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Volumn 6, Issue 11, 2011, Pages

Age-dependent changes in the proteome following complete spinal cord transection in a postnatal South American Opossum (Monodelphis domestica)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ENOLASE; BRAIN FATTY ACID BINDING PROTEIN; COFILIN 1; COLLAPSIN RESPONSE MEDIATOR PROTEIN; COLLAPSIN RESPONSE MEDIATOR PROTEIN 2A; COLLAPSIN RESPONSE MEDIATOR PROTEIN 3; FATTY ACID BINDING PROTEIN; GLUCOSE REGULATED PROTEIN 78; HEART FATTY ACID BINDING PROTEIN; HEAT SHOCK PROTEIN 10; HEAT SHOCK PROTEIN 60; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A2; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN B1; LIPOCORTIN 2; MESSENGER RNA; PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE A LIKE; PEPTIDYLPROLYL ISOMERASE B; PROTEIN 14 3 3; PROTEIN 14 3 3 EPSILON; PROTEIN 14 3 3 GAMMA; PROTEIN 14 3 3 ZETA; PROTEOME; TROPOMYOSIN; UBIQUITIN; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL 1;

EID: 81155128235     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027465     Document Type: Article
Times cited : (17)

References (78)
  • 2
    • 0027199358 scopus 로고
    • The early development of major projections from caudal levels of the spinal cord to the brainstem and cerebellum in the gray short-tailed Brazilian opossum, Monodelphis domestica
    • Qin YQ, Wang XM, Martin GF, (1993) The early development of major projections from caudal levels of the spinal cord to the brainstem and cerebellum in the gray short-tailed Brazilian opossum, Monodelphis domestica. Brain Res Dev Brain Res 75: 75-90.
    • (1993) Brain Res Dev Brain Res , vol.75 , pp. 75-90
    • Qin, Y.Q.1    Wang, X.M.2    Martin, G.F.3
  • 3
    • 0024383463 scopus 로고
    • Monodelphis domestica (grey short-tailed opossum): an accessible model for studies of early neocortical development
    • Saunders N, Adam E, Reader M, Møllgård K, (1989) Monodelphis domestica (grey short-tailed opossum): an accessible model for studies of early neocortical development. Anat Embryol (Berl) 180: 227-236.
    • (1989) Anat Embryol (Berl) , vol.180 , pp. 227-236
    • Saunders, N.1    Adam, E.2    Reader, M.3    Møllgård, K.4
  • 4
    • 0031975041 scopus 로고    scopus 로고
    • Development of walking, swimming and neuronal connections after complete spinal cord transection in neonatal opossum, Monodephis domestica
    • Saunders N, Kitchener P, Knott G, Nicholls J, Potter A, et al. (1998) Development of walking, swimming and neuronal connections after complete spinal cord transection in neonatal opossum, Monodephis domestica. J Neurosci 18: 339-355.
    • (1998) J Neurosci , vol.18 , pp. 339-355
    • Saunders, N.1    Kitchener, P.2    Knott, G.3    Nicholls, J.4    Potter, A.5
  • 5
    • 0032080263 scopus 로고    scopus 로고
    • Adult opossumns (Didelphis virginiana) demonstrate near normal locomotion after spinal cord transection as neonates
    • Wang X, Basso D, Terman J, Bresnahan J, Martin G, (1998) Adult opossumns (Didelphis virginiana) demonstrate near normal locomotion after spinal cord transection as neonates. Exp Neurol 151: 50-69.
    • (1998) Exp Neurol , vol.151 , pp. 50-69
    • Wang, X.1    Basso, D.2    Terman, J.3    Bresnahan, J.4    Martin, G.5
  • 6
    • 0032541462 scopus 로고    scopus 로고
    • Regeneration of supraspinal axons after transection of the thoracic spinal cord in the developing opossum, Didelphis virginiana
    • Wang X, Terman J, Martin G, (1998) Regeneration of supraspinal axons after transection of the thoracic spinal cord in the developing opossum, Didelphis virginiana. J Comp Neurol 398: 83-97.
    • (1998) J Comp Neurol , vol.398 , pp. 83-97
    • Wang, X.1    Terman, J.2    Martin, G.3
  • 7
    • 0142126329 scopus 로고    scopus 로고
    • Regeneration of supraspinal axons after complete transection of the thoracic spinal cord in neonatal opossums (Monodelphis domestica)
    • Fry E, Stolp H, Lane M, Dziegielewska K, Saunders N, (2003) Regeneration of supraspinal axons after complete transection of the thoracic spinal cord in neonatal opossums (Monodelphis domestica). J Comp Neurol 466: 422-444.
