메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Cytoplasmic sphingosine-1-phosphate pathway modulates neuronal autophagy

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; ENZYME INHIBITOR; LYASE; LYSOPHOSPHOLIPID; PHOSPHOTRANSFERASE; PROTEIN BINDING; SPHINGOSINE; SPHINGOSINE 1-PHOSPHATE; SPHINGOSINE 1-PHOSPHATE LYASE (ALDOLASE); SPHINGOSINE KINASE;

EID: 84945217654     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep15213     Document Type: Article
Times cited : (72)

References (51)
  • 1
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • Rubinsztein, D. C., Codogno, P., Levine, B. Autophagy modulation as a potential therapeutic target for diverse diseases. Nat rev 11, 709-730, doi: 10.1038/nrd3802 (2012).
    • (2012) Nat Rev , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3
  • 2
    • 84883452831 scopus 로고    scopus 로고
    • Up-to-date membrane biogenesis in the autophagosome formation
    • Hamasaki, M., Shibutani, S. T., Yoshimori, T. Up-to-date membrane biogenesis in the autophagosome formation. Curr Opin Cell Biol 25, 455-460, doi: 10.1016/j.ceb.2013.03.004 (2013).
    • (2013) Curr Opin Cell Biol , vol.25 , pp. 455-460
    • Hamasaki, M.1    Shibutani, S.T.2    Yoshimori, T.3
  • 3
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe, E. L. et al. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. JCB 182, 685-701, doi: 10.1083/jcb.200803137 (2008).
    • (2008) JCB , vol.182 , pp. 685-701
    • Axe, E.L.1
  • 4
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of preautophagosomal structures
    • Ravikumar, B., Moreau, K., Jahreiss, L., Puri, C., Rubinsztein, D. C. Plasma membrane contributes to the formation of preautophagosomal structures. Nat cell bio 12, 747-757, doi: 10.1038/ncb2078 (2010).
    • (2010) Nat Cell Bio , vol.12 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3    Puri, C.4    Rubinsztein, D.C.5
  • 5
    • 77952495224 scopus 로고    scopus 로고
    • Mitochondria supply membranes for autophagosome biogenesis during starvation
    • Hailey, D. W. et al. Mitochondria supply membranes for autophagosome biogenesis during starvation. Cell 141, 656-667, doi: 10.1016/j.cell.2010.04.009 (2010).
    • (2010) Cell , vol.141 , pp. 656-667
    • Hailey, D.W.1
  • 6
    • 33750366092 scopus 로고    scopus 로고
    • Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
    • Young, A. R. et al. Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. J Cell Sci 119, 3888-3900, doi: 10.1242/jcs.03172 (2006).
    • (2006) J Cell Sci , vol.119 , pp. 3888-3900
    • Young, A.R.1
  • 7
    • 84882254367 scopus 로고    scopus 로고
    • The role of autophagy in neurodegenerative disease
    • Nixon, R. A. The role of autophagy in neurodegenerative disease. Nat med 19, 983-997, doi: 10.1038/nm.3232 (2013).
    • (2013) Nat Med , vol.19 , pp. 983-997
    • Nixon, R.A.1
  • 8
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu, M. et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441, 880-884, doi: 10.1038/nature04723 (2006).
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1
  • 9
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara, T. et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441, 885-889, doi: 10.1038/nature04724 (2006).
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1
  • 11
    • 84904729990 scopus 로고    scopus 로고
    • Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models
    • Barmada, S. J. et al. Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models. Nat chem bio, doi: 10.1038/nchembio.1563 (2014).
    • (2014) Nat Chem Bio
    • Barmada, S.J.1
  • 12
    • 78049231804 scopus 로고    scopus 로고
    • A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model
    • Tsvetkov, A. S. et al. A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model. PNAS USA 107, 16982-16987, doi: 10.1073/pnas.1004498107 (2010).
    • (2010) PNAS USA , vol.107 , pp. 16982-16987
    • Tsvetkov, A.S.1
  • 13
    • 33646831810 scopus 로고    scopus 로고
    • Regulation of autophagy by sphingosine kinase 1 and its role in cell survival during nutrient starvation
    • Lavieu, G. et al. Regulation of autophagy by sphingosine kinase 1 and its role in cell survival during nutrient starvation. JBC 281, 8518-8527, doi: 10.1074/jbc.M506182200 (2006).
