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Volumn 1417, Issue , 2011, Pages 103-114

Proteolytic breakdown of cytoskeleton induces neurodegeneration during pathology of murine cerebral malaria

Author keywords

Calpain; Caspase; Cathepsin b; Cerebral malaria; Neurofilament; Post synaptic density protein 95; Synaptophysin; Vimentin

Indexed keywords

CALPAIN 1; CASPASE 3; CATHEPSIN B; NERVE PROTEIN; POST SYNAPTIC DENSITY PROTEIN 95; PROTEINASE; SYNAPTOPHYSIN; UNCLASSIFIED DRUG; VIMENTIN;

EID: 80053234734     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2011.08.025     Document Type: Article
Times cited : (4)

References (54)
  • 3
    • 0032848049 scopus 로고    scopus 로고
    • Pathophysiology of perinatal brain damage
    • DOI 10.1016/S0165-0173(99)00009-0, PII S0165017399000090
    • R. Berger, and Y. Garnier Pathophysiology of perinatal brain damage Brain Res. Brain Res. Rev. 30 1999 107 134 (Pubitemid 29440936)
    • (1999) Brain Research Reviews , vol.30 , Issue.2 , pp. 107-134
    • Berger, R.1    Garnier, Y.2
  • 4
    • 33646344203 scopus 로고    scopus 로고
    • Harbouring in the brain: A focus on immune evasion mechanisms and their deleterious effects in malaria and human African trypanosomiasis
    • DOI 10.1016/j.ijpara.2006.02.001, PII S0020751906000312, Blood-Brain Barrier in Parasitic Disease
    • S. Bisser, O.N. Ouwe-Missi-Oukem-Boyer, F.S. Toure, Z. Taoufiq, B. Bouteille, and A. Buguet Harbouring in the brain: a focus on immune evasion mechanisms and their deleterious effects in malaria and human African trypanosomiasis Int. J. Parasitol. 36 2006 529 540 (Pubitemid 43674513)
    • (2006) International Journal for Parasitology , vol.36 , Issue.5 , pp. 529-540
    • Bisser, S.1    Ouwe-Missi-Oukem-Boyer, O.N.2    Toure, F.S.3    Taoufiq, Z.4    Bouteille, B.5    Buguet, A.6    Mazier, D.7
  • 5
    • 52549100837 scopus 로고    scopus 로고
    • Activation of calpain, cathepsin-b and caspase-3 during transient focal cerebral ischemia in rat model
    • G.V. Chaitanya, and P.P. Babu Activation of calpain, cathepsin-b and caspase-3 during transient focal cerebral ischemia in rat model Neurochem. Res. 33 2008 2178 2186
    • (2008) Neurochem. Res. , vol.33 , pp. 2178-2186
    • Chaitanya, G.V.1    Babu, P.P.2
  • 6
    • 67449128454 scopus 로고    scopus 로고
    • Differential PARP cleavage: An indication of heterogeneous forms of cell death and involvement of multiple proteases in the infarct of focal cerebral ischemia in rat
    • G.V. Chaitanya, and P.P. Babu Differential PARP cleavage: an indication of heterogeneous forms of cell death and involvement of multiple proteases in the infarct of focal cerebral ischemia in rat Cell. Mol. Neurobiol. 29 2009 563 573
    • (2009) Cell. Mol. Neurobiol. , vol.29 , pp. 563-573
    • Chaitanya, G.V.1    Babu, P.P.2
  • 7
    • 73749085727 scopus 로고    scopus 로고
    • Granzyme-b is involved in mediating post-ischemic neuronal death during focal cerebral ischemia in rat model
    • G.V. Chaitanya, M. Schwaninger, J.S. Alexander, and P.P. Babu Granzyme-b is involved in mediating post-ischemic neuronal death during focal cerebral ischemia in rat model Neuroscience 165 2010 1203 1216
    • (2010) Neuroscience , vol.165 , pp. 1203-1216
    • Chaitanya, G.V.1    Schwaninger, M.2    Alexander, J.S.3    Babu, P.P.4
  • 10
    • 23244440196 scopus 로고    scopus 로고
    • The actin cytoskeleton: Integrating form and function at the synapse
    • DOI 10.1146/annurev.neuro.28.061604.135757