    • (2003) J Comp Neurol , vol.466 , pp. 422-444
    • Fry, E.1    Stolp, H.2    Lane, M.3    Dziegielewska, K.4    Saunders, N.5
  • 8
    • 80355136442 scopus 로고    scopus 로고
    • Spontaneous development of full weight-supported stepping after complete spinal cord transection in the neonatal opossum, Monodelphis domestica
    • Doi: 10.1371/journal.pone.0026826
    • Wheaton BJ, Callaway JK, Ek CJ, Dziegielewska KM, Saunders NR, (2011) Spontaneous development of full weight-supported stepping after complete spinal cord transection in the neonatal opossum, Monodelphis domestica. PLoS One pp. e26826 Doi:10.1371/journal.pone.0026826.
    • (2011) PLoS One
    • Wheaton, B.J.1    Callaway, J.K.2    Ek, C.J.3    Dziegielewska, K.M.4    Saunders, N.R.5
  • 9
    • 0018908523 scopus 로고
    • Axons from CNS neurones regenerate into PNS grafts
    • Richardson P, McGuinness U, Aguayo A, (1980) Axons from CNS neurones regenerate into PNS grafts. Nature 284: 264-265.
    • (1980) Nature , vol.284 , pp. 264-265
    • Richardson, P.1    McGuinness, U.2    Aguayo, A.3
  • 10
    • 0020040379 scopus 로고
    • Peripheral nerve autografts to the rat spinal cord: studies with axonal tracing methods
    • Richardson PM, McGuinness UM, Aguayo AJ, (1982) Peripheral nerve autografts to the rat spinal cord: studies with axonal tracing methods. Brain Res 237: 147-162.
    • (1982) Brain Res , vol.237 , pp. 147-162
    • Richardson, P.M.1    McGuinness, U.M.2    Aguayo, A.J.3
  • 11
    • 78751507491 scopus 로고    scopus 로고
    • Multipotent adult progenitor cells prevent macrophage-mediated axonal dieback and promote regrowth after spinal cord injury
    • Busch SA, Hamilton JA, Horn KP, Cuascut FX, Cutrone R, et al. (2011) Multipotent adult progenitor cells prevent macrophage-mediated axonal dieback and promote regrowth after spinal cord injury. J Neurosci 31: 944-953.
    • (2011) J Neurosci , vol.31 , pp. 944-953
    • Busch, S.A.1    Hamilton, J.A.2    Horn, K.P.3    Cuascut, F.X.4    Cutrone, R.5
  • 12
    • 78951487093 scopus 로고    scopus 로고
    • Cellular and paracellular transplants for spinal cord injury: a review of the literature
    • Mortazavi MM, Verma K, Tubbs RS, Theodore N, (2011) Cellular and paracellular transplants for spinal cord injury: a review of the literature. Childs Nerv Syst 27: 237-243.
    • (2011) Childs Nerv Syst , vol.27 , pp. 237-243
    • Mortazavi, M.M.1    Verma, K.2    Tubbs, R.S.3    Theodore, N.4
  • 13
    • 0006283636 scopus 로고
    • Development and maturation of central nervous system myelin: comparison of immunohistochemical localization of proteolipid protein and basic protein in myelin and oligodendrocyte
    • Hartman B, Agrawal H, DAgrawal D, Kalmbach S, (1982) Development and maturation of central nervous system myelin: comparison of immunohistochemical localization of proteolipid protein and basic protein in myelin and oligodendrocyte. Proc Natl Acad Sci U S A 79: 4217-4220.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 4217-4220
    • Hartman, B.1    Agrawal, H.2    DAgrawal, D.3    Kalmbach, S.4
  • 14
    • 0022345824 scopus 로고
    • Appearance of myelin proteins during development in the chick central nervous system
    • Macklin W, Weill C, (1985) Appearance of myelin proteins during development in the chick central nervous system. Dev Neurosc 7: 170-178.
    • (1985) Dev Neurosc , vol.7 , pp. 170-178
    • Macklin, W.1    Weill, C.2
  • 16
    • 0034533570 scopus 로고    scopus 로고
    • Gene expression monitoring for gene discovery in models of peripheral and central nervous system differentiation, regeneration, and trauma
    • Farlow DN, Vansant G, Cameron AA, Chang J, Khoh-Reiter S, et al. (2000) Gene expression monitoring for gene discovery in models of peripheral and central nervous system differentiation, regeneration, and trauma. J Cell Biochem 80: 171-180.
    • (2000) J Cell Biochem , vol.80 , pp. 171-180
    • Farlow, D.N.1    Vansant, G.2    Cameron, A.A.3    Chang, J.4    Khoh-Reiter, S.5
  • 17
    • 78149469909 scopus 로고    scopus 로고
    • Developmental changes of gene expression after spinal cord injury in neonatal opossums
    • Mladinic M, Lefevre C, Del Bel E, Nicholls J, Digby M, (2010) Developmental changes of gene expression after spinal cord injury in neonatal opossums. Brain Res 1363: 20-39.
