메뉴 건너뛰기




Volumn 5, Issue 12, 2014, Pages

Heme oxygenase-1 protects against Alzheimer's amyloid-β1-42-induced toxicity via carbon monoxide production

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; CARBON MONOXIDE; HEME OXYGENASE 1; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT; REACTIVE OXYGEN METABOLITE;

EID: 84927933879     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2014.529     Document Type: Article
Times cited : (78)

References (61)
  • 1
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ. Alzheimer's disease is a synaptic failure. Science 2002; 298: 789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 2
    • 0345276572 scopus 로고    scopus 로고
    • Synaptic slaughter in Alzheimer's disease
    • Coleman PD, Yao PJ. Synaptic slaughter in Alzheimer's disease. Neurobiol Aging 2003; 24: 1023-1027.
    • (2003) Neurobiol Aging , vol.24 , pp. 1023-1027
    • Coleman, P.D.1    Yao, P.J.2
  • 6
    • 24644453571 scopus 로고    scopus 로고
    • The role of apoptotic pathways in Alzheimer's disease neurodegeneration and cell death
    • LeBlanc AC. The role of apoptotic pathways in Alzheimer's disease neurodegeneration and cell death. Curr Alzheimer Res 2005; 2: 389-402.
    • (2005) Curr Alzheimer Res , vol.2 , pp. 389-402
    • Leblanc, A.C.1
  • 7
    • 33750292972 scopus 로고    scopus 로고
    • Cell death in the nervous system
    • Bredesen DE, Rao RV, Mehlen P. Cell death in the nervous system. Nature 2006; 443: 796-802.
    • (2006) Nature , vol.443 , pp. 796-802
    • Bredesen, D.E.1    Rao, R.V.2    Mehlen, P.3
  • 8
    • 33748473579 scopus 로고    scopus 로고
    • Molecular insights into mechanisms of the cell death program: Role in the progression of neurodegenerative disorders
    • Culmsee C, Landshamer S. Molecular insights into mechanisms of the cell death program: role in the progression of neurodegenerative disorders. Curr Alzheimer Res 2006; 3: 269-283.
    • (2006) Curr Alzheimer Res , vol.3 , pp. 269-283
    • Culmsee, C.1    Landshamer, S.2
  • 9
    • 33947628060 scopus 로고    scopus 로고
    • Molecular targets in cerebral ischemia for developing novel therapeutics
    • Mehta SL, Manhas N, Raghubir R. Molecular targets in cerebral ischemia for developing novel therapeutics. Brain Res Rev 2007; 54: 34-66.
    • (2007) Brain Res Rev , vol.54 , pp. 34-66
    • Mehta, S.L.1    Manhas, N.2    Raghubir, R.3
  • 10
    • 0029933840 scopus 로고    scopus 로고
    • Dementia after ischemic stroke: A population-based study in Rochester, Minnesota (1960-1984)
    • Kokmen E, Whisnant JP, O'Fallon WM, Chu CP, Beard CM. Dementia after ischemic stroke: a population-based study in Rochester, Minnesota (1960-1984). Neurology 1996; 46: 154-159.
    • (1996) Neurology , vol.46 , pp. 154-159
    • Kokmen, E.1    Whisnant, J.P.2    O'Fallon, W.M.3    Chu, C.P.4    Beard, C.M.5
  • 11
    • 0036714559 scopus 로고    scopus 로고
    • Incidence of dementia after ischemic stroke: Results of a longitudinal study
    • Desmond DW, Moroney JT, Sano M, Stern Y. Incidence of dementia after ischemic stroke: results of a longitudinal study. Stroke 2002; 33: 2254-2260.
