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Volumn 9, Issue 22, 2009, Pages 5016-5028

Interactions of the NPXY microdomains of the low density lipoprotein receptor-related protein 1

Author keywords

Cell biology; Lipoprotein receptor; Phosphotyrosine; Protein interactions; Receptor tyrosine kinase; Signal transduction

Indexed keywords

ALPHA AMINO ACID; BRAIN EXTRACT; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; NPXY PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 70949087099     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900457     Document Type: Article
Times cited : (54)

References (55)
  • 1
    • 0001665337 scopus 로고
    • LRP and senile plaques in Alzheimer's disease: Colocalization with apolipoprotein e and with activated astrocytes
    • Herz, J., Hamann, U., Rogne, S., Myklebost, O. et al., LRP and senile plaques in Alzheimer's disease: colocalization with apolipoprotein E and with activated astrocytes. EMBO J. 1988, 7, 4119-4127.
    • (1988) EMBO J. , vol.7 , pp. 4119-4127
    • Herz, J.1    Hamann, U.2    Rogne, S.3    Myklebost, O.4
  • 2
    • 0141832797 scopus 로고    scopus 로고
    • Diverse role of LDL receptor-related protein in the clearance of proteases and in signalling
    • Strickland, D. A., Ranganathan, S., Diverse role of LDL receptor-related protein in the clearance of proteases and in signalling. J. Thromb. Haemost. 2003, 1, 1663-1670.
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1663-1670
    • Strickland, D.A.1    Ranganathan, S.2
  • 3
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • DOI 10.1172/JCI200113992
    • Herz, J., Strickland, D. K., LRP: a multifunctional scavenger and signaling receptor. J. Clin. Invest. 2001, 108, 779-784. (Pubitemid 32880284)
    • (2001) Journal of Clinical Investigation , vol.108 , Issue.6 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 4
    • 0026315047 scopus 로고
    • The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation
    • Bansal, A., Gierasch, L. M., The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell 1991, 67, 1195-1201. (Pubitemid 121001531)
    • (1991) Cell , vol.67 , Issue.6 , pp. 1195-1201
    • Bansal, A.1    Gierasch, L.M.2
  • 5
    • 0037023693 scopus 로고    scopus 로고
    • Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP)
    • Su, H. P., Nakada-Tsukui, K., Tosello-Trampont, A. C., Li, Y. et al., Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP). J. Biol. Chem. 2002, 277, 11772-11779.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11772-11779
    • Su, H.P.1    Nakada-Tsukui, K.2    Tosello-Trampont, A.C.3    Li, Y.4
  • 6
    • 0035374620 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated low density lipoprotein receptor-related protein 1 (LRP1) associates with the adaptor protein SHC in SRC-transformed cells
    • Barnes, H., Larsen, B., Tyers, M., van der Geer, P., Tyrosine- phosphorylated low density lipoprotein receptor-related protein 1 (LRP1) associates with the adaptor protein SHC in SRC-transformed cells. J. Biol. Chem. 2001, 276, 19119-19125.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19119-19125
    • Barnes, H.1    Larsen, B.2    Tyers, M.3    Van Der Geer, P.4
  • 8
    • 0032509346 scopus 로고    scopus 로고
    • Interactions of cytosolic adaptor proteins with neuronal apolipoprotein e receptors and the amyloid precursor protein
    • Trommsdorff, M., Borg, J. P., Margolis, B., Herz, J., Interactions of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J. Biol. Chem. 1998, 273, 1031-1039.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1031-1039
    • Trommsdorff, M.1    Borg, J.P.2    Margolis, B.3    Herz, J.4
  • 9
    • 0034682827 scopus 로고    scopus 로고
    • Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction
    • DOI 10.1074/jbc.M000955200
