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Volumn 9, Issue 10, 2014, Pages

Pharmacological inhibition of dynamin II reduces constitutive protein secretion from primary human macrophages

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN E; CELL PROTEIN; CHITINASE 3 LIKE PROTEIN 1; CYCLOPHILIN A; DYNAMIN II; FIBRONECTIN; GELATINASE B; GUANOSINE TRIPHOSPHATASE; ISOPROTEIN; LYSOZYME; MESSENGER RNA; PROTEIN DERIVATIVE; PROTEIN DYNGO; PROTEIN DYNOLE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; 2-CYANO-N-OCTYL-3-(1-(3-DIMETHYLAMINOPROPYL)-1H-INDOL-3-YL)ACRYLAMIDE; ACRYLAMIDE DERIVATIVE; INDOLE DERIVATIVE;

EID: 84908647089     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0111186     Document Type: Article
Times cited : (9)

References (48)
  • 1
    • 0031720535 scopus 로고    scopus 로고
    • Differential distribution of dynamin isoforms in Mammalian cells
    • Cao H, Garcia F, McNiven MA (1998) Differential distribution of dynamin isoforms in mammalian cells. Mol Biol Cell 9: 2595-2609.
    • (1998) Mol Biol Cell , vol.9 , pp. 2595-2609
    • Cao, H.1    Garcia, F.2    McNiven, M.A.3
  • 2
    • 0028137796 scopus 로고
    • Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues
    • Cook TA, Urrutia R, McNiven MA (1994) Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues. Proc Natl Acad Sci USA 91: 644-648.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 644-648
    • Cook, T.A.1    Urrutia, R.2    McNiven, M.A.3
  • 3
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • Praefcke GJK, McMahon HT (2004) The dynamin superfamily: universal membrane tubulation and fission molecules? Nat Rev Mol Cell Biol 5: 133-147.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 133-147
    • Praefcke, G.J.K.1    McMahon, H.T.2
  • 4
    • 0032559342 scopus 로고    scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-golgi network
    • Jones SM, Howell KE, Henley J.R., Cao H., McNiven MA (1998) Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science 279: 573-577.
    • (1998) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 5
    • 59449088311 scopus 로고    scopus 로고
    • Isoform and splice-variant specific functions of dynamin-2 revealed by analysis of conditional knock-out cells
    • Liu Y-W, Surka M.C., Schroeter T., Lukiyanchuk V, Schmid SL (2008) Isoform and splice-variant specific functions of dynamin-2 revealed by analysis of conditional knock-out cells. Mol Biol Cell 19: 5347-5359.
    • (2008) Mol Biol Cell , vol.19 , pp. 5347-5359
    • Liu, Y.-W.1    Surka, M.C.2    Schroeter, T.3    Lukiyanchuk, V.4    Schmid, S.L.5
  • 6
    • 0032937045 scopus 로고    scopus 로고
    • Dynamin II is involved in endocytosis but not in the formation of transport vesicles from the trans-golgi network
    • Kasai K, Shin HW, Shinotsuka C, Murakami K., Nakayama K (1999) Dynamin II is involved in endocytosis but not in the formation of transport vesicles from the trans-Golgi network. J Biochem 125: 780-789.
    • (1999) J Biochem , vol.125 , pp. 780-789
    • Kasai, K.1    Shin, H.W.2    Shinotsuka, C.3    Murakami, K.4    Nakayama, K.5
  • 7
    • 0032576577 scopus 로고    scopus 로고
    • Redundant and distinct functions for dynamin-1 and dynamin-2 isoforms
    • Altschuler Y, Barbas SM, Terlecky L.J., Tang K., Hardy S, et al. (1998) Redundant and distinct functions for dynamin-1 and dynamin-2 isoforms. J Cell Biol 143: 1871-1881.