    • (2002) Stroke , vol.33 , pp. 2254-2260
    • Desmond, D.W.1    Moroney, J.T.2    Sano, M.3    Stern, Y.4
  • 14
    • 0034662853 scopus 로고    scopus 로고
    • Ions, cell volume, and apoptosis
    • Yu SP, Choi DW. Ions, cell volume, and apoptosis. Proc Natl Acad Sci USA 2000; 97: 9360-9362.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9360-9362
    • Yu, S.P.1    Choi, D.W.2
  • 15
    • 0031451872 scopus 로고    scopus 로고
    • A primary role for K+ and Na+ efflux in the activation of apoptosis
    • Bortner CD, Hughes FM Jr, Cidlowski JA. A primary role for K+ and Na+ efflux in the activation of apoptosis. J Biol Chem 1997; 272: 32436-32442.
    • (1997) J Biol Chem , vol.272 , pp. 32436-32442
    • Bortner, C.D.1    Hughes, Jr.F.M.2    Cidlowski, J.A.3
  • 16
    • 15644374609 scopus 로고    scopus 로고
    • Intracellular K+ suppresses the activation of apoptosis in lymphocytes
    • Hughes FM Jr, Bortner CD, Purdy GD, Cidlowski JA. Intracellular K+ suppresses the activation of apoptosis in lymphocytes. J Biol Chem 1997; 272: 30567-30576.
    • (1997) J Biol Chem , vol.272 , pp. 30567-30576
    • Hughes, Jr.F.M.1    Bortner, C.D.2    Purdy, G.D.3    Cidlowski, J.A.4
  • 17
  • 18
    • 0042829363 scopus 로고    scopus 로고
    • Regulation and critical role of potassium homeostasis in apoptosis
    • Yu SP. Regulation and critical role of potassium homeostasis in apoptosis. Prog Neurobiol 2003; 70: 363-386.
    • (2003) Prog Neurobiol , vol.70 , pp. 363-386
    • Yu, S.P.1
  • 21
    • 10744230660 scopus 로고    scopus 로고
    • Crosstalk between nitric oxide and zinc pathways to neuronal cell death involving mitochondrial dysfunction and p38-activated K+ channels
    • Bossy-Wetzel E, Talantova MV, Lee WD, Scholzke MN, Harrop A, Mathews E et al. Crosstalk between nitric oxide and zinc pathways to neuronal cell death involving mitochondrial dysfunction and p38-activated K+ channels. Neuron 2004; 41: 351-365.
    • (2004) Neuron , vol.41 , pp. 351-365
    • Bossy-Wetzel, E.1    Talantova, M.V.2    Lee, W.D.3    Scholzke, M.N.4    Harrop, A.5    Mathews, E.6
  • 23
    • 79955674569 scopus 로고    scopus 로고
    • Carbon monoxide protects against oxidant-induced apoptosis via inhibition of Kv2.1
    • Dallas ML, Boyle JP, Milligan CJ, Sayer R, Kerrigan TL, McKinstry C et al. Carbon monoxide protects against oxidant-induced apoptosis via inhibition of Kv2.1. FASEB J 2011; 25: 1519-1530.
    • (2011) FASEB J , vol.25 , pp. 1519-1530
    • Dallas, M.L.1    Boyle, J.P.2    Milligan, C.J.3    Sayer, R.4    Kerrigan, T.L.5    McKinstry, C.6
  • 25
    • 79952135798 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid beta-peptide exposure
    • Thornton C, Bright NJ, Sastre M, Muckett PJ, Carling D. AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid beta-peptide exposure. Biochem J 2011; 434: 503-512.
    • (2011) Biochem J , vol.434 , pp. 503-512
    • Thornton, C.1    Bright, N.J.2    Sastre, M.3    Muckett, P.J.4    Carling, D.5
  • 26
    • 84865966647 scopus 로고    scopus 로고
    • JNK3 perpetuates metabolic stress induced by Abeta peptides
    • Yoon SO, Park DJ, Ryu JC, Ozer HG, Tep C, Shin YJ et al. JNK3 perpetuates metabolic stress induced by Abeta peptides. Neuron 2012; 75: 824-837.