    • Gotthardt, M., Trommsdorff, M., Nevitt, M. F., Shelton, J. et al., Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. J. Biol. Chem. 2000, 275, 25616-25624. (Pubitemid 30687066)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.33 , pp. 25616-25624
    • Gotthardt, M.1    Trommsdorff, M.2    Nevitt, M.F.3    Shelton, J.4    Richardson, J.A.5    Stockinger, W.6    Nimpf, J.7    Herz, J.8
  • 10
    • 33847019563 scopus 로고    scopus 로고
    • Multiplicity of the interactions of Wnt proteins and their receptors
    • DOI 10.1016/j.cellsig.2006.11.001, PII S0898656806002956
    • Kikuchi, A., Yamamoto, H., Kishida, S., Multiplicity of the interactions of Wnt proteins and their receptors. Cell Signal. 2007, 19, 659-671. (Pubitemid 46275377)
    • (2007) Cellular Signalling , vol.19 , Issue.4 , pp. 659-671
    • Kikuchi, A.1    Yamamoto, H.2    Kishida, S.3
  • 11
    • 0037013188 scopus 로고    scopus 로고
    • Platelet-derived growth factor mediates tyrosine phosphorylation of the cytoplasmic domain of the low density lipoprotein receptor-related protein in caveolae
    • DOI 10.1074/jbc.M200428200
    • Boucher, P., Liu, P., Gotthardt, M., Hiesberger, T. et al., Platelet-derived growth factor mediates tyrosine phosphorylation of the cytoplasmic domain of the low Density lipoprotein receptor-related protein in caveolae. J. Biol. Chem. 2002, 277, 15507-15513. (Pubitemid 34967817)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15507-15513
    • Boucher, P.1    Liu, P.2    Gotthardt, M.3    Hiesberger, T.4    Anderson, R.G.W.5    Herz, J.6
  • 12
    • 0030032062 scopus 로고    scopus 로고
    • Identification of residues that control specific binding of the Shc phosphotyrosine-binding domain to phosphotyrosine sites
    • van der Geer, P., Wiley, S., Gish, G. D., Lai, V. K. et al., Identification of residues that control specific binding of the Shc phosphotyrosine-binding domain to phosphotyrosine sites. Proc. Natl. Acad. Sci. USA 1996, 93, 963-968.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 963-968
    • Van Der Geer, P.1    Wiley, S.2    Gish, G.D.3    Lai, V.K.4
  • 13
    • 47049086608 scopus 로고    scopus 로고
    • Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain
    • Betts, G. N., van der Geer, P., Komives, E. A., Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain. J. Biol. Chem. 2008, 283, 15656-15664.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15656-15664
    • Betts, G.N.1    Van Der Geer, P.2    Komives, E.A.3
  • 14
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A., Washburn, M. P., Yates, J. R. r., An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 2001, 73, 5683-5690.
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates, J.R.R.3
  • 15
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm, a next generation search engine that uses sequence temperature values sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • DOI 10.1074/mcp.T600050-MCP200
    • Shilov, I. V., Seymour, S. L., Patel, A. A., Loboda, A. et al., The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 2007, 6, 1638-1655. (Pubitemid 47506173)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.9 , pp. 1638-1655
    • Shilov, I.V.1    Seymourt, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 16
    • 23944526367 scopus 로고    scopus 로고
    • PRIDE: The proteomics identifications database
    • Martens, L., Hermjakob, H., Jones, P., Adamski, M. et al., PRIDE: the proteomics identifications database. Proteomics 2005, 5, 3537-3545.
    • (2005) Proteomics , vol.5 , pp. 3537-3545
    • Martens, L.1    Hermjakob, H.2    Jones, P.3    Adamski, M.4
  • 18
    • 0033051907 scopus 로고    scopus 로고
    • The measurement of ubiquitin and ubiquitinated proteins
    • Mimnaugh, E. G., Bonvini, P., Neckers, L., The measurement of ubiquitin and ubiquitinated proteins. Electrophoresis 1999, 20, 418-428.