    • (2010) Brain Res , vol.1363 , pp. 20-39
    • Mladinic, M.1    Lefevre, C.2    Del Bel, E.3    Nicholls, J.4    Digby, M.5
  • 18
    • 20044382245 scopus 로고    scopus 로고
    • Differential expression of genes at stages when regeneration can and cannot occur after injury to immature mammalian spinal cord
    • Mladinic M, Wintzer M, Del Bel E, Casseler C, Lazarevic D, et al. (2005) Differential expression of genes at stages when regeneration can and cannot occur after injury to immature mammalian spinal cord. Cell Mol Neurobiol 25: 407-426.
    • (2005) Cell Mol Neurobiol , vol.25 , pp. 407-426
    • Mladinic, M.1    Wintzer, M.2    Del Bel, E.3    Casseler, C.4    Lazarevic, D.5
  • 19
    • 34047246680 scopus 로고    scopus 로고
    • Age-related differences in the local cellular and molecular responses to injury in developing spinal cord of the opossum, Monodelphis domestica
    • Lane M, Truettner J, Brunschwig J, Gomez A, Bunge M, et al. (2007) Age-related differences in the local cellular and molecular responses to injury in developing spinal cord of the opossum, Monodelphis domestica. Eur J Neurosci 25.
    • (2007) Eur J Neurosci , vol.25
    • Lane, M.1    Truettner, J.2    Brunschwig, J.3    Gomez, A.4    Bunge, M.5
  • 20
    • 34248576291 scopus 로고    scopus 로고
    • Genome of the marsupial Monodelphis domestica reveals innovation in non-coding sequences
    • Mikkelsen TS, Wakefield MJ, Aken B, Amemiya CT, Chang JL, et al. (2007) Genome of the marsupial Monodelphis domestica reveals innovation in non-coding sequences. Nature 447: 167-177.
    • (2007) Nature , vol.447 , pp. 167-177
    • Mikkelsen, T.S.1    Wakefield, M.J.2    Aken, B.3    Amemiya, C.T.4    Chang, J.L.5
  • 21
    • 80051544206 scopus 로고    scopus 로고
    • Cograft of neural stem cells and schwann cells overexpressing TrkC and neurotrophin-3 respectively after rat spinal cord transection
    • Wang J-M, Zeng Y-S, Wu J-L, Li Y, Teng Y, (2011) Cograft of neural stem cells and schwann cells overexpressing TrkC and neurotrophin-3 respectively after rat spinal cord transection. Biomaterials 32: 7454-7468.
    • (2011) Biomaterials , vol.32 , pp. 7454-7468
    • Wang, J.-M.1    Zeng, Y.-S.2    Wu, J.-L.3    Li, Y.4    Teng, Y.5
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M, (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochem 72: 248-254.
    • (1976) Analytical Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 23
    • 0028920164 scopus 로고
    • Effect of incubation of solutions of proteins containing dodecyl sulfate on the cleavage of peptide bonds by boilling
    • Kubo K, (1995) Effect of incubation of solutions of proteins containing dodecyl sulfate on the cleavage of peptide bonds by boilling. Analytical Biochem 225: 351-353.
    • (1995) Analytical Biochem , vol.225 , pp. 351-353
    • Kubo, K.1
  • 24
    • 0034671735 scopus 로고    scopus 로고
    • The Fas-induced apoptosis analyzed by high throughput proteome analysis
    • Gerner C, Frohwein U, Gotzmann J, Bayer E, Gelbmann D, et al. (2000) The Fas-induced apoptosis analyzed by high throughput proteome analysis. J Biol Chem 275: 39018-39026.
    • (2000) J Biol Chem , vol.275 , pp. 39018-39026
    • Gerner, C.1    Frohwein, U.2    Gotzmann, J.3    Bayer, E.4    Gelbmann, D.5
  • 25
    • 0028063607 scopus 로고
    • Subcellular Localisation of 14-3-3 isoforms in rat brain using specific antibodies
    • Martin H, Rostas J, Patel Y, Aitken A, (1994) Subcellular Localisation of 14-3-3 isoforms in rat brain using specific antibodies. J Neurochem 63: 2259-2265.
    • (1994) J Neurochem , vol.63 , pp. 2259-2265
    • Martin, H.1    Rostas, J.2    Patel, Y.3    Aitken, A.4
  • 26
    • 0027186319 scopus 로고
    • Protein gene product 9.5 and ubiquitin immunoreactivities in rat epididymis epithelium
    • Santamaria L, Martin RP, R, Fraile B, Nistal M, Terenghi G, et al. (1993) Protein gene product 9.5 and ubiquitin immunoreactivities in rat epididymis epithelium. Histochemistry 100: 131-138.