    • (2012) Neuron , vol.75 , pp. 824-837
    • Yoon, S.O.1    Park, D.J.2    Ryu, J.C.3    Ozer, H.G.4    Tep, C.5    Shin, Y.J.6
  • 27
    • 8544257019 scopus 로고    scopus 로고
    • Heme oxygenase expression in human central nervous system disorders
    • Schipper HM. Heme oxygenase expression in human central nervous system disorders. Free Radic Biol Med 2004; 37: 1995-2011.
    • (2004) Free Radic Biol Med , vol.37 , pp. 1995-2011
    • Schipper, H.M.1
  • 29
    • 33645945014 scopus 로고    scopus 로고
    • Heme oxygenase-1/carbon monoxide: From basic science to therapeutic applications
    • Ryter SW, Alam J, Choi AM. Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications. Physiol Rev 2006; 86: 583-650.
    • (2006) Physiol Rev , vol.86 , pp. 583-650
    • Ryter, S.W.1    Alam, J.2    Choi, A.M.3
  • 30
    • 29844442868 scopus 로고    scopus 로고
    • Carbon monoxide: Endogenous production, physiological functions, and pharmacological applications
    • Wu L, Wang R. Carbon monoxide: endogenous production, physiological functions, and pharmacological applications. Pharmacol Rev 2005; 57: 585-630.
    • (2005) Pharmacol Rev , vol.57 , pp. 585-630
    • Wu, L.1    Wang, R.2
  • 31
    • 0033644002 scopus 로고    scopus 로고
    • Regulation and role of heme oxygenase in oxidative injury
    • Dennery PA. Regulation and role of heme oxygenase in oxidative injury. Curr Top Cell Regul 2000; 36: 181-199.
    • (2000) Curr Top Cell Regul , vol.36 , pp. 181-199
    • Dennery, P.A.1
  • 32
    • 0028929896 scopus 로고
    • Differential expression of heme oxygenase-1 in cultured cortical neurons and astrocytes determined by the aid of a new heme oxygenase antibody. Response to oxidative stress
    • Dwyer BE, Nishimura RN, Lu SY. Differential expression of heme oxygenase-1 in cultured cortical neurons and astrocytes determined by the aid of a new heme oxygenase antibody. Response to oxidative stress. Brain Res Mol Brain Res 1995; 30: 37-47.
    • (1995) Brain Res Mol Brain Res , vol.30 , pp. 37-47
    • Dwyer, B.E.1    Nishimura, R.N.2    Lu, S.Y.3
  • 33
    • 0031944692 scopus 로고    scopus 로고
    • Evidence of oxidative stress and in vivo neurotoxicity of beta-amyloid in a transgenic mouse model of Alzheimer's disease: A chronic oxidative paradigm for testing antioxidant therapies in vivo
    • Pappolla MA, Chyan YJ, Omar RA, Hsiao K, Perry G, Smith MA et al. Evidence of oxidative stress and in vivo neurotoxicity of beta-amyloid in a transgenic mouse model of Alzheimer's disease: a chronic oxidative paradigm for testing antioxidant therapies in vivo. Am J Pathol 1998; 152: 871-877.
    • (1998) Am J Pathol , vol.152 , pp. 871-877
    • Pappolla, M.A.1    Chyan, Y.J.2    Omar, R.A.3    Hsiao, K.4    Perry, G.5    Smith, M.A.6
  • 34
    • 0029032632 scopus 로고
    • Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain
    • Schipper HM, Cisse S, Stopa EG. Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain. Ann Neurol 1995; 37: 758-768.
    • (1995) Ann Neurol , vol.37 , pp. 758-768
    • Schipper, H.M.1    Cisse, S.2    Stopa, E.G.3
  • 36
    • 70349730056 scopus 로고    scopus 로고
    • Low doses of carbon monoxide protect against experimental focal brain ischemia
    • Zeynalov E, Dore S. Low doses of carbon monoxide protect against experimental focal brain ischemia. Neurotox Res 2009; 15: 133-137.
