176
    • 0015207786 scopus 로고
    • Irreversible effects on visible light on the retina: Role of vitamin A
    • Noell, W. K., and R. Albrecht. 1971. Irreversible effects on visible light on the retina: role of vitamin A. Science. 172: 76-79.
    • (1971) Science , vol.172 , pp. 76-79
    • Noell, W.K.1    Albrecht, R.2
  • 177
    • 0019190592 scopus 로고
    • Possible mechanisms of photoreceptor damage by light in mammalian eyes
    • Noell, W. K. 1980. Possible mechanisms of photoreceptor damage by light in mammalian eyes. Vision Res. 20: 1163-1171.
    • (1980) Vision Res , vol.20 , pp. 1163-1171
    • Noell, W.K.1
  • 179
    • 0033555829 scopus 로고    scopus 로고
    • Xid-like immunodeficiency in mice with disruption of the p85alpha subunit of phosphoinositide 3-kinase
    • Suzuki, H., Y. Terauchi, M. Fujiwara, S. Aizawa, Y. Yazaki, T. Kadowaki, and S. Koyasu. 1999. Xid-like immunodeficiency in mice with disruption of the p85alpha subunit of phosphoinositide 3-kinase. Science. 283: 390-392.
    • (1999) Science , vol.283 , pp. 390-392
    • Suzuki, H.1    Terauchi, Y.2    Fujiwara, M.3    Aizawa, S.4    Yazaki, Y.5    Kadowaki, T.6    Koyasu, S.7
  • 181
    • 0033556333 scopus 로고    scopus 로고
    • Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85alpha
    • Fruman, D. A., S. B. Snapper, C. M. Yballe, L. Davidson, J. Y. Yu, F. W. Alt, and L. C. Cantley. 1999. Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85alpha. Science. 283: 393-397.
    • (1999) Science , vol.283 , pp. 393-397
    • Fruman, D.A.1    Snapper, S.B.2    Yballe, C.M.3    Davidson, L.4    Yu, J.Y.5    Alt, F.W.6    Cantley, L.C.7
  • 184
    • 0346220260 scopus 로고    scopus 로고
    • Positive and negative roles of p85 alpha and p85 beta regulatory subunits of phosphoinositide 3-kinase in insulin signaling
    • Ueki, K., D. A. Fruman, C. M. Yballe, M. Fasshauer, J. Klein, T. Asano, L. C. Cantley, and C. R. Kahn. 2003. Positive and negative roles of p85 alpha and p85 beta regulatory subunits of phosphoinositide 3-kinase in insulin signaling. J. Biol. Chem. 278: 48453-48466.
    • (2003) J. Biol. Chem , vol.278 , pp. 48453-48466
    • Ueki, K.1    Fruman, D.A.2    Yballe, C.M.3    Fasshauer, M.4    Klein, J.5    Asano, T.6    Cantley, L.C.7    Kahn, C.R.8
  • 185
    • 0036143774 scopus 로고    scopus 로고
    • Molecular balance between the regulatory and catalytic subunits of phosphoinositide 3-kinase regulates cell signaling and survival
    • Ueki, K., D. A. Fruman, S. M. Brachmann, Y. H. Tseng, L. C. Cantley, and C. R. Kahn. 2002. Molecular balance between the regulatory and catalytic subunits of phosphoinositide 3-kinase regulates cell signaling and survival. Mol. Cell. Biol. 22: 965-977.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 965-977
    • Ueki, K.1    Fruman, D.A.2    Brachmann, S.M.3    Tseng, Y.H.4    Cantley, L.C.5    Kahn, C.R.6
  • 186
    • 0032496150 scopus 로고    scopus 로고
    • Dynamics of insulin signaling in 3T3-L1 adipocytes. Differential compartmentalization and trafficking of insulin receptor substrate (IRS)-1 and IRS-2
    • Inoue, G., B. Cheatham, R. Emkey, and C. R. Kahn. 1998. Dynamics of insulin signaling in 3T3-L1 adipocytes. Differential compartmentalization and trafficking of insulin receptor substrate (IRS)-1 and IRS-2. J. Biol. Chem. 273: 11548-11555.
    • (1998) J. Biol. Chem , vol.273 , pp. 11548-11555
    • Inoue, G.1    Cheatham, B.2    Emkey, R.3    Kahn, C.R.4
  • 187
    • 23744456586 scopus 로고    scopus 로고
    • The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complex
    • Luo, J., S. J. Field, J. Y. Lee, J. A. Engelman, and L. C. Cantley. 2005. The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complex. J. Cell Biol. 170: 455-464.
    • (2005) J. Cell Biol , vol.170 , pp. 455-464
    • Luo, J.1    Field, S.J.2    Lee, J.Y.3    Engelman, J.A.4    Cantley, L.C.5
  • 188
    • 35748980862 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-independent non-genomic signals transit from the androgen receptor to Akt1 in membrane raft microdomains
    • Cinar, B., N. K. Mukhopadhyay, G. Meng, and M. R. Freeman. 2007. Phosphoinositide 3-kinase-independent non-genomic signals transit from the androgen receptor to Akt1 in membrane raft microdomains. J. Biol. Chem. 282: 29584-29593.
    • (2007) J. Biol. Chem , vol.282 , pp. 29584-29593
    • Cinar, B.1    Mukhopadhyay, N.K.2    Meng, G.3    Freeman, M.R.4
  • 190
    • 0037448449 scopus 로고    scopus 로고
    • Modulation of phosphoinositide 3-kinase activation by cholesterol level suggests a novel positive role for lipid rafts in lysophosphatidic acid signalling
    • Peres, C., A. Yart, B. Perret, J. P. Salles, and P. Raynal. 2003. Modulation of phosphoinositide 3-kinase activation by cholesterol level suggests a novel positive role for lipid rafts in lysophosphatidic acid signalling. FEBS Lett. 534: 164-168.
    • (2003) FEBS Lett , vol.534 , pp. 164-168
    • Peres, C.1    Yart, A.2    Perret, B.3    Salles, J.P.4    Raynal, P.5
  • 191
    • 33747381343 scopus 로고    scopus 로고
    • Localization of the insulin receptor and phosphoinositide 3-kinase in detergent-resistant membrane rafts of rod photoreceptor outer segments
    • Rajala, R. V., M. H. Elliott, M. E. McClellan, and R. E. Anderson. 2006. Localization of the insulin receptor and phosphoinositide 3-kinase in detergent-resistant membrane rafts of rod photoreceptor outer segments. Adv. Exp. Med. Biol. 572: 491-497.
