메뉴 건너뛰기




Volumn 2006, Issue , 2006, Pages

Cellular prion protein and caveolin-1 interaction in a neuronal cell line precedes Fyn/Erk 1/2 signal transduction

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLIN 1; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PRION PROTEIN; PRION PROTEIN ANTIBODY; PROTEIN ANTIBODY; PROTEIN KINASE FYN; UNCLASSIFIED DRUG;

EID: 33746787634     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/JBB/2006/69469     Document Type: Article
Times cited : (44)

References (54)
  • 1
    • 0036142738 scopus 로고    scopus 로고
    • Involvement of caveolae and caveolae-like domains in signalling, cell survival and angiogenesis
    • M L Massimino C Griffoni E Spisni M Toni V Tomasi Involvement of caveolae and caveolae-like domains in signalling, cell survival and angiogenesis. Cellular Signalling 14 2 2002 93 98
    • (2002) Cellular Signalling , vol.14 , Issue.2 , pp. 93-98
    • Massimino, M.L.1    Griffoni, C.2    Spisni, E.3    Toni, M.4    Tomasi, V.5
  • 2
    • 0031765341 scopus 로고    scopus 로고
    • Role of plasmalemmal caveolae in signal transduction
    • 9815100
    • P W Shaul R GW Anderson Role of plasmalemmal caveolae in signal transduction. The American Journal of Physiology 275 5 pt 1 1998 L843 L851 9815100
    • (1998) The American Journal of Physiology , vol.275 , Issue.51
    • Shaul, P.W.1    Anderson, R.G.W.2
  • 3
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons@EMBL-Heidelberg.de
    • K Simons Simons@EMBL-Heidelberg.de D Toomre Lipid rafts and signal transduction. Nature Reviews Molecular Cell Biology 1 1 2000 31 39
    • (2000) Nature Reviews Molecular Cell Biology , vol.1 , Issue.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 4
    • 0034644538 scopus 로고    scopus 로고
    • Translocation and reversible localization of signaling proteins: A dynamic future for signal transduction
    • M N Teruel T Meyer Translocation and reversible localization of signaling proteins: a dynamic future for signal transduction. Cell 103 2 2000 181 184
    • (2000) Cell , vol.103 , Issue.2 , pp. 181-184
    • Teruel, M.N.1    Meyer, T.2
  • 5
    • 0034647940 scopus 로고    scopus 로고
    • A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo
    • lisanti@aecom.yu.edu
    • A Schlegel M P Lisanti lisanti@aecom.yu.edu A molecular dissection of caveolin-1 membrane attachment and oligomerization. Two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer/oligomer interactions in vivo. Journal of Biological Chemistry 275 28 2000 21605 21617
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21605-21617
    • Schlegel, A.1    Lisanti, M.P.2
  • 6
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • S-L Shyng M T Huber D A Harris A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. Journal of Biological Chemistry 268 21 1993 15922 15928
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.21 , pp. 15922-15928
    • Shyng, S.-L.1    Huber, M.T.2    Harris, D.A.3
  • 7
    • 0034931131 scopus 로고    scopus 로고
    • Interaction of prion proteins with cell surface receptors, molecular chaperones, and other molecules
    • S Gauczynski C Hundt C Leucht S Weiss Interaction of prion proteins with cell surface receptors, molecular chaperones, and other molecules. Advances in Protein Chemistry 2001 57 229 272
    • (2001) Advances in Protein Chemistry , vol.57 , pp. 229-272
    • Gauczynski, S.1    Hundt, C.2    Leucht, C.3    Weiss, S.4
  • 8
    • 17944377091 scopus 로고    scopus 로고
    • Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor
    • C Hundt J-M Peyrin S Haik Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor. EMBO Journal 20 21 2001 5876 5886
    • (2001) EMBO Journal , vol.20 , Issue.21 , pp. 5876-5886
    • Hundt, C.1    Peyrin, J.-M.2    Haik, S.3
  • 9
    • 2142728575 scopus 로고    scopus 로고
    • The cellular prion protein: Biochemistry, topology, and physiologic functions
    • C Griffoni M Toni E Spisni The cellular prion protein: biochemistry, topology, and physiologic functions. Cell Biochemistry and Biophysics 38 3 2003 287 304
    • (2003) Cell Biochemistry and Biophysics , vol.38 , Issue.3 , pp. 287-304
    • Griffoni, C.1    Toni, M.2    Spisni, E.3
  • 11
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • N Naslavsky R Stein A Yanai G Friedlander A Taraboulos Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. Journal of Biological Chemistry 272 10 1997 6324 6331
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.10 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 12
    • 0041888516 scopus 로고    scopus 로고
    • Trafficking of prion proteins through a caveolae-mediated endosomal pathway
    • p.peters@nki.nl
    • P J Peters p.peters@nki.nl A Jr Mironov D Peretz Trafficking of prion proteins through a caveolae-mediated endosomal pathway. Journal of Cell Biology 162 4 2003 703 717
    • (2003) Journal of Cell Biology , vol.162 , Issue.4 , pp. 703-717
    • Peters, P.J.1    Mironov Jr., A.2    Peretz, D.3
  • 13
    • 0034665847 scopus 로고    scopus 로고
    • Signal transduction through prion protein
    • S Mouillet-Richard M Ermonval C Chebassier Signal transduction through prion protein. Science 289 5486 2000 1925 1928
    • (2000) Science , vol.289 , Issue.5486 , pp. 1925-1928
    • Mouillet-Richard, S.1    Ermonval, M.2    Chebassier, C.3
  • 15
    • 0034648063 scopus 로고    scopus 로고
    • Neuroprotection by MAPK/ERK kinase inhibition with U0126 against oxidative stress in a mouse neuronal cell line and rat primary cultured cortical neurons
    • namura@ri.ncvc.go.jp
    • T Satoh D Nakatsuka Y Watanabe I Nagata H Kikuchi S Namura namura@ri.ncvc.go.jp Neuroprotection by MAPK/ERK kinase inhibition with U0126 against oxidative stress in a mouse neuronal cell line and rat primary cultured cortical neurons. Neuroscience Letters 288 2 2000 163 166
    • (2000) Neuroscience Letters , vol.288 , Issue.2 , pp. 163-166
    • Satoh, T.1    Nakatsuka, D.2    Watanabe, Y.3    Nagata, I.4    Kikuchi, H.5    Namura, S.6
  • 16
    • 0027493485 scopus 로고
    • Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl- phosphatidylinositol-anchored proteins
    • A M Shenoy-Scaria L KT Gauen J Kwong A S Shaw D M Lublin Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins. Molecular and Cellular Biology 13 10 1993 6385 6392
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.10 , pp. 6385-6392
    • Shenoy-Scaria, A.M.1    Gauen, L.K.T.2    Kwong, J.3    Shaw, A.S.4    Lublin, D.M.5
  • 17
    • 0026457327 scopus 로고
    • Signal transduction through decay-accelerating factor. Interaction of glycosyl-phosphatidylinositol anchor and protein tyrosine kinases p56lck and p59fyn 1
    • 1385527
    • A M Shenoy-Scaria J Kwong T Fujita M W Olszowy A S Shaw D M Lublin Signal transduction through decay-accelerating factor. Interaction of glycosyl-phosphatidylinositol anchor and protein tyrosine kinases p56lck and p59fyn 1. Journal of Immunology 149 11 1992 3535 3541 1385527
    • (1992) Journal of Immunology , vol.149 , Issue.11 , pp. 3535-3541
    • Shenoy-Scaria, A.M.1    Kwong, J.2    Fujita, T.3    Olszowy, M.W.4    Shaw, A.S.5    Lublin, D.M.6
  • 18
    • 0025823714 scopus 로고
