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Volumn 10, Issue 21, 2011, Pages 3678-3683

Morgana and Melusin: Two fairies chaperoning signal transduction

Author keywords

Centrosome duplication; ERK1 2; Genomic stability; Heart hypertrophy; Melusin; Morgana; ROCK

Indexed keywords

CHAPERONE; CYCLIN DEPENDENT KINASE 2; CYCLIN E; CYSTEINE; HEAT SHOCK PROTEIN 90; HISTIDINE; MELUSIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MORGANA; NUCLEOPHOSMIN; POLO LIKE KINASE; PROTEIN P58; RHO KINASE; UNCLASSIFIED DRUG;

EID: 80655123614     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.10.21.18202     Document Type: Review
Times cited : (28)

References (41)
  • 1
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • PMID:21776078; DOI:10.1038/nature10317
    • Hartl FU, Bracher A, Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 2011; 475:324-32; PMID:21776078; DOI:10.1038/nature10317.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 2
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • PMID:18290764; DOI:10.1042/BJ20071640
    • Pearl LH, Prodromou C, Workman P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J 2008; 410:439-53; PMID:18290764; DOI:10.1042/BJ20071640.
    • (2008) Biochem J , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 3
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • PMID:16756493; DOI:10.1146/annurev.biochem.75.103004.142738
    • Pearl LH, Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 2006; 75:271-94; PMID:16756493; DOI:10.1146/annurev.biochem.75.103004.142738.
    • (2006) Annu Rev Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 4
    • 34748871996 scopus 로고    scopus 로고
    • Hsp90 - From signal transduction to cell transformation
    • PMID:17826744; DOI:10.1016/j.bbrc.2007.08.054
    • Brown MA, Zhu L, Schmidt C, Tucker PW. Hsp90 - from signal transduction to cell transformation. Biochem Biophys Res Commun 2007; 363:241-6; PMID:17826744; DOI:10.1016/j.bbrc.2007.08.054.
    • (2007) Biochem Biophys Res Commun , vol.363 , pp. 241-246
    • Brown, M.A.1    Zhu, L.2    Schmidt, C.3    Tucker, P.W.4
  • 5
    • 76649103378 scopus 로고    scopus 로고
    • A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein
    • PMID:19875381; DOI:10.1074/mcp. M900261-MCP200
    • Gano JJ, Simon JA. A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein. Mol Cell Proteomics 2010; 9:255-70; PMID:19875381; DOI:10.1074/mcp. M900261-MCP200.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 255-270
    • Gano, J.J.1    Simon, J.A.2
  • 6
    • 0032724487 scopus 로고    scopus 로고
    • A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans
    • PMID:10571178; DOI:10.1016/S0092-8674(00)81522-6
    • Shirasu K, Lahaye T, Tan MW, Zhou F, Azevedo C, Schulze-Lefert P. A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans. Cell 1999; 99:355-66; PMID:10571178; DOI:10.1016/S0092-8674(00)81522-6.
    • (1999) Cell , vol.99 , pp. 355-366
    • Shirasu, K.1    Lahaye, T.2    Tan, M.W.3    Zhou, F.4    Azevedo, C.5    Schulze-Lefert, P.6
  • 7
    • 0036016432 scopus 로고    scopus 로고
    • Arabidopsis RAR1 exerts rate-limiting control of R gene-mediated defenses against multiple pathogens
    • PMID:12034891; DOI:10.1105/tpc.001040
    • Muskett PR, Kahn K, Austin MJ, Moisan LJ, Sadanandom A, Shirasu K, et al. Arabidopsis RAR1 exerts rate-limiting control of R gene-mediated defenses against multiple pathogens. Plant Cell 2002; 14:979-92; PMID:12034891; DOI:10.1105/tpc.001040.
    • (2002) Plant Cell , vol.14 , pp. 979-992
    • Muskett, P.R.1    Kahn, K.2    Austin, M.J.3    Moisan, L.J.4    Sadanandom, A.5    Shirasu, K.6
  • 8
    • 0036016434 scopus 로고    scopus 로고
    • RAR1 and NDR1 contribute quantitatively to disease resistance in Arabidopsis, and their relative contributions are dependent on the R gene assayed
    • PMID:12034893; DOI:10.1105/tpc.001032
    • Tornero P, Merritt P, Sadanandom A, Shirasu K, Innes RW, Dangl JL. RAR1 and NDR1 contribute quantitatively to disease resistance in Arabidopsis, and their relative contributions are dependent on the R gene assayed. Plant Cell 2002; 14:1005-15; PMID:12034893; DOI:10.1105/tpc.001032.
