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Volumn 4, Issue 4, 2013, Pages

NMDA receptor subunit composition determines beta-amyloid-induced neurodegeneration and synaptic loss

Author keywords

A ; Amyloid beta; Dendritic spine; Neurodegeneration; NMDA receptor; Tau

Indexed keywords

AMYLOID BETA PROTEIN; CASPASE 3; GLYCOGEN SYNTHASE KINASE 3BETA; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; TAU PROTEIN;

EID: 84876903457     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2013.129     Document Type: Article
Times cited : (107)

References (53)
  • 2
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: Vell biological roles of proteasome activators and inhibitors
    • Rechsteiner M, Hill CP. Mobilizing the proteolytic machine: Vell biological roles of proteasome activators and inhibitors. Trends Cell Biol 2005; 15: 27-33.
    • (2005) Trends Cell Biol , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 3
    • 70350150000 scopus 로고    scopus 로고
    • The emergin complexity of protein ubiquitination
    • Komander D. The emergin complexity of protein ubiquitination. Biochem Soc Trans 2009; 37: 937-953.
    • (2009) Biochem Soc Trans , vol.37 , pp. 937-953
    • Komander, D.1
  • 4
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Gaczynska M, Rock KL, Goldberg AL. Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 1993; 365: 264-267.
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 6
    • 0035070697 scopus 로고    scopus 로고
    • Regulation of proteasome complexes by gamma-interferon and phosphorylation
    • Rivett AJ, Bose S, Brooks P, Broadfoot KI. Regulation of proteasome complexes by gamma-interferon and phosphorylation. Biochimie 2001; 83: 363-366.
    • (2001) Biochimie , vol.83 , pp. 363-366
    • Rivett, A.J.1    Bose, S.2    Brooks, P.3    Broadfoot, K.I.4
  • 7
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451: 1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 8
    • 79551609332 scopus 로고    scopus 로고
    • BAG3 mediates chaperonebased aggresome-targeting and selective autophagy of misfolded proteins
    • Gamerdinger M, Kaya AM, Wolfrum U, Clement AM, Behl C. BAG3 mediates chaperonebased aggresome-targeting and selective autophagy of misfolded proteins. EMBO rep 2011; 12: 149-156.
    • (2011) EMBO Rep , vol.12 , pp. 149-156
    • Gamerdinger, M.1    Kaya, A.M.2    Wolfrum, U.3    Clement, A.M.4    Behl, C.5
  • 9
    • 65449117176 scopus 로고    scopus 로고
    • Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
    • Gamerdinger M, Hajieva P, Kaya AM, Wolfrum U, Hart FU, Behl C. Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3. EMBO J 2009; 28: 889-901.
    • (2009) EMBO J , vol.28 , pp. 889-901
    • Gamerdinger, M.1    Hajieva, P.2    Kaya, A.M.3    Wolfrum, U.4    Hart, F.U.5    Behl, C.6
  • 10
    • 0034790768 scopus 로고    scopus 로고
    • Molecular chaperone targeting and regulation by BAG family proteins
    • Takayama S, Reed JC. Molecular chaperone targeting and regulation by BAG family proteins. Nat Cell Biol 2001; 3: E237-E241.
    • (2001) Nat Cell Biol , vol.3
    • Takayama, S.1    Reed, J.C.2
  • 11
    • 79959939343 scopus 로고    scopus 로고
    • BAG3 and friends: Vo-chaperones in selective autophagy during aging and disease
    • Behl C. BAG3 and friends: Vo-chaperones in selective autophagy during aging and disease. Autophagy 2011; 7: 795-798.
    • (2011) Autophagy , vol.7 , pp. 795-798
    • Behl, C.1
  • 12
    • 0031466639 scopus 로고    scopus 로고
    • Mammalian cells express two 28. differently localized Bag-1 isoforms generated by alternative translation initiation
    • Packham G, Brinimeli M, Cleveland JL. Mammalian cells express two 28. differently localized Bag-1 isoforms generated by alternative translation initiation. Biochem J 1997; 328: 807-813.