    • Association of the CD59 and CD55 cell surface glycoproteins with other membrane molecules
    • I Stefanova V Horejsi Association of the CD59 and CD55 cell surface glycoproteins with other membrane molecules. Journal of Immunology 147 5 1991 1587 1592
    • (1991) Journal of Immunology , vol.147 , Issue.5 , pp. 1587-1592
    • Stefanova, I.1    Horejsi, V.2
  • 19
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae
    • A M Shenoy-Scaria D J Dietzen J Kwong D C Link D M Lublin Cysteine3 of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae. Journal of Cell Biology 126 2 1994 353 363
    • (1994) Journal of Cell Biology , vol.126 , Issue.2 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 20
    • 0026637568 scopus 로고
    • Glycosyl-phosphatidylinositol anchoring of membranes proteins
    • D M Lublin Glycosyl-phosphatidylinositol anchoring of membranes proteins. Current Topics in Microbiology and Immunology 1992 178 141 162
    • (1992) Current Topics in Microbiology and Immunology , vol.178 , pp. 141-162
    • Lublin, D.M.1
  • 21
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • S Mayor K G Rothberg F R Maxfield Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science 264 5167 1994 1948 1951
    • (1994) Science , vol.264 , Issue.5167 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 23
    • 13644266312 scopus 로고    scopus 로고
    • Caveolin-1 in oncogenic transformation, cancer, and metastasis
    • lisanti@aecom.yu.edu
    • T M Williams M P Lisanti lisanti@aecom.yu.edu Caveolin-1 in oncogenic transformation, cancer, and metastasis. American Journal of Physiology - Cell Physiology 288 3 2005 C494 C506
    • (2005) American Journal of Physiology - Cell Physiology , vol.288 , Issue.3
    • Williams, T.M.1    Lisanti, M.P.2
  • 25
    • 0032577647 scopus 로고    scopus 로고
    • Caveolin-mediated regulation of signaling along the p42/44 MAP kinase cascade in vivo. a role for the caveolin-scaffolding domain
    • J A Engelman C Chu A Lin Caveolin-mediated regulation of signaling along the p42/44 MAP kinase cascade in vivo. A role for the caveolin-scaffolding domain. FEBS Letters 428 3 1998 205 211
    • (1998) FEBS Letters , vol.428 , Issue.3 , pp. 205-211
    • Engelman, J.A.1    Chu, C.2    Lin, A.3
  • 26
    • 0034617296 scopus 로고    scopus 로고
    • Caveolin-1 inhibits epidermal growth factor-stimulated lamellipod extension and cell migration in metastatic mammary adenocarcinoma cells (MTLn3). Transformation suppressor effects of adenovirus-mediated gene delivery of caveolin-1
    • W Zhang B Razani Y Altschuler Caveolin-1 inhibits epidermal growth factor-stimulated lamellipod extension and cell migration in metastatic mammary adenocarcinoma cells (MTLn3). Transformation suppressor effects of adenovirus-mediated gene delivery of caveolin-1. Journal of Biological Chemistry 275 27 2000 20717 20725
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.27 , pp. 20717-20725
    • Zhang, W.1    Razani, B.2    Altschuler, Y.3
  • 27
    • 0032538790 scopus 로고    scopus 로고
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade
    • F Galbiati D Volonte J A Engelman Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade. EMBO Journal 17 22 1998 6633 6648
    • (1998) EMBO Journal , vol.17 , Issue.22 , pp. 6633-6648
    • Galbiati, F.1    Volonte, D.2    Engelman, J.A.3
  • 28
    • 21144453387 scopus 로고    scopus 로고
    • Caveolin-3 knockout mice show increased adiposity and whole body insulin resistance, with ligand-induced insulin receptor instability in skeletal muscle
