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Volumn 124, Issue 10, 2014, Pages 4503-4516

Syntaxin-binding protein STXBP5 inhibits endothelial exocytosis and promotes platelet secretion

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CELLUBREVIN; INSULIN; PADGEM PROTEIN; SNARE PROTEIN; SYNTAXIN; SYNTAXIN 4; SYNTAXIN BINDING PROTEIN 5; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR CLEAVING PROTEINASE; ADAM PROTEIN; ADAMTS13 PROTEIN, HUMAN; ADAMTS13 PROTEIN, MOUSE; METALLOPROTEINASE; NERVE PROTEIN; STXBP5 PROTEIN, HUMAN; SYNAPTOBREVIN; TOMOSYN PROTEIN, MOUSE;

EID: 84907495473     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI71245     Document Type: Article
Times cited : (67)

References (87)
  • 1
    • 50449098285 scopus 로고    scopus 로고
    • Mechanisms of thrombus formation
    • Furie B, Furie BC. Mechanisms of thrombus formation. N Engl J Med. 2008;359(9):938-949.
    • (2008) N Engl J Med. , vol.359 , Issue.9 , pp. 938-949
    • Furie, B.1    Furie, B.C.2
  • 2
    • 84894222894 scopus 로고    scopus 로고
    • Treatment of venous thromboembolism
    • Wells PS, Forgie MA, Rodger MA. Treatment of venous thromboembolism. JAMA. 2014;311(7):717-728.
    • (2014) JAMA. , vol.311 , Issue.7 , pp. 717-728
    • Wells, P.S.1    Forgie, M.A.2    Rodger, M.A.3
  • 3
    • 84873025833 scopus 로고    scopus 로고
    • International clinical practice guidelines for the treatment and prophylaxis of venous thromboembolism in patients with cancer
    • Farge D, et al. International clinical practice guidelines for the treatment and prophylaxis of venous thromboembolism in patients with cancer. J Thromb Haemost. 2013;11(1):56-70.
    • (2013) J Thromb Haemost. , vol.11 , Issue.1 , pp. 56-70
    • Farge, D.1
  • 4
    • 45949101608 scopus 로고    scopus 로고
    • The vessel wall and its interactions
    • Wagner DD, Frenette PS. The vessel wall and its interactions. Blood. 2008;111(11):5271-5281.
    • (2008) Blood , vol.111 , Issue.11 , pp. 5271-5281
    • Wagner, D.D.1    Frenette, P.S.2
  • 5
    • 39749109478 scopus 로고    scopus 로고
    • Triggers, targets and treatments for thrombosis
    • Mackman N. Triggers, targets and treatments for thrombosis. Nature. 2008;451(7181):914-918.
    • (2008) Nature , vol.451 , Issue.7181 , pp. 914-918
    • Mackman, N.1
  • 6
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide
    • Ignarro LJ, Buga GM, Wood KS, Byrns RE, Chaudhuri G. Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide. Proc Natl Acad Sci U S A. 1987;84(24):9265-9269.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , Issue.24 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 7
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer RM, Ferrige AG, Moncada S. Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature. 1987;327(6122):524-526.
    • (1987) Nature , vol.327 , Issue.6122 , pp. 524-526
    • Palmer, R.M.1    Ferrige, A.G.2    Moncada, S.3
  • 8
  • 9
    • 18044384409 scopus 로고    scopus 로고
    • Role of CD39 (NTPDase-1) in thromboregulation, cerebroprotection, and cardioprotection
    • Marcus AJ, et al. Role of CD39 (NTPDase-1) in thromboregulation, cerebroprotection, and cardioprotection. Semin Thromb Hemost. 2005;31(2):234-246.
    • (2005) Semin Thromb Hemost. , vol.31 , Issue.2 , pp. 234-246
    • Marcus, A.J.1
  • 11
    • 0000534956 scopus 로고
    • New cytoplasmic components in arterial endothelia
    • Weibel ER, Palade GE. New cytoplasmic components in arterial endothelia. J Cell Biol. 1964;23:101-112.
    • (1964) J Cell Biol. , vol.23 , pp. 101-112
    • Weibel, E.R.1    Palade, G.E.2
  • 12
    • 38949205667 scopus 로고    scopus 로고
    • Glycoprotein Ibalpha and von Willebrand factor in primary platelet adhesion and thrombus formation: Lessons from mutant mice
    • Bergmeier W, Chauhan AK, Wagner DD. Glycoprotein Ibalpha and von Willebrand factor in primary platelet adhesion and thrombus formation: lessons from mutant mice. Thromb Haemost. 2008;99(2):264-270.
    • (2008) Thromb Haemost. , vol.99 , Issue.2 , pp. 264-270
    • Bergmeier, W.1    Chauhan, A.K.2    Wagner, D.D.3
  • 13
    • 0027259388 scopus 로고
    • The Weibel-Palade body: The storage granule for von Willebrand factor and P-selectin
    • Wagner DD. The Weibel-Palade body: the storage granule for von Willebrand factor and P-selectin. Thromb Haemost. 1993;70(1):105-110.