    • (2006) Adv. Exp. Med. Biol , vol.572 , pp. 491-497
    • Rajala, R.V.1    Elliott, M.H.2    McClellan, M.E.3    Anderson, R.E.4
  • 194
  • 195
    • 0346271744 scopus 로고    scopus 로고
    • Regulation of retinal phosphoinositide 3-kinase activity in p85alpha-subunit knockout mice
    • Rajala, R. V., M. E. McClellan, J. D. Ash, and R. E. Anderson. 2003. Regulation of retinal phosphoinositide 3-kinase activity in p85alpha-subunit knockout mice. Adv. Exp. Med. Biol. 533: 369-376.
    • (2003) Adv. Exp. Med. Biol , vol.533 , pp. 369-376
    • Rajala, R.V.1    McClellan, M.E.2    Ash, J.D.3    Anderson, R.E.4
  • 196
    • 14144250240 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase catalytic subunit deletion and regulatory subunit deletion have opposite effects on insulin sensitivity in mice
    • Brachmann, S. M., K. Ueki, J. A. Engelman, R. C. Kahn, and L. C. Cantley. 2005. Phosphoinositide 3-kinase catalytic subunit deletion and regulatory subunit deletion have opposite effects on insulin sensitivity in mice. Mol. Cell. Biol. 25: 1596-1607.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 1596-1607
    • Brachmann, S.M.1    Ueki, K.2    Engelman, J.A.3    Kahn, R.C.4    Cantley, L.C.5
  • 199
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. 2000. Cell signaling by receptor tyrosine kinases. Cell. 103: 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 200
    • 0028246440 scopus 로고
    • Binding of G protein beta gamma-subunits to pleckstrin homology domains
    • Touhara, K., J. Inglese, J. A. Pitcher, G. Shaw, and R. J. Lefkowitz. 1994. Binding of G protein beta gamma-subunits to pleckstrin homology domains. J. Biol. Chem. 269: 10217-10220.
    • (1994) J. Biol. Chem , vol.269 , pp. 10217-10220
    • Touhara, K.1    Inglese, J.2    Pitcher, J.A.3    Shaw, G.4    Lefkowitz, R.J.5
  • 201
    • 0344289531 scopus 로고    scopus 로고
    • RACK1, a protein kinase C anchoring protein, coordinates the binding of activated protein kinase C and select pleckstrin homology domains in vitro
    • Rodriguez, M. M., D. Ron, K. Touhara, C. H. Chen, and D. Mochly-Rosen. 1999. RACK1, a protein kinase C anchoring protein, coordinates the binding of activated protein kinase C and select pleckstrin homology domains in vitro. Biochemistry. 38: 13787-13794.
    • (1999) Biochemistry , vol.38 , pp. 13787-13794
    • Rodriguez, M.M.1    Ron, D.2    Touhara, K.3    Chen, C.H.4    Mochly-Rosen, D.5
  • 202
    • 0033551051 scopus 로고    scopus 로고
    • Evectins: Vesicular proteins that carry a pleckstrin homology domain and localize to post-Golgi membranes
    • Krappa, R., A. Nguyen, P. Burrola, D. Deretic, and G. Lemke. 1999. Evectins: vesicular proteins that carry a pleckstrin homology domain and localize to post-Golgi membranes. Proc. Natl. Acad. Sci. USA. 96: 4633-4638.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4633-4638
    • Krappa, R.1    Nguyen, A.2    Burrola, P.3    Deretic, D.4    Lemke, G.5
  • 204
    • 0033544927 scopus 로고    scopus 로고
    • PHR1 encodes an abundant, pleckstrin homology domain-containing integral membrane protein in the photoreceptor outer segments
    • Xu, S., R. Ladak, D. A. Swanson, A. Soltyk, H. Sun, L. Ploder, D. Vidgen, A. M. Duncan, E. Garami, D. Valle, et al. 1999. PHR1 encodes an abundant, pleckstrin homology domain-containing integral membrane protein in the photoreceptor outer segments. J. Biol. Chem. 274: 35676-35685.
    • (1999) J. Biol. Chem , vol.274 , pp. 35676-35685
    • Xu, S.1    Ladak, R.2    Swanson, D.A.3    Soltyk, A.4    Sun, H.5    Ploder, L.6    Vidgen, D.7    Duncan, A.M.8    Garami, E.9    Valle, D.10
  • 205
    • 33947203621 scopus 로고    scopus 로고
    • PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms
    • Brognard, J., E. Sierecki, T. Gao, and A. C. Newton. 2007. PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms. Mol. Cell. 25: 917-931.
    • (2007) Mol. Cell , vol.25 , pp. 917-931
    • Brognard, J.1    Sierecki, E.2    Gao, T.3    Newton, A.C.4
  • 207
    • 0019174489 scopus 로고
    • Metabolism of phosphatidylethanolamine in the frog retina
    • Anderson, R. E., P. A. Kelleher, and M. B. Maude. 1980. Metabolism of phosphatidylethanolamine in the frog retina. Biochim. Biophys. Acta. 620: 227-235.
    • (1980) Biochim. Biophys. Acta , vol.620 , pp. 227-235
    • Anderson, R.E.1    Kelleher, P.A.2    Maude, M.B.3
  • 208
    • 0020513374 scopus 로고
    • Phosphoinositide metabolism in the retina: Localization to horizontal cells and regulation by light and divalent cations
    • Anderson, R. E., M. B. Maude, P. A. Kelleher, M. E. Rayborn, and J. G. Hollyfield. 1983. Phosphoinositide metabolism in the retina: localization to horizontal cells and regulation by light and divalent cations. J. Neurochem. 41: 764-771.
    • (1983) J. Neurochem , vol.41 , pp. 764-771
    • Anderson, R.E.1    Maude, M.B.2    Kelleher, P.A.3    Rayborn, M.E.4    Hollyfield, J.G.5
  • 209
    • 0021272958 scopus 로고
    • Inositol incorporation into phosphoinositides in retinal horizontal cells of Xenopus laevis: Enhancement by acetylcholine, inhibition by glycine
    • Anderson, R. E., and J. G. Hollyfield. 1984. Inositol incorporation into phosphoinositides in retinal horizontal cells of Xenopus laevis: enhancement by acetylcholine, inhibition by glycine. J. Cell Biol. 99: 686-691.
    • (1984) J. Cell Biol , vol.99 , pp. 686-691
    • Anderson, R.E.1    Hollyfield, J.G.2
  • 210
    • 0021940075 scopus 로고
    • Effect of light on the metabolism of lipids in the rat retina
    • Anderson, R. E., M. B. Maude, G. A. Pu, and J. G. Hollyfield. 1985. Effect of light on the metabolism of lipids in the rat retina. J. Neurochem. 44: 773-778.