    • (2006) JBC , vol.281 , pp. 8518-8527
    • Lavieu, G.1
  • 14
    • 0037144434 scopus 로고    scopus 로고
    • PKC-dependent activation of sphingosine kinase 1 and translocation to the plasma membrane Extracellular release of sphingosine-1-phosphate induced by phorbol 12-myristate 13-acetate (PMA)
    • Johnson, K. R., Becker, K. P., Facchinetti, M. M., Hannun, Y. A., Obeid, L. M. PKC-dependent activation of sphingosine kinase 1 and translocation to the plasma membrane. Extracellular release of sphingosine-1-phosphate induced by phorbol 12-myristate 13-acetate (PMA). JBC 277, 35257-35262, doi: 10.1074/jbc.M203033200 (2002).
    • (2002) JBC , vol.277 , pp. 35257-35262
    • Johnson, K.R.1    Becker, K.P.2    Facchinetti, M.M.3    Hannun, Y.A.4    Obeid, L.M.5
  • 15
    • 84855303523 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate signaling and its role in disease
    • Maceyka, M., Harikumar, K. B., Milstien, S., Spiegel, S. Sphingosine-1-phosphate signaling and its role in disease. Trends in cell bio 22, 50-60, doi: 10.1016/j.tcb.2011.09.003 (2012).
    • (2012) Trends in Cell Bio , vol.22 , pp. 50-60
    • Maceyka, M.1    Harikumar, K.B.2    Milstien, S.3    Spiegel, S.4
  • 16
    • 0028128763 scopus 로고
    • Sphingosine 1-phosphate generated in the endoplasmic reticulum membrane activates release of stored calcium
    • Ghosh, T. K., Bian, J., Gill, D. L. Sphingosine 1-phosphate generated in the endoplasmic reticulum membrane activates release of stored calcium. JBC 269, 22628-22635 (1994).
    • (1994) JBC , vol.269 , pp. 22628-22635
    • Ghosh, T.K.1    Bian, J.2    Gill, D.L.3
  • 17
    • 0027991078 scopus 로고
    • Sphingosine-1-phosphate a putative second messenger, mobilizes calcium from internal stores via an inositol trisphosphate-independent pathway
    • Mattie, M., Brooker, G., Spiegel, S. Sphingosine-1-phosphate, a putative second messenger, mobilizes calcium from internal stores via an inositol trisphosphate-independent pathway. JBC 269, 3181-3188 (1994).
    • (1994) JBC , vol.269 , pp. 3181-3188
    • Mattie, M.1    Brooker, G.2    Spiegel, S.3
  • 18
    • 80052638037 scopus 로고    scopus 로고
    • A dual role for Ca(2+ ) in autophagy regulation
    • Decuypere, J. P., Bultynck, G., Parys, J. B. A dual role for Ca(2+ ) in autophagy regulation. Cell calcium 50, 242-250, doi: 10.1016/j.ceca.2011.04.001 (2011).
    • (2011) Cell Calcium , vol.50 , pp. 242-250
    • Decuypere, J.P.1    Bultynck, G.2    Parys, J.B.3
  • 19
    • 84885348627 scopus 로고    scopus 로고
    • Calcium-permeable ion channels in control of autophagy and cancer
    • Kondratskyi, A. et al. Calcium-permeable ion channels in control of autophagy and cancer. Front in physiol 4, 272, doi: 10.3389/fphys.2013.00272 (2013).
    • (2013) Front in Physiol , vol.4 , pp. 272
    • Kondratskyi, A.1
  • 20
    • 84857858536 scopus 로고    scopus 로고
    • Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons
    • Maday, S., Wallace, K. E., Holzbaur, E. L. Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons. JCB 196, 407-417, doi: 10.1083/jcb.201106120 (2012).
    • (2012) JCB , vol.196 , pp. 407-417
    • Maday, S.1    Wallace, K.E.2    Holzbaur, E.L.3
  • 21
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex
    • Zhong, Y. et al. Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat cell bio 11, 468-476, doi: 10.1038/ncb1854 (2009).
