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Volumn 387, Issue 10-11, 2006, Pages 1377-1383

N-ethylmaleimide-sensitive factor: A redox sensor in exocytosis

Author keywords

Endothelial cell; Hydrogen peroxide; Nitric oxide; Peroxynitrite; Platelet; Reactive oxygen species; Superoxide; Weibel Palade bodies

Indexed keywords

CYSTEINE; HYDROGEN PEROXIDE; N ETHYLMALEIMIDE SENSITIVE FACTOR; NITRIC OXIDE; SNARE PROTEIN;

EID: 33750610483     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2006.173     Document Type: Conference Paper
Times cited : (28)

References (79)
  • 1
    • 0842299577 scopus 로고    scopus 로고
    • Antiinflammatory activity of soluble guanylate cyclase: cGMP-dependent down-regulation of P-selectin expression and leukocyte recruitment
    • Ahluwalia, A., Foster, P., Scotland, R.S., McLean, P.G., Mathur, A., Perretti, M., Moncada, S., and Hobbs, A.J. (2004). Antiinflammatory activity of soluble guanylate cyclase: cGMP-dependent down-regulation of P-selectin expression and leukocyte recruitment. Proc. Natl. Acad. Sci. USA 101, 1386-1391.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1386-1391
    • Ahluwalia, A.1    Foster, P.2    Scotland, R.S.3    McLean, P.G.4    Mathur, A.5    Perretti, M.6    Moncada, S.7    Hobbs, A.J.8
  • 3
    • 0033592895 scopus 로고    scopus 로고
    • Crystal structure of the Sec18p N-terminal domain
    • Babor, S.M. and Fass, D. (1999). Crystal structure of the Sec18p N-terminal domain. Proc. Natl. Acad. Sci. USA 96, 14759-14764.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14759-14764
    • Babor, S.M.1    Fass, D.2
  • 5
    • 0038299375 scopus 로고    scopus 로고
    • Inhaled NO inhibits platelet aggregation and elevates plasma but not intraplatelet cGMP in healthy human volunteers
    • Beghetti, M., Sparling, C., Cox, P.N., Stephens, D., and Adatia, I. (2003). Inhaled NO inhibits platelet aggregation and elevates plasma but not intraplatelet cGMP in healthy human volunteers. Am. J. Physiol. Heart Circ. Physiol. 285, H637-H642.
    • (2003) Am. J. Physiol. Heart Circ. Physiol. , vol.285
    • Beghetti, M.1    Sparling, C.2    Cox, P.N.3    Stephens, D.4    Adatia, I.5
  • 6
    • 0026709643 scopus 로고
    • Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components
    • Bittner, M.A. and Holz, R.W. (1992). Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components. J. Biol. Chem. 267, 16219-16225.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16219-16225
    • Bittner, M.A.1    Holz, R.W.2
  • 8
    • 0025277355 scopus 로고
    • Properties of a novel nitric oxide-stimulated ADP-ribosyltransferase
    • Brune, B. and Lapetina, E.G. (1990). Properties of a novel nitric oxide-stimulated ADP-ribosyltransferase. Arch. Biochem. Biophys. 279, 286-290.
    • (1990) Arch. Biochem. Biophys. , vol.279 , pp. 286-290
    • Brune, B.1    Lapetina, E.G.2
  • 9
    • 0032054866 scopus 로고    scopus 로고
    • Analysis of regulated exocytosis in adrenal chromaffin cells: Insights into NSF/SNAP/SNARE function
    • Burgoyne, R.D. and Morgan, A. (1998). Analysis of regulated exocytosis in adrenal chromaffin cells: insights into NSF/SNAP/SNARE function. Bioessays 20, 328-335.
    • (1998) Bioessays , vol.20 , pp. 328-335
    • Burgoyne, R.D.1    Morgan, A.2
  • 11
    • 0034634281 scopus 로고    scopus 로고
    • Endothelial dysfunction in cardiovascular diseases: The role of oxidant stress
    • Cai, H. and Harrison, D.G. (2000). Endothelial dysfunction in cardiovascular diseases: the role of oxidant stress. Circ. Res. 87, 840-844.