    • (1993) Thromb Haemost. , vol.70 , Issue.1 , pp. 105-110
    • Wagner, D.D.1
  • 14
    • 37349084977 scopus 로고    scopus 로고
    • Inhibition of N-ethylmaleimide-sensitive factor protects against myocardial ischemia/reperfusion injury
    • Calvert JW, et al. Inhibition of N-ethylmaleimide-sensitive factor protects against myocardial ischemia/reperfusion injury. Circ Res. 2007;101(12):1247-1254.
    • (2007) Circ Res. , vol.101 , Issue.12 , pp. 1247-1254
    • Calvert, J.W.1
  • 15
    • 20444452442 scopus 로고    scopus 로고
    • HMG-CoA reductase inhibitors inhibit endothelial exocytosis and decrease myocardial infarct size
    • Yamakuchi M, et al. HMG-CoA reductase inhibitors inhibit endothelial exocytosis and decrease myocardial infarct size. Circ Res. 2005;96(11):1185-1192.
    • (2005) Circ Res. , vol.96 , Issue.11 , pp. 1185-1192
    • Yamakuchi, M.1
  • 16
    • 84867159190 scopus 로고    scopus 로고
    • JAMA patient page. Bleeding disorders
    • Goodman DM, Burke AE, Livingston EH. JAMA patient page. Bleeding disorders. JAMA. 2012;308(14):1492.
    • (2012) JAMA. , vol.308 , Issue.14 , pp. 1492
    • Goodman, D.M.1    Burke, A.E.2    Livingston, E.H.3
  • 17
    • 0028909230 scopus 로고
    • Hemostatic factors and the risk of myocardial infarction or sudden death in patients with angina pectoris. European Concerted Action on Thrombosis and Disabilities Angina Pectoris Study Group
    • Thompson SG, Kienast J, Pyke SD, Haverkate F, Van De Loo JC. Hemostatic factors and the risk of myocardial infarction or sudden death in patients with angina pectoris. European Concerted Action on Thrombosis and Disabilities Angina Pectoris Study Group. N Engl J Med. 1995;332(10):635-641.
    • (1995) N Engl J Med. , vol.332 , Issue.10 , pp. 635-641
    • Thompson, S.G.1    Kienast, J.2    Pyke, S.D.3    Haverkate, F.4    Van De Loo, J.C.5
  • 18
    • 41649119245 scopus 로고    scopus 로고
    • Von Willebrand factor in cardiovascular disease: Focus on acute coronary syndromes
    • Spiel AO, Gilbert JC, Jilma B. von Willebrand factor in cardiovascular disease: focus on acute coronary syndromes. Circulation. 2008;117(11):1449-1459.
    • (2008) Circulation. , vol.117 , Issue.11 , pp. 1449-1459
    • Spiel, A.O.1    Gilbert, J.C.2    Jilma, B.3
  • 19
    • 33646771330 scopus 로고    scopus 로고
    • Von Willebrand factor, endothelial dysfunction, and cardiovascular disease
    • Vischer UM. von Willebrand factor, endothelial dysfunction, and cardiovascular disease. J Thromb Haemost. 2006;4(6):1186-1193.
    • (2006) J Thromb Haemost. , vol.4 , Issue.6 , pp. 1186-1193
    • Vischer, U.M.1
  • 20
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R, Sudhof TC. Membrane fusion and exocytosis. Annu Rev Biochem. 1999;68:863-911.
    • (1999) Annu Rev Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 21
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE. Mechanisms of intracellular protein transport. Nature. 1994;372(6501):55-63.
    • (1994) Nature , vol.372 , Issue.6501 , pp. 55-63
    • Rothman, J.E.1
  • 23
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Sudhof TC. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 1995;375(6533):645-653.
    • (1995) Nature , vol.375 , Issue.6533 , pp. 645-653
    • Sudhof, T.C.1
  • 24
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs - Engines for membrane fusion
    • Jahn R, Scheller RH. SNAREs - engines for membrane fusion. Nat Rev Mol Cell Biol. 2006;7(9):631-643.
    • (2006) Nat Rev Mol Cell Biol. , vol.7 , Issue.9 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 25
    • 0033637985 scopus 로고    scopus 로고
    • The synaptic vesicle cycle revisited
    • Sudhof TC. The synaptic vesicle cycle revisited. Neuron. 2000;28(2):317-320.
    • (2000) Neuron. , vol.28 , Issue.2 , pp. 317-320
    • Sudhof, T.C.1
  • 26
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: Disparate players and common principles
    • Martens S, McMahon HT. Mechanisms of membrane fusion: disparate players and common principles. Nat Rev Mol Cell Biol. 2008;9(7):543-556.