    • (2009) Nat Cell Bio , vol.11 , pp. 468-476
    • Zhong, Y.1
  • 22
    • 84872799206 scopus 로고    scopus 로고
    • The VMP1-Beclin 1 interaction regulates autophagy induction
    • Molejon, M. I., Ropolo, A., Re, A. L., Boggio, V., Vaccaro, M. I. The VMP1-Beclin 1 interaction regulates autophagy induction. Sci rep 3, 1055, doi: 10.1038/srep01055 (2013).
    • (2013) Sci Rep , vol.3 , pp. 1055
    • Molejon, M.I.1    Ropolo, A.2    Re, A.L.3    Boggio, V.4    Vaccaro, M.I.5
  • 23
    • 84883182319 scopus 로고    scopus 로고
    • Longitudinal imaging and analysis of neurons expressing polyglutamine-expanded proteins
    • Tsvetkov, A. S., Ando, D. M., Finkbeiner, S. Longitudinal imaging and analysis of neurons expressing polyglutamine-expanded proteins. Methods in mol biol 1017, 1-20, doi: 10.1007/978-1-62703-438-8-1 (2013).
    • (2013) Methods in Mol Biol , vol.1017 , pp. 1-20
    • Tsvetkov, A.S.1    Ando, D.M.2    Finkbeiner, S.3
  • 24
    • 32544449944 scopus 로고    scopus 로고
    • Splice variants of the NR1 subunit differentially induce NMDA receptor-dependent gene expression
    • Bradley, J., Carter, S. R., Rao, V. R., Wang, J., Finkbeiner, S. Splice variants of the NR1 subunit differentially induce NMDA receptor-dependent gene expression. J Neurosci 26, 1065-1076, doi: 10.1523/JNEUROSCI.3347-05.2006 (2006).
    • (2006) J Neurosci , vol.26 , pp. 1065-1076
    • Bradley, J.1    Carter, S.R.2    Rao, V.R.3    Wang, J.4    Finkbeiner, S.5
  • 25
    • 84883204078 scopus 로고    scopus 로고
    • Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration
    • Tsvetkov, A. S. et al. Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration. Nat chem bio 9, 586-592, doi: 10.1038/nchembio.1308 (2013).
    • (2013) Nat Chem Bio , vol.9 , pp. 586-592
    • Tsvetkov, A.S.1
  • 26
    • 78049231804 scopus 로고    scopus 로고
    • A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model
    • Tsvetkov, A. S. et al. A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model. PNAS USA 107, 16982-16987, doi: 10.1073/pnas.1004498107 (2010).
    • (2010) PNAS USA , vol.107 , pp. 16982-16987
    • Tsvetkov, A.S.1
  • 27
    • 59049094829 scopus 로고    scopus 로고
    • Nutrient deprivation induces neuronal autophagy and implicates reduced insulin signaling in neuroprotective autophagy activation
    • Young, J. E., Martinez, R. A., La Spada, A. R. Nutrient deprivation induces neuronal autophagy and implicates reduced insulin signaling in neuroprotective autophagy activation. JBC 284, 2363-2373, doi: 10.1074/jbc.M806088200 (2009).
    • (2009) JBC , vol.284 , pp. 2363-2373
    • Young, J.E.1    Martinez, R.A.2    La Spada, A.R.3
  • 28
    • 0034721844 scopus 로고    scopus 로고
    • Expression of a catalytically inactive sphingosine kinase mutant blocks agonist-induced sphingosine kinase activation A dominant-negative sphingosine kinase
    • Pitson, S. M. et al. Expression of a catalytically inactive sphingosine kinase mutant blocks agonist-induced sphingosine kinase activation. A dominant-negative sphingosine kinase. JBC 275, 33945-33950, doi: 10.1074/jbc.M006176200 (2000).
    • (2000) JBC , vol.275 , pp. 33945-33950
    • Pitson, S.M.1
  • 29
    • 84875365804 scopus 로고    scopus 로고
    • Autophagosomes form at ER-mitochondria contact sites
    • Hamasaki, M. et al. Autophagosomes form at ER-mitochondria contact sites. Nature, doi: 10.1038/nature11910 (2013).
    • (2013) Nature
    • Hamasaki, M.1
  • 30
    • 84875462369 scopus 로고    scopus 로고
    • Endoplasmic reticulum-endosome contact increases as endosomes traffic and mature
    • Friedman, J. R., Dibenedetto, J. R., West, M., Rowland, A. A., Voeltz, G. K. Endoplasmic reticulum-endosome contact increases as endosomes traffic and mature. Mol Biol of cell 24, 1030-1040, doi: 10.1091/mbc.E12-10-0733 (2013).