    • (2000) Circ. Res. , vol.87 , pp. 840-844
    • Cai, H.1    Harrison, D.G.2
  • 12
    • 0042379916 scopus 로고    scopus 로고
    • The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases
    • Cai, H., Griendling, K.K., and Harrison, D.G. (2003). The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases. Trends Pharmacol. Sci. 24, 471-478.
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 471-478
    • Cai, H.1    Griendling, K.K.2    Harrison, D.G.3
  • 13
    • 0034142239 scopus 로고    scopus 로고
    • Molecular mechanisms of platelet exocytosis: Role of SNAP-23 and syntaxin 2 in dense core granule release
    • Chen, D., Bernstein, A.M., Lemons, P.P., and Whiteheart, S.W. (2000a). Molecular mechanisms of platelet exocytosis: role of SNAP-23 and syntaxin 2 in dense core granule release. Blood 95, 921-929.
    • (2000) Blood , vol.95 , pp. 921-929
    • Chen, D.1    Bernstein, A.M.2    Lemons, P.P.3    Whiteheart, S.W.4
  • 14
    • 0034283702 scopus 로고    scopus 로고
    • Molecular mechanisms of platelet exocytosis: Role of SNAP-23 and syntaxin 2 and 4 in lysosome release
    • Chen, D., Lemons, P.P., Schraw, T., and Whiteheart, S.W. (2000b). Molecular mechanisms of platelet exocytosis: role of SNAP-23 and syntaxin 2 and 4 in lysosome release. Blood 96, 1782-1788.
    • (2000) Blood , vol.96 , pp. 1782-1788
    • Chen, D.1    Lemons, P.P.2    Schraw, T.3    Whiteheart, S.W.4
  • 15
    • 0030734267 scopus 로고    scopus 로고
    • Nitric oxide in excitable tissues: Physiological roles and disease
    • Christopherson, K.S. and Bredt, D.S. (1997). Nitric oxide in excitable tissues: physiological roles and disease. J. Clin. Invest. 100, 2424-2429.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2424-2429
    • Christopherson, K.S.1    Bredt, D.S.2
  • 16
    • 2942733214 scopus 로고    scopus 로고
    • Role of endothelial dysfunction in atherosclerosis
    • Davignon, J. and Ganz, P. (2004). Role of endothelial dysfunction in atherosclerosis. Circulation 109, III27-32.
    • (2004) Circulation , vol.109
    • Davignon, J.1    Ganz, P.2
  • 17
    • 0029159779 scopus 로고
    • Nitric oxide decreases cytokine-induced endothelial activation. Nitric oxide selectively reduces endothelial expression of adhesion molecules and proinflammatory cytokines
    • De Caterina, R., Libby, P., Peng, H.B., Thannickal, V.J., Rajavashisth, T.B., Gimbrone, M.A. Jr., Shin, W.S., and Liao, J.K. (1995). Nitric oxide decreases cytokine-induced endothelial activation. Nitric oxide selectively reduces endothelial expression of adhesion molecules and proinflammatory cytokines. J. Clin. Invest. 96, 60-68.
    • (1995) J. Clin. Invest. , vol.96 , pp. 60-68
    • De Caterina, R.1    Libby, P.2    Peng, H.B.3    Thannickal, V.J.4    Rajavashisth, T.B.5    Gimbrone Jr., M.A.6    Shin, W.S.7    Liao, J.K.8
  • 18
    • 0242552817 scopus 로고    scopus 로고
    • Cyclic GMP-dependent protein kinases and the cardiovascular system: Insights from genetically modified mice
    • Feil, R., Lohmann, S.M., de Jonge, H., Walter, U., and Hofmann, F. (2003). Cyclic GMP-dependent protein kinases and the cardiovascular system: insights from genetically modified mice. Circ. Res. 93, 907-916.