    • F Capozza T P Combs A W Cohen Caveolin-3 knockout mice show increased adiposity and whole body insulin resistance, with ligand-induced insulin receptor instability in skeletal muscle. American Journal of Physiology - Cell Physiology 288 6 2005 C1317 C1331
    • (2005) American Journal of Physiology - Cell Physiology , vol.288 , Issue.6
    • Capozza, F.1    Combs, T.P.2    Cohen, A.W.3
  • 29
    • 0037303007 scopus 로고    scopus 로고
    • Caveolin-1 null mice develop cardiac hypertrophy with hyperactivation of p42/44 MAP kinase in cardiac fibroblasts
    • A W Cohen D S Park S E Woodman Caveolin-1 null mice develop cardiac hypertrophy with hyperactivation of p42/44 MAP kinase in cardiac fibroblasts. American Journal of Physiology - Cell Physiology 284 2 2003 C457 C474
    • (2003) American Journal of Physiology - Cell Physiology , vol.284 , Issue.2
    • Cohen, A.W.1    Park, D.S.2    Woodman, S.E.3
  • 30
    • 0039252798 scopus 로고    scopus 로고
    • P42/44 MAP kinase-dependent and -independent signaling pathways regulate caveolin-1 gene expression. Activation of Ras-MAP kinase and protein kinase a signaling cascades transcriptionally down-regulates caveolin-1 promoter activity
    • lisanti@aecom.yu.edu
    • J A Engelman X L Zhang B Razani R G Pestell M P Lisanti lisanti@aecom.yu.edu p42/44 MAP kinase-dependent and -independent signaling pathways regulate caveolin-1 gene expression. Activation of Ras-MAP kinase and protein kinase A signaling cascades transcriptionally down-regulates caveolin-1 promoter activity. Journal of Biological Chemistry 274 45 1999 32333 32341
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.45 , pp. 32333-32341
    • Engelman, J.A.1    Zhang, X.L.2    Razani, B.3    Pestell, R.G.4    Lisanti, M.P.5
  • 31
    • 4944245071 scopus 로고    scopus 로고
    • Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells
    • C Monnet J Gavard R-M Mege A Sobel Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells. FEBS Letters 2004 576 1-2 114 118
    • (2004) FEBS Letters , vol.576 , Issue.1-2 , pp. 114-118
    • Monnet, C.1    Gavard, J.2    Mege, R.-M.3    Sobel, A.4
  • 33
    • 0035815709 scopus 로고    scopus 로고
    • In vivo conversion of cellular prion protein to pathogenic isoforms, as monitored by conformation-specific antibodies
    • T Yokoyama K M Kimura Y Ushiki In vivo conversion of cellular prion protein to pathogenic isoforms, as monitored by conformation-specific antibodies. Journal of Biological Chemistry 276 14 2001 11265 11271
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 11265-11271
    • Yokoyama, T.1    Kimura, K.M.2    Ushiki, Y.3
  • 35
    • 0035872246 scopus 로고    scopus 로고
    • Colocalization prostacyclin (PGI2) synthase-caveolin-1 in endothelial cells and new roles for PGI2 in angiogenesis
    • E Spisni C Griffoni S Santi Colocalization prostacyclin (PGI2) synthase-caveolin-1 in endothelial cells and new roles for PGI2 in angiogenesis. Experimental Cell Research 266 1 2001 31 43
    • (2001) Experimental Cell Research , vol.266 , Issue.1 , pp. 31-43
    • Spisni, E.1    Griffoni, C.2    Santi, S.3
  • 37
    • 0005453128 scopus 로고    scopus 로고
    • Expression of prostacyclin receptors in luteinizing hormone-releasing hormone immortalized neurons: Role in the control of hormone secretion
    • roberto.maggi@unimi.it
    • F Pimpinelli G E Rovati V Capra F Piva L Martini R Maggi roberto.maggi@unimi.it Expression of prostacyclin receptors in luteinizing hormone-releasing hormone immortalized neurons: role in the control of hormone secretion. Endocrinology 140 1 1999 171 177
    • (1999) Endocrinology , vol.140 , Issue.1 , pp. 171-177