    • (1999) Electrophoresis , vol.20 , pp. 418-428
    • Mimnaugh, E.G.1    Bonvini, P.2    Neckers, L.3
  • 19
    • 0037784051 scopus 로고    scopus 로고
    • V-Src induces Shc binding to tyrosine 63 in the cytoplasmic domain of the LDL receptor-related protein 1
    • DOI 10.1038/sj.onc.1206504
    • Barnes, H., Ackermann, E. J., van der Geer, P., v-Src induces Shc binding to tyrosine 63 in the cytoplasmic domain of the LDL receptor-related protein 1. Oncogene 2003, 22, 3589-3597. (Pubitemid 36765318)
    • (2003) Oncogene , vol.22 , Issue.23 , pp. 3589-3597
    • Barnes, H.1    Ackermann, E.J.2    Van Der Geer, P.3
  • 20
    • 18544378303 scopus 로고    scopus 로고
    • Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptor function betwenn LRP and the PDGF
    • Loukinova, E., Ranganathan, S., Kuznetsov, S., Gorlatova, N. et al., Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptor function betwenn LRP and the PDGF. J. Biol. Chem. 2002, 277, 15499-15506.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15499-15506
    • Loukinova, E.1    Ranganathan, S.2    Kuznetsov, S.3    Gorlatova, N.4
  • 21
    • 2442498577 scopus 로고    scopus 로고
    • FE65 constitutes the functional link between the low-density lipoprotein receptor-related protein and the amyloid precursor protein
    • Pietrzik, C. U., Yoon, I. S., Jaeger, S., Busse, T. et al., FE65 constitutes the functional link between the low-density lipoprotein receptor-related protein and the amyloid precursor protein. J. Neurosci. 2004, 4259-4265.
    • (2004) J. Neurosci. , pp. 4259-4265
    • Pietrzik, C.U.1    Yoon, I.S.2    Jaeger, S.3    Busse, T.4
  • 23
    • 23044469458 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor-beta (PDGFR-beta) activation promotes its association with the low density lipoprotein receptor-related protein (LRP). Evidence for co-receptor function
    • Newton, C. S., Loukinova, E., Mikhailenko, I., Ranganathan, S. et al., Platelet-derived growth factor receptor-beta (PDGFR-beta) activation promotes its association with the low density lipoprotein receptor-related protein (LRP). Evidence for co-receptor function. J. Biol. Chem. 2005, 280, 27872-27878.
    • (2005) J. Biol. Chem. , vol.280 , pp. 27872-27878
    • Newton, C.S.1    Loukinova, E.2    Mikhailenko, I.3    Ranganathan, S.4
  • 24
    • 28044434891 scopus 로고    scopus 로고
    • The low-density lipoprotein receptor-related protein-1 associates transiently with lipid rafts
    • DOI 10.1002/jcb.20596
    • Wu, L., Gonias, S. L., The low-density lipoprotein receptor-related protein-1 associates transiently with lipid rafts. J. Cell. Biochem. 2005, 96, 1021-1033. (Pubitemid 41688726)
    • (2005) Journal of Cellular Biochemistry , vol.96 , Issue.5 , pp. 1021-1033
    • Wu, L.1    Gonias, S.L.2
  • 25
    • 5644245275 scopus 로고    scopus 로고
    • Purification and identification of protein-tyrosine kinase-binding proteins using synthetic phosphopeptides as affinity reagents
    • DOI 10.1074/mcp.M400062-MCP200
    • Wilhelmsen, K. J. C., Glenn, G., Hoffman, R. C. et al., Purification and identification of protein-tyrosine kinase-binding proteins using synthetic phosphopeptides as affinity reagents. Mol. Cell. Proteomics. 2004, 3, 887-895. (Pubitemid 39369201)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.9 , pp. 887-895
    • Wilhelmsen, K.1    Copp, J.2    Glenn, G.3    Hoffman, R.C.4    Tucker, P.5    Van Der Geer, P.6