    • (1998) J Cell Biol , vol.143 , pp. 1871-1881
    • Altschuler, Y.1    Barbas, S.M.2    Terlecky, L.J.3    Tang, K.4    Hardy, S.5
  • 8
    • 77950531323 scopus 로고    scopus 로고
    • Src kinase regulates the integrity and function of the golgi apparatus via activation of dynamin 2
    • Weller SG, Capitani M, Cao H., Micaroni M, Luini A, et al. (2010) Src kinase regulates the integrity and function of the Golgi apparatus via activation of dynamin 2. Proc Natl Acad Sci USA 107: 5863-5868.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5863-5868
    • Weller, S.G.1    Capitani, M.2    Cao, H.3    Micaroni, M.4    Luini, A.5
  • 9
    • 20444414481 scopus 로고    scopus 로고
    • CtBP3/BARS drives membrane fission in dynamin-independent transport pathways
    • Bonazzi M, Spanò S, Turacchio G, Cericola C, Valente C, et al. (2005) CtBP3/BARS drives membrane fission in dynamin-independent transport pathways. Nat Cell Biol 7: 570-580.
    • (2005) Nat Cell Biol , vol.7 , pp. 570-580
    • Bonazzi, M.1    Spanò, S.2    Turacchio, G.3    Cericola, C.4    Valente, C.5
  • 11
    • 36348985073 scopus 로고    scopus 로고
    • Myristyl trimethyl ammonium bromide and octadecyl trimethyl ammonium bromide are surface-active small molecule dynamin inhibitors that block endocytosis mediated by dynamin I or dynamin II
    • Quan A, McGeachie AB, Keating D.J., van Dam EM, Rusak J, et al. (2007) Myristyl Trimethyl Ammonium Bromide and Octadecyl Trimethyl Ammonium Bromide Are Surface-Active Small Molecule Dynamin Inhibitors that Block Endocytosis Mediated by Dynamin I or Dynamin II. Molecular Pharmacology 72: 1425-1439.
    • (2007) Molecular Pharmacology , vol.72 , pp. 1425-1439
    • Quan, A.1    McGeachie, A.B.2    Keating, D.J.3    Van Dam, E.M.4    Rusak, J.5
  • 13
    • 84887610283 scopus 로고    scopus 로고
    • Building a better dynasore: The dyngo compounds potently inhibit dynamin and endocytosis
    • McCluskey A, Daniel JA, Hadzic G, Chau N., Clayton EL, et al. (2013) Building a better dynasore: the dyngo compounds potently inhibit dynamin and endocytosis. Traffic 14: 1272-1289.
    • (2013) Traffic , vol.14 , pp. 1272-1289
    • McCluskey, A.1    Daniel, J.A.2    Hadzic, G.3    Chau, N.4    Clayton, E.L.5
  • 14
    • 67549119243 scopus 로고    scopus 로고
    • Inhibition of dynamin mediated endocytosis by the dynoles-synthesis and functional activity of a family of indoles
    • Hill TA, Gordon CP, McGeachie A.B., Venn-Brown B, Odell LR, et al. (2009) Inhibition of dynamin mediated endocytosis by the dynoles-synthesis and functional activity of a family of indoles. J Med Chem 52: 3762-3773.
    • (2009) J Med Chem , vol.52 , pp. 3762-3773
    • Hill, T.A.1    Gordon, C.P.2    McGeachie, A.B.3    Venn-Brown, B.4    Odell, L.R.5
  • 16
    • 80053897195 scopus 로고    scopus 로고
    • Dynamin inhibition blocks botulinum neurotoxin type A endocytosis in neurons and delays botulism
    • Harper CB, Martin S, Nguyen T.H., Daniels SJ, Lavidis NA, et al. (2011) Dynamin inhibition blocks botulinum neurotoxin type A endocytosis in neurons and delays botulism. J Biol Chem 286: 35966-35976.
    • (2011) J Biol Chem , vol.286 , pp. 35966-35976
    • Harper, C.B.1    Martin, S.2    Nguyen, T.H.3    Daniels, S.J.4    Lavidis, N.A.5
  • 17
    • 0024299370 scopus 로고
    • Apolipoprotein E: Cholesterol transport protein with expanding role in cell biology
    • Mahley RW (1988) Apolipoprotein E: cholesterol transport protein with expanding role in cell biology. Science 240: 622-630.