    • (2009) Neurotox Res , vol.15 , pp. 133-137
    • Zeynalov, E.1    Dore, S.2
  • 37
    • 84863793904 scopus 로고    scopus 로고
    • Carbon monoxide mediates the anti-apoptotic effects of heme oxygenase-1 in medulloblastoma DAOY cells via K+ channel inhibition
    • Al-Owais MM, Scragg JL, Dallas ML, Boycott HE, Warburton P, Chakrabarty A et al. Carbon monoxide mediates the anti-apoptotic effects of heme oxygenase-1 in medulloblastoma DAOY cells via K+ channel inhibition. J Biol Chem 2012; 287: 24754-24764.
    • (2012) J Biol Chem , vol.287 , pp. 24754-24764
    • Al-Owais, M.M.1    Scragg, J.L.2    Dallas, M.L.3    Boycott, H.E.4    Warburton, P.5    Chakrabarty, A.6
  • 38
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 2009; 457: 1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 39
    • 84875981923 scopus 로고    scopus 로고
    • Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1
    • Rushworth JV, Griffiths HH, Watt NT, Hooper NM. Prion protein-mediated toxicity of amyloid-beta oligomers requires lipid rafts and the transmembrane LRP1. J Biol Chem 2013; 288: 8935-8951.
    • (2013) J Biol Chem , vol.288 , pp. 8935-8951
    • Rushworth, J.V.1    Griffiths, H.H.2    Watt, N.T.3    Hooper, N.M.4
  • 40
    • 84887851652 scopus 로고    scopus 로고
    • Amyloid-beta nanotubes are associated with prion protein-dependent synaptotoxicity
    • Nicoll AJ, Panico S, Freir DB, Wright D, Terry C, Risse E et al. Amyloid-beta nanotubes are associated with prion protein-dependent synaptotoxicity. Nat Commun 2013; 4: 2416.
    • (2013) Nat Commun , vol.4 , pp. 2416
    • Nicoll, A.J.1    Panico, S.2    Freir, D.B.3    Wright, D.4    Terry, C.5    Risse, E.6
  • 41
    • 0025868208 scopus 로고
    • The identification of heme oxygenase as a major hypoxic stress protein in Chinese hamster ovary cells
    • Murphy BJ, Laderoute KR, Short SM, Sutherland RM. The identification of heme oxygenase as a major hypoxic stress protein in Chinese hamster ovary cells. Br J Cancer 1991; 64: 69-73.
    • (1991) Br J Cancer , vol.64 , pp. 69-73
    • Murphy, B.J.1    Laderoute, K.R.2    Short, S.M.3    Sutherland, R.M.4
  • 42
    • 0031041377 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia
    • Lee PJ, Jiang BH, Chin BY, Iyer NV, Alam J, Semenza GL et al. Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia. J Biol Chem 1997; 272: 5375-5381.
    • (1997) J Biol Chem , vol.272 , pp. 5375-5381
    • Lee, P.J.1    Jiang, B.H.2    Chin, B.Y.3    Iyer, N.V.4    Alam, J.5    Semenza, G.L.6
  • 43
    • 50849112415 scopus 로고    scopus 로고
    • Inhibitors of the heme oxygenase-carbon monoxide system: On the doorstep of the clinic?
    • Kinobe RT, Dercho RA, Nakatsu K. Inhibitors of the heme oxygenase-carbon monoxide system: on the doorstep of the clinic? Can J Physiol Pharmacol 2008; 86: 577-599.
    • (2008) Can J Physiol Pharmacol , vol.86 , pp. 577-599
    • Kinobe, R.T.1    Dercho, R.A.2    Nakatsu, K.3
  • 45
    • 0034046911 scopus 로고    scopus 로고
    • Neurons overexpressing heme oxygenase-1 resist oxidative stress-mediated cell death
    • Chen K, Gunter K, Maines MD. Neurons overexpressing heme oxygenase-1 resist oxidative stress-mediated cell death. J Neurochem 2000; 75: 304-313.