    • (2002) Plant Cell , vol.14 , pp. 1005-1015
    • Tornero, P.1    Merritt, P.2    Sadanandom, A.3    Shirasu, K.4    Innes, R.W.5    Dangl, J.L.6
  • 9
    • 0037086007 scopus 로고    scopus 로고
    • The RAR1 interactor SGT1, an essential component of R gene-triggered disease resistance
    • PMID:11847307; DOI:10.1126/science. 1067554
    • Azevedo C, Sadanandom A, Kitagawa K, Freialdenhoven A, Shirasu K, Schulze-Lefert P. The RAR1 interactor SGT1, an essential component of R gene-triggered disease resistance. Science 2002; 295:2073-6; PMID:11847307; DOI:10.1126/science. 1067554.
    • (2002) Science , vol.295 , pp. 2073-2076
    • Azevedo, C.1    Sadanandom, A.2    Kitagawa, K.3    Freialdenhoven, A.4    Shirasu, K.5    Schulze-Lefert, P.6
  • 10
    • 0141705339 scopus 로고    scopus 로고
    • HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis
    • PMID:14504384; DOI:10.1073/pnas.2033934100
    • Takahashi A, Casais C, Ichimura K, Shirasu K. HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis. Proc Natl Acad Sci USA 2003; 100:11777-82; PMID:14504384; DOI:10.1073/pnas. 2033934100.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11777-11782
    • Takahashi, A.1    Casais, C.2    Ichimura, K.3    Shirasu, K.4
  • 11
    • 0033166694 scopus 로고    scopus 로고
    • SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex
    • PMID:10445024; DOI:10.1016/S1097-2765(00)80184-7
    • Kitagawa K, Skowyra D, Elledge SJ, Harper JW, Hieter P. SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex. Mol Cell 1999; 4:21-33; PMID:10445024; DOI:10.1016/S1097-2765(00)80184-7.
    • (1999) Mol Cell , vol.4 , pp. 21-33
    • Kitagawa, K.1    Skowyra, D.2    Elledge, S.J.3    Harper, J.W.4    Hieter, P.5
  • 12
    • 4344619975 scopus 로고    scopus 로고
    • Sgt1 is required for human kinetochore assembly
    • PMID:15133482; DOI:10.1038/sj.embor.7400154
    • Steensgaard P, Garre M, Muradore I, Transidico P, Nigg EA, Kitagawa K, et al. Sgt1 is required for human kinetochore assembly. EMBO Rep 2004; 5:626-31; PMID:15133482; DOI:10.1038/sj.embor.7400154.
    • (2004) EMBO Rep , vol.5 , pp. 626-631
    • Steensgaard, P.1    Garre, M.2    Muradore, I.3    Transidico, P.4    Nigg, E.A.5    Kitagawa, K.6
  • 13
    • 59649124272 scopus 로고    scopus 로고
    • Sgt1, a co-chaperone of Hsp90 stabilizes Polo and is required for centrosome organization
    • PMID:19131964; DOI:10.1038/emboj.2008.283
    • Martins T, Maia AF, Steffensen S, Sunkel CE. Sgt1, a co-chaperone of Hsp90 stabilizes Polo and is required for centrosome organization. EMBO J 2009; 28:234-47; PMID:19131964; DOI:10.1038/emboj.2008.283.
    • (2009) EMBO J , vol.28 , pp. 234-247
    • Martins, T.1    Maia, A.F.2    Steffensen, S.3    Sunkel, C.E.4
  • 14
    • 77955480981 scopus 로고    scopus 로고
    • Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: Implications for chaperoning of NLR innate immunity receptors
    • PMID:20670895; DOI:10.1016/j. molcel.2010.05.010
    • Zhang M, Kadota Y, Prodromou C, Shirasu K, Pearl LH. Structural basis for assembly of Hsp90-Sgt1-CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors. Mol Cell 2010; 39:269-81; PMID:20670895; DOI:10.1016/j. molcel.2010.05.010.