    • (1988) Science , vol.240 , pp. 622-630
    • Mahley, R.W.1
  • 18
    • 44849108970 scopus 로고    scopus 로고
    • Regulation of endogenous apolipoprotein E secretion by macrophages
    • Kockx M, Jessup W, Kritharides L (2008) Regulation of endogenous apolipoprotein E secretion by macrophages. Arterioscler Thromb Vasc Biol 28: 1060-1067.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 1060-1067
    • Kockx, M.1    Jessup, W.2    Kritharides, L.3
  • 19
    • 84876894324 scopus 로고    scopus 로고
    • Binding of apolipoprotein E inhibits the oligomer growth of amyloid-b peptide in solution as determined by fluorescence cross-correlation spectroscopy
    • Ly S, Altman R, Petrlova J., Lin Y, Hilt S, et al. (2013) Binding of apolipoprotein E inhibits the oligomer growth of amyloid-b peptide in solution as determined by fluorescence cross-correlation spectroscopy. J Biol Chem 288: 11628-11635.
    • (2013) J Biol Chem , vol.288 , pp. 11628-11635
    • Ly, S.1    Altman, R.2    Petrlova, J.3    Lin, Y.4    Hilt, S.5
  • 20
    • 19044365522 scopus 로고    scopus 로고
    • Apolipoproteins modulate the inflammatory response to lipopolysaccharide
    • Berbée JFP, Havekes LM, Rensen PCN (2005) Apolipoproteins modulate the inflammatory response to lipopolysaccharide. J Endotoxin Res 11: 97-103.
    • (2005) J Endotoxin Res , vol.11 , pp. 97-103
    • Berbée, J.F.P.1    Havekes, L.M.2    Rensen, P.C.N.3
  • 21
    • 84871234634 scopus 로고    scopus 로고
    • ApoE derived from adipose tissue does not suppress atherosclerosis or correct hyperlipidemia in apoE knockout mice
    • Huang ZH, Reardon CA, Subbaiah P.V., Getz GS, Mazzone T (2013) ApoE derived from adipose tissue does not suppress atherosclerosis or correct hyperlipidemia in apoE knockout mice. J Lipid Res 54: 202-213.
    • (2013) J Lipid Res , vol.54 , pp. 202-213
    • Huang, Z.H.1    Reardon, C.A.2    Subbaiah, P.V.3    Getz, G.S.4    Mazzone, T.5
  • 22
    • 84874094568 scopus 로고    scopus 로고
    • Protein kinase C controls vesicular transport and secretion of apolipoprotein E from primary human macrophages
    • Karunakaran D, Kockx M, Owen D.M., Burnett JR, Jessup W, et al. (2013) Protein kinase C controls vesicular transport and secretion of apolipoprotein E from primary human macrophages. J Biol Chem 288: 5186-5197.
    • (2013) J Biol Chem , vol.288 , pp. 5186-5197
    • Karunakaran, D.1    Kockx, M.2    Owen, D.M.3    Burnett, J.R.4    Jessup, W.5
  • 23
    • 2942731520 scopus 로고    scopus 로고
    • Apolipoprotein A-I-stimulated apolipoprotein E secretion from human macrophages is independent of cholesterol efflux
    • Kockx M, Rye K-A, Gaus K, Quinn C.M., Wright J., et al. (2004) Apolipoprotein A-I-stimulated apolipoprotein E secretion from human macrophages is independent of cholesterol efflux. J Biol Chem 279: 25966-25977.
    • (2004) J Biol Chem , vol.279 , pp. 25966-25977
    • Kockx, M.1    Rye, K.-A.2    Gaus, K.3    Quinn, C.M.4    Wright, J.5
  • 24
    • 69949134409 scopus 로고    scopus 로고
    • Cyclosporin A decreases apolipoprotein E secretion from human macrophages via a protein phosphatase 2B-dependent and ATP-binding cassette transporter A1 (ABCA1)-independent pathway
    • Kockx M, Guo DL, Traini M, Gaus K., Kay J, et al. (2009) Cyclosporin A decreases apolipoprotein E secretion from human macrophages via a protein phosphatase 2B-dependent and ATP-binding cassette transporter A1 (ABCA1)-independent pathway. J Biol Chem 284: 24144-24154. doi:10.1074/jbc.M109.032615.
