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Volumn 79, Issue 1, 2014, Pages 76-82

Temporal-spatial expression of ENOLASE after acute spinal cord injury in adult rats

Author keywords

ENOLASE; Glial proliferation; Rats; Spinal cord injury

Indexed keywords

CYCLINE; ENOLASE; BIOLOGICAL MARKER; GLYCOLYTIC ENZYME; NEUROTROPHIC FACTOR;

EID: 84896721427     PISSN: 01680102     EISSN: 18728111     Source Type: Journal    
DOI: 10.1016/j.neures.2013.12.001     Document Type: Article
Times cited : (17)

References (27)
  • 3
    • 0026802223 scopus 로고
    • A monitored contusion model of spinal cord injury in the rat
    • discussion 126-128
    • Gruner J.A. A monitored contusion model of spinal cord injury in the rat. J. Neurotrauma 1992, 9(2):123-126. discussion 126-128.
    • (1992) J. Neurotrauma , vol.9 , Issue.2 , pp. 123-126
    • Gruner, J.A.1
  • 4
    • 0027930332 scopus 로고
    • Synthetic peptide corresponding to 30 amino acids of the C-terminal of neuron-specific enolase promotes survival of neocortical neurons in culture
    • Hattori T., Ohsawa K., Mizuno Y., Kato K., Kohsaka S. Synthetic peptide corresponding to 30 amino acids of the C-terminal of neuron-specific enolase promotes survival of neocortical neurons in culture. Biochem. Biophys. Res. Commun. 1994, 202:25-30.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 25-30
    • Hattori, T.1    Ohsawa, K.2    Mizuno, Y.3    Kato, K.4    Kohsaka, S.5
  • 5
    • 0028899956 scopus 로고
    • Neurotrophic and neuroprotective effects of neuron-specific enolase on cultured neurons from embryonic rat brain
    • Hattori T., Takei N., Mizuno Y., Kato K., Kohsaka S. Neurotrophic and neuroprotective effects of neuron-specific enolase on cultured neurons from embryonic rat brain. Neurosci. Res. 1995, 21:191-198.
    • (1995) Neurosci. Res. , vol.21 , pp. 191-198
    • Hattori, T.1    Takei, N.2    Mizuno, Y.3    Kato, K.4    Kohsaka, S.5
  • 6
    • 0026693656 scopus 로고
    • Enolase is present at the centrosome of HeLa cells
    • Johnstone S.A., Waisman D.M., Rattner J.B. Enolase is present at the centrosome of HeLa cells. Exp. Cell Res. 1992, 202(2):458-463.
    • (1992) Exp. Cell Res. , vol.202 , Issue.2 , pp. 458-463
    • Johnstone, S.A.1    Waisman, D.M.2    Rattner, J.B.3
  • 7
    • 3342967871 scopus 로고    scopus 로고
    • Pathophysiology and pharmacologic treatment of acute spinal cord injury
    • Kwon B.K., Tetzlaff W., Grauer J.N., Beiner J., Vaccaro A.R. Pathophysiology and pharmacologic treatment of acute spinal cord injury. Spine J. 2004, 4(4):451-464.
    • (2004) Spine J. , vol.4 , Issue.4 , pp. 451-464
    • Kwon, B.K.1    Tetzlaff, W.2    Grauer, J.N.3    Beiner, J.4    Vaccaro, A.R.5
  • 8
    • 79958042556 scopus 로고    scopus 로고
    • Increased expression of transcription initiation factor IIB after rat traumatic brain injury
    • Liu Z., Wang D., Shao B., Wu X., Xu J., Lu Q., Wang Y., Li C., Shen A., Wu Q. Increased expression of transcription initiation factor IIB after rat traumatic brain injury. J. Mol. Histol. 2011, 42(3):265-271.
    • (2011) J. Mol. Histol. , vol.42 , Issue.3 , pp. 265-271
    • Liu, Z.1    Wang, D.2    Shao, B.3    Wu, X.4    Xu, J.5    Lu, Q.6    Wang, Y.7    Li, C.8    Shen, A.9    Wu, Q.10
  • 10
    • 0026609068 scopus 로고
    • Investigation of lens glycolytic enzymes: species distribution and interaction with supramolecular order
    • Mathur R.L., Reddy M.C., Yee S., Imbesi R., Groth-Vasselli B., Farnsworth P.N. Investigation of lens glycolytic enzymes: species distribution and interaction with supramolecular order. Exp. Eye Res. 1992, 54(2):253-260.
    • (1992) Exp. Eye Res. , vol.54 , Issue.2 , pp. 253-260
    • Mathur, R.L.1    Reddy, M.C.2    Yee, S.3    Imbesi, R.4    Groth-Vasselli, B.5    Farnsworth, P.N.6
  • 11
    • 0037006387 scopus 로고    scopus 로고
    • Spinal-cord injury
    • McDonald J.W., Sadowsky C. Spinal-cord injury. Lancet 2002, 359(9304):417-425.
    • (2002) Lancet , vol.359 , Issue.9304 , pp. 417-425
    • McDonald, J.W.1    Sadowsky, C.2
  • 12
    • 0030908790 scopus 로고    scopus 로고
    • Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins
    • Merkulova T., Lucas M., Jabet C., et al. Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins. Biochem. J. 1997, 323(3):791-800.
    • (1997) Biochem. J. , vol.323 , Issue.3 , pp. 791-800
    • Merkulova, T.1    Lucas, M.2    Jabet, C.3
  • 14
    • 0024364302 scopus 로고
    • Regulation of proliferating cell nuclear antigen during the cell cycle
    • Morris G.F., Mathews M.B. Regulation of proliferating cell nuclear antigen during the cell cycle. J. Biol. Chem. 1989, 264(23):13856-13864.
    • (1989) J. Biol. Chem. , vol.264 , Issue.23 , pp. 13856-13864
