p66Shc, a multifaceted protein linking Erk signalling, glucose metabolism, and oxidative stress

References

• Alldridge LC, Bryant CE. (2003). Annexin 1 regulates cell proliferation by disruption of cell morphology and inhibition of cyclin D1 expression through sustained activation of the ERK1/2 MAPK signal. Exp Cell Res 290:93–107.
   PubMed Web of Science ®Google Scholar
• Arany I, Faisal A, Nagamine Y, Safirstein RL. (2008). p66shc inhibits pro-survival epidermal growth factor receptor/ERK signalling during severe oxidative stress in mouse renal proximal tubule cells. J Biol Chem 283:6110–17.
   PubMed Web of Science ®Google Scholar
• Ballard VLT, Edelberg JM. (2007). Stem cells and the regeneration of the aging cardiovascular system. Circ Res 100:1116–27.
   PubMed Web of Science ®Google Scholar
• Biggs 3rd WH, Cavenee WK, Arden KC. (2001). Identification and characterization of members of the FKHR [FOXO] subclass of winged-helix transcription factors in the mouse. Mamm Genome 12:416–25.
   PubMed Web of Science ®Google Scholar
• Bonfini L, Migliaccio E, Pelicci G, Lanfrancone L, Pelicci PG. (1996). Not all Shc’s roads lead to Ras. Trends Biochem Sci 21:257–61.
   PubMed Web of Science ®Google Scholar
• Brownlee M. (2001). Biochemistry and molecular cell biology of diabetic complications. Nature 414:813–20.
   PubMed Web of Science ®Google Scholar
• Brunet A, Bonni A, Zigmond MJ, Lin MZ, Juo P, Hu LS, Anderson MJ, Arden KC, Blenis J, Greenberg ME. (1999). Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 96:857–68.
   PubMed Web of Science ®Google Scholar
• Camici GG, Cosentino F, Tanner FC, Lüscher TF. (2008). The role of p66Shc deletion in age-associated arterial dysfunction and disease states. J Appl Physiol 105:1628–631.
   PubMed Web of Science ®Google Scholar
• Carlsson C, Borg LA, Welsh N. (1999). Sodium palmitate induces partial mitochondrial uncoupling and reactive oxygen species in rat pancreatic islets in vitro. Endocrinology 140:3422–8.
   PubMed Web of Science ®Google Scholar
• Dandona P, Mohanty P, Hamouda W, Ghanim H, Aljada A, Garg R, Kumar V. (2001). Inhibitory effect of a two day fast on reactive oxygen species (ROS) generation by leucocytes and plasma ortho-tyrosine and meta-tyrosine concentrations. J Clin Endocrinol Metab 86:2899–2902.
   PubMed Web of Science ®Google Scholar
• Davol PA, Bagdasaryan R, Elfenbein GJ, Maizel AL, Frackelton AR Jr. (2003). Shc proteins are strong, independent prognostic markers for both node-negative and node-positive primary breast cancer. Cancer Res 63:6772–83.
   PubMed Web of Science ®Google Scholar
• Dijkers PF, Medema RH, Lammers JW, Koenderman L, Coffer PJ. (2000). Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1. Curr Biol 10:1201–4.
   PubMed Web of Science ®Google Scholar
• El-Shemerly MY, Besser D, Nagasawa M, Nagamine Y. (1997). 12-O- Tetradecanoylphorbol-13-acetate activates the Ras/extracellular signal-regulated kinase [ERK] signalling pathway upstream of SOS involving serine phosphorylation of Shc in NIH3T3 cells. J Biol Chemistry 272:30599–602.
   PubMed Web of Science ®Google Scholar
• Engebraaten O, Bjerkvig R, Pedersen PH, Laerum, OD. (1993). Effects of EGF, bFGF, NGF, and PDGF on cell proliferative, migratory, and invasive capacities of human brain tumour biopsies in vitro. Int J Cancer 53:209–14.
   PubMed Web of Science ®Google Scholar
• Faisal A, el-Shemerly M, Hess D, Nagamine Y. (2002). Serine/threonine phosphorylation of ShcA. Regulation of proteintyrosine phosphatase-pest binding and involvement in insulin signalling. J Biol Chem 277:30144–52.