    • (2010) Mol Cell , vol.39 , pp. 269-281
    • Zhang, M.1    Kadota, Y.2    Prodromou, C.3    Shirasu, K.4    Pearl, L.H.5
  • 15
    • 0142134262 scopus 로고    scopus 로고
    • Chp-1 and melusin, two CHORD containing proteins in vertebrates
    • PMID:12965203; DOI:10.1016/S0014-5793(03)00892-5
    • Brancaccio M, Menini N, Bongioanni D, Ferretti R, De Acetis M, Silengo L, et al. Chp-1 and melusin, two CHORD containing proteins in vertebrates. FEBS Lett 2003; 551:47-52; PMID:12965203; DOI:10.1016/S0014-5793(03)00892-5.
    • (2003) FEBS Lett , vol.551 , pp. 47-52
    • Brancaccio, M.1    Menini, N.2    Bongioanni, D.3    Ferretti, R.4    De Acetis, M.5    Silengo, L.6
  • 16
    • 44449149304 scopus 로고    scopus 로고
    • The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1
    • PMID:18474241; DOI:10.1016/j.febslet.2008.04.058
    • Sbroggiò M, Ferretti R, Percivalle E, Gutkowska M, Zylicz A, Michowski W, et al. The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1. FEBS Lett 2008; 582:1788-94; PMID:18474241; DOI:10.1016/j.febslet.2008.04.058.
    • (2008) FEBS Lett , vol.582 , pp. 1788-1794
    • Sbroggiò, M.1    Ferretti, R.2    Percivalle, E.3    Gutkowska, M.4    Zylicz, A.5    Michowski, W.6
  • 17
    • 77954954043 scopus 로고    scopus 로고
    • Morgana/CHP-1 is a novel chaperone able to protect cells from stress
    • PMID:20493909; DOI:10.1016/j. bbamcr.2010.05.005
    • Michowski W, Ferretti R, Wisniewska MB, Ambrozkiewicz M, Beresewicz M, Fusella F, et al. Morgana/CHP-1 is a novel chaperone able to protect cells from stress. Biochim Biophys Acta 2010; 1803:1043-9; PMID:20493909; DOI:10.1016/j. bbamcr.2010.05.005.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 1043-1049
    • Michowski, W.1    Ferretti, R.2    Wisniewska, M.B.3    Ambrozkiewicz, M.4    Beresewicz, M.5    Fusella, F.6
  • 18
    • 11844252634 scopus 로고    scopus 로고
    • Mammalian CHORD-containing protein 1 is a novel heat shock protein 90-interacting protein
    • PMID:15642353; DOI:10.1016/j.febslet. 2004.12.005
    • Wu J, Luo S, Jiang H, Li H. Mammalian CHORD-containing protein 1 is a novel heat shock protein 90-interacting protein. FEBS Lett 2005; 579:421-6; PMID:15642353; DOI:10.1016/j.febslet. 2004.12.005.
    • (2005) FEBS Lett , vol.579 , pp. 421-426
    • Wu, J.1    Luo, S.2    Jiang, H.3    Li, H.4
  • 19
    • 23644448266 scopus 로고    scopus 로고
    • Regulation of Nod1 by Hsp90 chaperone complex
    • PMID:16083881; DOI:10.1016/j.febslet. 2005.07.024
    • Hahn JS. Regulation of Nod1 by Hsp90 chaperone complex. FEBS Lett 2005; 579:4513- 9; PMID:16083881; DOI:10.1016/j.febslet. 2005.07.024.
    • (2005) FEBS Lett , vol.579 , pp. 4513-4519
    • Hahn, J.S.1
  • 20
    • 77950566888 scopus 로고    scopus 로고
    • Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication and tumorigenesis
    • PMID:20230755; DOI:10.1016/j.devcel. 2009.12.020
    • Ferretti R, Palumbo V, Di Savino A, Velasco S, Sbroggiò M, Sportoletti P, et al. Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication and tumorigenesis. Dev Cell 2010; 18:486-95; PMID:20230755; DOI:10.1016/j.devcel. 2009.12.020.