    • (1985) J. Neurochem , vol.44 , pp. 773-778
    • Anderson, R.E.1    Maude, M.B.2    Pu, G.A.3    Hollyfield, J.G.4
  • 211
    • 0027184503 scopus 로고
    • Light evoked inositol trisphosphate release in the rat retina in vitro
    • Jung, H. H., C. E. Reme, and J. Pfeilschifter. 1993. Light evoked inositol trisphosphate release in the rat retina in vitro. Curr. Eye Res. 12: 727-732.
    • (1993) Curr. Eye Res , vol.12 , pp. 727-732
    • Jung, H.H.1    Reme, C.E.2    Pfeilschifter, J.3
  • 212
    • 0020955704 scopus 로고
    • Phosphatidylinositol synthesis and phosphorylation are enhanced by light in rat retinas
    • Schmidt, S. Y. 1983. Phosphatidylinositol synthesis and phosphorylation are enhanced by light in rat retinas. J. Biol. Chem. 258: 6863-6868.
    • (1983) J. Biol. Chem , vol.258 , pp. 6863-6868
    • Schmidt, S.Y.1
  • 213
    • 0020538461 scopus 로고
    • Light enhances the turnover of phosphatidylinositol in rat retinas
    • Schmidt, S. Y. 1983. Light enhances the turnover of phosphatidylinositol in rat retinas. J. Neurochem. 40: 1630-1638.
    • (1983) J. Neurochem , vol.40 , pp. 1630-1638
    • Schmidt, S.Y.1
  • 214
    • 0020548172 scopus 로고
    • Light- and cytidine-dependent phosphatidylinositol synthesis in photoreceptor cells of the rat
    • Schmidt, S. Y. 1983. Light- and cytidine-dependent phosphatidylinositol synthesis in photoreceptor cells of the rat. J. Cell Biol. 97: 832-837.
    • (1983) J. Cell Biol , vol.97 , pp. 832-837
    • Schmidt, S.Y.1
  • 215
    • 0025125139 scopus 로고
    • Phosphoinositide metabolism in frog rod outer segments
    • Choe, H. G., A. J. Ghalayini, and R. E. Anderson. 1990. Phosphoinositide metabolism in frog rod outer segments. Exp. Eye Res. 51: 167-176.
    • (1990) Exp. Eye Res , vol.51 , pp. 167-176
    • Choe, H.G.1    Ghalayini, A.J.2    Anderson, R.E.3
  • 216
    • 0031662594 scopus 로고    scopus 로고
    • Light stimulates tyrosine phosphorylation of rat rod outer segments in vivo
    • Ghalayini, A. J., X. X. Guo, C. A. Koutz, and R. E. Anderson. 1998. Light stimulates tyrosine phosphorylation of rat rod outer segments in vivo. Exp. Eye Res. 66: 817-821.
    • (1998) Exp. Eye Res , vol.66 , pp. 817-821
    • Ghalayini, A.J.1    Guo, X.X.2    Koutz, C.A.3    Anderson, R.E.4
  • 217
    • 0023653268 scopus 로고
    • Light induces a rapid and transient increase in inositol-trisphosphate in toad rod outer segments
    • Brown, J. E., C. Blazynski, and A. I. Cohen. 1987. Light induces a rapid and transient increase in inositol-trisphosphate in toad rod outer segments. Biochem. Biophys. Res. Commun. 146: 1392-1396.
    • (1987) Biochem. Biophys. Res. Commun , vol.146 , pp. 1392-1396
    • Brown, J.E.1    Blazynski, C.2    Cohen, A.I.3
  • 219
    • 0022878487 scopus 로고
    • Immunocytochemical localization of phosphatidylinositol-4,5-bisphosphate in dark- and light-adapted rat retinas
    • Das, N. D., T. Yoshioka, D. Samuelson, and H. Shichi. 1986. Immunocytochemical localization of phosphatidylinositol-4,5-bisphosphate in dark- and light-adapted rat retinas. Cell Struct. Funct. 11: 53-63.
    • (1986) Cell Struct. Funct , vol.11 , pp. 53-63
    • Das, N.D.1    Yoshioka, T.2    Samuelson, D.3    Shichi, H.4
  • 220
    • 0023621694 scopus 로고
    • Immunochemical evidence for the light-regulated modulation of phosphatidylinositol-4,5-bisphosphate in rat photoreceptor cells
    • Das, N. D., T. Yoshioka, D. Samuelson, R. J. Cohen, and H. Shichi. 1987. Immunochemical evidence for the light-regulated modulation of phosphatidylinositol-4,5-bisphosphate in rat photoreceptor cells. Cell Struct. Funct. 12: 471-481.
    • (1987) Cell Struct. Funct , vol.12 , pp. 471-481
    • Das, N.D.1    Yoshioka, T.2    Samuelson, D.3    Cohen, R.J.4    Shichi, H.5
  • 221
    • 0027160149 scopus 로고
    • Distinctive subtypes of bovine phospholipase C that have preferential expression in the retina and high homology to the norpA gene product of Drosophila
    • Ferreira, P. A., R. D. Shortridge, and W. L. Pak. 1993. Distinctive subtypes of bovine phospholipase C that have preferential expression in the retina and high homology to the norpA gene product of Drosophila. Proc. Natl. Acad. Sci. USA. 90: 6042-6046.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6042-6046
    • Ferreira, P.A.1    Shortridge, R.D.2    Pak, W.L.3
  • 222
    • 0025366032 scopus 로고
    • Phosphoinositide synthesis in bovine rod outer segments
    • Gehm, B. D., and D. G. Mc Connell. 1990. Phosphoinositide synthesis in bovine rod outer segments. Biochemistry. 29: 5442-5446.
    • (1990) Biochemistry , vol.29 , pp. 5442-5446
    • Gehm, B.D.1    Mc Connell, D.G.2
  • 223
    • 0026337661 scopus 로고
    • Activation of bovine rod outer segment phosphatidylinositol-4,5-bisphosphate phospholipase C by calmodulin antagonists does not depend on calmodulin
    • Gehm, B. D., R. M. Pinke, S. Laquerre, J. G. Chafouleas, D. A. Schultz, D. J. Pepperl, and D. G. McConnell. 1991. Activation of bovine rod outer segment phosphatidylinositol-4,5-bisphosphate phospholipase C by calmodulin antagonists does not depend on calmodulin. Biochemistry. 30: 11302-11306.