   PubMed Web of Science ®Google Scholar
• Francia P, delli Gatti C, Bachschmid M, Martin-Padura I, Savoia C, Migliaccio E, Pelicci PG, Schiavoni M, Lüscher TF, Volpe M, et al. (2004). Deletion of p66shc gene protects against age-related endothelial dysfunction. Circulation, 110:2889–95.
   PubMed Web of Science ®Google Scholar
• Giorgio M, Migliaccio E, Orsini F, Paolucci D, Moroni M, Contursi C, Pelliccia G, Luzi L, Minucci S, Marcaccio M, et al. (2005). Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 122, 221–33.
   PubMed Web of Science ®Google Scholar
• Graiani G, Lagrasta C, Migliaccio E, Spillmann F, Meloni M, Madeddu P, Quaini F, Padura IM, Lanfrancone L, Pelicci P, et al. (2005). Genetic deletion of the p66Shc adaptor protein protects from angiotensin II-induced myocardial damage. Hypertension 46:433–40.
   PubMed Web of Science ®Google Scholar
• Gu J, Tamura M, Pankov R, Danen EH, Takino T, Matsumoto K, Yamada KM. (1999). Shc and FAK differentially regulate cell motility and directionality modulated by PTEN. J Cell Biol 146:389–403.
   PubMed Web of Science ®Google Scholar
• Holt KH, Kasson BG, Pessin JE. (1996). Insulin stimulation of a MEK- dependent but ERK-independent SOS protein kinase. Mol Cell Biol 16:577–583.
   PubMed Web of Science ®Google Scholar
• Inoue M, Sato EF, Nishikawa M, Kira Y, Imada I, Utsumi K. (2003). Mitochondrial generation of reactive oxygen species, and its role in aerobic life. Curr Med Chem 10:2495–505.
   PubMed Web of Science ®Google Scholar
• Jackson JG, Yoneda T, Clark GM, Yee D. (2000). Elevated levels of p66 Shc are found in breast cancer cell lines and primary tumors with high metastatic potential. Clin Cancer Res 6:1135–9.
   PubMed Web of Science ®Google Scholar
• Jain SK, McVie R, Duett J, Herbst JJ. (1989). Erythrocyte membrane lipid peroxidation and glycosylated hemoglobin in diabetes. Diabetes 38:1539–43.
   PubMed Web of Science ®Google Scholar
• Jain SK, Kannan K, Lim G, McVie R, Bocchini JA Jr. (2002). Hyperketonemia increases tumor necrosis factor-alpha secretion in cultured U937 monocytes and type 1 diabetic patients and is apparently mediated by oxidative stress and cAMP deficiency. Diabetes 51:2287–93.
   PubMed Web of Science ®Google Scholar
• Jain SK, Kannan K, Lim G, Matthews-Greer J, McVie R, Bocchini JA Jr. (2003). Elevated blood interleukin-6 levels in hyperketonemic type 1 diabetic patients and secretion by acetoacetate-treated cultured U937 monocytes. Diabetes Care 26:2139–43.
   PubMed Web of Science ®Google Scholar
• Kao AW, Waters SB, Okada S, Pessin JE. (1997). Insulin stimulates the phosphorylation of the 66- and 52- kilodalton Shc isoforms by distinct pathways. Endocrinology, 138:2474–80.
   PubMed Web of Science ®Google Scholar
• Kim CS, Jung SB, Naqvi A, Hoffman TA, DeRicco J, Yamamori T, Cole MP, Jeon BH, Irani K. (2008). P53 impairs endothelium-dependent vasomotor function through transcriptional upregulation of p66Shc. Circ Res 103:1441–50.
   PubMed Web of Science ®Google Scholar
• Klemke RL, Cai S, Giannini AL, Gallagher PJ, de Lanerolle P, Cheresh, DA. (1997). Regulation of cell motility by mitogen-activated protein kinase. J Cell Biol 137:481–92.
   PubMed Web of Science ®Google Scholar
• Koch OR, Fusco S, Ranieri SC, Maulucci G, Palozza P, Larocca LM, Cravero AA, Farré SM, De Spirito M, Galeotti T, et al. (2008). Role of the life span determinant P66[shcA] in ethanol-induced liver damage. Lab Invest 88:750–60.