  • 26
    • 33750987920 scopus 로고    scopus 로고
    • Screening for PTB domain binding partners and ligand specificity using proteome-derived NPXY peptide arrays
    • DOI 10.1128/MCB.01491-06
    • Smith, M. J., Hardy, W. R., Murphy, J. M., Jones, N., Pawson, T., Screening for PTB domain binding partners and ligand specificity using proteome-derived NPXY peptide arrays. Mol. Cell. Biol. 2006, 26, 8461-8474. (Pubitemid 44748579)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.22 , pp. 8461-8474
    • Smith, M.J.1    Hardy, W.R.2    Murphy, J.M.3    Jones, N.4    Pawson, T.5
  • 27
    • 0025681492 scopus 로고
    • g1, GAP, and Src to activated growth factor receptors
    • Anderson, D., Koch, C. A., Grey, L., Ellis, C. et al., Binding of SH2 domains of phospholipase Cg1, GAP, and Src to activated growth factor receptors. Science 1990, 250, 979-982. (Pubitemid 120031802)
    • (1990) Science , vol.250 , Issue.4983 , pp. 979-982
    • Anderson, D.1    Koch, C.A.2    Grey, L.3    Ellis, C.4    Moran, M.F.5    Pawson, T.6
  • 28
    • 0026664293 scopus 로고
    • GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor b subunit
    • Kazlauskas, A., Kashishian, A., Cooper, J. A., Valius, M., GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor b subunit. Mol. Cell. Biol. 1992, 12, 2534-2544.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2534-2544
    • Kazlauskas, A.1    Kashishian, A.2    Cooper, J.A.3    Valius, M.4
  • 29
    • 0032544418 scopus 로고    scopus 로고
    • Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling
    • Keilhack, H., Tenev, T., Nyakatura, E., Godovac-Zimmermann, J. et al., Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling. J. Biol. Chem. 1998, 273, 24839-24846.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24839-24846
    • Keilhack, H.1    Tenev, T.2    Nyakatura, E.3    Godovac-Zimmermann, J.4
  • 30
    • 0031924794 scopus 로고    scopus 로고
    • SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain
    • Kozlowski, M., Larose, L., Lee, F., Le, D. M. et al., SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain. Mol. Cell. Biol. 1998, 18, 2089-2099. (Pubitemid 28152658)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.4 , pp. 2089-2099
    • Kozlowski, M.1    Larose, L.2    Lee, F.3    Le, D.M.4    Rottapel, R.5    Siminovitch, K.A.6
  • 31
    • 0033600129 scopus 로고    scopus 로고
    • SHP-2 binds to Tyr763 and Tyr1009 in the PDGF beta-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis
    • DOI 10.1038/sj.onc.1202705
    • Ronnstrand, L., Arvidsson, A. K., Kallin, A., Rorsman, C. et al., SHP-2 binds to Tyr763 and Tyr1009 in the PDGF beta-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis. Oncogene 1999, 18, 3696-3702. (Pubitemid 29338502)
    • (1999) Oncogene , vol.18 , Issue.25 , pp. 3696-3702
    • Ronnstrand, L.1    Arvidsson, A.-K.2    Kallin, A.3    Rorsman, C.4    Hellman, U.5    Engstrom, U.6    Wernstedt, C.7    Heldin, C.-H.8
  • 32
    • 0026668932 scopus 로고
    • Association of Fyn with the actvated platelet-derived growth factor receptor: Requirements for binding and phosphorylation
    • Twamley, G. M., Kypta, R. M., Hall, B., Courtneidge, S. A., Association of Fyn with the actvated platelet-derived growth factor receptor: requirements for binding and phosphorylation. Oncogene 1992, 7, 1893-1901.