    • (1993) Histochemistry , vol.100 , pp. 131-138
    • Santamaria, L.1    Martin, R.P.R.2    Fraile, B.3    Nistal, M.4    Terenghi, G.5
  • 27
    • 4444267190 scopus 로고    scopus 로고
    • Cross-reactivity of antibodies to actin-depolymerizing factor/cofilin family proteins and identification of the major epitope recognized by a mammalian actin-depolymerizing factor/cofilin antibody
    • Shaw A, Minamide L, Bill C, Funk J, Maiti S, et al. (2004) Cross-reactivity of antibodies to actin-depolymerizing factor/cofilin family proteins and identification of the major epitope recognized by a mammalian actin-depolymerizing factor/cofilin antibody. Electrophoresis 25: 2611-2620.
    • (2004) Electrophoresis , vol.25 , pp. 2611-2620
    • Shaw, A.1    Minamide, L.2    Bill, C.3    Funk, J.4    Maiti, S.5
  • 28
    • 77957912321 scopus 로고    scopus 로고
    • Spatio-temporal progression of grey and white matter damage following cintusion injury in rat spinal cord
    • doi:10.1371/journal.pone.0012021
    • Ek CJ, Habgood M, Callaway J, Dennis R, Dziegielewska KM, et al. (2010) Spatio-temporal progression of grey and white matter damage following cintusion injury in rat spinal cord. PLoS One 5 (8): e12021 doi:10.1371/journal.pone.0012021.
    • (2010) PLoS One , vol.5 , Issue.8
    • Ek, C.J.1    Habgood, M.2    Callaway, J.3    Dennis, R.4    Dziegielewska, K.M.5
  • 29
    • 33750631580 scopus 로고    scopus 로고
    • Efficient fractionation and improved protein identification by peptide OFFGEL electrophoresis
    • Hörth P, Miller CA, Preckel T, Wenz C, (2006) Efficient fractionation and improved protein identification by peptide OFFGEL electrophoresis. Mol Cell Proteomics 10: 1968-1974.
    • (2006) Mol Cell Proteomics , vol.10 , pp. 1968-1974
    • Hörth, P.1    Miller, C.A.2    Preckel, T.3    Wenz, C.4
  • 30
    • 0027528854 scopus 로고
    • The development of myelin in the spinal cord of the North American opossum and its possible role in loss of rubrospinal plasticity. A study using myelin basic proein and galactocerebroside immunohistochemistry
    • Ghooray G, Martin G, (1993) The development of myelin in the spinal cord of the North American opossum and its possible role in loss of rubrospinal plasticity. A study using myelin basic proein and galactocerebroside immunohistochemistry. Brain Res Dev Brain Res 72: 67-74.
    • (1993) Brain Res Dev Brain Res , vol.72 , pp. 67-74
    • Ghooray, G.1    Martin, G.2
  • 31
    • 0030769139 scopus 로고    scopus 로고
    • Myelination of the ventral and dorsal roots of the C8 and L4 segments of the spinal cord at different stages of development in the gray opossum, Monodelphis domestica
    • Leblond H, Cabana T, (1997) Myelination of the ventral and dorsal roots of the C8 and L4 segments of the spinal cord at different stages of development in the gray opossum, Monodelphis domestica. J Comp Neurol 386: 203-216.
    • (1997) J Comp Neurol , vol.386 , pp. 203-216
    • Leblond, H.1    Cabana, T.2
  • 32
    • 0026733421 scopus 로고
    • A comparison between low background silver diammine and silver nitrate protein stains
    • Rabilloud T, (1992) A comparison between low background silver diammine and silver nitrate protein stains. Electrophoresis 13: 429-439.
    • (1992) Electrophoresis , vol.13 , pp. 429-439
    • Rabilloud, T.1
  • 33
    • 33646723866 scopus 로고    scopus 로고
    • Proteomic analysis of injured spinal cord tissue proteins using 2-DE and MALDI-TOF MS
    • Kang S, So H, Moon Y, Kim C, (2006) Proteomic analysis of injured spinal cord tissue proteins using 2-DE and MALDI-TOF MS. Proteomics 6: 2797-2812.
    • (2006) Proteomics , vol.6 , pp. 2797-2812
    • Kang, S.1    So, H.2    Moon, Y.3    Kim, C.4
  • 34
    • 77952877273 scopus 로고    scopus 로고
    • Proteomic profiling of proteins in rat spinal cord induced by contusion injury
    • Yan X, Liu J, Luo Z, Ding Q, Mao X, et al. (2010) Proteomic profiling of proteins in rat spinal cord induced by contusion injury. Neurochemistry International 56: 971-983.
    • (2010) Neurochemistry International , vol.56 , pp. 971-983
    • Yan, X.1    Liu, J.2    Luo, Z.3    Ding, Q.4    Mao, X.5
  • 35
    • 0037039823 scopus 로고    scopus 로고
    • Repairing the injured spinal cord
    • Schwab M, (2002) Repairing the injured spinal cord. Science 295: 1029-1031.