    • (2008) Nat Rev Mol Cell Biol. , vol.9 , Issue.7 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 28
    • 84866050788 scopus 로고    scopus 로고
    • Secretion of soluble vascular endothelial growth factor receptor 1 (sVEGFR1/sFlt1) requires Arf1, Arf6, and Rab11 GTPases
    • Jung JJ, Tiwari A, Inamdar SM, Thomas CP, Goel A, Choudhury A. Secretion of soluble vascular endothelial growth factor receptor 1 (sVEGFR1/sFlt1) requires Arf1, Arf6, and Rab11 GTPases. PLoS One. 2012;7(9):e44572.
    • (2012) PLoS One. , vol.7 , Issue.9 , pp. e44572
    • Jung, J.J.1    Tiwari, A.2    Inamdar, S.M.3    Thomas, C.P.4    Goel, A.5    Choudhury, A.6
  • 29
  • 30
    • 84934439592 scopus 로고    scopus 로고
    • Exocytosis of endothelial cells is regulated by N-ethylmaleimide-sensitive factor
    • Yamakuchi M, et al. Exocytosis of endothelial cells is regulated by N-ethylmaleimide-sensitive factor. Methods Mol Biol. 2008;440:203-215.
    • (2008) Methods Mol Biol. , vol.440 , pp. 203-215
    • Yamakuchi, M.1
  • 31
    • 84866851005 scopus 로고    scopus 로고
    • The interplay between the Rab27A effectors Slp4-a and MyRIP controls hormone-evoked Weibel-Palade body exocytosis
    • Bierings R, et al. The interplay between the Rab27A effectors Slp4-a and MyRIP controls hormone-evoked Weibel-Palade body exocytosis. Blood. 2012;120(13):2757-2767.
    • (2012) Blood , vol.120 , Issue.13 , pp. 2757-2767
    • Bierings, R.1
  • 32
    • 80052630604 scopus 로고    scopus 로고
    • Myosin Va acts in concert with Rab27a and MyRIP to regulate acute von-Willebrand factor release from endothelial cells
    • Pulido IR, Nightingale TD, Darchen F, Seabra MC, Cutler DF, Gerke V. Myosin Va acts in concert with Rab27a and MyRIP to regulate acute von-Willebrand factor release from endothelial cells. Traffic. 2011;12(10):1371-1382.
    • (2011) Traffic. , vol.12 , Issue.10 , pp. 1371-1382
    • Pulido, I.R.1    Nightingale, T.D.2    Darchen, F.3    Seabra, M.C.4    Cutler, D.F.5    Gerke, V.6
  • 33
    • 66549127369 scopus 로고    scopus 로고
    • Rab27a and MyRIP regulate the amount and multimeric state of VWF released from endothelial cells
    • Nightingale TD, Pattni K, Hume AN, Seabra MC, Cutler DF. Rab27a and MyRIP regulate the amount and multimeric state of VWF released from endothelial cells. Blood. 2009;113(20):5010-5018.
    • (2009) Blood , vol.113 , Issue.20 , pp. 5010-5018
    • Nightingale, T.D.1    Pattni, K.2    Hume, A.N.3    Seabra, M.C.4    Cutler, D.F.5
  • 34
    • 77954368879 scopus 로고    scopus 로고
    • Regulation of Weibel-Palade body exocytosis by alphasynuclein in endothelial cells
    • Kim KS, Park JY, Jou I, Park SM. Regulation of Weibel-Palade body exocytosis by alphasynuclein in endothelial cells. J Biol Chem. 2010;285(28):21416-21425.
    • (2010) J Biol Chem. , vol.285 , Issue.28 , pp. 21416-21425
    • Kim, K.S.1    Park, J.Y.2    Jou, I.3    Park, S.M.4
  • 35
    • 10744220088 scopus 로고    scopus 로고
    • Nitric oxide regulates exocytosis by S-nitrosylation of N-ethylmaleimidesensitive factor
    • Matsushita K, et al. Nitric oxide regulates exocytosis by S-nitrosylation of N-ethylmaleimidesensitive factor. Cell. 2003;115(2):139-150.
    • (2003) Cell , vol.115 , Issue.2 , pp. 139-150
    • Matsushita, K.1
  • 36
    • 79953182367 scopus 로고    scopus 로고
    • Thioredoxin increases exocytosis by denitrosylating N-ethylmaleimide-sensitive factor
    • Ito T, Yamakuchi M, Lowenstein CJ. Thioredoxin increases exocytosis by denitrosylating N-ethylmaleimide-sensitive factor. J Biol Chem. 2011;286(13):11179-11184.
    • (2011) J Biol Chem. , vol.286 , Issue.13 , pp. 11179-11184
    • Ito, T.1    Yamakuchi, M.2    Lowenstein, C.J.3
  • 37
    • 78149336370 scopus 로고    scopus 로고
    • Shiga toxin B subunits induce VWF secretion by human endothelial cells and thrombotic microangiopathy in ADAMTS13-deficient mice
    • Huang J, Motto DG, Bundle DR, Sadler JE. Shiga toxin B subunits induce VWF secretion by human endothelial cells and thrombotic microangiopathy in ADAMTS13-deficient mice. Blood. 2010;116(18):3653-3659.