   PubMed Web of Science ®Google Scholar
• Kops GJ, Dansen TB., Polderman PE, Saarloos I, Wirtz KW, Coffer PJ, Huang TT, Bos JL, Medema RH, Burgering BM. (2002). Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress. Nature 419:316–32.
   PubMed Web of Science ®Google Scholar
• Lai KM, Pawson T. (2000). The ShcA phosphotyrosine docking protein sensitizes cardiovascular signalling in the mouse embryo. Genes Dev 14:1132–45.
   PubMed Web of Science ®Google Scholar
• Le S, Connors TJ, Maroney AC. (2001). c-Jun N-terminal Kinase specifically phosphorylates p66 ShcA at serine 36 in response to ultraviolet irradiation. J Biol Chem 276:48332–6.
   PubMed Web of Science ®Google Scholar
• Lebiedzinska M, Duszynski J, Rizzuto R, Pinton P, Wieckowski MR. (2009). Age-related changes in levels of p66Shc and serine 36-phosphorylated p66Shc in organs and mouse tissues. Arch Biochem Biophys 486:73–80.
   Google Scholar
• Lee MS, Igawa T, Chen SJ, Van Bemmel D, Lin JS, Lin FF, Johansson SL, Christman JK, Lin MF. (2004). p66Shc protein is upregulated by steroid hormones in hormone-sensitive cancer cells and in primary prostate carcinomas. Int J Cancer, 108:672–8.
   PubMed Web of Science ®Google Scholar
• Li PF, Dietz R, von Harsdorf R. (1999). p53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by Bcl-2. EMBO J 18:6027–36.
   PubMed Web of Science ®Google Scholar
• Luzi L, Confalonieri S, Di Fiore PP, Pelicci PG. (2000). Evolution of Shc functions from nematode to human. Curr Opin Genet Dev 10:668–74.
   PubMed Web of Science ®Google Scholar
• Maytin M, Leopold J, Loscalzo J. (1999). Oxidant stress in vasculature. Curr Atheroscler Rep 1:156–64.
   PubMedGoogle Scholar
• Menini S, Amadio L, Oddi G, Ricci C, Pesce C, Pugliese F, Giorgio M, Migliaccio E, Pelicci P, Iacobini C, et al. (2006). Deletion of p66Shc longevity gene protects against experimental diabetic glomerulopathy by preventing diabetes-induced oxidative stress. Diabetes 55:1642–50.
   PubMed Web of Science ®Google Scholar
• Migliaccio E, Mele S, Salcini AE, Pelicci G, Lai KM, Superti-Furga G, Pawson T, Di Fiore PP, Lanfrancone L, Pelicci PG. (1997). Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on the EGF receptor-MAP kinase-fos signalling pathway. EMBO J 16:706–16
   PubMed Web of Science ®Google Scholar
• Migliaccio E, Giorgio M, Mele S, Pelicci G, Reboldi P, Pandolfi PP, Lanfrancone L, Pelicci, PG. (1999). The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature 402, 309–13.
   PubMed Web of Science ®Google Scholar
• Mohanty P, Hamouda W, Garg R, Aljada A, Ghanim H, Dandona P. (2000). Glucose challenge stimulates reactive oxygen species (ROS) generation by leucocytes. J Clin Endocrinol Metab 85:2970–73.
   PubMed Web of Science ®Google Scholar
• Nakamura T, Muraoka S, Sanokawa R, Mori N. (1998). N-Shc and Sck, two neuronally expressed Shc adapter homologs. Their differential regional espression in the brain and roles in neurotrophin and Src signalling. J Biol Chem 273:6960–67.
   PubMed Web of Science ®Google Scholar
• Napoli C, Martin-Padura I, de Nigris F, Giorgio M, Mansueto G, Somma P, Condorelli M, Sica G, De Rosa G, Pelicci P. (2003). Deletion of the p66Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet. Proc Natl Acad Sci USA 100:2112–16.