    • Morris, G.F.1    Mathews, M.B.2
  • 15
    • 11444256801 scopus 로고    scopus 로고
    • Glia and their cytokines in progression of neurodegeneration
    • Mrak R.E., Griffin W.S. Glia and their cytokines in progression of neurodegeneration. Neurobiol. Aging 2005, 26(3):349-354.
    • (2005) Neurobiol. Aging , vol.26 , Issue.3 , pp. 349-354
    • Mrak, R.E.1    Griffin, W.S.2
  • 17
    • 0033824172 scopus 로고    scopus 로고
    • Urokinase receptor and integrin partnership: coordination of signaling for cell adhesion, migration and growth
    • Ossowski L., Aguirre-Ghiso J.A. Urokinase receptor and integrin partnership: coordination of signaling for cell adhesion, migration and growth. Curr. Opin. Cell Biol. 2000, 12(5):613-620.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , Issue.5 , pp. 613-620
    • Ossowski, L.1    Aguirre-Ghiso, J.A.2
  • 18
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional α-enolase: its role in diseases
    • Pancholi V. Multifunctional α-enolase: its role in diseases. Cell. Mol. Life Sci. 2001, 58(7):902-920.
    • (2001) Cell. Mol. Life Sci. , vol.58 , Issue.7 , pp. 902-920
    • Pancholi, V.1
  • 19
    • 0032486286 scopus 로고    scopus 로고
    • α-Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic Streptococci
    • Pancholi V., Fischetti V.A. α-Enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic Streptococci. J. Biol. Chem. 1998, 273:14503-14515.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 21
    • 0026078478 scopus 로고
    • Cloning and characterization of a human c-myc promoter-binding protein
    • Ray R., Miller D.M. Cloning and characterization of a human c-myc promoter-binding protein. Mol. Cell. Biol. 1991, 11:2154-2161.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2154-2161
    • Ray, R.1    Miller, D.M.2
  • 22
    • 40949158349 scopus 로고    scopus 로고
    • Temporal-spatial expressions of p27kip1 and its phosphorylation on serine-10 after acute spinal cord injury in adult rat: implications for post-traumatic glial proliferation
    • Shen A., Liu Y., Zhao J., Qin J., Shi S., Chen M., Gao S., Xiao F., Lu Q., Cheng C. Temporal-spatial expressions of p27kip1 and its phosphorylation on serine-10 after acute spinal cord injury in adult rat: implications for post-traumatic glial proliferation. Neurochem. Int. 2008, 52(6):1266-1275.
    • (2008) Neurochem. Int. , vol.52 , Issue.6 , pp. 1266-1275
    • Shen, A.1    Liu, Y.2    Zhao, J.3    Qin, J.4    Shi, S.5    Chen, M.6    Gao, S.7    Xiao, F.8    Lu, Q.9    Cheng, C.10
  • 23
    • 34548405715 scopus 로고    scopus 로고
    • Glial activation links early-life seizures and long-term neurologic dysfunction: evidence using a small molecule inhibitor of proinflammatory cytokine upregulation
    • Somera-Molina K.C., Robin B., Somera C.A., Anderson C., Stine C., Koh S., Behanna H.A., Van Eldik L.J., Watterson D.M., Wainwright M.S. Glial activation links early-life seizures and long-term neurologic dysfunction: evidence using a small molecule inhibitor of proinflammatory cytokine upregulation. Epilepsia 2007, 48(9):1785-1800.
    • (2007) Epilepsia , vol.48 , Issue.9 , pp. 1785-1800
    • Somera-Molina, K.C.1    Robin, B.2    Somera, C.A.3    Anderson, C.4    Stine, C.5    Koh, S.6    Behanna, H.A.7    Van Eldik, L.J.8    Watterson, D.M.9    Wainwright, M.S.10
  • 25
    • 0026096540 scopus 로고
    • Control of c-myc regulation in normal and neoplastic cells
    • Spencer C.A., Groudine M. Control of c-myc regulation in normal and neoplastic cells. Adv. Cancer Res. 1991, 56:1-48.
    • (1991) Adv. Cancer Res. , vol.56 , pp. 1-48
    • Spencer, C.A.1    Groudine, M.2
  • 26
    • 77952584341 scopus 로고    scopus 로고
    • ENO1, a potential prognostic head and neck cancer marker, promotes transformation partly via chemokine CCL20 induction
    • Tsai S.T., Chien I.H., Shen W.H., et al. ENO1, a potential prognostic head and neck cancer marker, promotes transformation partly via chemokine CCL20 induction. Eur. J. Cancer 2010, 46(9):1712-1723.
    • (2010) Eur. J. Cancer , vol.46 , Issue.9 , pp. 1712-1723
    • Tsai, S.T.1    Chien, I.H.2    Shen, W.H.3
  • 27
    • 79954422848 scopus 로고    scopus 로고
    • KPC1 expression and essential role after acute spinal cord injury in adult rat
    • Zhao J., Zhang S., Wu X., Huan W., Liu Z., Wei H., Shen A., Teng H. KPC1 expression and essential role after acute spinal cord injury in adult rat. Neurochem. Res. 2011, 36(3):549-558.
    • (2011) Neurochem. Res. , vol.36 , Issue.3 , pp. 549-558
    • Zhao, J.1    Zhang, S.2    Wu, X.3    Huan, W.4    Liu, Z.5    Wei, H.6    Shen, A.7    Teng, H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.