    • (2003) Circ. Res. , vol.93 , pp. 907-916
    • Feil, R.1    Lohmann, S.M.2    De Jonge, H.3    Walter, U.4    Hofmann, F.5
  • 19
    • 0036624735 scopus 로고    scopus 로고
    • Subcellular distribution of three functional platelet SNARE proteins: Human cellubrevin, SNAP-23, and syntaxin 2
    • Feng, D., Crane, K., Rozenvayn, N., Dvorak, A.M., and Flaumenhaft, R. (2002). Subcellular distribution of three functional platelet SNARE proteins: human cellubrevin, SNAP-23, and syntaxin 2. Blood 99, 4006-4014.
    • (2002) Blood , vol.99 , pp. 4006-4014
    • Feng, D.1    Crane, K.2    Rozenvayn, N.3    Dvorak, A.M.4    Flaumenhaft, R.5
  • 20
    • 0024390169 scopus 로고
    • Endothelium-derived relaxing and contracting factors
    • Furchgott, R.F. and Vanhoutte, P.M. (1989). Endothelium-derived relaxing and contracting factors. FASEB J. 3, 2007-2018.
    • (1989) FASEB J. , vol.3 , pp. 2007-2018
    • Furchgott, R.F.1    Vanhoutte, P.M.2
  • 21
    • 0031920694 scopus 로고    scopus 로고
    • Evidence for a cyclic GMP-independent mechanism in the anti-platelet action of S-nitrosoglutathione
    • Gordge, M.P., Hothersall, J.S., and Noronha-Dutra, A.A. (1998). Evidence for a cyclic GMP-independent mechanism in the anti-platelet action of S-nitrosoglutathione. Br. J. Pharmacol. 124, 141-148.
    • (1998) Br. J. Pharmacol. , vol.124 , pp. 141-148
    • Gordge, M.P.1    Hothersall, J.S.2    Noronha-Dutra, A.A.3
  • 22
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisaki, H., Jahn, R., and Heuser, J.E. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 23
    • 0025042832 scopus 로고
    • Haem-dependent activation of guanylate cyclase and cyclic GMP formation by endogenous nitric oxide: A unique transduction mechanism for transcellular signaling
    • Ignarro, L.J. (1990). Haem-dependent activation of guanylate cyclase and cyclic GMP formation by endogenous nitric oxide: a unique transduction mechanism for transcellular signaling. Pharmacol. Toxicol. 67, 1-7.
    • (1990) Pharmacol. Toxicol. , vol.67 , pp. 1-7
    • Ignarro, L.J.1
  • 25
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R. and Sudhof, T.C. (1999). Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 26
    • 0025731835 scopus 로고
    • Nitric oxide: An endogenous modulator of leukocyte adhesion
    • Kubes, P., Suzuki, M., and Granger, D.N. (1991). Nitric oxide: an endogenous modulator of leukocyte adhesion. Proc. Natl. Acad. Sci. USA 88, 4651-4655.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4651-4655
    • Kubes, P.1    Suzuki, M.2    Granger, D.N.3
  • 27
    • 0035954312 scopus 로고    scopus 로고
    • Genetic deficiency of inducible nitric oxide synthase reduces atherosclerosis and lowers plasma lipid peroxides in apolipoprotein E-knockout mice
    • Kuhlencordt, P.J., Chen, J., Han, F., Astern, J., and Huang, P.L. (2001a). Genetic deficiency of inducible nitric oxide synthase reduces atherosclerosis and lowers plasma lipid peroxides in apolipoprotein E-knockout mice. Circulation 103, 3099-3104.
    • (2001) Circulation , vol.103 , pp. 3099-3104
    • Kuhlencordt, P.J.1    Chen, J.2    Han, F.3    Astern, J.4    Huang, P.L.5
  • 28
    • 0035943042 scopus 로고    scopus 로고
    • Accelerated atherosclerosis, aortic aneurysm formation, and ischemic heart disease in apolipoprotein E/endothelial nitric oxide synthase double-knockout mice
    • Kuhlencordt, P.J., Gyurko, R., Han, F., Scherrer-Crosbie, M., Aretz, T.H., Hajjar, R., Picard, M.H., and Huang, P.L. (2001b). Accelerated atherosclerosis, aortic aneurysm formation, and ischemic heart disease in apolipoprotein E/endothelial nitric oxide synthase double-knockout mice. Circulation 104, 448-454.