    • (2002) Science , vol.295 , pp. 1029-1031
    • Schwab, M.1
  • 36
    • 77956113769 scopus 로고    scopus 로고
    • Unexpected survival of neurons of origin of the pyrimidal tract after spinal cord injury
    • Nielson J, Sears-Kraxberger I, Strong M, Wong J, Willenberg R, et al. (2010) Unexpected survival of neurons of origin of the pyrimidal tract after spinal cord injury. J Neurosci 30: 11516-11528.
    • (2010) J Neurosci , vol.30 , pp. 11516-11528
    • Nielson, J.1    Sears-Kraxberger, I.2    Strong, M.3    Wong, J.4    Willenberg, R.5
  • 37
    • 54849419669 scopus 로고    scopus 로고
    • Neutralization of the membrane protein Nogo-A enhances growth and reactive sprouting in established organotypic hippocampal slice cultures
    • Craveiro L, Hakkoum D, Weinmann O, Montani L, Stoppini L, et al. (2008) Neutralization of the membrane protein Nogo-A enhances growth and reactive sprouting in established organotypic hippocampal slice cultures. Eur J Neurosci 28: 1808-1824.
    • (2008) Eur J Neurosci , vol.28 , pp. 1808-1824
    • Craveiro, L.1    Hakkoum, D.2    Weinmann, O.3    Montani, L.4    Stoppini, L.5
  • 38
    • 77956286388 scopus 로고    scopus 로고
    • Differential expression of FABP 3,5,7 in infantile and adult monkey cerebellum
    • Boneva N, Mori Y, Kaplamadzhiev D, Kikuchi H, Zhu H, et al. (2010) Differential expression of FABP 3,5,7 in infantile and adult monkey cerebellum. Neurosci Res 68: 94-102.
    • (2010) Neurosci Res , vol.68 , pp. 94-102
    • Boneva, N.1    Mori, Y.2    Kaplamadzhiev, D.3    Kikuchi, H.4    Zhu, H.5
  • 39
    • 77957717487 scopus 로고    scopus 로고
    • Fatty acid binding proteins in brain development and disease
    • Liu R, Mita R, Beaulieu M, Gao Z, Godbout R, (2010) Fatty acid binding proteins in brain development and disease. Int J Dev Biol 54: 1229-1239.
    • (2010) Int J Dev Biol , vol.54 , pp. 1229-1239
    • Liu, R.1    Mita, R.2    Beaulieu, M.3    Gao, Z.4    Godbout, R.5
  • 40
    • 77954505638 scopus 로고    scopus 로고
    • Distinct caspase pathways mediate necrosis and apoptosis in subpopulations of hippocampal neurons after status epilepticus
    • Lopez-Meraz M, Niquet J, Wasterlain C, (2010) Distinct caspase pathways mediate necrosis and apoptosis in subpopulations of hippocampal neurons after status epilepticus. Epilepsia 51: S56-S60.
    • (2010) Epilepsia , vol.51
    • Lopez-Meraz, M.1    Niquet, J.2    Wasterlain, C.3
  • 41
    • 74449083097 scopus 로고    scopus 로고
    • Secondary retinal ganglion cell death and the neuroprotective effects of the calcium channel blocker lomerizine
    • Fitzgerald M, Payne S, Bartlett C, Evill L, Harvey A, et al. (2009) Secondary retinal ganglion cell death and the neuroprotective effects of the calcium channel blocker lomerizine. Invest Ophthalmol Vis Sci 50: 5456-5462.
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , pp. 5456-5462
    • Fitzgerald, M.1    Payne, S.2    Bartlett, C.3    Evill, L.4    Harvey, A.5
  • 43
    • 0142185061 scopus 로고    scopus 로고
    • Inflammation in central nervous system injury
    • Allan S, Rothwell N, (2003) Inflammation in central nervous system injury. Phil Trans R Soc Lon B 358: 1669-1677.
    • (2003) Phil Trans R Soc Lon B , vol.358 , pp. 1669-1677
    • Allan, S.1    Rothwell, N.2
  • 44
    • 77954661355 scopus 로고    scopus 로고
    • Isolates of the Enterobacter cloacae complex induce apoptosis of human intestinal epithelial cells
    • Krzyminska S, Koczura R, Mokracka J, Puton T, Kaznowski A, (2010) Isolates of the Enterobacter cloacae complex induce apoptosis of human intestinal epithelial cells. Microb Pathog 49: 83-89.
    • (2010) Microb Pathog , vol.49 , pp. 83-89
    • Krzyminska, S.1    Koczura, R.2    Mokracka, J.3    Puton, T.4    Kaznowski, A.5
  • 46
    • 77955659811 scopus 로고    scopus 로고
    • miR-1/miR-206 regulate HSP60 expression contributing to glucose-mediated apoptosis in cardiomyocytes
    • Shan Z, Lin Q, Deng C, Zhu J, Mai L, et al. (2010) miR-1/miR-206 regulate HSP60 expression contributing to glucose-mediated apoptosis in cardiomyocytes. FEBS Lett 584: 3592-3600.