    • C. Dillon, and Y. Goda The actin cytoskeleton: integrating form and function at the synapse Annu. Rev. Neurosci. 28 2005 25 55 (Pubitemid 41098898)
    • (2005) Annual Review of Neuroscience , vol.28 , pp. 25-55
    • Dillon, C.1    Goda, Y.2
  • 13
    • 0034949086 scopus 로고    scopus 로고
    • Characterization of the necrotic cleavage of poly (ADP-ribose) polymerase (PARP-1): Implication of lysosomal proteases
    • DOI 10.1038/sj.cdd.4400851
    • S. Gobeil, C.C. Boucher, D. Nadeau, and G.G. Poirier Characterization of the necrotic cleavage of poly(ADP-ribose) polymerase (PARP-1): implication of lysosomal proteases Cell Death Differ. 8 2001 588 594 (Pubitemid 32586595)
    • (2001) Cell Death and Differentiation , vol.8 , Issue.6 , pp. 588-594
    • Gobeil, S.1    Boucher, C.C.2    Nadeau, D.3    Poirier, G.G.4
  • 15
    • 57649178045 scopus 로고    scopus 로고
    • Short report: Failure of two distinct anti-apoptotic approaches to reduce mortality in experimental cerebral malaria
    • A.J. Helmers, F.E. Lovegrove, J.M. Harlan, K.C. Kain, and W.C. Liles Short report: failure of two distinct anti-apoptotic approaches to reduce mortality in experimental cerebral malaria Am. J. Trop. Med. Hyg. 79 2008 823 825
    • (2008) Am. J. Trop. Med. Hyg. , vol.79 , pp. 823-825
    • Helmers, A.J.1    Lovegrove, F.E.2    Harlan, J.M.3    Kain, K.C.4    Liles, W.C.5
  • 16
    • 17644393902 scopus 로고    scopus 로고
    • Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors
    • DOI 10.1074/jbc.M500939200
    • M. Higuchi, M. Tomioka, J. Takano, K. Shirotani, N. Iwata, and H. Masumoto Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors J. Biol. Chem. 280 2005 15229 15237 (Pubitemid 40562879)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15229-15237
    • Higuchi, M.1    Tomioka, M.2    Takano, J.3    Shirotani, K.4    Iwata, N.5    Masumoto, H.6    Maki, M.7    Itohara, S.8    Saido, T.C.9
  • 18
    • 27744563110 scopus 로고    scopus 로고
    • Pathogenesis, clinical features, and neurological outcome of cerebral malaria
    • DOI 10.1016/S1474-4422(05)70247-7, PII S1474442205702477
    • R. Idro, N.E. Jenkins, and C.R. Newton Pathogenesis, clinical features, and neurological outcome of cerebral malaria Lancet Neurol. 4 2005 827 840 (Pubitemid 41619438)
    • (2005) Lancet Neurology , vol.4 , Issue.12 , pp. 827-840
    • Idro, R.1    Jenkins, N.E.2    Newton, C.R.J.3
  • 19
    • 33644637973 scopus 로고    scopus 로고
    • Risk factors for persisting neurological and cognitive impairments following cerebral malaria
    • DOI 10.1136/adc.2005.077784
    • R. Idro, J.A. Carter, G. Fegan, B.G.R. Neville, and C.R.J.C. Newton Risk factors for persisting neurological and cognitive impairments following cerebral malaria Arch. Dis. Child. 91 2006 142 148 (Pubitemid 43362519)
    • (2006) Archives of Disease in Childhood , vol.91 , Issue.2 , pp. 142-148
    • Idro, R.1    Carter, J.A.2    Fegan, G.3    Neville, B.G.R.4    Newton, C.R.J.C.5
  • 20
    • 44449105631 scopus 로고    scopus 로고
    • Plasma IP-10, apoptotic and angiogenic factors associated with fatal cerebral malaria in India
    • V. Jain, H.B. Armah, J.E. Tongren, R.M. Ned, N.O. Wilson, and S. Crawford Plasma IP-10, apoptotic and angiogenic factors associated with fatal cerebral malaria in India Malar. J. 7 2008 83
    • (2008) Malar. J. , vol.7 , pp. 83
    • Jain, V.1    Armah, H.B.2    Tongren, J.E.3    Ned, R.M.4    Wilson, N.O.5    Crawford, S.6
  • 21
    • 0027518491 scopus 로고
    • Cytoadherence of Plasmodium falciparum-infected erythrocytes to microvascular endothelium is regulatable by cytokines and phorbol ester