   PubMed Web of Science ®Google Scholar
• Natalicchio A, Laviola L, De Tullio C, Renna LA, Montrone C, Perrini S, Valenti G, Procino G, Svelto M, Giorgino F. (2004). Role of p66SHC isoform in IGF-I receptor signal through MEK/ERK and regulation of actin cytoskeleton in rat myoblasts. J Biol Chem 279:43900–9.
   PubMed Web of Science ®Google Scholar
• Natalicchio A, De Stefano F, Perrini S, Laviola L, Cignarelli A, Caccioppoli C, Quagliara A, Melchiorre M, Leonardini A, Conserva A, et al. (2009). Involvement of the p66Shc protein in glucose transport regulation in skeletal muscle myoblasts. Am J Physiol Endocrinol Metab 296:E228–37
   PubMed Web of Science ®Google Scholar
• Nemoto S, Finkel T. (2002). Redox regulation of forkhead proteins through a p66shc-dependent signalling pathway. Science 295:2450–52.
   PubMed Web of Science ®Google Scholar
• Nemoto S, Combs CA, French S, Ahn BH, Fergusson MM, Balaban RS, Finkel T. (2006). The mammalian longevity associated gene product p66shc regulates mitochondrial metabolism. J Biol Chem 281:10555–60.
   PubMed Web of Science ®Google Scholar
• Nishikawa T, Edelstein D, Brownlee M. (2000). The missing link: a single unifying mechanism for diabetic complications. Kidney Int Suppl 77:S26–30
   PubMed Web of Science ®Google Scholar
• Nolan MK, Jankowska L, Prisco M, Xu S, Guvakova MA, Surmacz E. (1997). Differential roles of IRS-1 and SHC signalling pathways in breast cancer cells. Int J Cancer 72:828–34.
   PubMed Web of Science ®Google Scholar
• Okada S, Kao AW, Ceresa BP, Blaikie P, Margolis B, Pessin JE. (1997). The 66-kDa Shc isoform is a negative regulator of the epidermal growth factor-stimulated mitogen-activated protein kinase pathway. J Biol Chem 272:28042–9.
   PubMed Web of Science ®Google Scholar
• Omata W, Shibata H, Li L, Takata K, Kojima I. (2000). Actin filaments play a critical role in insulin-induced exocytolytic recruitment but not in endocytosis of GLUT4 in isolated rat adipocyres. Biochem J 346:321–8.
   PubMed Web of Science ®Google Scholar
• Orlando MR, Laviola L, Tortosa F, Incalza MA, Melchiorre M, Leonardini A, Perrini S, Natalicchio A, Giorgino F. (2010). Inolvement of p66Shc in TNFα-induced endothelial dysfunction. Diabetes 59(Suppl 1):A241.
   Google Scholar
• Orr, WC, Sohal RS. (1994). Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science 263:1128–30.
   PubMed Web of Science ®Google Scholar
• Orsini F, Migliaccio E, Moroni M, Contursi C, Raker VA, Piccini D, Martin-Padura I, Pelliccia G, Trinei M, Bono M, et al. (2004). The life span determinant p66Shc localizes to mitochondria where it associates with mitochondrial heat shock protein 70 and regulates trans-membrane potential. J Biol Chem 279:25689–95.
   PubMed Web of Science ®Google Scholar
• Pacini S, Pellegrini M, Migliaccio E, Patrussi L, Ulivieri C, Ventura A, Carraro F, Naldini A, Lanfrancone L, Pelicci P, et al. (2004). p66SHC promotes apoptosis and antagonizes mitogenic signalling in T cells. Mol Cell Biol 24:1747–57.
   PubMed Web of Science ®Google Scholar
• Pagnin E, Fadini G, de Toni R, Tiengo A, Calò L, Avogaro A. (2005). Diabetes induces p66shc gene expression in human peripheral blood mononuclear cells: relationship to oxidative stress. J Clin Endocrinol Metab 90:1130–36.
   PubMed Web of Science ®Google Scholar
• Pelicci G, Lanfrancone L, Grignani F, McGlade J, Cavallo F, Forni G, Nicoletti I, Grignani F, Pawson T, Pelicci PG. (1992). A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell, 70:93–104.