    • (1997) Biochem J , vol.328 , pp. 807-813
    • Packham, G.1    Brinimeli, M.2    Cleveland, J.L.3
  • 13
    • 9644262422 scopus 로고    scopus 로고
    • Inhibitors of the eukaryotic 20S proteasome core particle: A structural approach
    • Groll M, Huber R. Inhibitors of the eukaryotic 20S proteasome core particle: A structural approach. Biochim Biophys Acta 2004; 1695: 33-44.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 33-44
    • Groll, M.1    Huber, R.2
  • 14
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtininduced cell death
    • Bjørkøy G, Lamark T, Brech A, Outzen H, Perander M, Øvervatn A et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtininduced cell death. J Cell Biol 2005; 171: 603-614.
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Øvervatn, A.6
  • 15
    • 34248583762 scopus 로고    scopus 로고
    • Methods for monitoring autophagy from yeast to human
    • Klionsky DJ, Cuervo AM, Seglen PO. Methods for monitoring autophagy from yeast to human. Autophagy 2007; 3: 181-206.
    • (2007) Autophagy , vol.3 , pp. 181-206
    • Klionsky, D.J.1    Cuervo, A.M.2    Seglen, P.O.3
  • 16
    • 34548259958 scopus 로고    scopus 로고
    • P62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • Pankiv S, Hoyvarde Clausen T, Lamark T, Brech A, Bruun JA et al. p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J Biol Chem 2007; 282: 24131-24145.
    • (2007) J Biol Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Hoyvarde Clausen, T.2    Lamark, T.3    Brech, A.4    Bruun, J.A.5
  • 17
    • 38349114036 scopus 로고    scopus 로고
    • Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases
    • Tan JM, Wong ES, Kirkpatrick DS, Pletnikova O, Ko HS, Tay SP et al. Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum Mol Genet 2008; 17: 431-439.
    • (2008) Hum Mol Genet , vol.17 , pp. 431-439
    • Tan, J.M.1    Wong, E.S.2    Kirkpatrick, D.S.3    Pletnikova, O.4    Ko, H.S.5    Tay, S.P.6
  • 18
    • 79955978424 scopus 로고    scopus 로고
    • K63-linked ubiquitination and neurodegeneration
    • Lim KL, Lim GG. K63-linked ubiquitination and neurodegeneration. Neurobiol Dis 2011; 43: 9-16.
    • (2011) Neurobiol Dis , vol.43 , pp. 9-16
    • Lim, K.L.1    Lim, G.G.2
  • 19
    • 77951200644 scopus 로고    scopus 로고
    • GSK-3b promotes cell survival by modulating Bif-1-dependent autophagy and cell death
    • Yang J, Takahashi Y, Cheng E, Liu J, Terranova PF, Zhao B et al. GSK-3b promotes cell survival by modulating Bif-1-dependent autophagy and cell death. J Cell Sci 2010; 123: 861-870.
    • (2010) J Cell Sci , vol.123 , pp. 861-870
    • Yang, J.1    Takahashi, Y.2    Cheng, E.3    Liu, J.4    Terranova, P.F.5    Zhao, B.6
  • 20
    • 77951169413 scopus 로고    scopus 로고
    • ErbB2 requires integrin alpha5 for anoikis resistance via Src regulation of receptor activity in human mammary epithelial cells
    • Haenssen KK, Caldwell SA, Shahriari KS, Jackson SR, Whelan KA, Klein-Szanto AJ et al. ErbB2 requires integrin alpha5 for anoikis resistance via Src regulation of receptor activity in human mammary epithelial cells. J Cell Sci 2010; 123: 1373-1382.
    • (2010) J Cell Sci , vol.123 , pp. 1373-1382
    • Haenssen, K.K.1    Caldwell, S.A.2    Shahriari, K.S.3    Jackson, S.R.4    Whelan, K.A.5    Klein-Szanto, A.J.6
  • 21
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3 beta in cellular signaling
    • Grimes CA, Jope RS. The multifaceted roles of glycogen synthase kinase 3 beta in cellular signaling. Prog Neurobiol 2001; 65: 391-426.
    • (2001) Prog Neurobiol , vol.65 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 22
    • 0032529634 scopus 로고    scopus 로고
    • Down-regulation of the transporter for antigen presentation, proteasome subunits, and class I major histocompatibility complex in tumor cell lines
    • Johnsen A, France J, Sy MS, Harding CV. Down-regulation of the transporter for antigen presentation, proteasome subunits, and class I major histocompatibility complex in tumor cell lines. Cancer Res 1998; 58: 3660-3667.