    • (2010) Blood , vol.116 , Issue.18 , pp. 3653-3659
    • Huang, J.1    Motto, D.G.2    Bundle, D.R.3    Sadler, J.E.4
  • 38
    • 80053181057 scopus 로고    scopus 로고
    • Shiga toxin (Stx) 1B and Stx2B induce von Willebrand factor secretion from human umbilical vein endothelial cells through different signaling pathways
    • Liu F, Huang J, Sadler JE. Shiga toxin (Stx) 1B and Stx2B induce von Willebrand factor secretion from human umbilical vein endothelial cells through different signaling pathways. Blood. 2011;118(12):3392-3398.
    • (2011) Blood , vol.118 , Issue.12 , pp. 3392-3398
    • Liu, F.1    Huang, J.2    Sadler, J.E.3
  • 39
    • 77957200674 scopus 로고    scopus 로고
    • A revised model for the secretion of tPA and cytokines from cultured endothelial cells
    • Knipe L, et al. A revised model for the secretion of tPA and cytokines from cultured endothelial cells. Blood. 2010;116(12):2183-2191.
    • (2010) Blood , vol.116 , Issue.12 , pp. 2183-2191
    • Knipe, L.1
  • 40
    • 34247265992 scopus 로고    scopus 로고
    • Pathogen recognition by Toll-like receptor 2 activates Weibel-Palade body exocytosis in human aortic endothelial cells
    • Into T, et al. Pathogen recognition by Toll-like receptor 2 activates Weibel-Palade body exocytosis in human aortic endothelial cells. J Biol Chem. 2007;282(11):8134-8141.
    • (2007) J Biol Chem. , vol.282 , Issue.11 , pp. 8134-8141
    • Into, T.1
  • 42
    • 3843054498 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate activates Weibel-Palade body exocytosis
    • Matsushita K, Morrell CN, Lowenstein CJ. Sphingosine 1-phosphate activates Weibel-Palade body exocytosis. Proc Natl Acad Sci U S A. 2004;101(31):11483-11487.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.31 , pp. 11483-11487
    • Matsushita, K.1    Morrell, C.N.2    Lowenstein, C.J.3
  • 43
    • 62649094917 scopus 로고    scopus 로고
    • Aldosterone activates endothelial exocytosis
    • Jeong Y, et al. Aldosterone activates endothelial exocytosis. Proc Natl Acad Sci U S A. 2009;106(10):3782-3787.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.10 , pp. 3782-3787
    • Jeong, Y.1
  • 44
    • 33846586525 scopus 로고    scopus 로고
    • Antibody to human leukocyte antigen triggers endothelial exocytosis
    • Yamakuchi M, et al. Antibody to human leukocyte antigen triggers endothelial exocytosis. Proc Natl Acad Sci U S A. 2007;104(4):1301-1306.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.4 , pp. 1301-1306
    • Yamakuchi, M.1
  • 45
    • 77950217693 scopus 로고    scopus 로고
    • Novel associations of multiple genetic loci with plasma levels of factor VII, factor VIII, and von Willebrand factor: The CHARGE (Cohorts for Heart and Aging Research in Genome Epidemiology) Consortium
    • Smith NL, et al. Novel associations of multiple genetic loci with plasma levels of factor VII, factor VIII, and von Willebrand factor: The CHARGE (Cohorts for Heart and Aging Research in Genome Epidemiology) Consortium. Circulation. 2010;121(12):1382-1392.
    • (2010) Circulation. , vol.121 , Issue.12 , pp. 1382-1392
    • Smith, N.L.1
  • 46
    • 79960890548 scopus 로고    scopus 로고
    • Combined analysis of three genome-wide association studies on vWF and FVIII plasma levels
    • Antoni G, et al. Combined analysis of three genome-wide association studies on vWF and FVIII plasma levels. BMC Med Genet. 2011;12:102.
    • (2011) BMC Med Genet. , vol.12 , pp. 102
    • Antoni, G.1
  • 47
    • 79952813198 scopus 로고    scopus 로고
    • Effect of genetic variations in syntaxin-binding protein-5 and syntaxin-2 on von Willebrand factor concentration and cardiovascular risk
    • Van Loon JE, et al. Effect of genetic variations in syntaxin-binding protein-5 and syntaxin-2 on von Willebrand factor concentration and cardiovascular risk. Circ Cardiovasc Genet. 2010;3(6):507-512.