    • (1992) Oncogene , vol.7 , pp. 1893-1901
    • Twamley, G.M.1    Kypta, R.M.2    Hall, B.3    Courtneidge, S.A.4
  • 33
    • 0037135603 scopus 로고    scopus 로고
    • ShcB and ShcC activation by the Trk family of receptor tyrosine kinases
    • DOI 10.1074/jbc.M111659200
    • Liu, H. Y., Meakin, S. O., ShcB and ShcC activation by the Trk family of receptor tyrosine kinases. J. Biol. Chem. 2002, 277, 26046-26056. (Pubitemid 34967087)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 26046-26056
    • Liu, H.-Y.1    Meakin, S.O.2
  • 34
    • 0034646610 scopus 로고    scopus 로고
    • Signaling of hepatocyte growth factor/scatter factor (HGF) to the small GTPase Rap1 via the large docking protein Gab1 and the adapter protein CRKL
    • DOI 10.1074/jbc.275.15.10772
    • Sakkab, D., Lewitzky, M., Posern, G., Schaeper, U. et al., Signaling of hepatocyte growth factor/scatter factor (HGF) to the small GTPase Rap1 via the large docking protein Gab1 and the adapter protein CRKL. J. Biol. Chem. 2000, 275, 10772-10778. (Pubitemid 30212706)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 10772-10778
    • Sakkab, D.1    Lewitzky, M.2    Posern, G.3    Schaeper, U.4    Sachs, M.5    Birchmeier, W.6    Feller, S.M.7
  • 35
    • 0029961705 scopus 로고    scopus 로고
    • A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain
    • O'Bryan, J. P., Songyang, Z., Cantley, L., Der, C. J., Pawson, T., A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine- binding domains is related to Shc and is specifically expressed in the brain. Proc. Natl. Acad. Sci. USA 1996, 93, 2729-2734.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2729-2734
    • O'Bryan, J.P.1    Songyang, Z.2    Cantley, L.3    Der, C.J.4    Pawson, T.5
  • 36
    • 18844363974 scopus 로고    scopus 로고
    • Comparative expression profiles of ShcB and ShcC phosphotyrosine adapter molecules in the adult brain
    • DOI 10.1016/j.neuroscience.2005.02.014, PII S0306452205002198
    • Ponti, G., Conti, L., Cataudella, T., Zuccato, C. et al., Comparative expression profiles of ShcB and ShcC phosphotyrosine adapter molecules in the adult brain. Neuroscience 2005, 133, 105-115. (Pubitemid 40694162)
    • (2005) Neuroscience , vol.133 , Issue.1 , pp. 105-115
    • Ponti, G.1    Conti, L.2    Cataudella, T.3    Zuccato, C.4    Magrassi, L.5    Rossi, F.6    Bonfanti, L.7    Cattaneo, E.8
  • 37
    • 0028773467 scopus 로고
    • Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase
    • DOI 10.1016/S0969-2126(00)00044-7
    • Lee, C. H., Kominos, D., Jacques, S., Margolis, B. et al., Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase. Structure 1994, 2, 423-438. (Pubitemid 2085245)
    • (1994) Structure , vol.2 , Issue.5 , pp. 423-438
    • Lee Chi, H.1    Kominos, D.2    Jacques, S.3    Margolis, B.4    Schlessinger, J.5    Shoelson, S.E.6    Kuriyan, J.7
  • 38
    • 23044455604 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor beta (PDGFR beta)
    • DOI 10.1074/jbc.M410265200
    • Takayama, Y., May, P., Anderson, R. G., Herz, J., Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor beta (PDGFR beta). J. Biol. Chem. 2005, 280, 18504-18510. (Pubitemid 41389100)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 18504-18510
    • Takayama, Y.1    May, P.2    Anderson, R.G.W.3    Herz, J.4
  • 39
    • 0029128232 scopus 로고
    • LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted beta-amyloid precursor protein and mediates its degradation
    • Kounnas, M. Z., Moir, R. D., Rebeck, G. W., Bush, A. I. et al., LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted beta-amyloid precursor protein and mediates its degradation. Cell 1995, 82, 331-340.