    • (2000) J Neurochem , vol.75 , pp. 304-313
    • Chen, K.1    Gunter, K.2    Maines, M.D.3
  • 46
    • 84867070957 scopus 로고    scopus 로고
    • Unregulated brain iron deposition in transgenic mice over-expressing HMOX1 in the astrocytic compartment
    • Song W, Zukor H, Lin SH, Liberman A, Tavitian A, Mui J et al. Unregulated brain iron deposition in transgenic mice over-expressing HMOX1 in the astrocytic compartment. J Neurochem 2012; 123: 325-336.
    • (2012) J Neurochem , vol.123 , pp. 325-336
    • Song, W.1    Zukor, H.2    Lin, S.H.3    Liberman, A.4    Tavitian, A.5    Mui, J.6
  • 47
    • 67649628772 scopus 로고    scopus 로고
    • Heme oxygenase-1 and neurodegeneration: Expanding frontiers of engagement
    • Schipper HM, Song W, Zukor H, Hascalovici JR, Zeligman D. Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement. J Neurochem 2009; 110: 469-485.
    • (2009) J Neurochem , vol.110 , pp. 469-485
    • Schipper, H.M.1    Song, W.2    Zukor, H.3    Hascalovici, J.R.4    Zeligman, D.5
  • 48
    • 67649617842 scopus 로고    scopus 로고
    • Suppression of glial HO-1 activity as a potential neurotherapeutic intervention in AD
    • Schipper HM, Gupta A, Szarek WA. Suppression of glial HO-1 activity as a potential neurotherapeutic intervention in AD. Curr Alzheimer Res 2009; 6: 424-430.
    • (2009) Curr Alzheimer Res , vol.6 , pp. 424-430
    • Schipper, H.M.1    Gupta, A.2    Szarek, W.A.3
  • 49
    • 34247171289 scopus 로고    scopus 로고
    • Hypoxia-mediated induction of heme oxygenase type i and carbon monoxide release from astrocytes protects nearby cerebral neurons from hypoxia-mediated apoptosis
    • Imuta N, Hori O, Kitao Y, Tabata Y, Yoshimoto T, Matsuyama T et al. Hypoxia-mediated induction of heme oxygenase type I and carbon monoxide release from astrocytes protects nearby cerebral neurons from hypoxia-mediated apoptosis. Antioxid Redox Signal 2007; 9: 543-552.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 543-552
    • Imuta, N.1    Hori, O.2    Kitao, Y.3    Tabata, Y.4    Yoshimoto, T.5    Matsuyama, T.6
  • 50
    • 0035799312 scopus 로고    scopus 로고
    • Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region
    • Perera WS, Hooper NM. Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region. Curr Biol 2001; 11: 519-523.
    • (2001) Curr Biol , vol.11 , pp. 519-523
    • Perera, W.S.1    Hooper, N.M.2
  • 51
    • 84866065959 scopus 로고    scopus 로고
    • Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
    • Um JW, Nygaard HB, Heiss JK, Kostylev MA, Stagi M, Vortmeyer A et al. Alzheimer amyloid-beta oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nat Neurosci 2012; 15: 1227-1235.
    • (2012) Nat Neurosci , vol.15 , pp. 1227-1235
    • Um, J.W.1    Nygaard, H.B.2    Heiss, J.K.3    Kostylev, M.A.4    Stagi, M.5    Vortmeyer, A.6
  • 52
    • 79956110918 scopus 로고    scopus 로고
    • The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication
    • Resenberger UK, Harmeier A, Woerner AC, Goodman JL, Muller V, Krishnan R et al. The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication. EMBO J 2011; 30: 2057-2070.