    • (2013) Mol Biol of Cell , vol.24 , pp. 1030-1040
    • Friedman, J.R.1    Dibenedetto, J.R.2    West, M.3    Rowland, A.A.4    Voeltz, G.K.5
  • 31
    • 67649600680 scopus 로고    scopus 로고
    • Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning
    • Rocha, N. et al. Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning. JCB 185, 1209-1225, doi: 10.1083/jcb.200811005 (2009).
    • (2009) JCB , vol.185 , pp. 1209-1225
    • Rocha, N.1
  • 32
    • 77955884684 scopus 로고    scopus 로고
    • Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins
    • Itakura, E., Mizushima, N. Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins. Autophagy 6, 764-776 (2010).
    • (2010) Autophagy , vol.6 , pp. 764-776
    • Itakura, E.1    Mizushima, N.2
  • 33
    • 84921366480 scopus 로고    scopus 로고
    • WIPI proteins: Essential PtdIns3P effectors at the nascent autophagosome
    • Proikas-Cezanne, T., Takacs, Z., Donnes, P., Kohlbacher, O. WIPI proteins: essential PtdIns3P effectors at the nascent autophagosome. J Cell Sci 128, 207-217, doi: 10.1242/jcs.146258 (2015).
    • (2015) J Cell Sci , vol.128 , pp. 207-217
    • Proikas-Cezanne, T.1    Takacs, Z.2    Donnes, P.3    Kohlbacher, O.4
  • 34
    • 57649227693 scopus 로고    scopus 로고
    • Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies
    • Sarkar, S., Ravikumar, B., Floto, R. A., Rubinsztein, D. C. Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. Cell death and diff 16, 46-56, doi:10.1038/cdd.2008.110 (2009).
    • (2009) Cell Death and Diff , vol.16 , pp. 46-56
    • Sarkar, S.1    Ravikumar, B.2    Floto, R.A.3    Rubinsztein, D.C.4
  • 35
    • 14844359962 scopus 로고    scopus 로고
    • Automated microscope system for determining factors that predict neuronal fate
    • Arrasate, M., Finkbeiner, S. Automated microscope system for determining factors that predict neuronal fate. PNAS USA 102, 3840-3845, doi: 10.1073/pnas.0409777102 (2005).
    • (2005) PNAS USA , vol.102 , pp. 3840-3845
    • Arrasate, M.1    Finkbeiner, S.2
  • 36
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., Finkbeiner, S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810, doi: 10.1038/nature02998 (2004).
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 37
    • 63249135140 scopus 로고    scopus 로고
    • Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease
    • Mitra, S., Tsvetkov, A. S., Finkbeiner, S. Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease. JBC 284, 4398-4403, doi: 10.1074/jbc.M806269200 (2009).
    • (2009) JBC , vol.284 , pp. 4398-4403
    • Mitra, S.1    Tsvetkov, A.S.2    Finkbeiner, S.3
  • 38
    • 70349640049 scopus 로고    scopus 로고
    • Protein turnover and inclusion body formation
    • Mitra, S., Tsvetkov, A. S., Finkbeiner, S. Protein turnover and inclusion body formation. Autophagy 5, 1037-1038 (2009).
    • (2009) Autophagy , vol.5 , pp. 1037-1038
    • Mitra, S.1    Tsvetkov, A.S.2    Finkbeiner, S.3
  • 39
    • 84873463075 scopus 로고    scopus 로고
    • Aberrant splicing of HTT generates the pathogenic exon 1 protein in Huntington disease
    • Sathasivam, K. et al. Aberrant splicing of HTT generates the pathogenic exon 1 protein in Huntington disease. PNAS USA 110, 2366-2370, doi: 10.1073/pnas.1221891110 (2013).
    • (2013) PNAS USA , vol.110 , pp. 2366-2370
    • Sathasivam, K.1
  • 40
    • 0033953015 scopus 로고    scopus 로고
    • Caspases and neurodegeneration: On the cutting edge of new therapeutic approaches
    • Wellington, C. L., Hayden, M. R. Caspases and neurodegeneration: on the cutting edge of new therapeutic approaches. Clin gen 57, 1-10 (2000).