    • (1995) Cell , vol.82 , pp. 331-340
    • Kounnas, M.Z.1    Moir, R.D.2    Rebeck, G.W.3    Bush, A.I.4
  • 42
    • 0030752288 scopus 로고    scopus 로고
    • Genetic association of the low-density lipoprotein receptor-related protein gene (LRP), an apolipoprotein e receptor, with late-onset Alzheimer's disease
    • Kang, D. E., Saitoh, T., Chen, X., Xia, Y. et al., Genetic association of the low-density lipoprotein receptor-related protein gene (LRP), an apolipoprotein E receptor, with late-onset Alzheimer's disease. Neurology 1997, 49, 56-61. (Pubitemid 27328682)
    • (1997) Neurology , vol.49 , Issue.1 , pp. 56-61
    • Kang, D.E.1    Saitoh, T.2    Chen, X.3    Xia, Y.4    Masliah, E.5    Hansen, L.A.6    Thomas, R.G.7    Thal, L.J.8    Katzman, R.9
  • 44
    • 0036846405 scopus 로고    scopus 로고
    • The cytoplasmic domain of the LDL receptor-related protein regulates multiple steps in APP processing
    • DOI 10.1093/emboj/cdf568
    • Pietrzik, C. U., Busse, T., Merriam, D. E., Weggen, S., Koo, E. H., The cytoplasmic domain of the LDL receptor-related protein regulates multible steps in APP processing. EMBO J. 2002, 21, 5691-5700. (Pubitemid 35315269)
    • (2002) EMBO Journal , vol.21 , Issue.21 , pp. 5691-5700
    • Pietrzik, C.U.1    Busse, T.2    Merriam, D.E.3    Weggen, S.4    Koo, E.H.5
  • 45
    • 21244506747 scopus 로고    scopus 로고
    • Sequences from the low density lipoprotein receptor-related protein (LRP) cytoplasmic domain enhance amyloid {beta} protein production via the {beta}-secretase pathway without altering amyloid precursor protein/LRP nuclear signaling
    • Yoon, I.-S., Pietrzik, C. U., Kang, D. E., Koo, E. H., Sequences from the low density lipoprotein receptor-related protein (LRP) cytoplasmic domain enhance amyloid {beta} protein production via the {beta}-secretase pathway without altering amyloid precursor protein/LRP nuclear signaling. J. Biol. Chem. 2005, 280, 20140-20147.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20140-20147
    • Yoon, I.-S.1    Pietrzik, C.U.2    Kang, D.E.3    Koo, E.H.4
  • 46
    • 33947529531 scopus 로고    scopus 로고
    • RNA interference silencing of the adaptor molecules ShcC and Fe65 differentially affect amyloid precursor protein processing and Abeta generation
    • DOI 10.1074/jbc.M609293200
    • Xie, Z., Dong, Y., Maeda, U., Xia, W., Tanzi, R. E., RNA interference silencing of the adaptor molecules ShcC and Fe65 differentially affect amyloid precursor protein processing and Abeta generation. J. Biol. Chem. 2007, 282, 4318-4325. (Pubitemid 47100999)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 4318-4325
    • Xie, Z.1    Dong, Y.2    Maeda, U.3    Xia, W.4    Tanzi, R.E.5
  • 47
    • 0037053281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc
    • DOI 10.1074/jbc.M110286200
    • Tarr, P. E., Roncarati, R., Pelicci, G., Pelicci, P. G., D'Adamio, L., Tyrosine Phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc. J. Biol. Chem. 2002, 277, 16798-16804. (Pubitemid 34967702)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16798-16804
    • Tarr, P.E.1    Roncarati, R.2    Pelicci, G.3    Pelicci, P.G.4    D'Adamio, L.5
  • 48
    • 34347251931 scopus 로고    scopus 로고