    • (2001) Circulation , vol.104 , pp. 448-454
    • Kuhlencordt, P.J.1    Gyurko, R.2    Han, F.3    Scherrer-Crosbie, M.4    Aretz, T.H.5    Hajjar, R.6    Picard, M.H.7    Huang, P.L.8
  • 30
    • 0030846534 scopus 로고    scopus 로고
    • Regulated secretion in platelets: Identification of elements of the platelet exocytosis machinery
    • Lemons, P.P., Chen, D., Bernstein, A.M., Bennett, M.K., and Whiteheart, S.W. (1997). Regulated secretion in platelets: identification of elements of the platelet exocytosis machinery. Blood 90, 1490-1500.
    • (1997) Blood , vol.90 , pp. 1490-1500
    • Lemons, P.P.1    Chen, D.2    Bernstein, A.M.3    Bennett, M.K.4    Whiteheart, S.W.5
  • 31
    • 0034719338 scopus 로고    scopus 로고
    • Molecular mechanisms of platelet exocytosis: Requirements for α-granule release
    • Lemons, P.P., Chen, D., and Whiteheart, S.W. (2000). Molecular mechanisms of platelet exocytosis: requirements for α-granule release. Biochem. Biophys. Res. Commun. 267, 875-880.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 875-880
    • Lemons, P.P.1    Chen, D.2    Whiteheart, S.W.3
  • 32
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide- sensitive fusion protein
    • Lenzen, C.U., Steinmann, D., Whiteheart, S.W., and Weis, W.I. (1998). Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 33
    • 0034523701 scopus 로고    scopus 로고
    • Mechanisms of synaptic vesicle exocytosis
    • Lin, R.C. and Scheller, R.H. (2000). Mechanisms of synaptic vesicle exocytosis. Annu. Rev. Cell Dev. Biol. 16, 19-49.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 19-49
    • Lin, R.C.1    Scheller, R.H.2
  • 34
    • 0029420271 scopus 로고
    • Presynaptic proteins involved in exocytosis in Drosophila melanogaster: A genetic analysis
    • Littleton, J.T. and Bellen, H.J. (1995). Presynaptic proteins involved in exocytosis in Drosophila melanogaster: a genetic analysis. Invert. Neurosci. 1, 3-13.
    • (1995) Invert. Neurosci. , vol.1 , pp. 3-13
    • Littleton, J.T.1    Bellen, H.J.2
  • 35
    • 0032142949 scopus 로고    scopus 로고
    • Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly
    • Littleton, J.T., Chapman, E.R., Kreber, R., Garment, M.B., Carlson, S.D., and Ganetzky, B. (1998). Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly. Neuron 21, 401-413.
    • (1998) Neuron , vol.21 , pp. 401-413
    • Littleton, J.T.1    Chapman, E.R.2    Kreber, R.3    Garment, M.B.4    Carlson, S.D.5    Ganetzky, B.6
  • 36
    • 0026666810 scopus 로고
    • Antiplatelet and antithrombotic effects of organic nitrates
    • Loscalzo, J. (1992). Antiplatelet and antithrombotic effects of organic nitrates. Am. J. Cardiol. 70, 18B-22B.
    • (1992) Am. J. Cardiol. , vol.70
    • Loscalzo, J.1
  • 37
    • 0035957630 scopus 로고    scopus 로고
    • Nitric oxide insufficiency, platelet activation, and arterial thrombosis
    • Loscalzo, J. (2001). Nitric oxide insufficiency, platelet activation, and arterial thrombosis. Circ. Res. 88, 756-762.
    • (2001) Circ. Res. , vol.88 , pp. 756-762
    • Loscalzo, J.1
  • 39
    • 0023707176 scopus 로고
    • Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack
    • Malhotra, V., Orci, L., Glick, B.S., Block, M.R., and Rothman, J.E. (1988). Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack. Cell 54, 221-227.