    • (2000) Clin Gen , vol.57 , pp. 1-10
    • Wellington, C.L.1    Hayden, M.R.2
  • 41
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini, L. et al. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87, 493-506 (1996).
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1
  • 42
    • 65549163327 scopus 로고    scopus 로고
    • Cytoplasmic retention of polyglutamine-expanded androgen receptor ameliorates disease via autophagy in a mouse model of spinal and bulbar muscular atrophy
    • Montie, H. L. et al. Cytoplasmic retention of polyglutamine-expanded androgen receptor ameliorates disease via autophagy in a mouse model of spinal and bulbar muscular atrophy. Hum mol gen 18, 1937-1950, doi: Doi 10.1093/Hmg/Ddp115 (2009).
    • (2009) Hum Mol Gen , vol.18 , pp. 1937-1950
    • Montie, H.L.1
  • 44
    • 0142105397 scopus 로고    scopus 로고
    • Activation of sphingosine kinase 1 by ERK1/2-mediated phosphorylation
    • Pitson, S. M. et al. Activation of sphingosine kinase 1 by ERK1/2-mediated phosphorylation. EMBO 22, 5491-5500, doi: 10.1093/emboj/cdg540 (2003).
    • (2003) EMBO , vol.22 , pp. 5491-5500
    • Pitson, S.M.1
  • 45
    • 31144472414 scopus 로고    scopus 로고
    • Mutant huntingtin alters MAPK signaling pathways in PC12 and striatal cells: ERK1/2 protects against mutant huntingtin-associated toxicity
    • Apostol, B. L. et al. Mutant huntingtin alters MAPK signaling pathways in PC12 and striatal cells: ERK1/2 protects against mutant huntingtin-associated toxicity. Hum mol gen 15, 273-285, doi: 10.1093/hmg/ddi443 (2006).
    • (2006) Hum Mol Gen , vol.15 , pp. 273-285
    • Apostol, B.L.1
  • 46
    • 78650525484 scopus 로고    scopus 로고
    • ERK activation by the polyphenols fisetin and resveratrol provides neuroprotection in multiple models of Huntington's disease
    • Maher, P. et al. ERK activation by the polyphenols fisetin and resveratrol provides neuroprotection in multiple models of Huntington's disease. Hum mol gen 20, 261-270, doi: 10.1093/hmg/ddq460 (2011).
    • (2011) Hum Mol Gen , vol.20 , pp. 261-270
    • Maher, P.1
  • 47
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya, Y. et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO 19, 5720-5728, doi: 10.1093/emboj/19.21.5720 (2000).
    • (2000) EMBO , vol.19 , pp. 5720-5728
    • Kabeya, Y.1
  • 48
    • 34547659144 scopus 로고    scopus 로고
    • Bright monomeric red fluorescent protein with an extended fluorescence lifetime
    • Merzlyak, E. M. et al. Bright monomeric red fluorescent protein with an extended fluorescence lifetime. Nat meth 4, 555-557, doi: 10.1038/nmeth1062 (2007).
    • (2007) Nat Meth , vol.4 , pp. 555-557
    • Merzlyak, E.M.1
  • 49
    • 66349120877 scopus 로고    scopus 로고
    • Autophagy protects neuron from Abeta-induced cytotoxicity
    • Hung, S. Y., Huang, W. P., Liou, H. C., Fu, W. M. Autophagy protects neuron from Abeta-induced cytotoxicity. Autophagy 5, 502-510 (2009).
    • (2009) Autophagy , vol.5 , pp. 502-510
    • Hung, S.Y.1    Huang, W.P.2    Liou, H.C.3    Fu, W.M.4
  • 50
    • 84945214607 scopus 로고    scopus 로고
    • Isolation, characterization and antifungal docking studies of wortmannin isolated from Penicillium radicum
    • Singh, V. et al. Isolation, characterization and antifungal docking studies of wortmannin isolated from Penicillium radicum. Sci rep 5, 11948, doi: 10.1038/srep11948 (2015).
    • (2015) Sci Rep , vol.5 , pp. 11948
    • Singh, V.1
  • 51
    • 84904729990 scopus 로고    scopus 로고
    • Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models
    • Barmada, S. J. et al. Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models. Nat chem bio 10, 677-685, doi: 10.1038/nchembio.1563 (2014).
    • (2014) Nat Chem Bio , vol.10 , pp. 677-685
    • Barmada, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.