    • J.K. Johnson, R.A. Swerlick, K.K. Grady, P. Millet, and T.M. Wick Cytoadherence of Plasmodium falciparum-infected erythrocytes to microvascular endothelium is regulatable by cytokines and phorbol ester J. Infect. Dis. 167 1993 698 703 (Pubitemid 23056337)
    • (1993) Journal of Infectious Diseases , vol.167 , Issue.3 , pp. 698-703
    • Johnson, J.K.1    Swerlick, R.A.2    Grady, K.K.3    Millet, P.4    Wick, T.M.5
  • 22
    • 0034011860 scopus 로고    scopus 로고
    • Caspases cleave the amino-terminal calpain inhibitory unit of calpastatin during apoptosis in human Jurkat T cells
    • M. Kato, T. Nonaka, M. Maki, H. Kikuchi, and S. Imajoh-Ohmi Caspases cleave the amino-terminal calpain inhibitory unit of calpastatin during apoptosis in human Jurkat T cells J. Biochem. 127 2000 297 305 (Pubitemid 30136913)
    • (2000) Journal of Biochemistry , vol.127 , Issue.2 , pp. 297-305
    • Kato, M.1    Nonaka, T.2    Maki, M.3    Kikuchi, H.4    Imajoh-Ohmi, S.5
  • 26
    • 0026928705 scopus 로고
    • Overview: Pathophysiology and management of cerebral malaria
    • S. Looareesuwan Overview: pathophysiology and management of cerebral malaria Southeast Asian J. Trop. Med. Public Health 23 Suppl 4 1992 155 165
    • (1992) Southeast Asian J. Trop. Med. Public Health , vol.23 , Issue.SUPPL 4 , pp. 155-165
    • Looareesuwan, S.1
  • 27
    • 33748692883 scopus 로고    scopus 로고
    • Detection and localization of calpain 3-like protease in a neuronal cell line: Possible regulation of apoptotic cell death through degradation of nuclear IκBα
    • DOI 10.1016/j.biocel.2006.06.005, PII S1357272506001932
    • A. Marcilhac, F. Raynaud, I. Clerc, and Y. Benyamin Detection and localization of calpain 3-like protease in a neuronal cell line: possible regulation of apoptotic cell death through degradation of nuclear I kappa B alpha Int. J. Biochem. Cell Biol. 38 2006 2128 2140 (Pubitemid 44397620)
    • (2006) International Journal of Biochemistry and Cell Biology , vol.38 , Issue.12 , pp. 2128-2140
    • Marcilhac, A.1    Raynaud, F.2    Clerc, I.3    Benyamin, Y.4
  • 28
    • 0033058875 scopus 로고    scopus 로고
    • Recent advances on neuronal caspases in development and neurodegeneration
    • DOI 10.1016/S0197-0186(99)00061-3, PII S0197018699000613
    • N. Marks, and M.J. Berg Recent advances on neuronal caspases in development and neurodegeneration Neurochem. Int. 35 1999 195 220 (Pubitemid 29320083)
    • (1999) Neurochemistry International , vol.35 , Issue.3 , pp. 195-220
    • Marks, N.1    Berg, M.J.2
  • 29
    • 33646337645 scopus 로고    scopus 로고
    • Human cerebral malaria and the blood-brain barrier
    • DOI 10.1016/j.ijpara.2006.02.004, PII S0020751906000610, Blood-Brain Barrier in Parasitic Disease
    • I.M. Medana, and G.D. Turner Human cerebral malaria and the blood-brain barrier Int. J. Parasitol. 36 2006 555 568 (Pubitemid 43674514)
    • (2006) International Journal for Parasitology , vol.36 , Issue.5 , pp. 555-568
    • Medana, I.M.1    Turner, G.D.H.2
  • 30
    • 33947421712 scopus 로고    scopus 로고
    • Plasmodium falciparum, and the Blood-Brain Barrier - Contacts and Consequences
    • DOI 10.1086/512089
    • I.M. Medana, and G.D. Turner Plasmodium falciparum and the blood-brain barrier-contacts and consequences J. Infect. Dis. 195 2007 921 923 (Pubitemid 46452094)
    • (2007) Journal of Infectious Diseases , vol.195 , Issue.7 , pp. 921-923
    • Medana, I.M.1    Turner, G.D.H.2
  • 31
    • 46249084578 scopus 로고    scopus 로고
    • Worms and malaria: Blind men feeling the elephant?