    • (1991) Biochemistry , vol.30 , pp. 11302-11306
    • Gehm, B.D.1    Pinke, R.M.2    Laquerre, S.3    Chafouleas, J.G.4    Schultz, D.A.5    Pepperl, D.J.6    McConnell, D.G.7
  • 224
    • 0021861729 scopus 로고
    • Light-mediated breakdown of phosphatidylinositol-4,5-bisphosphate in isolated rod outer segments of frog photoreceptor
    • Hayashi, F., and T. Amakawa. 1985. Light-mediated breakdown of phosphatidylinositol-4,5-bisphosphate in isolated rod outer segments of frog photoreceptor. Biochem. Biophys. Res. Commun. 128: 954-959.
    • (1985) Biochem. Biophys. Res. Commun , vol.128 , pp. 954-959
    • Hayashi, F.1    Amakawa, T.2
  • 225
    • 0024473629 scopus 로고
    • Regulation of phospholipase A2 and phospholipase C in rod outer segments of bovine retina involves a common GTP-binding protein but different mechanisms of action
    • Jelsema, C. L. 1989. Regulation of phospholipase A2 and phospholipase C in rod outer segments of bovine retina involves a common GTP-binding protein but different mechanisms of action. Ann. N. Y. Acad. Sci. 559: 158-177.
    • (1989) Ann. N. Y. Acad. Sci , vol.559 , pp. 158-177
    • Jelsema, C.L.1
  • 226
    • 0023929388 scopus 로고
    • Polyphosphoinositide hydrolysis in response to light stimulation of rat and chick retina and retinal rod outer segments
    • Millar, F. A., S. C. Fisher, C. A. Muir, E. Edwards, and J. N. Hawthorne. 1988. Polyphosphoinositide hydrolysis in response to light stimulation of rat and chick retina and retinal rod outer segments. Biochim. Biophys. Acta. 970: 205-211.
    • (1988) Biochim. Biophys. Acta , vol.970 , pp. 205-211
    • Millar, F.A.1    Fisher, S.C.2    Muir, C.A.3    Edwards, E.4    Hawthorne, J.N.5
  • 227
    • 0031042620 scopus 로고    scopus 로고
    • Identification of components of a phosphoinositide signaling pathway in retinal rod outer segments
    • Peng, Y. W., S. G. Rhee, W. P. Yu, Y. K. Ho, T. Schoen, G. J. Chader, and K. W. Yau. 1997. Identification of components of a phosphoinositide signaling pathway in retinal rod outer segments. Proc. Natl. Acad. Sci. USA. 94: 1995-2000.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1995-2000
    • Peng, Y.W.1    Rhee, S.G.2    Yu, W.P.3    Ho, Y.K.4    Schoen, T.5    Chader, G.J.6    Yau, K.W.7
  • 228
    • 0035901488 scopus 로고    scopus 로고
    • Regulation of type II phosphatidylinositol phosphate kinase by tyrosine phosphorylation in bovine rod outer segments
    • Huang, Z., X. X. Guo, S. X. Chen, K. M. Alvarez, M. W. Bell, and R. E. Anderson. 2001. Regulation of type II phosphatidylinositol phosphate kinase by tyrosine phosphorylation in bovine rod outer segments. Biochemistry. 40: 4550-4559.
    • (2001) Biochemistry , vol.40 , pp. 4550-4559
    • Huang, Z.1    Guo, X.X.2    Chen, S.X.3    Alvarez, K.M.4    Bell, M.W.5    Anderson, R.E.6
  • 229
    • 0021739360 scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate: Light-mediated breakdown in the vertebrate retina
    • Ghalayini, A., and R. E. Anderson. 1984. Phosphatidylinositol 4,5-bisphosphate: light-mediated breakdown in the vertebrate retina. Biochem. Biophys. Res. Commun. 124: 503-506.
    • (1984) Biochem. Biophys. Res. Commun , vol.124 , pp. 503-506
    • Ghalayini, A.1    Anderson, R.E.2
  • 230
    • 0023484050 scopus 로고
    • Phorbol ester- and light-induced endogenous phosphorylation of rat rod outer-segment proteins
    • Kapoor, C. L., P. J. O'Brien, and G. J. Chader. 1987. Phorbol ester- and light-induced endogenous phosphorylation of rat rod outer-segment proteins. Exp. Eye Res. 45: 545-556.
    • (1987) Exp. Eye Res , vol.45 , pp. 545-556
    • Kapoor, C.L.1    O'Brien, P.J.2    Chader, G.J.3
  • 231
    • 0021241334 scopus 로고
    • Endogenous phosphorylation of retinal photoreceptor outer segment proteins by calcium phospholipid-dependent protein kinase
    • Kapoor, C. L., and G. J. Chader. 1984. Endogenous phosphorylation of retinal photoreceptor outer segment proteins by calcium phospholipid-dependent protein kinase. Biochem. Biophys. Res. Commun. 122: 1397-1403.
    • (1984) Biochem. Biophys. Res. Commun , vol.122 , pp. 1397-1403
    • Kapoor, C.L.1    Chader, G.J.2
  • 233
    • 0023030791 scopus 로고
    • Phosphorylation of rhodopsin by protein kinase C in vitro
    • Kelleher, D. J., and G. L. Johnson. 1986. Phosphorylation of rhodopsin by protein kinase C in vitro. J. Biol. Chem. 261: 4749-4757.
    • (1986) J. Biol. Chem , vol.261 , pp. 4749-4757
    • Kelleher, D.J.1    Johnson, G.L.2
  • 234
    • 0027327229 scopus 로고
    • Rhodopsin is the major in situ substrate of protein kinase C in rod outer segments of photoreceptors
    • Newton, A. C., and D. S. Williams. 1993. Rhodopsin is the major in situ substrate of protein kinase C in rod outer segments of photoreceptors. J. Biol. Chem. 268: 18181-18186.
    • (1993) J. Biol. Chem , vol.268 , pp. 18181-18186
    • Newton, A.C.1    Williams, D.S.2
  • 235
    • 0030964078 scopus 로고    scopus 로고
    • Identification of protein kinase C phosphorylation sites on bovine rhodopsin
    • Greene, N. M., D. S. Williams, and A. C. Newton. 1997. Identification of protein kinase C phosphorylation sites on bovine rhodopsin. J. Biol. Chem. 272: 10341-10344.
    • (1997) J. Biol. Chem , vol.272 , pp. 10341-10344
    • Greene, N.M.1    Williams, D.S.2    Newton, A.C.3
  • 236
    • 85177001665 scopus 로고    scopus 로고
    • Greene, N. M., D. S. Williams, and A. C. Newton. 1995. Kinetics and localization of the phosphorylation of rhodopsin by protein kinase C. J. Biol. Chem. 270: 6710-6717.
    • Greene, N. M., D. S. Williams, and A. C. Newton. 1995. Kinetics and localization of the phosphorylation of rhodopsin by protein kinase C. J. Biol. Chem. 270: 6710-6717.