    • (2009) J Biol Chem , vol.284 , pp. 24144-24154
    • Kockx, M.1    Guo, D.L.2    Traini, M.3    Gaus, K.4    Kay, J.5
  • 25
    • 71649086146 scopus 로고    scopus 로고
    • Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits
    • Ferguson SM, Ferguson S, Raimondi A., Paradise S, Shen H, et al. (2009) Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits. Dev Cell 17: 811-822.
    • (2009) Dev Cell , vol.17 , pp. 811-822
    • Ferguson, S.M.1    Ferguson, S.2    Raimondi, A.3    Paradise, S.4    Shen, H.5
  • 26
    • 79959316429 scopus 로고    scopus 로고
    • Overlapping role of dynamin isoforms in synaptic vesicle endocytosis
    • Raimondi A, Ferguson SM, Lou X, Armbruster M., Paradise S, et al. (2011) Overlapping role of dynamin isoforms in synaptic vesicle endocytosis. Neuron 70: 1100-1114.
    • (2011) Neuron , vol.70 , pp. 1100-1114
    • Raimondi, A.1    Ferguson, S.M.2    Lou, X.3    Armbruster, M.4    Paradise, S.5
  • 27
    • 84866382901 scopus 로고    scopus 로고
    • Cholesterol accumulation inhibits ER to golgi transport and protein secretion: Studies of apolipoprotein E and VSVGt
    • Kockx M, Dinnes DL, Huang K-Y, Sharpe LJ, Jessup W, et al. (2012) Cholesterol accumulation inhibits ER to Golgi transport and protein secretion: studies of apolipoprotein E and VSVGt. Biochem J 447: 51-60.
    • (2012) Biochem J , vol.447 , pp. 51-60
    • Kockx, M.1    Dinnes, D.L.2    Huang, K.-Y.3    Sharpe, L.J.4    Jessup, W.5
  • 28
    • 77956542058 scopus 로고    scopus 로고
    • Glycosylation and sialylation of macrophage-derived human apolipoprotein E analyzed by SDS-PAGE and mass Spectrometry: Evidence for a novel site of glycosylation on ser290
    • Lee Y, Kockx M, Raftery M.J., Jessup W., Griffith R, et al. (2010) Glycosylation and sialylation of macrophage-derived human apolipoprotein E analyzed by SDS-PAGE and mass spectrometry: evidence for a novel site of glycosylation on Ser290. Mol Cell Proteomics 9: 1968-1981.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1968-1981
    • Lee, Y.1    Kockx, M.2    Raftery, M.J.3    Jessup, W.4    Griffith, R.5
  • 29
    • 34748911230 scopus 로고    scopus 로고
    • Secretion of apolipoprotein E from macrophages occurs via a protein kinase A and calcium-dependent pathway along the microtubule network
    • Kockx M, Guo DL, Huby T, Lesnik P., Kay J, et al. (2007) Secretion of apolipoprotein E from macrophages occurs via a protein kinase A and calcium-dependent pathway along the microtubule network. Circ Res 101: 607-616.
    • (2007) Circ Res , vol.101 , pp. 607-616
    • Kockx, M.1    Guo, D.L.2    Huby, T.3    Lesnik, P.4    Kay, J.5
  • 30
    • 0024380582 scopus 로고
    • Isolation of exocytic carrier vesicles from BHK cells
    • de Curtis I, Simons K (1989) Isolation of exocytic carrier vesicles from BHK cells. Cell 58: 719-727.
    • (1989) Cell , vol.58 , pp. 719-727
    • De Curtis, I.1    Simons, K.2
  • 31
    • 0022834188 scopus 로고
    • ATP-coupled transport of vesicular stomatitis virus G protein. Functional boundaries of secretory compartments
    • Balch WE, Keller DS (1986) ATP-coupled transport of vesicular stomatitis virus G protein. Functional boundaries of secretory compartments. J Biol Chem 261: 14690-14696.