    • DOI 10.1017/S0031182008000358, PII S0031182008000358
    • M. Nacher Worms and malaria: blind men feeling the elephant? Parasitology 135 2008 861 868 (Pubitemid 351913471)
    • (2008) Parasitology , vol.135 , Issue.7 , pp. 861-868
    • Nacher, M.1
  • 32
    • 0037648485 scopus 로고    scopus 로고
    • Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis
    • DOI 10.1074/jbc.M212255200
    • R.W. Neumar, Y.A. Xu, H. Gada, R.P. Guttmann, and R. Siman Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis J. Biol. Chem. 278 2003 14162 14167 (Pubitemid 36799963)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14162-14167
    • Neumar, R.W.1    Xu, Y.A.2    Gada, H.3    Guttmann, R.P.4    Siman, R.5
  • 34
    • 1342326755 scopus 로고    scopus 로고
    • Redox-Dependent Apoptosis in Human Endothelial Cells after Adhesion of Plasmodium falciparum - Infected Erythrocytes
    • DOI 10.1196/annals.1299.109
    • P. Pino, I. Vouldoukis, N. Dugas, G. Hassani-Loppion, B. Dugas, and D. Mazier Redox-dependent apoptosis in human endothelial cells after adhesion of Plasmodium falciparum-infected erythrocytes Ann. N. Y. Acad. Sci. 1010 2003 582 586 (Pubitemid 38265050)
    • (2003) Annals of the New York Academy of Sciences , vol.1010 , pp. 582-586
    • Pino, P.1    Vouldoukis, I.2    Dugas, N.3    Hassani-Loppion, G.4    Dugas, B.5    Mazier, D.6
  • 36
    • 23744492477 scopus 로고    scopus 로고
    • Blood-brain barrier breakdown during cerebral malaria: Suicide or murder?
    • DOI 10.1160/TH05-05-0354
    • P. Pino, Z. Taoufiq, J. Nitcheu, I. Vouldoukis, and D. Mazier Blood-brain barrier breakdown during cerebral malaria: suicide or murder? Thromb. Haemost. 94 2005 336 340 (Pubitemid 41122488)
    • (2005) Thrombosis and Haemostasis , vol.94 , Issue.2 , pp. 336-340
    • Pino, P.1    Taoufiq, Z.2    Nitcheu, J.3    Vouldoukis, I.4    Mazier, D.5
  • 37
    • 0038725886 scopus 로고    scopus 로고
    • Ischemic neuronal death in the rat hippocampus: The calpain-calpastatin- caspase hypothesis
    • DOI 10.1016/S0969-9961(03)00018-4
    • A. Rami Ischemic neuronal death in the rat hippocampus: the calpain-calpastatin-caspase hypothesis Neurobiol. Dis. 13 2003 75 88 (Pubitemid 36793974)
    • (2003) Neurobiology of Disease , vol.13 , Issue.2 , pp. 75-88
    • Rami, A.1
  • 38
    • 33746126134 scopus 로고    scopus 로고
    • Implication of calpain in neuronal apoptosis: A possible regulation of Alzheimer's disease
    • DOI 10.1111/j.1742-4658.2006.05352.x
    • F. Raynaud, and A. Marcilhac Implication of calpain in neuronal apoptosis-a possible regulation of Alzheimer's disease FEBS J. 273 2006 3437 3443 (Pubitemid 44086944)
    • (2006) FEBS Journal , vol.273 , Issue.15 , pp. 3437-3443
    • Raynaud, F.1    Marcilhac, A.2
  • 39
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • DOI 10.1038/nrm1496
    • S.J. Riedl, and Y.G. Shi Molecular mechanisms of caspase regulation during apoptosis Nat. Rev. Mol. Cell Biol. 5 2004 897 907 (Pubitemid 39486541)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.11 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 40
    • 0034922481 scopus 로고    scopus 로고
    • The role of cerebral oedema in the pathogenesis of cerebral malaria
    • DOI 10.1179/135100001101536238
    • L.A. Sanni The role of cerebral oedema in the pathogenesis of cerebral malaria Redox Rep. 6 2001 137 142 (Pubitemid 32694475)
    • (2001) Redox Report , vol.6 , Issue.3 , pp. 137-142
    • Sanni, L.A.1
  • 41
    • 29244461405 scopus 로고    scopus 로고
    • Activation of calpains, calpastatin and spectrin cleavage in the brain during the pathology of fatal murine cerebral malaria