  • 237
  • 238
    • 0029934023 scopus 로고    scopus 로고
    • Protein kinase C in rod outer segments: Effects of phosphorylation of the phosphodiesterase inhibitory subunit
    • Udovichenko, I. P., J. Cunnick, K. Gonzalez, A. Yakhnin, and D. J. Takemoto. 1996. Protein kinase C in rod outer segments: effects of phosphorylation of the phosphodiesterase inhibitory subunit. Biochem. J. 317: 291-295.
    • (1996) Biochem. J , vol.317 , pp. 291-295
    • Udovichenko, I.P.1    Cunnick, J.2    Gonzalez, K.3    Yakhnin, A.4    Takemoto, D.J.5
  • 239
    • 85177148998 scopus 로고    scopus 로고
    • Udovichenko, I. P., J. Cunnick, K. Gonzalez, and D. J. Takemoto. 1994. Functional effect of phosphorylation of the photoreceptor phosphodiesterase inhibitory subunit by protein kinase C. J. Biol. Chem. 269: 9850-9856.
    • Udovichenko, I. P., J. Cunnick, K. Gonzalez, and D. J. Takemoto. 1994. Functional effect of phosphorylation of the photoreceptor phosphodiesterase inhibitory subunit by protein kinase C. J. Biol. Chem. 269: 9850-9856.
  • 241
    • 1542365255 scopus 로고    scopus 로고
    • Enhancement of phototransduction g protein-effector interactions by phosphoinositides
    • He, F., M. Mao, and T. G. Wensel. 2004. Enhancement of phototransduction g protein-effector interactions by phosphoinositides. J. Biol. Chem. 279: 8986-8990.
    • (2004) J. Biol. Chem , vol.279 , pp. 8986-8990
    • He, F.1    Mao, M.2    Wensel, T.G.3
  • 242
    • 34547559208 scopus 로고    scopus 로고
    • SARA-regulated vesicular targeting underlies formation of the light-sensing organelle in mammalian rods
    • Chuang, J. Z., Y. Zhao, and C. H. Sung. 2007. SARA-regulated vesicular targeting underlies formation of the light-sensing organelle in mammalian rods. Cell. 130: 535-547.
    • (2007) Cell , vol.130 , pp. 535-547
    • Chuang, J.Z.1    Zhao, Y.2    Sung, C.H.3
  • 243
    • 0038644177 scopus 로고    scopus 로고
    • Light adaptation through phosphoinositide-regulated translocation of Drosophila visual arrestin
    • Lee, S. J., H. Xu, L. W. Kang, L. M. Amzel, and C. Montell. 2003. Light adaptation through phosphoinositide-regulated translocation of Drosophila visual arrestin. Neuron. 39: 121-132.
    • (2003) Neuron , vol.39 , pp. 121-132
    • Lee, S.J.1    Xu, H.2    Kang, L.W.3    Amzel, L.M.4    Montell, C.5
  • 246
    • 0035980149 scopus 로고    scopus 로고
    • Insulin rescues retinal neurons from apoptosis by a phosphatidylinositol 3-kinase/Akt-mediated mechanism that reduces the activation of caspase-3
    • Barber, A. J., M. Nakamura, E. B. Wolpert, C. E. Reiter, G. M. Seigel, D. A. Antonetti, and T. W. Gardner. 2001. Insulin rescues retinal neurons from apoptosis by a phosphatidylinositol 3-kinase/Akt-mediated mechanism that reduces the activation of caspase-3. J. Biol. Chem. 276: 32814-32821.
    • (2001) J. Biol. Chem , vol.276 , pp. 32814-32821
    • Barber, A.J.1    Nakamura, M.2    Wolpert, E.B.3    Reiter, C.E.4    Seigel, G.M.5    Antonetti, D.A.6    Gardner, T.W.7
  • 247
    • 11144354902 scopus 로고    scopus 로고
    • Involvement of insulin/phosphoinositide 3-kinase/Akt signal pathway in 17 beta-estradiol-mediated neuroprotection
    • Yu, X., R. V. Rajala, J. F. McGinnis, F. Li, R. E. Anderson, X. Yan, S. Li, R. V. Elias, R. R. Knapp, X. Zhou, et al. 2004. Involvement of insulin/phosphoinositide 3-kinase/Akt signal pathway in 17 beta-estradiol-mediated neuroprotection. J. Biol. Chem. 279: 13086-13094.
    • (2004) J. Biol. Chem , vol.279 , pp. 13086-13094
    • Yu, X.1    Rajala, R.V.2    McGinnis, J.F.3    Li, F.4    Anderson, R.E.5    Yan, X.6    Li, S.7    Elias, R.V.8    Knapp, R.R.9    Zhou, X.10
  • 249
    • 19944367877 scopus 로고    scopus 로고
    • Substrates modified by advanced glycation end-products cause dysfunction and death in retinal pericytes by reducing survival signals mediated by platelet-derived growth factor
    • Stitt, A. W., S. J. Hughes, P. Canning, O. Lynch, O. Cox, N. Frizzell, S. R. Thorpe, T. G. Cotter, T. M. Curtis, and T. A. Gardiner. 2004. Substrates modified by advanced glycation end-products cause dysfunction and death in retinal pericytes by reducing survival signals mediated by platelet-derived growth factor. Diabetologia. 47: 1735-1746.
    • (2004) Diabetologia , vol.47 , pp. 1735-1746
    • Stitt, A.W.1    Hughes, S.J.2    Canning, P.3    Lynch, O.4    Cox, O.5    Frizzell, N.6    Thorpe, S.R.7    Cotter, T.G.8    Curtis, T.M.9    Gardiner, T.A.10
  • 250
    • 33747600101 scopus 로고    scopus 로고
    • Induction of BIM(EL) following growth factor withdrawal is a key event in caspase-dependent apoptosis of 661W photoreceptor cells
    • Gomez-Vicente, V., F. Doonan, M. Donovan, and T. G. Cotter. 2006. Induction of BIM(EL) following growth factor withdrawal is a key event in caspase-dependent apoptosis of 661W photoreceptor cells. Eur. J. Neurosci. 24: 981-990.
    • (2006) Eur. J. Neurosci , vol.24 , pp. 981-990
    • Gomez-Vicente, V.1    Doonan, F.2    Donovan, M.3    Cotter, T.G.4
  • 251
    • 30944433152 scopus 로고    scopus 로고
    • Regulated and polarized PtdIns(3,4,5)P3 accumulation is essential for apical membrane morphogenesis in photoreceptor epithelial cells
    • Pinal, N., D. C. Goberdhan, L. Collinson, Y. Fujita, I. M. Cox, C. Wilson, and F. Pichaud. 2006. Regulated and polarized PtdIns(3,4,5)P3 accumulation is essential for apical membrane morphogenesis in photoreceptor epithelial cells. Curr. Biol. 16: 140-149.