    • (1986) J Biol Chem , vol.261 , pp. 14690-14696
    • Balch, W.E.1    Keller, D.S.2
  • 32
    • 0024342278 scopus 로고
    • Identification of dynamin, a novel mechano-chemical enzyme that mediates interactions between microtubules
    • Shpetner HS, Vallee RB (1989) Identification of dynamin, a novel mechano-chemical enzyme that mediates interactions between microtubules. Cell 59: 421-432.
    • (1989) Cell , vol.59 , pp. 421-432
    • Shpetner, H.S.1    Vallee, R.B.2
  • 33
    • 67449124363 scopus 로고    scopus 로고
    • Dynamic instability of microtubules requires dynamin 2 and is impaired in a charcot-marie-tooth mutant
    • Tanabe K, Takei K (2009) Dynamic instability of microtubules requires dynamin 2 and is impaired in a Charcot-Marie-Tooth mutant. J Cell Biol 185: 939-948.
    • (2009) J Cell Biol , vol.185 , pp. 939-948
    • Tanabe, K.1    Takei, K.2
  • 34
    • 84888112438 scopus 로고    scopus 로고
    • Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors
    • Park RJ, Shen H, Liu L., Liu X, Ferguson SM, et al. (2013) Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors. J Cell Sci 126: 5305-5312.
    • (2013) J Cell Sci , vol.126 , pp. 5305-5312
    • Park, R.J.1    Shen, H.2    Liu, L.3    Liu, X.4    Ferguson, S.M.5
  • 35
    • 0035132427 scopus 로고    scopus 로고
    • Beta-arrestin-and dynamin-dependent endocytosis of the AT1 angiotensin receptor
    • Gáborik Z, Szaszák M, Szidonya L., Balla B, Paku S, et al. (2001) Beta-arrestin-and dynamin-dependent endocytosis of the AT1 angiotensin receptor. Molecular Pharmacology 59: 239-247.
    • (2001) Molecular Pharmacology , vol.59 , pp. 239-247
    • Gáborik, Z.1    Szaszák, M.2    Szidonya, L.3    Balla, B.4    Paku, S.5
  • 36
    • 0037448671 scopus 로고    scopus 로고
    • Cell biology: Tubulin acetylation and cell motility
    • Palazzo A, Ackerman B, Gundersen GG (2003) Cell biology: Tubulin acetylation and cell motility. Nature 421: 230.
    • (2003) Nature , vol.421 , pp. 230
    • Palazzo, A.1    Ackerman, B.2    Gundersen, G.G.3
  • 37
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov R, Yamada KM (2002) Fibronectin at a glance. J Cell Sci 115: 3861-3863.
    • (2002) J Cell Sci , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 38
    • 84863467640 scopus 로고    scopus 로고
    • Plasma fibronectin deficiency impedes atherosclerosis progression and fibrous cap formation
    • Rohwedder I, Montanez E, Beckmann K., Bengtsson E, Dunér P, et al. (2012) Plasma fibronectin deficiency impedes atherosclerosis progression and fibrous cap formation. EMBO Mol Med 4: 564-576.
    • (2012) EMBO Mol Med , vol.4 , pp. 564-576
    • Rohwedder, I.1    Montanez, E.2    Beckmann, K.3    Bengtsson, E.4    Dunér, P.5
  • 39
    • 0038059516 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9)
    • Van den Steen PE, Dubois B, Nelissen I., Rudd PM, Dwek RA, et al. (2002) Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit Rev Biochem Mol Biol 37: 375-536. doi:10.1080/10409230290771546.
    • (2002) Crit Rev Biochem Mol Biol , vol.37 , pp. 375-536
    • Van Den Steen, P.E.1    Dubois, B.2    Nelissen, I.3    Rudd, P.M.4    Dwek, R.A.5
  • 40
    • 0034954054 scopus 로고    scopus 로고
    • Fibronectin activates matrix metalloproteinase-9 secretion via the MEK1-MAPK and the PI3K-akt pathways in ovarian cancer cells
    • Thant AA, Nawa A, Kikkawa F., Ichigotani Y, Zhang Y, et al. (2000) Fibronectin activates matrix metalloproteinase-9 secretion via the MEK1-MAPK and the PI3K-Akt pathways in ovarian cancer cells. Clin Exp Metastasis 18: 423-428.