    • DOI 10.1016/j.neuint.2005.09.001, PII S0197018605002299
    • M. Shukla, Y. Rajgopal, and P.P. Babu Activation of calpains, calpastatin and spectrin cleavage in the brain during the pathology of fatal murine cerebral malaria Neurochem. Int. 48 2006 108 113 (Pubitemid 41832445)
    • (2006) Neurochemistry International , vol.48 , Issue.2 , pp. 108-113
    • Shukla, M.1    Rajgopal, Y.2    Babu, P.P.3
  • 42
    • 27644472289 scopus 로고    scopus 로고
    • E2F1 induces cell death, calpain activation, and MDMX degradation in a transcription independent manner implicating a novel role for E2F1 in neuronal loss in SIV encephalitis
    • DOI 10.1002/jcb.20574
    • G.D. Strachan, M.A. Koike, R. Siman, D.J. Hall, and K.L. Jordan-Sciutto E2F1 induces cell death, calpain activation, and MDMX degradation in a transcription independent manner implicating a novel role for E2F1 in neuronal loss in SIV encephalitis J. Cell. Biochem. 96 2005 728 740 (Pubitemid 41567544)
    • (2005) Journal of Cellular Biochemistry , vol.96 , Issue.4 , pp. 728-740
    • Strachan, G.D.1    Koike, M.A.2    Siman, R.3    Hall, D.J.4    Jordan-Sciutto, K.L.5
  • 43
    • 0037047484 scopus 로고    scopus 로고
    • Calpain-dependent neurofilament breakdown in anoxic and ischemic rat central axons
    • DOI 10.1016/S0304-3940(02)00469-X, PII S030439400200469X
    • P.K. Stys, and Q.B. Jiang Calpain-dependent neurofilament breakdown in anoxic and ischemic rat central axons Neurosci. Lett. 328 2002 150 154 (Pubitemid 34804732)
    • (2002) Neuroscience Letters , vol.328 , Issue.2 , pp. 150-154
    • Stys, P.K.1    Jiang, Q.2
  • 44
    • 24144468635 scopus 로고    scopus 로고
    • Calpain-dependent α-fodrin cleavage at the sarcolemma in muscle diseases
    • DOI 10.1002/mus.20362
    • M. Takamure, K.Y. Murata, Y. Tamada, M. Azuma, and S. Ueno Calpain-dependent alpha-fodrin cleavage at the sarcolemma in muscle diseases Muscle Nerve 32 2005 303 309 (Pubitemid 41232613)
    • (2005) Muscle and Nerve , vol.32 , Issue.3 , pp. 303-309
    • Takamure, M.1    Murata, K.-Y.2    Tamada, Y.3    Azuma, M.4    Ueno, S.5
  • 45
    • 51349169541 scopus 로고    scopus 로고
    • In vitro susceptibility of P. falciparum isolates from Abidjan (Cote d'Ivoire) to quinine, artesunate and chloroquine
    • A.O. Toure, L.P. Kone, R. Jambou, T.D. Konan, S. Demba, and G.E. Beugre In vitro susceptibility of P. falciparum isolates from Abidjan (Cote d'Ivoire) to quinine, artesunate and chloroquine Sante 18 2008 43 47
    • (2008) Sante , vol.18 , pp. 43-47
    • Toure, A.O.1    Kone, L.P.2    Jambou, R.3    Konan, T.D.4    Demba, S.5    Beugre, G.E.6
  • 46
    • 33749266350 scopus 로고    scopus 로고
    • A unified hypothesis for the genesis of cerebral malaria: Sequestration, inflammation and hemostasis leading to microcirculatory dysfunction
    • DOI 10.1016/j.pt.2006.09.002, PII S1471492206002352
    • H.C. van der Heyde, J. Nolan, V. Combes, I. Gramaglia, and Grau A unified hypothesis for the genesis of cerebral malaria: sequestration, inflammation and hemostasis leading to microcirculatory dysfunction Trends Parasitol. 22 2006 503 508 (Pubitemid 44479847)
    • (2006) Trends in Parasitology , vol.22 , Issue.11 , pp. 503-508
    • Van Der Heyde, H.C.1    Nolan, J.2    Combes, V.3    Gramaglia, I.4    Grau, G.E.5
  • 47
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • DOI 10.1016/S0166-2236(99)01479-4, PII S0166223699014794
    • K.K. Wang Calpain and caspase: can you tell the difference? Trends Neurosci. 23 2000 20 26 (Pubitemid 30100309)
    • (2000) Trends in Neurosciences , vol.23 , Issue.1 , pp. 20-26
    • Wang, K.K.W.1