    • (2010) Circ Cardiovasc Genet. , vol.3 , Issue.6 , pp. 507-512
    • Van Loon, J.E.1
  • 48
    • 79957977435 scopus 로고    scopus 로고
    • Genetic variation associated with plasma von Willebrand factor levels and the risk of incident venous thrombosis
    • Smith NL, et al. Genetic variation associated with plasma von Willebrand factor levels and the risk of incident venous thrombosis. Blood. 2011;117(22):6007-6011.
    • (2011) Blood , vol.117 , Issue.22 , pp. 6007-6011
    • Smith, N.L.1
  • 49
    • 17344376286 scopus 로고    scopus 로고
    • Tomosyn: A syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process
    • Fujita Y, et al. Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process. Neuron. 1998;20(5):905-915.
    • (1998) Neuron. , vol.20 , Issue.5 , pp. 905-915
    • Fujita, Y.1
  • 50
    • 0033525719 scopus 로고    scopus 로고
    • Three splicing variants of tomosyn and identification of their syntaxin-binding region
    • Yokoyama S, Shirataki H, Sakisaka T, Takai Y. Three splicing variants of tomosyn and identification of their syntaxin-binding region. Biochem Biophys Res Commun. 1999;256(1):218-222.
    • (1999) Biochem Biophys Res Commun. , vol.256 , Issue.1 , pp. 218-222
    • Yokoyama, S.1    Shirataki, H.2    Sakisaka, T.3    Takai, Y.4
  • 51
    • 13244292391 scopus 로고    scopus 로고
    • Two distinct genes drive expression of seven tomosyn isoforms in the mammalian brain, sharing a conserved structure with a unique variable domain
    • Groffen AJ, Jacobsen L, Schut D, Verhage M. Two distinct genes drive expression of seven tomosyn isoforms in the mammalian brain, sharing a conserved structure with a unique variable domain. J Neurochem. 2005;92(3):554-568.
    • (2005) J Neurochem. , vol.92 , Issue.3 , pp. 554-568
    • Groffen, A.J.1    Jacobsen, L.2    Schut, D.3    Verhage, M.4
  • 52
    • 8744252596 scopus 로고    scopus 로고
    • Structural basis for the inhibitory role of tomosyn in exocytosis
    • Pobbati AV, Razeto A, Boddener M, Becker S, Fasshauer D. Structural basis for the inhibitory role of tomosyn in exocytosis. J Biol Chem. 2004;279(45):47192-47200.
    • (2004) J Biol Chem. , vol.279 , Issue.45 , pp. 47192-47200
    • Pobbati, A.V.1    Razeto, A.2    Boddener, M.3    Becker, S.4    Fasshauer, D.5
  • 53
    • 0042733066 scopus 로고    scopus 로고
    • The R-SNARE motif of tomosyn forms SNARE core complexes with syntaxin 1 and SNAP-25 and down-regulates exocytosis
    • Hatsuzawa K, Lang T, Fasshauer D, Bruns D, Jahn R. The R-SNARE motif of tomosyn forms SNARE core complexes with syntaxin 1 and SNAP-25 and down-regulates exocytosis. J Biol Chem. 2003;278(33):31159-31166.
    • (2003) J Biol Chem. , vol.278 , Issue.33 , pp. 31159-31166
    • Hatsuzawa, K.1    Lang, T.2    Fasshauer, D.3    Bruns, D.4    Jahn, R.5
  • 54
    • 0031696595 scopus 로고    scopus 로고
    • Tomosyn binds t-SNARE proteins via a VAMP-like coiled coil
    • Masuda ES, Huang BC, Fisher JM, Luo Y, Scheller RH. Tomosyn binds t-SNARE proteins via a VAMP-like coiled coil. Neuron. 1998;21(3):479-480.
    • (1998) Neuron. , vol.21 , Issue.3 , pp. 479-480
    • Masuda, E.S.1    Huang, B.C.2    Fisher, J.M.3    Luo, Y.4    Scheller, R.H.5
  • 55
    • 34848928507 scopus 로고    scopus 로고
    • Multiple functional domains are involved in tomosyn regulation of exocytosis
    • Yizhar O, et al. Multiple functional domains are involved in tomosyn regulation of exocytosis. J Neurochem. 2007;103(2):604-616.
    • (2007) J Neurochem. , vol.103 , Issue.2 , pp. 604-616
    • Yizhar, O.1
  • 56
    • 55949121583 scopus 로고    scopus 로고
    • Dual inhibition of SNARE complex formation by tomosyn ensures controlled neurotransmitter release
    • Sakisaka T, et al. Dual inhibition of SNARE complex formation by tomosyn ensures controlled neurotransmitter release. J Cell Biol. 2008;183(2):323-337.