    • (2010) Dev Cell , vol.18 , pp. 486-495
    • Ferretti, R.1    Palumbo, V.2    Di Savino, A.3    Velasco, S.4    Sbroggiò, M.5    Sportoletti, P.6
  • 21
    • 34249336078 scopus 로고    scopus 로고
    • Centrosome biogenesis and function: Centrosomics brings new understanding
    • PMID:17505520; DOI:10.1038/nrm2180
    • Bettencourt-Dias M, Glover DM. Centrosome biogenesis and function: centrosomics brings new understanding. Nat Rev Mol Cell Biol 2007; 8:451-63; PMID:17505520; DOI:10.1038/nrm2180.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 451-463
    • Bettencourt-Dias, M.1    Glover, D.M.2
  • 22
    • 0036468420 scopus 로고    scopus 로고
    • Centrosome composition and microtubule anchoring mechanisms
    • PMID:11792541; DOI:10.1016/S0955-0674(01)00290-3
    • Bornens M. Centrosome composition and microtubule anchoring mechanisms. Curr Opin Cell Biol 2002; 14:25-34; PMID:11792541; DOI:10.1016/S0955-0674(01) 00290-3.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 25-34
    • Bornens, M.1
  • 23
    • 36448987217 scopus 로고    scopus 로고
    • Oncogenes and tumour suppressors take on centrosomes
    • PMID:18004399; DOI:10.1038/nrc2249
    • Fukasawa K. Oncogenes and tumour suppressors take on centrosomes. Nat Rev Cancer 2007; 7:911-24; PMID:18004399; DOI:10.1038/nrc2249.
    • (2007) Nat Rev Cancer , vol.7 , pp. 911-924
    • Fukasawa, K.1
  • 24
    • 0037182591 scopus 로고    scopus 로고
    • The Rho-associated protein kinase p160ROCK is required for centrosome positioning
    • PMID:12034773; DOI:10.1083/jcb.200203034
    • Chevrier V, Piel M, Collomb N, Saoudi Y, Frank R, Paintrand M, et al. The Rho-associated protein kinase p160ROCK is required for centrosome positioning. J Cell Biol 2002; 157:807-17; PMID:12034773; DOI:10.1083/jcb.200203034.
    • (2002) J Cell Biol , vol.157 , pp. 807-817
    • Chevrier, V.1    Piel, M.2    Collomb, N.3    Saoudi, Y.4    Frank, R.5    Paintrand, M.6
  • 25
    • 2942661328 scopus 로고    scopus 로고
    • ROCK bypasses cell cycle arrest after Aurora-A/STK15 depletion
    • PMID:15178765; DOI:10.1073/pnas.0308484101
    • ROCK bypasses cell cycle arrest after Aurora-A/STK15 depletion. Proc Natl Acad Sci USA 2004; 101:8975-80; PMID:15178765; DOI:10.1073/pnas.0308484101.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8975-8980
    • Du, J.1    Hannon, G.J.2
  • 26
    • 0034653849 scopus 로고    scopus 로고
    • Hsp90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates
    • PMID:10716925; DOI:10.1093/emboj/19.6.1252
    • Lange BM, Bachi A, Wilm M, Gonzalez C. Hsp90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates. EMBO J 2000; 19:1252-62; PMID:10716925; DOI:10.1093/emboj/19.6.1252.
    • (2000) EMBO J , vol.19 , pp. 1252-1262
    • Lange, B.M.1    Bachi, A.2    Wilm, M.3    Gonzalez, C.4
  • 27
    • 33845228036 scopus 로고    scopus 로고
    • Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication
    • PMID:17015463; DOI:10.1128/MCB.01383-06
    • Ma Z, Kanai M, Kawamura K, Kaibuchi K, Ye K, Fukasawa K. Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication. Mol Cell Biol 2006; 26:9016-34; PMID:17015463; DOI:10.1128/MCB. 01383-06.
    • (2006) Mol Cell Biol , vol.26 , pp. 9016-9034
    • Ma, Z.1    Kanai, M.2    Kawamura, K.3    Kaibuchi, K.4    Ye, K.5    Fukasawa, K.6
  • 28
    • 79955876581 scopus 로고    scopus 로고
    • Activated ROCK II by-passes the requirement of the CDK2 activity for centrosome duplication and amplification
    • PMID:21242972; DOI:10.1038/onc.2010.607
    • Hanashiro K, Brancaccio M, Fukasawa K. Activated ROCK II by-passes the requirement of the CDK2 activity for centrosome duplication and amplification. Oncogene 2011; 30:2188-97; PMID:21242972; DOI:10.1038/onc.2010.607.
    • (2011) Oncogene , vol.30 , pp. 2188-2197
    • Hanashiro, K.1    Brancaccio, M.2    Fukasawa, K.3
  • 29
    • 0036831681 scopus 로고    scopus 로고
    • Centrosome aberrations: Cause or consequence of cancer progression?