  • 48
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • DOI 10.1016/S0166-2236(99)01479-4, PII S0166223699014794
    • K.K.W. Wang Calpain and caspase: can you tell the difference? Trends in Neurosci. 23 2000 20 26 (Pubitemid 30100309)
    • (2000) Trends in Neurosciences , vol.23 , Issue.1 , pp. 20-26
    • Wang, K.K.W.1
  • 49
    • 22544447638 scopus 로고    scopus 로고
    • Postmortem brain smear assessment of fatal malaria
    • author reply 547-8
    • N.J. White, and K. Silamut Postmortem brain smear assessment of fatal malaria J. Infect. Dis. 192 2005 547 author reply 547-8
    • (2005) J. Infect. Dis. , vol.192 , pp. 547
    • White, N.J.1    Silamut, K.2
  • 50
    • 33746263669 scopus 로고    scopus 로고
    • Neuronal apoptosis, metallothionein expression and proinflammatory responses during cerebral malaria in mice
    • DOI 10.1016/j.expneurol.2006.02.011, PII S0014488606000665
    • L. Wiese, J.A. Kurtzhals, and M. Penkowa Neuronal apoptosis, metallothionein expression and proinflammatory responses during cerebral malaria in mice Exp. Neurol. 200 2006 216 226 (Pubitemid 44097022)
    • (2006) Experimental Neurology , vol.200 , Issue.1 , pp. 216-226
    • Wiese, L.1    Kurtzhals, J.A.L.2    Penkowa, M.3
  • 51
    • 0035478060 scopus 로고    scopus 로고
    • Differential expression of apoptotic protease-activating factor-1 and caspase-3 genes and susceptibility to apoptosis during brain development and after traumatic brain injury
    • A.G. Yakovlev, K. Ota, G. Geping Wang, V. Vilen Movsesyan, W.L. Wei-Li Bao, and K. Yoshihara Differential expression of apoptotic protease-activating factor-1 and caspase-3 genes and susceptibility to apoptosis during brain development and after traumatic brain injury J. Neurosci. 21 2001 7439 7446 (Pubitemid 32904942)
    • (2001) Journal of Neuroscience , vol.21 , Issue.19 , pp. 7439-7446
    • Yakovlev, A.G.1    Ota, K.2    Wang, G.3    Movsesyan, V.4    Bao, W.-L.5    Yoshihara, K.6    Faden, A.I.7
  • 52
    • 0034739734 scopus 로고    scopus 로고
    • Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
    • DOI 10.1016/S0301-0082(00)00006-X, PII S030100820000006X
    • T. Yamashima Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates Prog. Neurobiol. 62 2000 273 295 (Pubitemid 30326777)
    • (2000) Progress in Neurobiology , vol.62 , Issue.3 , pp. 273-295
    • Yamashima, T.1
  • 53
    • 0242539781 scopus 로고    scopus 로고
    • Sustained calpain activation associated with lysosomal rupture executes necrosis of the postischemic CA1 neurons in primates
    • DOI 10.1002/hipo.10127
    • T. Yamashima, A.B. Tonchev, T. Tsukada, T.C. Saido, S. Imajoh-Ohmi, and T. Momoi Sustained calpain activation associated with lysosomal rupture executes necrosis of the postischemic CA1 neurons in primates Hippocampus 13 2003 791 800 (Pubitemid 37407965)
    • (2003) Hippocampus , vol.13 , Issue.7 , pp. 791-800
    • Yamashima, T.1    Tonchev, A.B.2    Tsukada, T.3    Saido, T.C.4    Imajoh-Ohmi, S.5    Momoi, T.6    Kominami, E.7
  • 54
    • 69849085156 scopus 로고    scopus 로고
    • The cytotoxic T lymphocyte protease granzyme A cleaves and inactivates poly (adenosine 5′-diphosphate-ribose) polymerase-1
    • P.C. Zhu, D. Martinvalet, D. Chowdhury, D. Zhang, A. Schlesinger, and Lieberman The cytotoxic T lymphocyte protease granzyme A cleaves and inactivates poly (adenosine 5′-diphosphate-ribose) polymerase-1 Blood 114 2009 1205 1216
    • (2009) Blood , vol.114 , pp. 1205-1216
    • Zhu, P.C.1    Martinvalet, D.2    Chowdhury, D.3    Zhang, D.4    Schlesinger, A.5    Lieberman6


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