    • (2008) J Cell Biol. , vol.183 , Issue.2 , pp. 323-337
    • Sakisaka, T.1
  • 57
    • 1442354782 scopus 로고    scopus 로고
    • Tomosyn inhibits priming of large dense-core vesicles in a calciumdependent manner
    • Yizhar O, et al. Tomosyn inhibits priming of large dense-core vesicles in a calciumdependent manner. Proc Natl Acad Sci U S A. 2004;101(8):2578-2583.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.8 , pp. 2578-2583
    • Yizhar, O.1
  • 58
    • 77955585462 scopus 로고    scopus 로고
    • The tail domain of tomosyn controls membrane fusion through tomosyn displacement by VAMP2
    • Yamamoto Y, et al. The tail domain of tomosyn controls membrane fusion through tomosyn displacement by VAMP2. Biochem Biophys Res Commun. 2010;399(1):24-30.
    • (2010) Biochem Biophys Res Commun. , vol.399 , Issue.1 , pp. 24-30
    • Yamamoto, Y.1
  • 59
    • 79954613382 scopus 로고    scopus 로고
    • Structural and functional analysis of tomosyn identifies domains important in exocytotic regulation
    • Williams AL, et al. Structural and functional analysis of tomosyn identifies domains important in exocytotic regulation. J Biol Chem. 2011;286(16):14542-14553.
    • (2011) J Biol Chem. , vol.286 , Issue.16 , pp. 14542-14553
    • Williams, A.L.1
  • 61
    • 34547942015 scopus 로고    scopus 로고
    • Receptor-mediated regulation of tomosyn-syntaxin 1A interactions in bovine adrenal chromaffin cells
    • Gladycheva SE, et al. Receptor-mediated regulation of tomosyn-syntaxin 1A interactions in bovine adrenal chromaffin cells. J Biol Chem. 2007;282(31):22887-22899.
    • (2007) J Biol Chem. , vol.282 , Issue.31 , pp. 22887-22899
    • Gladycheva, S.E.1
  • 62
    • 0024364675 scopus 로고
    • GMP-140, a platelet α-granule membrane protein, is also synthesized by vascular endothelial cells and is localized in Weibel-Palade bodies
    • Mcever RP, Beckstead JH, Moore KL, Marshallcarlson L, Bainton DF. GMP-140, a platelet α-granule membrane protein, is also synthesized by vascular endothelial cells and is localized in Weibel-Palade bodies. J Clin Invest. 1989;84(1):92-99.
    • (1989) J Clin Invest. , vol.84 , Issue.1 , pp. 92-99
    • Mcever, R.P.1    Beckstead, J.H.2    Moore, K.L.3    Marshallcarlson, L.4    Bainton, D.F.5
  • 63
    • 77957014978 scopus 로고    scopus 로고
    • Arterial thrombus formation. Novel mechanisms and targets
    • Hagedorn I, Vogtle T, Nieswandt B. Arterial thrombus formation. Novel mechanisms and targets. Hamostaseologie. 2010;30(3):127-135.
    • (2010) Hamostaseologie. , vol.30 , Issue.3 , pp. 127-135
    • Hagedorn, I.1    Vogtle, T.2    Nieswandt, B.3
  • 64
    • 55749101354 scopus 로고    scopus 로고
    • Molecular mechanisms of thrombus formation in ischemic stroke: Novel insights and targets for treatment
    • Stoll G, Kleinschnitz C, Nieswandt B. Molecular mechanisms of thrombus formation in ischemic stroke: novel insights and targets for treatment. Blood. 2008;112(9):3555-3562.
    • (2008) Blood , vol.112 , Issue.9 , pp. 3555-3562
    • Stoll, G.1    Kleinschnitz, C.2    Nieswandt, B.3
  • 65
    • 13244265094 scopus 로고    scopus 로고
    • Clotting mechanisms and cancer: Implications in thrombus formation and tumor progression
    • Falanga A, Marchetti M, Vignoli A, Balducci D. Clotting mechanisms and cancer: implications in thrombus formation and tumor progression. Clin Adv Hematol Oncol. 2003;1(11):673-678.
    • (2003) Clin Adv Hematol Oncol. , vol.1 , Issue.11 , pp. 673-678
    • Falanga, A.1    Marchetti, M.2    Vignoli, A.3    Balducci, D.4
  • 66
    • 13544273188 scopus 로고    scopus 로고
    • Protease-activated receptor-1 activation of endothelial cells induces protein kinase Cα-dependent phosphorylation of syntaxin 4 and Munc18c: Role in signaling p-selectin expression
    • Fu J, Naren AP, Gao X, Ahmmed GU, Malik AB. Protease-activated receptor-1 activation of endothelial cells induces protein kinase Cα-dependent phosphorylation of syntaxin 4 and Munc18c: role in signaling p-selectin expression. J Biol Chem. 2005;280(5):3178-3184.
    • (2005) J Biol Chem. , vol.280 , Issue.5 , pp. 3178-3184
    • Fu, J.1    Naren, A.P.2    Gao, X.3    Ahmmed, G.U.4    Malik, A.B.5
  • 68
    • 78650365993 scopus 로고    scopus 로고
    • 2+-dependent neurotransmitter release through its N-terminal WD40 repeats
    • 2+-dependent neurotransmitter release through its N-terminal WD40 repeats. J Biol Chem. 2010;285(52):40943-40955.