    • (2010) FEBS Lett , vol.584 , pp. 3592-3600
    • Shan, Z.1    Lin, Q.2    Deng, C.3    Zhu, J.4    Mai, L.5
  • 47
    • 77950553736 scopus 로고    scopus 로고
    • Overexpression of 60 kDa heat shock protein enhances cytoprotective function of small intestinal epithelial cells
    • Takada M, Otaka M, Takahashi T, Izumi Y, Tamaki K, et al. (2010) Overexpression of 60 kDa heat shock protein enhances cytoprotective function of small intestinal epithelial cells. Life Sci 86: 499-504.
    • (2010) Life Sci , vol.86 , pp. 499-504
    • Takada, M.1    Otaka, M.2    Takahashi, T.3    Izumi, Y.4    Tamaki, K.5
  • 48
    • 58249142180 scopus 로고    scopus 로고
    • Isoform-dependant immunolocalization of 14-3-3 proteins in developing rat cerebellum
    • Umahara T, Uchihara T, Nakamura A, Iwamoto T, (2009) Isoform-dependant immunolocalization of 14-3-3 proteins in developing rat cerebellum. Brain Res 1253: 15-26.
    • (2009) Brain Res , vol.1253 , pp. 15-26
    • Umahara, T.1    Uchihara, T.2    Nakamura, A.3    Iwamoto, T.4
  • 49
    • 3242749629 scopus 로고    scopus 로고
    • The 14-3-3 protein epsilon isoform expressed in reactive astrocytes in demyelinating lesions of multiple slerosis binds to vimentin and glial fibrillary acidid protein in cultured human astrocytes
    • Satoh J, Yamamura T, Arima K, (2004) The 14-3-3 protein epsilon isoform expressed in reactive astrocytes in demyelinating lesions of multiple slerosis binds to vimentin and glial fibrillary acidid protein in cultured human astrocytes. Am J Pathol 165: 577-592.
    • (2004) Am J Pathol , vol.165 , pp. 577-592
    • Satoh, J.1    Yamamura, T.2    Arima, K.3
  • 50
    • 0028825581 scopus 로고
    • Myelin-associated neurite growth inhibitory proteins and suppression of regeneration of immature mammalian spinal cord in culture
    • Varga Z, Schwab M, Nicholls J, (1995) Myelin-associated neurite growth inhibitory proteins and suppression of regeneration of immature mammalian spinal cord in culture. Proc Natl Acad Sci U S A 92: 10959-10963.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10959-10963
    • Varga, Z.1    Schwab, M.2    Nicholls, J.3
  • 51
    • 0029898873 scopus 로고    scopus 로고
    • Evidence for growth of supraspinal axons through the lesions after transection of the thoracic spinal cord in the developing opossum, Didelphis virginiana
    • Wang X, Terman J, Martin G, (1996) Evidence for growth of supraspinal axons through the lesions after transection of the thoracic spinal cord in the developing opossum, Didelphis virginiana. J Comp Neurol 371.
    • (1996) J Comp Neurol , vol.371
    • Wang, X.1    Terman, J.2    Martin, G.3
  • 52
    • 33646762480 scopus 로고    scopus 로고
    • Localization of GRP78 to mitochondria under the unfolded protein response
    • Sun F, Wei S, Li C, Chang Y, Chao C, et al. (2006) Localization of GRP78 to mitochondria under the unfolded protein response. Biochem J 396: 31-39.
    • (2006) Biochem J , vol.396 , pp. 31-39
    • Sun, F.1    Wei, S.2    Li, C.3    Chang, Y.4    Chao, C.5
  • 53
    • 77956500946 scopus 로고    scopus 로고
    • Binding of anti-GRP78 autoantibodies to cell surface GRP78 increases tissue factor procoagulant activity via the release of calcium from endoplasmic reticulum stores
    • Al-Hashimi A, Caldwell J, Gonzalez-Gronow M, Pizzo S, Aboumrad D, et al. (2010) Binding of anti-GRP78 autoantibodies to cell surface GRP78 increases tissue factor procoagulant activity via the release of calcium from endoplasmic reticulum stores. J Biol Chem 285: 28912-28923.
    • (2010) J Biol Chem , vol.285 , pp. 28912-28923
    • Al-Hashimi, A.1    Caldwell, J.2    Gonzalez-Gronow, M.3    Pizzo, S.4    Aboumrad, D.5
  • 54
    • 77952151815 scopus 로고    scopus 로고
    • PI3K/Akt promotes GRP78 accumulation and inhibits endoplasmic reticulum stress-induced apoptosis in HEK293 cells
    • Dai R, Chen S, Yan D, Chen R, Lui Y, et al. (2010) PI3K/Akt promotes GRP78 accumulation and inhibits endoplasmic reticulum stress-induced apoptosis in HEK293 cells. Folia Biol (Praha) 56: 37-46.