    • PMID:12415252; DOI:10.1038/nrc924
    • Nigg EA. Centrosome aberrations: cause or consequence of cancer progression? Nat Rev Cancer 2002; 2:815-25; PMID:12415252; DOI:10.1038/nrc924.
    • (2002) Nat Rev Cancer , vol.2 , pp. 815-825
    • Nigg, E.A.1
  • 30
    • 0036752341 scopus 로고    scopus 로고
    • Duplicating dangerously: Linking centrosome duplication and aneuploidy
    • PMID:12408813; DOI:10.1016/S1097-2765(02)00654-8
    • Doxsey S. Duplicating dangerously: linking centrosome duplication and aneuploidy. Mol Cell 2002; 10:439-40; PMID:12408813; DOI:10.1016/S1097-2765(02) 00654-8.
    • (2002) Mol Cell , vol.10 , pp. 439-440
    • Doxsey, S.1
  • 31
    • 1642412809 scopus 로고    scopus 로고
    • The good, the bad and the ugly: The practical consequences of centrosome amplification
    • PMID:15037304; DOI:10.1016/j.ceb.2003.11.006
    • Sluder G, Nordberg JJ. The good, the bad and the ugly: the practical consequences of centrosome amplification. Curr Opin Cell Biol 2004; 16:49-54; PMID:15037304; DOI:10.1016/j.ceb.2003.11.006.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 49-54
    • Sluder, G.1    Nordberg, J.J.2
  • 32
    • 44649117902 scopus 로고    scopus 로고
    • Centrosome amplification can initiate tumorigenesis in flies
    • PMID:18555779; DOI:10.1016/j. cell.2008.05.039
    • Basto R, Brunk K, Vinadogrova T, Peel N, Franz A, Khodjakov A, et al. Centrosome amplification can initiate tumorigenesis in flies. Cell 2008; 133:1032-42; PMID:18555779; DOI:10.1016/j. cell.2008.05.039.
    • (2008) Cell , vol.133 , pp. 1032-1042
    • Basto, R.1    Brunk, K.2    Vinadogrova, T.3    Peel, N.4    Franz, A.5    Khodjakov, A.6
  • 33
    • 4143089230 scopus 로고    scopus 로고
    • CHPA, a cysteine- And histidinerich-domain-containing protein, contributes to maintenance of the diploid state in Aspergillus nidulans
    • PMID:15302831; DOI:10.1128/EC.3.4.984-91.2004
    • Sadanandom A, Findlay K, Doonan JH, Schulze-Lefert P, Shirasu K. CHPA, a cysteine- and histidinerich-domain-containing protein, contributes to maintenance of the diploid state in Aspergillus nidulans. Eukaryot Cell 2004; 3:984-91; PMID:15302831; DOI:10.1128/EC.3.4.984-91.2004.
    • (2004) Eukaryot Cell , vol.3 , pp. 984-991
    • Sadanandom, A.1    Findlay, K.2    Doonan, J.H.3    Schulze-Lefert, P.4    Shirasu, K.5
  • 34
    • 0032879692 scopus 로고    scopus 로고
    • Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic domain
    • PMID:10506186; DOI:10.1074/jbc.274.41.29282
    • Brancaccio M, Guazzone S, Menini N, Sibona E, Hirsch E, De Andrea M, et al. Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic domain. J Biol Chem 1999; 274:29282-8; PMID:10506186; DOI:10.1074/jbc.274.41. 29282.
    • (1999) J Biol Chem , vol.274 , pp. 29282-29288
    • Brancaccio, M.1    Guazzone, S.2    Menini, N.3    Sibona, E.4    Hirsch, E.5    De Andrea, M.6
  • 35
    • 0037236642 scopus 로고    scopus 로고
    • Melusin, a muscle-specific integrin beta1-interacting protein, is required to prevent cardiac failure in response to chronic pressure overload
    • PMID:12496958; DOI:10.1038/nm805
    • Brancaccio M, Fratta L, Notte A, Hirsch E, Poulet R, Guazzone S, et al. Melusin, a muscle-specific integrin beta1-interacting protein, is required to prevent cardiac failure in response to chronic pressure overload. Nat Med 2003; 9:68-75; PMID:12496958; DOI:10.1038/nm805.