    • (2010) J Biol Chem. , vol.285 , Issue.52 , pp. 40943-40955
    • Yamamoto, Y.1
  • 69
    • 0032879824 scopus 로고    scopus 로고
    • Influence of fibrillar collagen structure on the mechanisms of platelet thrombus formation under flow
    • Savage B, Ginsberg MH, Ruggeri ZM. Influence of fibrillar collagen structure on the mechanisms of platelet thrombus formation under flow. Blood. 1999;94(8):2704-2715.
    • (1999) Blood , vol.94 , Issue.8 , pp. 2704-2715
    • Savage, B.1    Ginsberg, M.H.2    Ruggeri, Z.M.3
  • 70
    • 84863636752 scopus 로고    scopus 로고
    • Effect of genetic variation in STXBP5 and STX2 on von Wille brand factor and bleeding phenotype in type 1 von Willebrand disease patients
    • Van Loon JE, Sanders YV, De Wee EM, Kruip MJ, De Maat MP, Leebeek FW. Effect of genetic variation in STXBP5 and STX2 on von Wille brand factor and bleeding phenotype in type 1 von Willebrand disease patients. PLoS One. 2012;7(7):e40624.
    • (2012) PLoS One. , vol.7 , Issue.7 , pp. e40624
    • Van Loon, J.E.1    Sanders, Y.V.2    De Wee, E.M.3    Kruip, M.J.4    De Maat, M.P.5    Leebeek, F.W.6
  • 71
    • 33746726458 scopus 로고    scopus 로고
    • Antagonistic regulation of synaptic vesicle priming by Tomosyn and UNC-13
    • McEwen JM, Madison JM, Dybbs M, Kaplan JM. Antagonistic regulation of synaptic vesicle priming by Tomosyn and UNC-13. Neuron. 2006;51(3):303-315.
    • (2006) Neuron. , vol.51 , Issue.3 , pp. 303-315
    • McEwen, J.M.1    Madison, J.M.2    Dybbs, M.3    Kaplan, J.M.4
  • 72
    • 29944443664 scopus 로고    scopus 로고
    • The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p
    • Grosshans BL, et al. The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p. J Cell Biol. 2006;172(1):55-66.
    • (2006) J Cell Biol. , vol.172 , Issue.1 , pp. 55-66
    • Grosshans, B.L.1
  • 73
    • 34047100822 scopus 로고    scopus 로고
    • Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism
    • Hattendorf DA, Andreeva A, Gangar A, Brennwald PJ, Weis WI. Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism. Nature. 2007;446(7135):567-571.
    • (2007) Nature , vol.446 , Issue.7135 , pp. 567-571
    • Hattendorf, D.A.1    Andreeva, A.2    Gangar, A.3    Brennwald, P.J.4    Weis, W.I.5
  • 74
    • 0035976798 scopus 로고    scopus 로고
    • Calcium-dependent translocation of synaptotagmin to the plasma membrane in the dendrites of developing neurones
    • Schwab Y, Mouton J, Chasserot-Golaz S, Marty I, Maulet Y, Jover E. Calcium-dependent translocation of synaptotagmin to the plasma membrane in the dendrites of developing neurones. Mol Brain Res. 2001;96(1-2):1-13.
    • (2001) Mol Brain Res. , vol.96 , Issue.1-2 , pp. 1-13
    • Schwab, Y.1    Mouton, J.2    Chasserot-Golaz, S.3    Marty, I.4    Maulet, Y.5    Jover, E.6
  • 75
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang J, Maximov A, Shin OH, Dai H, Rizo J, Sudhof TC. A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell. 2006;126(6):1175-1187.
    • (2006) Cell , vol.126 , Issue.6 , pp. 1175-1187
    • Tang, J.1    Maximov, A.2    Shin, O.H.3    Dai, H.4    Rizo, J.5    Sudhof, T.C.6
  • 77
    • 84883308384 scopus 로고    scopus 로고
    • Subtle Interplay between synaptotagmin and complexin binding to the SNARE complex
    • Xu JJ, Brewer KD, Perez-Castillejos R, Rizo J. Subtle Interplay between synaptotagmin and complexin binding to the SNARE complex. J Mol Biol. 2013;425(18):3461-3475.
    • (2013) J Mol Biol. , vol.425 , Issue.18 , pp. 3461-3475
    • Xu, J.J.1    Brewer, K.D.2    Perez-Castillejos, R.3    Rizo, J.4
  • 78
    • 0035999998 scopus 로고    scopus 로고
    • Selective and signal-dependent recruitment of membrane proteins to secretory granules formed by heterologously expressed von Willebrand factor
    • Blagoveshchenskaya AD, Hannah MJ, Allen S, Cutler DF. Selective and signal-dependent recruitment of membrane proteins to secretory granules formed by heterologously expressed von Willebrand factor. Mol Biol Cell. 2002;13(5):1582-1593.