    • (2010) Folia Biol (Praha) , vol.56 , pp. 37-46
    • Dai, R.1    Chen, S.2    Yan, D.3    Chen, R.4    Lui, Y.5
  • 55
    • 2442680458 scopus 로고    scopus 로고
    • A novel receptor function for the heat shock protein GRP78: silencing of GRP78 gene expression attenuates alpha2M*-induced signalling
    • Misra U, Gonzalez-Gronow M, Gawdi G, Wang F, Pizzo S, (2004) A novel receptor function for the heat shock protein GRP78: silencing of GRP78 gene expression attenuates alpha2M*-induced signalling. Cell Signal 16: 929-938.
    • (2004) Cell Signal , vol.16 , pp. 929-938
    • Misra, U.1    Gonzalez-Gronow, M.2    Gawdi, G.3    Wang, F.4    Pizzo, S.5
  • 56
    • 77951197000 scopus 로고    scopus 로고
    • Overlapping and distinct functions for cofilin, coronin and Aip1 in actin dynamics in vivo
    • Lin M, Galetta B, Sept D, Cooper J, (2010) Overlapping and distinct functions for cofilin, coronin and Aip1 in actin dynamics in vivo. J Cell Sci 123: 1329-1342.
    • (2010) J Cell Sci , vol.123 , pp. 1329-1342
    • Lin, M.1    Galetta, B.2    Sept, D.3    Cooper, J.4
  • 57
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac mediated actin reorganization
    • Yang N, Higuchi O, K O, Nagata K, Wada A, et al. (1998) Cofilin phosphorylation by LIM-kinase 1 and its role in Rac mediated actin reorganization. Nature 393: 809-812.
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    K, O.3    Nagata, K.4    Wada, A.5
  • 58
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin
    • Gohla A, Bokoch G, (2002) 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr Biol 12: 1704-1710.
    • (2002) Curr Biol , vol.12 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.2
  • 59
    • 0037270323 scopus 로고    scopus 로고
    • Identification of cofilin and LIM-domain containing protein kinase 1 as novel interaction partners of 14-3-3 zeta
    • Birkenfield J, Betz H, Roth D, (2003) Identification of cofilin and LIM-domain containing protein kinase 1 as novel interaction partners of 14-3-3 zeta. Biochem J 369: 45-54.
    • (2003) Biochem J , vol.369 , pp. 45-54
    • Birkenfield, J.1    Betz, H.2    Roth, D.3
  • 60
    • 77954415606 scopus 로고    scopus 로고
    • Activation of ADF/cofilin mediates attractive growth cone turning toward nerve growth factor and netrin-1
    • Marsick B, Flynn K, Santiago-Medina M, Bamburg J, Lerourneau P, (2010) Activation of ADF/cofilin mediates attractive growth cone turning toward nerve growth factor and netrin-1. Dev Neurobiol 70: 565-588.
    • (2010) Dev Neurobiol , vol.70 , pp. 565-588
    • Marsick, B.1    Flynn, K.2    Santiago-Medina, M.3    Bamburg, J.4    Lerourneau, P.5
  • 61
    • 77049121446 scopus 로고    scopus 로고
    • Modulation of actin filament dynamics by actin binding proteins residing in lamellipodia
    • Mazur A, Gremm D, Dansranjavin T, Litwin M, Jockusch B, et al. (2010) Modulation of actin filament dynamics by actin binding proteins residing in lamellipodia. Eur J Cell Biol 89: 402-413.
    • (2010) Eur J Cell Biol , vol.89 , pp. 402-413
    • Mazur, A.1    Gremm, D.2    Dansranjavin, T.3    Litwin, M.4    Jockusch, B.5
  • 63
    • 77956594742 scopus 로고    scopus 로고
    • Microtubule dysfunction precedes transport impairment and mitochondria damage in MPP+ induced neurodegeneration
    • Cartelli D, Ronchi C, Maggioni M, Rodighiero S, Giavini E, et al. (2010) Microtubule dysfunction precedes transport impairment and mitochondria damage in MPP+ induced neurodegeneration. J Neurochem 115: 247-258.
    • (2010) J Neurochem , vol.115 , pp. 247-258
    • Cartelli, D.1    Ronchi, C.2    Maggioni, M.3    Rodighiero, S.4    Giavini, E.5
  • 64
    • 81155128061 scopus 로고
    • Neuronal metabolism and ATP synthesis in narcosis
    • Grenell R, Mendelson J, McElroy W, (1955) Neuronal metabolism and ATP synthesis in narcosis. J Cell Physiol 46: 143-161.
    • (1955) J Cell Physiol , vol.46 , pp. 143-161
    • Grenell, R.1    Mendelson, J.2    McElroy, W.3
  • 65
    • 0011175251 scopus 로고
    • A plant biochemist's view of H+-ATPases and ATP synthases
    • McCarty R, (1992) A plant biochemist's view of H+-ATPases and ATP synthases. J Exp Biol 172: 431-441.