    • (2003) Nat Med , vol.9 , pp. 68-75
    • Brancaccio, M.1    Fratta, L.2    Notte, A.3    Hirsch, E.4    Poulet, R.5    Guazzone, S.6
  • 36
    • 20344399430 scopus 로고    scopus 로고
    • Cardiac over-expression of melusin protects from dilated cardiomyopathy due to long-standing pressure overload
    • PMID:15860758; DOI:10.1161/01.RES.0000168028.36081.e0
    • De Acetis M, Notte A, Accornero F, Selvetella G, Brancaccio M, Vecchione C, et al. Cardiac over-expression of melusin protects from dilated cardiomyopathy due to long-standing pressure overload. Circ Res 2005; 96:1087-94; PMID:15860758; DOI:10.1161/01.RES.0000168028.36081.e0.
    • (2005) Circ Res , vol.96 , pp. 1087-1094
    • De Acetis, M.1    Notte, A.2    Accornero, F.3    Selvetella, G.4    Brancaccio, M.5    Vecchione, C.6
  • 37
    • 80655129398 scopus 로고    scopus 로고
    • ERK1/2 activation in heart is controlled by Melusin, Focal adhesion kinase and the scaffold protein IQGAP1
    • Sbroggiò M, Bertero A, Velasco S, Fusella F, De Blasio E, Bahou WF, et al. ERK1/2 activation in heart is controlled by Melusin, Focal adhesion kinase and the scaffold protein IQGAP1. J Cell Sci 2011; 124:3515-24.
    • (2011) J Cell Sci , vol.124 , pp. 3515-3524
    • Sbroggiò, M.1    Bertero, A.2    Velasco, S.3    Fusella, F.4    De Blasio, E.5    Bahou, W.F.6
  • 38
    • 34547548629 scopus 로고    scopus 로고
    • IQGAP1 modulates activation of B-Raf
    • PMID:17563371; DOI:10.1073/pnas.0611308104
    • Ren JG, Li Z, Sacks DB. IQGAP1 modulates activation of B-Raf. Proc Natl Acad Sci USA 2007; 104:10465-9; PMID:17563371; DOI:10.1073/pnas.0611308104.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10465-10469
    • Ren, J.G.1    Li, Z.2    Sacks, D.B.3
  • 39
    • 24344491858 scopus 로고    scopus 로고
    • IQGAP1 is a scaffold for mitogen-activated protein kinase signaling
    • PMID:16135787; DOI:10.1128/MCB.25.18.7940-52.2005
    • Roy M, Li Z, Sacks DB. IQGAP1 is a scaffold for mitogen-activated protein kinase signaling. Mol Cell Biol 2005; 25:7940-52; PMID:16135787; DOI:10.1128/MCB.25.18.7940-52.2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 7940-7952
    • Roy, M.1    Li, Z.2    Sacks, D.B.3
  • 40
    • 79960791372 scopus 로고    scopus 로고
    • IQGAP1 regulates ERK1/2 and AKT signalling in the heart and sustains functional remodelling upon pressure overload
    • PMID:21493702; DOI:10.1093/cvr/cvr103
    • Sbroggiò M, Carnevale D, Bertero A, Cifelli G, De Blasio E, Mascio G, et al. IQGAP1 regulates ERK1/2 and AKT signalling in the heart and sustains functional remodelling upon pressure overload. Cardiovasc Res 2011; 91:456-64; PMID:21493702; DOI:10.1093/cvr/cvr103.
    • (2011) Cardiovasc Res , vol.91 , pp. 456-464
    • Sbroggiò, M.1    Carnevale, D.2    Bertero, A.3    Cifelli, G.4    De Blasio, E.5    Mascio, G.6
  • 41
    • 80052201664 scopus 로고    scopus 로고
    • Phosphoinositide-3-Kinase (PI3K(p110{alpha})) Directly Regulates Key Components of the Z-disc and Cardiac Structure
    • PMID:21757757; DOI:10.1074/jbc.M111.271684
    • Waardenberg AJ, Bernardo BC, Ng DC, Shepherd PR, Cemerlang N, Sbroggiò M, et al. Phosphoinositide-3-Kinase (PI3K(p110{alpha})) Directly Regulates Key Components of the Z-disc and Cardiac Structure. J Biol Chem 2011; 286:30837-46; PMID:21757757; DOI:10.1074/jbc.M111.271684.
    • (2011) J Biol Chem , vol.286 , pp. 30837-30846
    • Waardenberg, A.J.1    Bernardo, B.C.2    Ng, D.C.3    Shepherd, P.R.4    Cemerlang, N.5    Sbroggiò, M.6


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