    • (2002) Mol Biol Cell. , vol.13 , Issue.5 , pp. 1582-1593
    • Blagoveshchenskaya, A.D.1    Hannah, M.J.2    Allen, S.3    Cutler, D.F.4
  • 79
    • 45549087119 scopus 로고    scopus 로고
    • Basal secretion of von Willebrand factor from human endothelial cells
    • Giblin JP, Hewlett LJ, Hannah MJ. Basal secretion of von Willebrand factor from human endothelial cells. Blood. 2008;112(4):957-964.
    • (2008) Blood , vol.112 , Issue.4 , pp. 957-964
    • Giblin, J.P.1    Hewlett, L.J.2    Hannah, M.J.3
  • 80
    • 33746853822 scopus 로고    scopus 로고
    • Tomosyn-1 is involved in a postdocking event required for pancreatic β-cell exocytosis
    • Cheviet S, et al. Tomosyn-1 is involved in a postdocking event required for pancreatic β-cell exocytosis. J Cell Sci. 2006;119(pt 14):2912-2920.
    • (2006) J Cell Sci. , vol.119 , pp. 2912-2920
    • Cheviet, S.1
  • 81
    • 84865237107 scopus 로고    scopus 로고
    • Contribution of platelet vs endothelial VWF to platelet adhesion and hemostasis
    • Kanaji S, Fahs SA, Shi Q, Haberichter SL, Montgomery RR. Contribution of platelet vs. endothelial VWF to platelet adhesion and hemostasis. J Thromb Haemost. 2012;10(8):1646-1652.
    • (2012) J Thromb Haemost. , vol.10 , Issue.8 , pp. 1646-1652
    • Kanaji, S.1    Fahs, S.A.2    Shi, Q.3    Haberichter, S.L.4    Montgomery, R.R.5
  • 82
    • 23044513025 scopus 로고    scopus 로고
    • A novel inhibitor of N-ethylmaleimide-sensitive factor decreases leukocyte trafficking and peritonitis
    • Morrell CN, Matsushita K, Lowenstein CJ. A novel inhibitor of N-ethylmaleimide-sensitive factor decreases leukocyte trafficking and peritonitis. J Pharmacol Exp Ther. 2005;314(1):155-161.
    • (2005) J Pharmacol Exp Ther. , vol.314 , Issue.1 , pp. 155-161
    • Morrell, C.N.1    Matsushita, K.2    Lowenstein, C.J.3
  • 83
    • 79551539785 scopus 로고    scopus 로고
    • Escherichia coli-derived von Willebrand factor-A2 domain fluorescence/Forster resonance energy transfer proteins that quantify ADAMTS13 activity
    • Dayananda KM, Gogia S, Neelamegham S. Escherichia coli-derived von Willebrand factor-A2 domain fluorescence/Forster resonance energy transfer proteins that quantify ADAMTS13 activity. Anal Biochem. 2011;410(2):206-213.
    • (2011) Anal Biochem. , vol.410 , Issue.2 , pp. 206-213
    • Dayananda, K.M.1    Gogia, S.2    Neelamegham, S.3
  • 84
    • 0042818205 scopus 로고    scopus 로고
    • Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulinstimulated GLUT4 translocation
    • Widberg CH, Bryant NJ, Girotti M, Rea S, James DE. Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulinstimulated GLUT4 translocation. J Biol Chem. 2003;278(37):35093-35101.
    • (2003) J Biol Chem. , vol.278 , Issue.37 , pp. 35093-35101
    • Widberg, C.H.1    Bryant, N.J.2    Girotti, M.3    Rea, S.4    James, D.E.5
  • 85
    • 41149152337 scopus 로고    scopus 로고
    • Glutamate mediates platelet activation through the AMPA receptor
    • Morrell CN, et al. Glutamate mediates platelet activation through the AMPA receptor. J Exp Med. 2008;205(3):575-584.
    • (2008) J Exp Med. , vol.205 , Issue.3 , pp. 575-584
    • Morrell, C.N.1
  • 86
    • 80052421895 scopus 로고    scopus 로고
    • Towards a standardization of the murine ferric chloride-induced carotid arterial thrombosis model
    • Owens AP, et al. Towards a standardization of the murine ferric chloride-induced carotid arterial thrombosis model. J Thromb Haemost. 2011;9(9):1862-1863.
    • (2011) J Thromb Haemost. , vol.9 , Issue.9 , pp. 1862-1863
    • Owens, A.P.1
  • 87
    • 79953314017 scopus 로고    scopus 로고
    • Mechanisms underlying FeCl3-induced arterial thrombosis
    • Eckly A, et al. Mechanisms underlying FeCl3-induced arterial thrombosis. J Thromb Haemost. 2011;9(4):779-789.
    • (2011) J Thromb Haemost. , vol.9 , Issue.4 , pp. 779-789
    • Eckly, A.1


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