    • (2006) Curr. Biol , vol.16 , pp. 140-149
    • Pinal, N.1    Goberdhan, D.C.2    Collinson, L.3    Fujita, Y.4    Cox, I.M.5    Wilson, C.6    Pichaud, F.7
  • 252
    • 33646013922 scopus 로고    scopus 로고
    • Inactivation of the Akt survival pathway during photoreceptor apoptosis in the retinal degeneration mouse
    • Jomary, C., J. Cullen, and S. E. Jones. 2006. Inactivation of the Akt survival pathway during photoreceptor apoptosis in the retinal degeneration mouse. Invest. Ophthalmol. Vis. Sci. 47: 1620-1629.
    • (2006) Invest. Ophthalmol. Vis. Sci , vol.47 , pp. 1620-1629
    • Jomary, C.1    Cullen, J.2    Jones, S.E.3
  • 253
    • 56549104692 scopus 로고    scopus 로고
    • Retinal degeneration triggered by inactivation of PTEN in the retinal pigment epithelium
    • Kim, J. W., K. H. Kang, P. Burrola, T. W. Mak, and G. Lemke. 2008. Retinal degeneration triggered by inactivation of PTEN in the retinal pigment epithelium. Genes Dev. 22: 3147-3157.
    • (2008) Genes Dev , vol.22 , pp. 3147-3157
    • Kim, J.W.1    Kang, K.H.2    Burrola, P.3    Mak, T.W.4    Lemke, G.5
  • 256
    • 11144273817 scopus 로고    scopus 로고
    • Molecular mechanisms of light-induced photoreceptor apoptosis and neuroprotection for retinal degeneration
    • Wenzel, A., C. Grimm, M. Samardzija, and C. E. Reme. 2005. Molecular mechanisms of light-induced photoreceptor apoptosis and neuroprotection for retinal degeneration. Prog. Retin. Eye Res. 24: 275-306.
    • (2005) Prog. Retin. Eye Res , vol.24 , pp. 275-306
    • Wenzel, A.1    Grimm, C.2    Samardzija, M.3    Reme, C.E.4
  • 257
    • 0037036358 scopus 로고    scopus 로고
    • Reversible inactivation of the tumor suppressor PTEN by H2O2
    • Lee, S. R., K. S. Yang, J. Kwon, C. Lee, W. Jeong, and S. G. Rhee. 2002. Reversible inactivation of the tumor suppressor PTEN by H2O2. J. Biol. Chem. 277: 20336-20342.
    • (2002) J. Biol. Chem , vol.277 , pp. 20336-20342
    • Lee, S.R.1    Yang, K.S.2    Kwon, J.3    Lee, C.4    Jeong, W.5    Rhee, S.G.6
  • 258
    • 0142137134 scopus 로고    scopus 로고
    • Redox regulation of PI 3-kinase signalling via inactivation of PTEN
    • Leslie, N. R., D. Bennett, Y. E. Lindsay, H. Stewart, A. Gray, and C. P. Downes. 2003. Redox regulation of PI 3-kinase signalling via inactivation of PTEN. EMBO J. 22: 5501-5510.
    • (2003) EMBO J , vol.22 , pp. 5501-5510
    • Leslie, N.R.1    Bennett, D.2    Lindsay, Y.E.3    Stewart, H.4    Gray, A.5    Downes, C.P.6
  • 260
    • 42249110548 scopus 로고    scopus 로고
    • Suppressing PTEN activity by tobacco smoke plus interleukin-1beta modulates dissociation of VE-cadherin/beta-catenin complexes in endothelium
    • Barbieri, S. S., L. Ruggiero, E. Tremoli, and B. B. Weksler. 2008. Suppressing PTEN activity by tobacco smoke plus interleukin-1beta modulates dissociation of VE-cadherin/beta-catenin complexes in endothelium. Arterioscler. Thromb. Vasc. Biol. 28: 732-738.
    • (2008) Arterioscler. Thromb. Vasc. Biol , vol.28 , pp. 732-738
    • Barbieri, S.S.1    Ruggiero, L.2    Tremoli, E.3    Weksler, B.B.4
  • 261
    • 0033863553 scopus 로고    scopus 로고
    • Alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner
    • Wang, K., and A. Spector. 2000. Alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner. Eur. J. Biochem. 267: 4705-4712.
    • (2000) Eur. J. Biochem , vol.267 , pp. 4705-4712
    • Wang, K.1    Spector, A.2
  • 262
    • 2942528976 scopus 로고    scopus 로고
    • Epidermal growth factor stimulation of RPE cell survival: Contribution of phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways
    • Defoe, D. M., and R. D. Grindstaff. 2004. Epidermal growth factor stimulation of RPE cell survival: contribution of phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways. Exp. Eye Res. 79: 51-59.
    • (2004) Exp. Eye Res , vol.79 , pp. 51-59
    • Defoe, D.M.1    Grindstaff, R.D.2
  • 264
    • 0030891463 scopus 로고    scopus 로고
    • Wortmannin blocks goldfish retinal phosphatidylinositol 3-kinase and neurite outgrowth
    • Lavie, Y., J. Dybowski, and B. W. Agranoff. 1997. Wortmannin blocks goldfish retinal phosphatidylinositol 3-kinase and neurite outgrowth. Neurochem. Res. 22: 373-378.
    • (1997) Neurochem. Res , vol.22 , pp. 373-378
    • Lavie, Y.1    Dybowski, J.2    Agranoff, B.W.3
  • 265
    • 0036302389 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in the control of cell division and survival during retinal development
    • Pimentel, B., L. Rodriguez-Borlado, C. Hernandez, and A. C. Carrera. 2002. A role for phosphoinositide 3-kinase in the control of cell division and survival during retinal development. Dev. Biol. 247: 295-306.
    • (2002) Dev. Biol , vol.247 , pp. 295-306
    • Pimentel, B.1    Rodriguez-Borlado, L.2    Hernandez, C.3    Carrera, A.C.4
  • 266
    • 0042266463 scopus 로고    scopus 로고
    • Intrinsic activation of PI3K/Akt signaling pathway and its neuroprotective effect against retinal injury
    • Nakazawa, T., M. Shimura, H. Tomita, H. Akiyama, Y. Yoshioka, H. Kudou, and M. Tamai. 2003. Intrinsic activation of PI3K/Akt signaling pathway and its neuroprotective effect against retinal injury. Curr. Eye Res. 26: 55-63.