    • (1998) Cancer Res , vol.58 , pp. 3660-3667
    • Johnsen, A.1    France, J.2    Sy, M.S.3    Harding, C.V.4
  • 23
    • 0033034333 scopus 로고    scopus 로고
    • Down-regulation of HLA class I antigen processing molecules in malignant melanoma: Association with disease progression
    • Kageshita T, Hirai S, Ono T, Hicklin DJ, Ferrone S. Down-regulation of HLA class I antigen processing molecules in malignant melanoma: Association with disease progression. Am J Pathol 1999; 154: 745-754.
    • (1999) Am J Pathol , vol.154 , pp. 745-754
    • Kageshita, T.1    Hirai, S.2    Ono, T.3    Hicklin, D.J.4    Ferrone, S.5
  • 24
    • 4344644908 scopus 로고    scopus 로고
    • High frequency of functionally active Melan-aspecific T cells in a patient with progressive immunoproteasome-deficient melanoma
    • Meidenbauer N, Zippelius A, Pittet MJ, Laumer M, Vogl S, Heymann J et al. High frequency of functionally active Melan-aspecific T cells in a patient with progressive immunoproteasome-deficient melanoma. Cancer Res 2004; 64: 6319-6326.
    • (2004) Cancer Res , vol.64 , pp. 6319-6326
    • Meidenbauer, N.1    Zippelius, A.2    Pittet, M.J.3    Laumer, M.4    Vogl, S.5    Heymann, J.6
  • 25
    • 31544452256 scopus 로고    scopus 로고
    • Tumor cell lines expressing the proteasome subunit isoform LMP7E1 exhibit immunoproteasome deficiency
    • Heink S, Fricke B, Ludwig D, Kloetzel PM, Krüger E. Tumor cell lines expressing the proteasome subunit isoform LMP7E1 exhibit immunoproteasome deficiency. Cancer Res 2006; 66: 649-652.
    • (2006) Cancer Res , vol.66 , pp. 649-652
    • Heink, S.1    Fricke, B.2    Ludwig, D.3    Kloetzel, P.M.4    Krüger, E.5
  • 26
    • 82655181320 scopus 로고    scopus 로고
    • The LMP7-K allele of the immunoproteasome exhibits reduced transcript stability and predicts high risk of colon cancer
    • Fellerhoff B, Gu S, Laumbacher B, Nerlich AG, Weiss EH, Glas J et al. The LMP7-K allele of the immunoproteasome exhibits reduced transcript stability and predicts high risk of colon cancer. Cancer Res 2011; 71: 7145-7154.
    • (2011) Cancer Res , vol.71 , pp. 7145-7154
    • Fellerhoff, B.1    Gu, S.2    Laumbacher, B.3    Nerlich, A.G.4    Weiss, E.H.5    Glas, J.6
  • 27
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy: Ubiquitin-mediated recognition and beyond
    • Kraft C, Peter M, Hofmann K. Selective autophagy: Ubiquitin-mediated recognition and beyond. Nat Cell Biol 2010; 12: 836-841.
    • (2010) Nat Cell Biol , vol.12 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 28
    • 38949184241 scopus 로고    scopus 로고
    • HspB8 and Bag3: A new chaperone complex targeting misfolded proteins to macroautophagy
    • Carra S, Seguin SJ, Landry J. HspB8 and Bag3: A new chaperone complex targeting misfolded proteins to macroautophagy. Autophagy 2008; 4: 237-239.
    • (2008) Autophagy , vol.4 , pp. 237-239
    • Carra, S.1    Seguin, S.J.2    Landry, J.3
  • 29
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers J, Mogk A, Bukau B. Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 2010; 11: 777-788.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 30
    • 58549084167 scopus 로고    scopus 로고
    • Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes
    • Kim PK, Hailey DW, Mullen RT, Lippincott-Schwartz J. Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes. Proc Natl Acad Sci 2008; 105: 20567-20574.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 20567-20574
    • Kim, P.K.1    Hailey, D.W.2    Mullen, R.T.3    Lippincott -Schwartz, J.4
  • 31
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice
    • Komatsu M, Waguri S, Koike M, Sou YS, Ueno T, Hara T et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 2007; 131: 1149-1163.