   PubMed Web of Science ®Google Scholar
• Pelicci G, Giordano S, Zhen Z, Salcini AE, Lanfrancone L, Bardelli A, Panayotou G, Waterfield MD, Ponzetto C, Pelicci PG, et al. (1995). The motogenic and mitogenic responses to HGF are amplified by the Shc adaptor protein. Oncogene 10:1631–8.
   PubMed Web of Science ®Google Scholar
• Pelicci G, Dente L, De Giuseppe A, Verducci-Galletti B, Giuli S, Mele S, Vetriani C, Giorgio M, Pandolfi PP, Cesareni G, et al. (1996). A family of Shc related proteins with conserved PTB, CH1 and SH2 regions. Oncogene 13:633–64.
   PubMed Web of Science ®Google Scholar
• Perrini S, De Stefano F, Natalicchio A, Tortosa F, Peschechera A, Cignarelli A, Ficarella R, Melchiorre M, Losurdo F, Laviola L, et al. (2010). Genetic mutation of p66Shc protein at Ser36 prevents oxidative stress human liver cells. Diabetes 59(Suppl 1):A24.
   Google Scholar
• Pinton P, Rimessi A, Marchi S, Orsini F, Migliaccio E, Giorgio M, Contursi C, Minucci S, Mantovani F, Wieckowski MR, et al. (2007). Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc. Science 315:659–63.
   PubMed Web of Science ®Google Scholar
• Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B. (1997). A model for p53-induced apoptosis. Nature 389:300–5.
   PubMed Web of Science ®Google Scholar
• Ratner S, Patrick P, Bora G. (1992). Lymphocyte development of adherence and motility in extracellular matrix during IL-2 stimulation. The Journal of Immunology, 149, 681–88.
   PubMed Web of Science ®Google Scholar
• Ravichandran KS. (2001). Signalling via Shc family adapter proteins. Oncogene 20:6322–30.
   PubMed Web of Science ®Google Scholar
• Rescan C, Coutant A, Talarmin H, Theret N, Glaise D, Guguen-Guillouzo C, Baffet G. (2001). Mechanism in the sequential control of cell morphology and S phase entry by epidermal growth factor involves distinct MEK/ERK activations. Mol Biol Cell 12:725–38.
   PubMed Web of Science ®Google Scholar
• Sastre J, Pallardo FV, Vina J. (2003). The role of mitochondrial oxidative stress in aging. Free Radic Biol Med 35:1–8.
   PubMed Web of Science ®Google Scholar
• Schuler M, Bossy-Wetzel E, Goldstein JC, Fitzgerald P, Green DR. (2000). P53 induces apoptosis by caspase activation through mitochondrial cytochrome c release. J Biol Chem 275:7337–42.
   PubMed Web of Science ®Google Scholar
• Smith WW, Norton DD, Gorospe M, Jiang H, Nemoto S, Holbrook NJ, Finkel T, Kusiak JW. (2005). Phosphorylation of p66Shc and forkhead proteins mediates Aβ toxicity. J Cell Biol 169:331–39.
   PubMed Web of Science ®Google Scholar
• Spranger J, Kroke A, Mohlig M, Hoffmann K, Bergmann MM, Ristow M, Boeing H, Pfeiffer AF. (2003). Inflammatory cytokines and the risk to develop type 2 diabetes: results of the prospective population-based European Prospective Investigation into Cancer and Nutrition (EPIC)-Potsdam Study. Diabetes 52:812–17.
   PubMed Web of Science ®Google Scholar
• Stevenson MA, Pollock SS, Coleman CN, Calderwood SK. (1994). X-irradiation, phorbol esters, and H2O2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates. Cancer Res 54:12–15.
   PubMed Web of Science ®Google Scholar
• Stevenson LE, Frackelton AR Jr. (1998). Constitutively tyrosine phosphorylated p52 Shc in breast cancer cells:correlation with ErbB2 and p66 Shc expression. Breast Cancer Res Treat 49:119–28.
   PubMed Web of Science ®Google Scholar
• Tang ED, Nuñez G, Barr FG, Guan KL. (1999). Negative regulation of the forkhead transcription factor FKHR by Akt. J Biol Chem 274:16741–6.