    • Pimpinelli, F.1    Rovati, G.E.2    Capra, V.3    Piva, F.4    Martini, L.5    Maggi, R.6
  • 39
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • T Harder P Scheiffele P Verkade K Simons Lipid domain structure of the plasma membrane revealed by patching of membrane components. Journal of Cell Biology 141 4 1998 929 942
    • (1998) Journal of Cell Biology , vol.141 , Issue.4 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 40
    • 0035069622 scopus 로고    scopus 로고
    • The metabolism and imaging in live cells of the bovine prion protein in its native form or carrying single amino acid substitutions
    • A Negro C Ballarin A Bertoli M L Massimino M C Sorgato The metabolism and imaging in live cells of the bovine prion protein in its native form or carrying single amino acid substitutions. Molecular and Cellular Neuroscience 17 3 2001 521 538
    • (2001) Molecular and Cellular Neuroscience , vol.17 , Issue.3 , pp. 521-538
    • Negro, A.1    Ballarin, C.2    Bertoli, A.3    Massimino, M.L.4    Sorgato, M.C.5
  • 41
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • R Riek S Hornemann G Wider R Glockshuber K Wuthrich NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Letters 413 2 1997 282 288
    • (1997) FEBS Letters , vol.413 , Issue.2 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wuthrich, K.5
  • 42
    • 0033215478 scopus 로고    scopus 로고
    • Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel
    • R C Moore I Y Lee G L Silverman Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. Journal of Molecular Biology 292 4 1999 797 817
    • (1999) Journal of Molecular Biology , vol.292 , Issue.4 , pp. 797-817
    • Moore, R.C.1    Lee, I.Y.2    Silverman, G.L.3
  • 43
    • 0036498430 scopus 로고    scopus 로고
    • Small is not beautiful: Antagonizing functions for the prion protein PrPC and its homologue Dpl
    • A Behrens A Aguzzi Small is not beautiful: antagonizing functions for the prion protein PrPC and its homologue Dpl. Trends in Neurosciences 25 3 2002 150 154
    • (2002) Trends in Neurosciences , vol.25 , Issue.3 , pp. 150-154
    • Behrens, A.1    Aguzzi, A.2
  • 44
    • 0036694905 scopus 로고    scopus 로고
    • Sphingolipid metabolism and caveolin expression in gonadotropin-releasing hormone-expressing GN11 and gonadotropin-releasing hormone-secreting GT1-7 neuronal cells
    • S Prioni N Loberto A Prinetti Sphingolipid metabolism and caveolin expression in gonadotropin-releasing hormone-expressing GN11 and gonadotropin-releasing hormone-secreting GT1-7 neuronal cells. Neurochemical Research 27 7-8 2002 831 840
    • (2002) Neurochemical Research , vol.27 , Issue.7-8 , pp. 831-840
    • Prioni, S.1    Loberto, N.2    Prinetti, A.3
  • 45
    • 0034282872 scopus 로고    scopus 로고
    • Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein: Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to purkinje cell loss
    • G L Silverman K Qin R C Moore Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein: expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to purkinje cell loss. Journal of Biological Chemistry 275 35 2000 26834 26841
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.35 , pp. 26834-26841
    • Silverman, G.L.1    Qin, K.2    Moore, R.C.3
  • 46
    • 0033049539 scopus 로고    scopus 로고
    • A mouse prion protein transgene rescues mice deficient for the prion protein gene from Purkinje cell degeneration and demyelination
    • N Nishida P Tremblay T Sugimoto A mouse prion protein transgene rescues mice deficient for the prion protein gene from Purkinje cell degeneration and demyelination. Laboratory Investigation 79 6 1999 689 697