    • (2003) Curr. Eye Res , vol.26 , pp. 55-63
    • Nakazawa, T.1    Shimura, M.2    Tomita, H.3    Akiyama, H.4    Yoshioka, Y.5    Kudou, H.6    Tamai, M.7
  • 267
    • 41949089610 scopus 로고    scopus 로고
    • Differential roles of phosphatidylinositol 3-kinase/akt pathway in retinal ganglion cell survival in rats with or without acute ocular hypertension
    • Huang, Y., L. P. Cen, J. M. Luo, N. Wang, M. Z. Zhang, N. van Rooijen, C. P. Pang, and Q. Cui. 2008. Differential roles of phosphatidylinositol 3-kinase/akt pathway in retinal ganglion cell survival in rats with or without acute ocular hypertension. Neuroscience. 153: 214-225.
    • (2008) Neuroscience , vol.153 , pp. 214-225
    • Huang, Y.1    Cen, L.P.2    Luo, J.M.3    Wang, N.4    Zhang, M.Z.5    van Rooijen, N.6    Pang, C.P.7    Cui, Q.8
  • 268
    • 51349147635 scopus 로고    scopus 로고
    • Roles of PI3K and JAK pathways in viability of retinal ganglion cells after acute elevation of intraocular pressure in rats with different autoimmune backgrounds
    • Huang, Y., Z. Li, N. Wang, N. van Rooijen, and Q. Cui. 2008. Roles of PI3K and JAK pathways in viability of retinal ganglion cells after acute elevation of intraocular pressure in rats with different autoimmune backgrounds. BMC Neurosci. 9: 78.
    • (2008) BMC Neurosci , vol.9 , pp. 78
    • Huang, Y.1    Li, Z.2    Wang, N.3    van Rooijen, N.4    Cui, Q.5
  • 269
    • 59449107917 scopus 로고    scopus 로고
    • Phosphatidylinositol 3 kinase pathway and 4-hydroxy-2-nonenal-induced oxidative injury in the RPE
    • Chen, J., L. Wang, Y. Chen, P. Sternberg, and J. Cai. 2009. Phosphatidylinositol 3 kinase pathway and 4-hydroxy-2-nonenal-induced oxidative injury in the RPE. Invest. Ophthalmol. Vis. Sci. 50: 936-942.
    • (2009) Invest. Ophthalmol. Vis. Sci , vol.50 , pp. 936-942
    • Chen, J.1    Wang, L.2    Chen, Y.3    Sternberg, P.4    Cai, J.5
  • 271
    • 41549086261 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-kinase-atypical protein kinase C signaling is required for Wnt attraction and anterior-posterior axon guidance
    • Wolf, A. M., A. I. Lyuksyutova, A. G. Fenstermaker, B. Shafer, C. G. Lo, and Y. Zou. 2008. Phosphatidylinositol-3-kinase-atypical protein kinase C signaling is required for Wnt attraction and anterior-posterior axon guidance. J. Neurosci. 28: 3456-3467.
    • (2008) J. Neurosci , vol.28 , pp. 3456-3467
    • Wolf, A.M.1    Lyuksyutova, A.I.2    Fenstermaker, A.G.3    Shafer, B.4    Lo, C.G.5    Zou, Y.6
  • 272
    • 61349185130 scopus 로고    scopus 로고
    • Phosphatidylinositol 3 kinase-Akt signaling serves as a circadian output in the retina
    • Ko, M. L., K. Jian, L. Shi, and G. Y. Ko. 2009. Phosphatidylinositol 3 kinase-Akt signaling serves as a circadian output in the retina. J. Neurochem. 108: 1607-1620.
    • (2009) J. Neurochem , vol.108 , pp. 1607-1620
    • Ko, M.L.1    Jian, K.2    Shi, L.3    Ko, G.Y.4
  • 273
    • 0030207118 scopus 로고    scopus 로고
    • Signaling via the insulin-like growth factor-I receptor: Does it differ from insulin receptor signaling?
    • Blakesley, V. A., A. Scrimgeour, D. Esposito, and D. Le Roith. 1996. Signaling via the insulin-like growth factor-I receptor: does it differ from insulin receptor signaling? Cytokine Growth Factor Rev. 7: 153-159.
    • (1996) Cytokine Growth Factor Rev , vol.7 , pp. 153-159
    • Blakesley, V.A.1    Scrimgeour, A.2    Esposito, D.3    Le Roith, D.4
  • 274
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • Saltiel, A. R., and C. R. Kahn. 2001. Insulin signalling and the regulation of glucose and lipid metabolism. Nature. 414: 799-806.
    • (2001) Nature , vol.414 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 275
    • 0041743158 scopus 로고    scopus 로고
    • Knockout of insulin and IGF-1 receptors on vascular endothelial cells protects against retinal neovascularization
    • Kondo, T., D. Vicent, K. Suzuma, M. Yanagisawa, G. L. King, M. Holzenberger, and C. R. Kahn. 2003. Knockout of insulin and IGF-1 receptors on vascular endothelial cells protects against retinal neovascularization. J. Clin. Invest. 111: 1835-1842.
    • (2003) J. Clin. Invest , vol.111 , pp. 1835-1842
    • Kondo, T.1    Vicent, D.2    Suzuma, K.3    Yanagisawa, M.4    King, G.L.5    Holzenberger, M.6    Kahn, C.R.7
  • 276
    • 18844370917 scopus 로고    scopus 로고
    • Differential Akt activation in the photoreceptors of normal and rd1 mice
    • Johnson, L. E., T. van Veen, and P. A. Ekstrom. 2005. Differential Akt activation in the photoreceptors of normal and rd1 mice. Cell Tissue Res. 320: 213-222.
    • (2005) Cell Tissue Res , vol.320 , pp. 213-222
    • Johnson, L.E.1    van Veen, T.2    Ekstrom, P.A.3
  • 277
    • 61349118767 scopus 로고    scopus 로고
    • Retinal insulin receptor signaling in hyperosmotic stress
    • Rajala, R. V., I. Ivanovic, and A. K. Dilly. 2009. Retinal insulin receptor signaling in hyperosmotic stress. Vitam. Horm. 80: 583-612.
    • (2009) Vitam. Horm , vol.80 , pp. 583-612
    • Rajala, R.V.1    Ivanovic, I.2    Dilly, A.K.3
  • 278
    • 0027523157 scopus 로고
    • Li(+)-induced structural changes of synaptic ribbons are related to the phosphoinositide metabolism in photoreceptor synapses
    • Schmitz, F., and D. Drenckhahn. 1993. Li(+)-induced structural changes of synaptic ribbons are related to the phosphoinositide metabolism in photoreceptor synapses. Brain Res. 604: 142-148.