    • (1992) J Exp Biol , vol.172 , pp. 431-441
    • McCarty, R.1
  • 67
    • 0025882959 scopus 로고
    • Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analog of the intermediate on the reaction pathway
    • Davenport R, Bash P, Seaton B, Karplus M, Petsko G, et al. (1991) Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analog of the intermediate on the reaction pathway. Biochem 30: 5821-5826.
    • (1991) Biochem , vol.30 , pp. 5821-5826
    • Davenport, R.1    Bash, P.2    Seaton, B.3    Karplus, M.4    Petsko, G.5
  • 68
    • 0002335520 scopus 로고
    • The relationships between substrates and enzymes of gycolysis in brain
    • Lowry O, Passonneau J, (1964) The relationships between substrates and enzymes of gycolysis in brain. J Biol Chem 239: 31-42.
    • (1964) J Biol Chem , vol.239 , pp. 31-42
    • Lowry, O.1    Passonneau, J.2
  • 69
    • 0017639978 scopus 로고
    • Activity patterns of phosphofructokinase, glyceraldehyphosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle
    • Spamer C, Pette D, (1977) Activity patterns of phosphofructokinase, glyceraldehyphosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle. Histochem Cell Biol 52: 201-206.
    • (1977) Histochem Cell Biol , vol.52 , pp. 201-206
    • Spamer, C.1    Pette, D.2
  • 70
    • 0031013236 scopus 로고    scopus 로고
    • Cellular inflammatory response after spinal cord injury in Sprague-Dawley and Lewis rats
    • Popovich P, Wei P, Stokes B, (1997) Cellular inflammatory response after spinal cord injury in Sprague-Dawley and Lewis rats. J Comp Neurol 377: 443-464.
    • (1997) J Comp Neurol , vol.377 , pp. 443-464
    • Popovich, P.1    Wei, P.2    Stokes, B.3
  • 71
    • 0030746939 scopus 로고    scopus 로고
    • Effects of pro-inflammatory cytokines in experimental spinal cord injury
    • Klusman IS, ME, (1997) Effects of pro-inflammatory cytokines in experimental spinal cord injury. Brain Res 762: 173-184.
    • (1997) Brain Res , vol.762 , pp. 173-184
    • Klusman, I.S.M.E.1
  • 72
    • 0342617481 scopus 로고
    • Antibody production in the opossum embryo
    • Kalmutz S, (1962) Antibody production in the opossum embryo. Nature 193: 851-853.
    • (1962) Nature , vol.193 , pp. 851-853
    • Kalmutz, S.1
  • 73
    • 0022448953 scopus 로고
    • Passively acquired immunity in the newborn of a marsupial (Monodelphis domestica)
    • Samples N, VandeBerg J, Stone W, (1986) Passively acquired immunity in the newborn of a marsupial (Monodelphis domestica). Am J Reprod Immunol Microbiol 11: 94-97.
    • (1986) Am J Reprod Immunol Microbiol , vol.11 , pp. 94-97
    • Samples, N.1    VandeBerg, J.2    Stone, W.3
  • 75
    • 0030764903 scopus 로고    scopus 로고
    • Changes in ubiquitin immunoreactivity in developing rat brain: a putative role for ubiquitin and ubiquitin conjugates in dendrite outgrowth and differentiation
    • Flann S, Hawkes RB, Riederer BM, Rider CC, Beesley PW, (1997) Changes in ubiquitin immunoreactivity in developing rat brain: a putative role for ubiquitin and ubiquitin conjugates in dendrite outgrowth and differentiation. Neurosci 81: 173-187.
    • (1997) Neurosci , vol.81 , pp. 173-187
    • Flann, S.1    Hawkes, R.B.2    Riederer, B.M.3    Rider, C.C.4    Beesley, P.W.5
  • 76
    • 32044461117 scopus 로고    scopus 로고
    • Subcellular distribution of components of the ubiquitin-proteosome system in non-diseased human and rat brain
    • Adori C, Low P, Moszkovkin G, Bagdy G, Laszlo L, Kovacs GG, (2006) Subcellular distribution of components of the ubiquitin-proteosome system in non-diseased human and rat brain. J Hist & Cyto 54: 263-267.
    • (2006) J Hist & Cyto , vol.54 , pp. 263-267
    • Adori, C.1    Low, P.2    Moszkovkin, G.3    Bagdy, G.4    Laszlo, L.5    Kovacs, G.G.6
  • 78
    • 4544335403 scopus 로고    scopus 로고
    • Spatial and temporal gene expression profiling of the contused rat spinal cord
    • Aimone JB, Leasure JL, Perreau VM, Thallmair M, (2004) Spatial and temporal gene expression profiling of the contused rat spinal cord. Exp Neurol 189: 204-221.
    • (2004) Exp Neurol , vol.189 , pp. 204-221
    • Aimone, J.B.1    Leasure, J.L.2    Perreau, V.M.3    Thallmair, M.4


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