    • (2011) EMBO J , vol.30 , pp. 2057-2070
    • Resenberger, U.K.1    Harmeier, A.2    Woerner, A.C.3    Goodman, J.L.4    Muller, V.5    Krishnan, R.6
  • 53
    • 77956197815 scopus 로고    scopus 로고
    • Interaction between human prion protein and amyloid-beta (Abeta) oligomers: Role of N-terminal residues
    • Chen S, Yadav SP, Surewicz WK. Interaction between human prion protein and amyloid-beta (Abeta) oligomers: role OF N-terminal residues. J Biol Chem 2010; 285: 26377-26383.
    • (2010) J Biol Chem , vol.285 , pp. 26377-26383
    • Chen, S.1    Yadav, S.P.2    Surewicz, W.K.3
  • 54
    • 71649085107 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: A new hope to counteract neurodegeneration?
    • Correia SC, Moreira PI. Hypoxia-inducible factor 1: a new hope to counteract neurodegeneration? J Neurochem 2010; 112: 1-12.
    • (2010) J Neurochem , vol.112 , pp. 1-12
    • Correia, S.C.1    Moreira, P.I.2
  • 55
    • 0004491134 scopus 로고    scopus 로고
    • Enhancement of outward potassium current may participate in beta-amyloid peptide-induced cortical neuronal death
    • Yu SP, Farhangrazi ZS, Ying HS, Yeh CH, Choi DW. Enhancement of outward potassium current may participate in beta-amyloid peptide-induced cortical neuronal death. Neurobiol Dis 1998; 5: 81-88.
    • (1998) Neurobiol Dis , vol.5 , pp. 81-88
    • Yu, S.P.1    Farhangrazi, Z.S.2    Ying, H.S.3    Yeh, C.H.4    Choi, D.W.5
  • 57
    • 84891454249 scopus 로고    scopus 로고
    • The prion protein modulates A-type K+ currents mediated by Kv4.2 complexes through dipeptidyl aminopeptidase-like protein 6
    • Mercer RC, Ma L, Watts JC, Strome R, Wohlgemuth S, Yang J et al. The prion protein modulates A-type K+ currents mediated by Kv4.2 complexes through dipeptidyl aminopeptidase-like protein 6. J Biol Chem 2013; 288: 37241-37255.
    • (2013) J Biol Chem , vol.288 , pp. 37241-37255
    • Mercer, R.C.1    Ma, L.2    Watts, J.C.3    Strome, R.4    Wohlgemuth, S.5    Yang, J.6
  • 58
    • 84862976418 scopus 로고    scopus 로고
    • Calcium channel blockers and Alzheimer's disease: Potential relevance in treatment strategies of metabolic syndrome
    • Goodison WV, Frisardi V, Kehoe PG. Calcium channel blockers and Alzheimer's disease: potential relevance in treatment strategies of metabolic syndrome. J Alzheimers Dis 2012; 30: S269-S282.
    • (2012) J Alzheimers Dis , vol.30 , pp. S269-S282
    • Goodison, W.V.1    Frisardi, V.2    Kehoe, P.G.3
  • 59
    • 84876078566 scopus 로고    scopus 로고
    • The CAMKK2-AMPK Kinase Pathway Mediates the Synaptotoxic Effects of Abeta Oligomers through Tau Phosphorylation
    • Mairet-Coello G, Courchet J, Pieraut S, Courchet V, Maximov A, Polleux F. The CAMKK2-AMPK Kinase Pathway Mediates the Synaptotoxic Effects of Abeta Oligomers through Tau Phosphorylation. Neuron 2013; 78: 94-108.
    • (2013) Neuron , vol.78 , pp. 94-108
    • Mairet-Coello, G.1    Courchet, J.2    Pieraut, S.3    Courchet, V.4    Maximov, A.5    Polleux, F.6
  • 60
    • 77956323967 scopus 로고    scopus 로고
    • The therapeutic potential of carbon monoxide
    • Motterlini R, Otterbein LE. The therapeutic potential of carbon monoxide. Nat Rev Drug Discov 2010; 9: 728-743.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 728-743
    • Motterlini, R.1    Otterbein, L.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.