    • (1999) Laboratory Investigation , vol.79 , Issue.6 , pp. 689-697
    • Nishida, N.1    Tremblay, P.2    Sugimoto, T.3
  • 47
    • 0033900833 scopus 로고    scopus 로고
    • Gene expression profile in prion protein-deficient fibroblasts in culture
    • J-I Satoh Y Kuroda S Katamine Gene expression profile in prion protein-deficient fibroblasts in culture. American Journal of Pathology 157 1 2000 59 68
    • (2000) American Journal of Pathology , vol.157 , Issue.1 , pp. 59-68
    • Satoh, J.-I.1    Kuroda, Y.2    Katamine, S.3
  • 48
    • 0033566067 scopus 로고    scopus 로고
    • Prions prevent neuronal cell-line death
    • C Kuwahara A M Takeuchi T Nishimura Prions prevent neuronal cell-line death. Nature 400 6741 1999 225 226
    • (1999) Nature , vol.400 , Issue.6741 , pp. 225-226
    • Kuwahara, C.1    Takeuchi, A.M.2    Nishimura, T.3
  • 49
    • 0033179849 scopus 로고    scopus 로고
    • Membrane microdomains and caveolae
    • kurzchal@mdc-berlin.de r.parton@mailbox.uq.edu.au
    • T V Kurzchalia kurzchal@mdc-berlin.de R G Parton r.parton@mailbox.uq.edu. au Membrane microdomains and caveolae. Current Opinion in Cell Biology 11 4 1999 424 431
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.4 , pp. 424-431
    • Kurzchalia, T.V.1    Parton, R.G.2
  • 50
    • 0345257087 scopus 로고    scopus 로고
    • Specificity of insulin-like growth factor I and insulin on Shc phosphorylation and Grb2 recruitment in caveolae
    • record@unige.it
    • C Biedi D Panetta D Segat R Cordera record@unige.it D Maggi Specificity of insulin-like growth factor I and insulin on Shc phosphorylation and Grb2 recruitment in caveolae. Endocrinology 144 12 2003 5497 5503
    • (2003) Endocrinology , vol.144 , Issue.12 , pp. 5497-5503
    • Biedi, C.1    Panetta, D.2    Segat, D.3    Cordera, R.4    Maggi, D.5
  • 51
    • 1342273153 scopus 로고    scopus 로고
    • Immunoseparation of Prion protein-enriched domains from other detergent-resistant membrane fractions, isolated from neuronal cells
    • paola.palestini@unimib.it
    • L Botto M Masserini A Cassetti P Palestini paola.palestini@unimib.it Immunoseparation of Prion protein-enriched domains from other detergent-resistant membrane fractions, isolated from neuronal cells. FEBS Letters 557 1-3 2004 143 147
    • (2004) FEBS Letters , vol.557 , Issue.1-3 , pp. 143-147
    • Botto, L.1    Masserini, M.2    Cassetti, A.3    Palestini, P.4
  • 52
    • 0035848665 scopus 로고    scopus 로고
    • Differential requirements for ERK1/2 and P38 MAPK activation by thrombin in T cells. Role of P59Fyn and PKCε
    • L Maulon B Mari C Bertolotto Differential requirements for ERK1/2 and P38 MAPK activation by thrombin in T cells. Role of P59Fyn and PKCε Oncogene 20 16 2001 1964 1972
    • (2001) Oncogene , vol.20 , Issue.16 , pp. 1964-1972
    • Maulon, L.1    Mari, B.2    Bertolotto, C.3
  • 54
    • 2642549186 scopus 로고    scopus 로고
    • Combined loss of INK4a and caveolin-1 synergistically enhances cell proliferation and oncogene-induced tumorigenesis. Role of INK4a/CAV-1 in mammary epithelial cell hyperplasia
    • T M Williams H Lee M W-C Cheung Combined loss of INK4a and caveolin-1 synergistically enhances cell proliferation and oncogene-induced tumorigenesis. Role of INK4a/CAV-1 in mammary epithelial cell hyperplasia. Journal of Biological Chemistry 279 23 2004 24745 24756
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 24745-24756
    • Williams, T.M.1    Lee, H.2    Cheung, M.W.-C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.