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1    Waguri, S.2    Koike, M.3    Sou, Y.S.4    Ueno, T.5    Hara, T.6
  • 32
    • 64549154396 scopus 로고    scopus 로고
    • Diversity of polyubiquitin chains
    • Adhikari A, Chen ZJ. Diversity of polyubiquitin chains. Dev Cell 2009; 16: 485-486.
    • (2009) Dev Cell , vol.16 , pp. 485-486
    • Adhikari, A.1    Chen, Z.J.2
  • 33
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • Seibenhener ML, Babu JR, Geetha T, Wong HC, Krishna NR, Wooten MW. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol Cell Biol 2004; 24: 8055-8068.
    • (2004) Mol Cell Biol , vol.24 , pp. 8055-8068
    • Seibenhener, M.L.1    Babu, J.R.2    Geetha, T.3    Wong, H.C.4    Krishna, N.R.5    Wooten, M.W.6
  • 34
    • 34548851476 scopus 로고    scopus 로고
    • Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6
    • Olzmann JA, Li L, Chudaev MV, Chen J, Perez FA, Palmiter RD et al. Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J Cell Biol 2007; 178: 1025-1038.
    • (2007) J Cell Biol , vol.178 , pp. 1025-1038
    • Olzmann, J.A.1    Li, L.2    Chudaev, M.V.3    Chen, J.4    Perez, F.A.5    Palmiter, R.D.6
  • 35
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V, McEwan DG, Novak I, Dikic I. A role for ubiquitin in selective autophagy. Mol Cell 2009; 34: 259-269.
    • (2009) Mol Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 36
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T, Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy 2011; 7: 279-296.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 37
    • 84862829824 scopus 로고    scopus 로고
    • Proteasome inhibition-induced p38 MAPK/ERK signaling regulates autophagy and apoptosis through the dual phosphorylation of glycogen synthase kinase 3b
    • Choi CH, Lee BH, Ahn SG, Oh SH. Proteasome inhibition-induced p38 MAPK/ERK signaling regulates autophagy and apoptosis through the dual phosphorylation of glycogen synthase kinase 3b. Biochem Biophys Res Commun 2012; 418: 759-764.
    • (2012) Biochem Biophys Res Commun , vol.418 , pp. 759-764
    • Choi, C.H.1    Lee, B.H.2    Ahn, S.G.3    Oh, S.H.4
  • 38
    • 74049104138 scopus 로고    scopus 로고
    • Dysfunction of the unfolded protein response increases neurodegeneration in aged rat hippocampus following proteasome inhibition
    • Gavilán MP, Pintado C, Gavilán E, Jiménez S, Ríos RM, Vitorica J et al. Dysfunction of the unfolded protein response increases neurodegeneration in aged rat hippocampus following proteasome inhibition. Aging Cell 2009; 8: 654-665.
    • (2009) Aging Cell , vol.8 , pp. 654-665
    • Gavilán, M.P.1    Pintado, C.2    Gavilán, E.3    Jiménez, S.4    Ríos, R.M.5    Vitorica, J.6
  • 39
    • 66249085237 scopus 로고    scopus 로고
    • The role of ATF4 stabilization and autophagy in resistance of breast cancer cells treated with Bortezomib
    • Milani M, Rzymski T, Mellor HR, Pike L, Bottini A, Generali D et al. The role of ATF4 stabilization and autophagy in resistance of breast cancer cells treated with Bortezomib. Cancer Res 2009; 69: 4415-4423.
    • (2009) Cancer Res , vol.69 , pp. 4415-4423
    • Milani, M.1    Rzymski, T.2    Mellor, H.R.3    Pike, L.4    Bottini, A.5    Generali, D.6
  • 40
    • 84872462504 scopus 로고    scopus 로고
    • Integration of autophagy, proteasomal degradation, unfolded protein response and apoptosis
    • Benbrook DM, Long A. Integration of autophagy, proteasomal degradation, unfolded protein response and apoptosis. Exp Oncol 2012; 34: 286-297.