    • Receptor- And non-receptor tyrosine kinases induce processing of the amyloid precursor protein: Role of the low-density lipoprotein receptor-related protein
    • DOI 10.1159/000101833
    • Minopoli, G., Passaro, F., Aloia, L., Carlomagno, F. et al., Receptor- and non-receptor tyrosine kinases induce processing of the amyloid precursor protein: role of the low-density lipoprotein receptor-related protein. Neurodegener. Dis. 2007, 4, 94-100. (Pubitemid 47000402)
    • (2007) Neurodegenerative Diseases , vol.4 , Issue.2-3 , pp. 94-100
    • Minopoli, G.1    Passaro, F.2    Aloia, L.3    Carlomagno, F.4    Melillo, R.M.5    Santoro, M.6    Forzati, F.7    Zambrano, N.8    Russo, T.9
  • 49
    • 33748319508 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy (FLIM) detects stimulus-dependent phosphorylation of the low density lipoprotein receptor-related protein (LRP) in primary neurons
    • DOI 10.1016/j.bbrc.2006.07.212, PII S0006291X06016470
    • Peltan, I. D., Thomas, A. V., Mikhailenko, I., Strickland, D. K. et al., Fluorescence lifetime imaging microscopy (FLIM) detects stimulus-dependent phosphorylation of the low density lipoprotein receptor-related protein (LRP) in primary neurons. Biochem. Biophys. Res. Commun. 2006, 349, 24-30. (Pubitemid 44331759)
    • (2006) Biochemical and Biophysical Research Communications , vol.349 , Issue.1 , pp. 24-30
    • Peltan, I.D.1    Thomas, A.V.2    Mikhailenko, I.3    Strickland, D.K.4    Hyman, B.T.5    Von Arnim, C.A.F.6
  • 50
    • 29644441522 scopus 로고    scopus 로고
    • Role of 14-3-3{gamma} in FE65-dependent gene transactivation mediated by the amyloid {beta}-protein precursor cytoplasmic fragment
    • DOI 10.1074/jbc.M504278200
    • Sumioka, A., Nagaishi, S., Yoshida, T., Lin, A. et al., Role of 14-3-3{gamma} in FE65-dependent gene transactivation mediated by the amyloid { beta} -protein precursor cytoplasmic fragment 10.1074/jbc.M504278200. J. Biol. Chem. 2005, 280, 42364-42374. (Pubitemid 43023208)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.51 , pp. 42364-42374
    • Sumioka, A.1    Nagaishi, S.2    Yoshida, T.3    Lin, A.4    Miura, M.5    Suzuki, T.6
  • 51
    • 33845425431 scopus 로고    scopus 로고
    • Regulation of phosphorylation of tau by protein kinases in rat brain
    • DOI 10.1007/s11064-006-9205-9
    • Sengupta, A., Grundke-Iqbal, I., Iqbal, K., Regulation of phosphorylation of tau by protein kinases in rat brain. Neurochem. Res. 2006, 31, 1473-1480. (Pubitemid 44900588)
    • (2006) Neurochemical Research , vol.31 , Issue.12 , pp. 1473-1480
    • Sengupta, A.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 52
    • 0036919644 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II in its tubulin binding sites
    • DOI 10.1016/S0003-9861(02)00556-8, PII S0003986102005568
    • Yamamoto, H., Yamauchi, E., Taniguchi, H., Ono, T., Miyamoto, E., Phosphorylation of microtubule-associated protein tau by Ca21/calmodulin- dependent protein kinase II in its tubulin binding sites. Arch. Biochem. Biophys. 2002, 408, 255-262. (Pubitemid 36027047)
    • (2002) Archives of Biochemistry and Biophysics , vol.408 , Issue.2 , pp. 255-262
    • Yamamoto, H.1    Yamauchi, E.2    Taniguchi, H.3    Ono, T.4    Miyamoto, E.5


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