    • (2000) Clin Exp Metastasis , vol.18 , pp. 423-428
    • Thant, A.A.1    Nawa, A.2    Kikkawa, F.3    Ichigotani, Y.4    Zhang, Y.5
  • 41
    • 55949100194 scopus 로고    scopus 로고
    • Chitinase 3-like-1 (CHI3L1): A putative disease marker at the interface of proteomics and glycomics
    • Coffman FD (2008) Chitinase 3-Like-1 (CHI3L1): a putative disease marker at the interface of proteomics and glycomics. Crit Rev Clin Lab Sci 45: 531-562.
    • (2008) Crit Rev Clin Lab Sci , vol.45 , pp. 531-562
    • Coffman, F.D.1
  • 42
    • 0032975495 scopus 로고    scopus 로고
    • Strong induction of members of the chitinase family of proteins in atherosclerosis: Chitotriosidase and human cartilage gp-39 expressed in lesion macrophages
    • Boot RG, van Achterberg TA, van Aken BE, Renkema GH, Jacobs MJ, et al. (1999) Strong induction of members of the chitinase family of proteins in atherosclerosis: chitotriosidase and human cartilage gp-39 expressed in lesion macrophages. Arterioscler Thromb Vasc Biol 19: 687-694.
    • (1999) Arterioscler Thromb Vasc Biol , vol.19 , pp. 687-694
    • Boot, R.G.1    Van Achterberg, T.A.2    Van Aken, B.E.3    Renkema, G.H.4    Jacobs, M.J.5
  • 43
    • 0021243692 scopus 로고
    • Secretory products of macrophages and their physiological functions
    • Takemura R, Werb Z (1984) Secretory products of macrophages and their physiological functions. Am J Physiol 246: C1-C9.
    • (1984) Am J Physiol , vol.246 , pp. C1-C9
    • Takemura, R.1    Werb, Z.2
  • 44
    • 33745714780 scopus 로고    scopus 로고
    • Reduced acute vascular injury and atherosclerosis in hyperlipidemic mice transgenic for lysozyme
    • Liu H, Zheng F, Li Z., Uribarri J, Ren B, et al. (2006) Reduced acute vascular injury and atherosclerosis in hyperlipidemic mice transgenic for lysozyme. Am J Pathol 169: 303-313.
    • (2006) Am J Pathol , vol.169 , pp. 303-313
    • Liu, H.1    Zheng, F.2    Li, Z.3    Uribarri, J.4    Ren, B.5
  • 46
    • 0034721931 scopus 로고    scopus 로고
    • Cyclophilin A is a secreted growth factor induced by oxidative stress
    • Jin ZG, Melaragno MG, Liao D.F., Yan C., Haendeler J, et al. (2000) Cyclophilin A is a secreted growth factor induced by oxidative stress. Circ Res 87: 789-796.
    • (2000) Circ Res , vol.87 , pp. 789-796
    • Jin, Z.G.1    Melaragno, M.G.2    Liao, D.F.3    Yan, C.4    Haendeler, J.5
  • 47
    • 78651502102 scopus 로고    scopus 로고
    • Cyclophilin A is an inflammatory mediator that promotes atherosclerosis in apolipoprotein E-deficient mice
    • Nigro P, Satoh K, O'Dell MR, Soe NN, Cui Z, et al. (2011) Cyclophilin A is an inflammatory mediator that promotes atherosclerosis in apolipoprotein E-deficient mice. J Exp Med 208: 53-66.
    • (2011) J Exp Med , vol.208 , pp. 53-66
    • Nigro, P.1    Satoh, K.2    O'Dell, M.R.3    Soe, N.N.4    Cui, Z.5
  • 48
    • 12144291702 scopus 로고    scopus 로고
    • Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions
    • Coppinger JA, Cagney G, Toomey S., Kislinger T, Belton O, et al. (2004) Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions. Blood 103: 2096-2104.
    • (2004) Blood , vol.103 , pp. 2096-2104
    • Coppinger, J.A.1    Cagney, G.2    Toomey, S.3    Kislinger, T.4    Belton, O.5


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