    • (2012) Exp Oncol , vol.34 , pp. 286-297
    • Benbrook, D.M.1    Long, A.2
  • 41
    • 68349135032 scopus 로고    scopus 로고
    • Regulation of autophagy through multiple independent hypoxic signaling pathways
    • Rouschop KM, Wouters BG. Regulation of autophagy through multiple independent hypoxic signaling pathways. Curr Mol Med 2009; 9: 417-424.
    • (2009) Curr Mol Med , vol.9 , pp. 417-424
    • Rouschop, K.M.1    Wouters, B.G.2
  • 45
    • 0037631325 scopus 로고    scopus 로고
    • Inhibition of glucose metabolism sensitizes tumor cells to death receptor-triggered apoptosis through enhancement of death-inducing signaling complex formation and apical procaspase-8 processing
    • Muñoz-Pinedo C, Ruiz-Ruiz C, Ruiz de Almodó var C, Palacios C, López-Rivas A. Inhibition of glucose metabolism sensitizes tumor cells to death receptor-triggered apoptosis through enhancement of death-inducing signaling complex formation and apical procaspase-8 processing. J Biol Chem 2003; 278: 12759-12768.
    • (2003) J Biol Chem , vol.278 , pp. 12759-12768
    • Muñoz-Pinedo, C.1    Ruiz-Ruiz, C.2    Ruiz De Almodó Var, C.3    Palacios, C.4    López-Rivas, A.5
  • 46
    • 68349154339 scopus 로고    scopus 로고
    • Reconstitution of the death-inducing signaling complex reveals a substrate switch that determines CD95-mediated death or survival
    • Hughes MA, Harper N, Butterworth M, Cain K, Cohen GM, MacFarlane M. Reconstitution of the death-inducing signaling complex reveals a substrate switch that determines CD95-mediated death or survival. Mol Cell 2009; 35: 265-279.
    • (2009) Mol Cell , vol.35 , pp. 265-279
    • Hughes, M.A.1    Harper, N.2    Butterworth, M.3    Cain, K.4    Cohen, G.M.5    MacFarlane, M.6
  • 49
    • 84868687820 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 inhibition promotes lysosomal biogenesis and autophagic degradation of the amyloid-b precursor protein
    • Parr C, Carzaniga R, Gentleman SM, Van Leuven F, Walter J, Sastre M. Glycogen synthase kinase 3 inhibition promotes lysosomal biogenesis and autophagic degradation of the amyloid-b precursor protein. Mol Cell Biol 2012; 32: 4410-4418.
    • (2012) Mol Cell Biol , vol.32 , pp. 4410-4418
    • Parr, C.1    Carzaniga, R.2    Gentleman, S.M.3    Van Leuven, F.4    Walter, J.5    Sastre, M.6
  • 52
    • 0025878872 scopus 로고
    • Comparison of the sulforhodamine B protein and tetrazolium (MTT) assays for in vitro chemosensitivity testing
    • Keepers YP, Pizao PE, Peters GJ, van Ark-Otte J, Winograd B, Pinedo HM. Comparison of the sulforhodamine B protein and tetrazolium (MTT) assays for in vitro chemosensitivity testing. Eur J Cancer 1991; 27: 897-900.
    • (1991) Eur J Cancer , vol.27 , pp. 897-900
    • Keepers, Y.P.1    Pizao, P.E.2    Peters, G.J.3    Van Ark-Otte, J.4    Winograd, B.5    Pinedo, H.M.6
  • 53
    • 74049104138 scopus 로고    scopus 로고
    • Dysfunction of the unfolded protein response increases neurodegeneration in aged rat hippocampus following proteasome inhibition
    • Gavilán MP, Pintado C, Gavilán E, Jiménez S, Ríos RM, Vitorica J et al. Dysfunction of the unfolded protein response increases neurodegeneration in aged rat hippocampus following proteasome inhibition. Aging Cell 2009; 8: 654-665.
    • (2009) Aging Cell , vol.8 , pp. 654-665
    • Gavilán, M.P.1    Pintado, C.2    Gavilán, E.3    Jiménez, S.4    Ríos, R.M.5    Vitorica, J.6


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