    • (1993) Brain Res , vol.604 , pp. 142-148
    • Schmitz, F.1    Drenckhahn, D.2
  • 279
    • 0017297815 scopus 로고
    • Rod outer segment disk shedding in rat retina: Relationship to cyclic lighting
    • LaVail, M. M. 1976. Rod outer segment disk shedding in rat retina: relationship to cyclic lighting. Science. 194: 1071-1074.
    • (1976) Science , vol.194 , pp. 1071-1074
    • LaVail, M.M.1
  • 280
    • 0016706352 scopus 로고
    • Membrane biosynthesis in the frog retina: Opsin transport in the photoreceptor cell
    • Papermaster, D. S., C. A. Converse, and J. Siuss. 1975. Membrane biosynthesis in the frog retina: opsin transport in the photoreceptor cell. Biochemistry. 14: 1343-1352.
    • (1975) Biochemistry , vol.14 , pp. 1343-1352
    • Papermaster, D.S.1    Converse, C.A.2    Siuss, J.3
  • 281
    • 0026769876 scopus 로고
    • Transient, cyclic changes in mouse visual cell gene products during the light-dark cycle
    • McGinnis, J. F., J. P. Whelan, and L. A. Donoso. 1992. Transient, cyclic changes in mouse visual cell gene products during the light-dark cycle. J. Neurosci. Res. 31: 584-590.
    • (1992) J. Neurosci. Res , vol.31 , pp. 584-590
    • McGinnis, J.F.1    Whelan, J.P.2    Donoso, L.A.3
  • 283
    • 0034554765 scopus 로고    scopus 로고
    • Phase shifting the retinal circadian clock: XPer2 mRNA induction by light and dopamine
    • Steenhard, B. M., and J. C. Besharse. 2000. Phase shifting the retinal circadian clock: xPer2 mRNA induction by light and dopamine. J. Neurosci. 20: 8572-8577.
    • (2000) J. Neurosci , vol.20 , pp. 8572-8577
    • Steenhard, B.M.1    Besharse, J.C.2
  • 284
    • 0035175337 scopus 로고    scopus 로고
    • Protection of photoreceptor cells in adult rats from light-induced degeneration by adaptation to bright cyclic light
    • Li, F., W. Cao, and R. E. Anderson. 2001. Protection of photoreceptor cells in adult rats from light-induced degeneration by adaptation to bright cyclic light. Exp. Eye Res. 73: 569-577.
    • (2001) Exp. Eye Res , vol.73 , pp. 569-577
    • Li, F.1    Cao, W.2    Anderson, R.E.3
  • 285
    • 0023219698 scopus 로고
    • Effect of light history on rod outer-segment membrane composition in the rat
    • Penn, J. S., and R. E. Anderson. 1987. Effect of light history on rod outer-segment membrane composition in the rat. Exp. Eye Res. 44: 767-778.
    • (1987) Exp. Eye Res , vol.44 , pp. 767-778
    • Penn, J.S.1    Anderson, R.E.2
  • 286
    • 0024556887 scopus 로고
    • Diacylglycerol kinase defect in a Drosophila retinal degeneration mutant rdgA
    • Inoue, H., T. Yoshioka, and Y. Hotta. 1989. Diacylglycerol kinase defect in a Drosophila retinal degeneration mutant rdgA. J. Biol. Chem. 264: 5996-6000.
    • (1989) J. Biol. Chem , vol.264 , pp. 5996-6000
    • Inoue, H.1    Yoshioka, T.2    Hotta, Y.3
  • 287
    • 0029001604 scopus 로고
    • Multiple subtypes of phospholipase C are encoded by the norpA gene of Drosophila melanogaster
    • Kim, S., R. R. McKay, K. Miller, and R. D. Shortridge. 1995. Multiple subtypes of phospholipase C are encoded by the norpA gene of Drosophila melanogaster. J. Biol. Chem. 270: 14376-14382.
    • (1995) J. Biol. Chem , vol.270 , pp. 14376-14382
    • Kim, S.1    McKay, R.R.2    Miller, K.3    Shortridge, R.D.4
  • 288
    • 0029035546 scopus 로고
    • Phospholipase C rescues visual defect in norpA mutant of Drosophila melanogaster
    • McKay, R. R., D. M. Chen, K. Miller, S. Kim, W. S. Stark, and R. D. Shortridge. 1995. Phospholipase C rescues visual defect in norpA mutant of Drosophila melanogaster. J. Biol. Chem. 270: 13271-13276.
    • (1995) J. Biol. Chem , vol.270 , pp. 13271-13276
    • McKay, R.R.1    Chen, D.M.2    Miller, K.3    Kim, S.4    Stark, W.S.5    Shortridge, R.D.6
  • 289
    • 0026742127 scopus 로고
    • The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase
    • Attree, O., I. M. Olivos, I. Okabe, L. C. Bailey, D. L. Nelson, R. A. Lewis, R. R. McInnes, and R. L. Nussbaum. 1992. The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature. 358: 239-242.
    • (1992) Nature , vol.358 , pp. 239-242
    • Attree, O.1    Olivos, I.M.2    Okabe, I.3    Bailey, L.C.4    Nelson, D.L.5    Lewis, R.A.6    McInnes, R.R.7    Nussbaum, R.L.8
  • 290
    • 0033574526 scopus 로고    scopus 로고
    • The role of phosphatases in inositol signaling reactions
    • Majerus, P. W., M. V. Kisseleva, and F. A. Norris. 1999. The role of phosphatases in inositol signaling reactions. J. Biol. Chem. 274: 10669-10672.
    • (1999) J. Biol. Chem , vol.274 , pp. 10669-10672
    • Majerus, P.W.1    Kisseleva, M.V.2    Norris, F.A.3
  • 291
    • 34249728994 scopus 로고    scopus 로고
    • Mutation in the PYK2-binding domain of PITPNM3 causes autosomal dominant cone dystrophy (CORD5) in two Swedish families
    • Kohn, L., K. Kadzhaev, M. S. Burstedt, S. Haraldsson, B. Hallberg, O. Sandgren, and I. Golovleva. 2007. Mutation in the PYK2-binding domain of PITPNM3 causes autosomal dominant cone dystrophy (CORD5) in two Swedish families. Eur. J. Hum. Genet. 15: 664-671.
    • (2007) Eur. J. Hum. Genet , vol.15 , pp. 664-671
    • Kohn, L.1    Kadzhaev, K.2    Burstedt, M.S.3    Haraldsson, S.4    Hallberg, B.5    Sandgren, O.6    Golovleva, I.7


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