    • (1988) Cell , vol.54 , pp. 221-227
    • Malhotra, V.1    Orci, L.2    Glick, B.S.3    Block, M.R.4    Rothman, J.E.5
  • 40
    • 0025053420 scopus 로고
    • Unraveling the biological significance of nitric oxide
    • Marletta, M.A., Tayeh, M.A., and Hevel, J.M. (1990). Unraveling the biological significance of nitric oxide. Biofactors 2, 219-225.
    • (1990) Biofactors , vol.2 , pp. 219-225
    • Marletta, M.A.1    Tayeh, M.A.2    Hevel, J.M.3
  • 41
    • 0035852845 scopus 로고    scopus 로고
    • Inhibition of NF-κB by S-nitrosylation
    • Marshall, H.E. and Stamler, J.S. (2001). Inhibition of NF-κB by S-nitrosylation. Biochemistry 40, 1688-1693.
    • (2001) Biochemistry , vol.40 , pp. 1688-1693
    • Marshall, H.E.1    Stamler, J.S.2
  • 45
    • 0031040763 scopus 로고    scopus 로고
    • Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
    • Mayer, A. and Wickner, W. (1997). Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J. Cell Biol. 136, 307-317.
    • (1997) J. Cell Biol. , vol.136 , pp. 307-317
    • Mayer, A.1    Wickner, W.2
  • 46
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W., and Haas, A. (1996). Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 47
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • McBride, H.M., Rybin, V., Murphy, C., Giner, A., Teasdale, R., and Zerial, M. (1999). Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 98, 377-386.
    • (1999) Cell , vol.98 , pp. 377-386
    • McBride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5    Zerial, M.6
  • 48
    • 0029438321 scopus 로고
    • Nitric oxide and cGMP signaling
    • McDonald, L.J. and Murad, F. (1995). Nitric oxide and cGMP signaling. Adv. Pharmacol. 34, 263-275.
    • (1995) Adv. Pharmacol. , vol.34 , pp. 263-275
    • McDonald, L.J.1    Murad, F.2
  • 49
    • 0019430671 scopus 로고
    • Evidence for the inhibitory role of guanosine 3′,5′- monophosphate in ADP-induced human platelet aggregation in the presence of nitric oxide and related vasodilators
    • Mellion, B.T., Ignarro, L.J., Ohlstein, E.H., Pontecorvo, E.G., Hyman, A.L., and Kadowitz, P.J. (1981). Evidence for the inhibitory role of guanosine 3′,5′-monophosphate in ADP-induced human platelet aggregation in the presence of nitric oxide and related vasodilators. Blood 57, 946-955.
    • (1981) Blood , vol.57 , pp. 946-955
    • Mellion, B.T.1    Ignarro, L.J.2    Ohlstein, E.H.3    Pontecorvo, E.G.4    Hyman, A.L.5    Kadowitz, P.J.6
  • 50
    • 0025001733 scopus 로고
    • Inhibition of fibrinogen binding to human platelets by S-nitroso N-acetylcysteine
    • Mendelsohn, M.E., O'Neill, S., George, D., and Loscalzo, J. (1990). Inhibition of fibrinogen binding to human platelets by S-nitroso N-acetylcysteine. J. Biol. Chem. 265, 19028-19034.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19028-19034
    • Mendelsohn, M.E.1    O'Neill, S.2    George, D.3    Loscalzo, J.4
  • 51
    • 0030711558 scopus 로고    scopus 로고
    • Nitric oxide synthases: Which, where, how, and why?
    • Michel, T. and Feron, O. (1997). Nitric oxide synthases: which, where, how, and why? J. Clin. Invest. 100, 2146-2152.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2146-2152
    • Michel, T.1    Feron, O.2
  • 52
    • 16044369508 scopus 로고    scopus 로고
    • Classic clues to NSF function
    • Morgan, A. (1996). Classic clues to NSF function. Nature 382, 680.
    • (1996) Nature , vol.382 , pp. 680
    • Morgan, A.1
  • 57
    • 0033566680 scopus 로고    scopus 로고
    • Molecular control of nitric oxide synthases in the cardiovascular system
    • Papapetropoulos, A., Rudic, R.D., and Sessa, W.C. (1999). Molecular control of nitric oxide synthases in the cardiovascular system. Cardiovasc. Res. 43, 509-520.