   PubMed Web of Science ®Google Scholar
• Taylor WR, Greenberg AH, Turley EA, Wright JA. (1993). Cell motility, invasion, and malignancy induced by overexpression of K-FGF or bFGF. Exp Cell Res 204, 295–301.
   PubMed Web of Science ®Google Scholar
• Trinei M, Giorgio M, Cicalese A, Barozzi S, Ventura A, Migliaccio E, Milia E, Padura IM, Raker VA, Maccarana M, et al. (2002). A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis. Oncogene 21:3872–8.
   PubMed Web of Science ®Google Scholar
• Tripathy D, Mohanty P, Dhindsa S, Syed T, Ghanim H, Aljada A, Dandona P. (2003). Elevation of free fatty acids induces inflammation and impairs vascular reactivity in healthy subjects. Diabetes 52:2882–7.
   PubMed Web of Science ®Google Scholar
• Tsakiridis T, Vranic M, Klip A. (1994). Disassembly of the actin network inhibits insulin-dependent stimulation of glucose transport and prevents recruitment of glucose transporters to the plasma membrane. J Biol Chem 269:29934–42.
   PubMed Web of Science ®Google Scholar
• Veeramani S, Igawa T, Yuan TC, Lin FF, Lee MS, Lin JS, Johansson SL, Lin MF. (2005). Expression of p66 [Shc] protein correlates with proliferation of human prostate cancer cells. Oncogene 24:7203–12.
   PubMed Web of Science ®Google Scholar
• Ventura A, Luzi L, Pacini S, Baldari CT, Pelicci PG. (2002). The p66Shc longevity gene is silenced through epigenetic modifications of an alternative promoter. J Biol Chem 277:22370–76.
   PubMed Web of Science ®Google Scholar
• Ventura A, Maccarana M, Raker VA, Pelicci PG. (2004). A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria. J Biol Chem 279:2299–306.
   PubMed Web of Science ®Google Scholar
• Wang Q, Bilan PJ, Tsakiridis T, Hinek A, Klip A. (1998). Actin filament participate in the relocalization of phosphatidyl 3-kinase to glucose transporter-containing compartments and in the stimulation of glucose uptake in 3T3-L1 adipocytes. Biochem J 331:917–28.
   PubMed Web of Science ®Google Scholar
• Xi G, Shen X, Clemmons DR. (2010). p66shc inhibits insulin-like growth factor-I signalling via direct binding to Src through its polyproline and Src homology 2 domains, resulting in impairment of Src kinase activation. J Biol Chem 285:6937–51.
   PubMed Web of Science ®Google Scholar
• Xie Y, Hung MC. (1996). p66Shc isoform down-regulated and not required for HER-2/neu signalling pathway in human breast cancer cell lines with HER-2/neu overexpression. Biochem Biophys Res Comm 221:140–45.
   PubMed Web of Science ®Google Scholar
• Yamamoto Y, Yoshimasa Y, Koh M, Suga J, Masuzaki H, Ogawa Y, Hosoda K, Nishimura H, Watanabe Y, Inoue G, et al. (2000). Constitutively active mitogen-activated protein kinase kinase increases GLUT1 expressions and recruits both GLUT1 and GLUT4 at the cell surface in 3T3-L1 adipocytes. Diabetes 49:332–9.
   PubMed Web of Science ®Google Scholar
• Yang CP, Horwitz SB. (2000). Taxol mediates serine phosphorylation of the 66-kDa Shc isoform. Cancer Res 60:5171–8.
   PubMed Web of Science ®Google Scholar
• Yang CP, Horwitz SB. (2002). Distinct mechanisms of taxol-induced serine phosphorylation of the 66-kDa Shc isoform in A549 and RAW 264.7 cells. Biochim Biophys Acta 1590:76–83.
   PubMed Web of Science ®Google Scholar
• Zaccagnini G, Martelli F, Fasanaro P, Magenta A, Gaetano C, Di Carlo A, Biglioli P, Giorgio M, Martin-Padura I, et al. (2004). p66ShcA modulates tissue response to hindlimb ischemia. Circulation 109:2917–23.
   PubMed Web of Science ®Google Scholar