    • (1999) Cardiovasc. Res. , vol.43 , pp. 509-520
    • Papapetropoulos, A.1    Rudic, R.D.2    Sessa, W.C.3
  • 58
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATP-ases with diverse functions
    • Patel, S. and Latterich, M. (1998). The AAA team: related ATP-ases with diverse functions. Trends Cell Biol. 8, 65-71.
    • (1998) Trends Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 59
    • 0032570313 scopus 로고    scopus 로고
    • Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation
    • Pawloski, J.R., Swaminathan, R.V., and Stamler, J.S. (1998). Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation. Circulation 97, 263-267.
    • (1998) Circulation , vol.97 , pp. 263-267
    • Pawloski, J.R.1    Swaminathan, R.V.2    Stamler, J.S.3
  • 60
    • 0029011129 scopus 로고
    • Induction and stabilization of IκBα by nitric oxide mediates inhibition of NF-κB
    • Peng, H.B., Libby, P., and Liao, J.K. (1995). Induction and stabilization of IκBα by nitric oxide mediates inhibition of NF-κB. J. Biol. Chem. 270, 14214-14219.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14214-14219
    • Peng, H.B.1    Libby, P.2    Liao, J.K.3
  • 62
    • 0033553494 scopus 로고    scopus 로고
    • Nitric oxide inhibits thrombin receptor-activating peptide-induced phosphoinositide 3-kinase activity in human platelets
    • Pigazzi, A., Heydrick, S., Folli, F., Benoit, S., Michelson, A., and Loscalzo, J. (1999). Nitric oxide inhibits thrombin receptor-activating peptide-induced phosphoinositide 3-kinase activity in human platelets. J. Biol. Chem. 274, 14368-14375.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14368-14375
    • Pigazzi, A.1    Heydrick, S.2    Folli, F.3    Benoit, S.4    Michelson, A.5    Loscalzo, J.6
  • 63
    • 0033566920 scopus 로고    scopus 로고
    • A critical role for N-ethylmaleimide-sensitive fusion protein (NSF) in platelet granule secretion
    • Polgar, J. and Reed, G.L. (1999). A critical role for N-ethylmaleimide-sensitive fusion protein (NSF) in platelet granule secretion. Blood 94, 1313-1318.
    • (1999) Blood , vol.94 , pp. 1313-1318
    • Polgar, J.1    Reed, G.L.2
  • 64
    • 0036683001 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion
    • Polgar, J., Chung, S.H., and Reed, G.L. (2002). Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion. Blood 100, 1081-1083.
    • (2002) Blood , vol.100 , pp. 1081-1083
    • Polgar, J.1    Chung, S.H.2    Reed, G.L.3
  • 65
    • 0027226283 scopus 로고
    • Regulation of vascular homeostasis by nitric oxide
    • Radomski, M.W. and Moncada, S. (1993). Regulation of vascular homeostasis by nitric oxide. Thromb. Haemost. 70, 36-41.
    • (1993) Thromb. Haemost. , vol.70 , pp. 36-41
    • Radomski, M.W.1    Moncada, S.2
  • 66
    • 0023200487 scopus 로고
    • Endogenous nitric oxide inhibits human platelet adhesion to vascular endothelium
    • Radomski, M.W., Palmer, R.M., and Moncada, S. (1987). Endogenous nitric oxide inhibits human platelet adhesion to vascular endothelium. Lancet 2, 1057-1058.
    • (1987) Lancet , vol.2 , pp. 1057-1058
    • Radomski, M.W.1    Palmer, R.M.2    Moncada, S.3
  • 67
    • 0033561424 scopus 로고    scopus 로고
    • Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: Implications for platelet secretion
    • Reed, G.L., Houng, A.K., and Fitzgerald, M.L. (1999). Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion. Blood 93, 2617-2626.
    • (1999) Blood , vol.93 , pp. 2617-2626
    • Reed, G.L.1    Houng, A.K.2    Fitzgerald, M.L.3
  • 68
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 69
    • 0031551130 scopus 로고    scopus 로고
    • Membrane fusion. Bridging the gap by AAA ATPases
    • Rowe, T. and Balch, W.E. (1997). Membrane fusion. Bridging the gap by AAA ATPases. Nature 388, 20-21.
    • (1997) Nature , vol.388 , pp. 20-21
    • Rowe, T.1    Balch, W.E.2
  • 70
    • 0025804983 scopus 로고
    • Endothelium-derived relaxing and contracting factors
    • Rubanyi, G.M. (1991). Endothelium-derived relaxing and contracting factors. J. Cell Biochem. 46, 27-36.
    • (1991) J. Cell Biochem. , vol.46 , pp. 27-36
    • Rubanyi, G.M.1
  • 71
    • 0032520153 scopus 로고    scopus 로고
    • Direct evidence for the importance of endothelium-derived nitric oxide in vascular remodeling
    • Rudic, R.D., Shesely, E.G., Maeda, N., Smithies, O., Segal, S.S., and Sessa, W.C. (1998). Direct evidence for the importance of endothelium-derived nitric oxide in vascular remodeling. J. Clin. Invest. 101, 731-736.
    • (1998) J. Clin. Invest. , vol.101 , pp. 731-736
    • Rudic, R.D.1    Shesely, E.G.2    Maeda, N.3    Smithies, O.4    Segal, S.S.5    Sessa, W.C.6
  • 72
    • 0034694667 scopus 로고    scopus 로고
    • Inhibition of human platelet aggregation by nitric oxide donor drugs: Relative contribution of cGMP-independent mechanisms
    • Sogo, N., Magid, K.S., Shaw, C.A., Webb, D.J., and Megson, I.L. (2000). Inhibition of human platelet aggregation by nitric oxide donor drugs: relative contribution of cGMP-independent mechanisms. Biochem. Biophys. Res. Commun. 279, 412-419.
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 412-419
    • Sogo, N.1    Magid, K.S.2    Shaw, C.A.3    Webb, D.J.4    Megson, I.L.5
  • 73
    • 10744231672 scopus 로고    scopus 로고
    • S-Nitrosylation of NSF controls membrane trafficking
    • Sollner, T.H. and Sequeira, S. (2003). S-Nitrosylation of NSF controls membrane trafficking. Cell 115, 127-129.
    • (2003) Cell , vol.115 , pp. 127-129
    • Sollner, T.H.1    Sequeira, S.2
  • 75
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler, J.S., Singel, D.J., and Loscalzo, J. (1992). Biochemistry of nitric oxide and its redox-activated forms. Science 258, 1898-1902.
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 76
    • 0032955272 scopus 로고    scopus 로고
    • Inhibition of platelet aggregation by S-nitroso-cysteine via cGMP-independent mechanisms: Evidence of inhibition of thromboxane A2 synthesis in human blood platelets
    • Tsikas, D., Ikic, M., Tewes, K.S., Raida, M., and Frolich, J.C. (1999). Inhibition of platelet aggregation by S-nitroso-cysteine via cGMP-independent mechanisms: evidence of inhibition of thromboxane A2 synthesis in human blood platelets. FEBS Lett. 442, 162-166.
    • (1999) FEBS Lett. , vol.442 , pp. 162-166
    • Tsikas, D.1    Ikic, M.2    Tewes, K.S.3    Raida, M.4    Frolich, J.C.5
  • 77
    • 0028132782 scopus 로고
    • N-Ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart, S.W., Rossnagel, K., Buhrow, S.A., Brunner, M., Jaenicke, R., and Rothman, J.E. (1994). N-Ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 126, 945-954.
    • (1994) J. Cell Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 78
    • 0036193746 scopus 로고    scopus 로고
    • Oxidants painting the cysteine chapel: Redox regulation of PTPs
    • Xu, D., Rovira, I.I., and Finkel, T. (2002). Oxidants painting the cysteine chapel: redox regulation of PTPs. Dev. Cell 2, 251-252.
    • (2002) Dev. Cell , vol.2 , pp. 251-252
    • Xu, D.1    Rovira, I.I.2    Finkel, T.3
  • 79
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu, R.C., Hanson, P.I., Jahn, R., and Brunger, A.T. (1998). Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol. 5, 803-811.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4


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