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Volumn 36, Issue 6, 2016, Pages 1164-1173

Intracellular trafficking, localization, and mobilization of platelet-borne thiol isomerases

Author keywords

blood platelets; megakaryocytes; membrane fusion; protein disulfide isomerases; secretory vesicles

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ISOMERASE; PROTEIN DISULFIDE ISOMERASE; THIOL ISOMERASE; UNCLASSIFIED DRUG; ACTIN; CALNEXIN; MEMBRANE PROTEIN; NBEAL2 PROTEIN, MOUSE; PDIA3 PROTEIN, HUMAN; PDIA3 PROTEIN, MOUSE; PLASMA PROTEIN; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNC13D PROTEIN, HUMAN; UNC13D PROTEIN, MOUSE;

EID: 84963575819     PISSN: 10795642     EISSN: 15244636     Source Type: Journal    
DOI: 10.1161/ATVBAHA.116.307461     Document Type: Article
Times cited : (51)

References (58)
  • 1
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari DM, Söling HD, The protein disulphide-isomerase family: unravelling a string of folds. Biochem J 1999 339 pt 1 1 10
    • (1999) Biochem J , vol.339 , Issue.PT1 , pp. 1-10
    • Ferrari, D.M.1    Söling, H.D.2
  • 2
    • 33646698875 scopus 로고    scopus 로고
    • Extracellular disulfide exchange and the regulation of cellular function
    • Jordan PA, Gibbins JM, Extracellular disulfide exchange and the regulation of cellular function. Antioxid Redox Signal 2006 8 312 324. doi: 10.1089/ars.2006.8.312
    • (2006) Antioxid Redox Signal , vol.8 , pp. 312-324
    • Jordan, P.A.1    Gibbins, J.M.2
  • 3
    • 78649466923 scopus 로고    scopus 로고
    • Endothelium-derived but not platelet-derived protein disulfide isomerase is required for thrombus formation in vivo
    • Jasuja R, Furie B, Furie BC, Endothelium-derived but not platelet-derived protein disulfide isomerase is required for thrombus formation in vivo. Blood 2010 116 4665 4674. doi: 10.1182/blood-2010-04-278184
    • (2010) Blood , vol.116 , pp. 4665-4674
    • Jasuja, R.1    Furie, B.2    Furie, B.C.3
  • 5
    • 0028292443 scopus 로고
    • Thiol-proteindisulfide-oxidoreductase (proteindisulfide isomerase): A new plasma membrane constituent of mature human B lymphocytes
    • Kröning H, Kähne T, Ittenson A, Franke A, Ansorge S, Thiol-proteindisulfide-oxidoreductase (proteindisulfide isomerase): a new plasma membrane constituent of mature human B lymphocytes. Scand J Immunol 1994 39 346 350
    • (1994) Scand J Immunol , vol.39 , pp. 346-350
    • Kröning, H.1    Kähne, T.2    Ittenson, A.3    Franke, A.4    Ansorge, S.5
  • 8
    • 84886930949 scopus 로고    scopus 로고
    • Platelet protein disulfide isomerase is required for thrombus formation but not for hemostasis in mice
    • Kim K, Hahm E, Li J, Holbrook LM, Sasikumar P, Stanley RG, Ushio-Fukai M, Gibbins JM, Cho J, Platelet protein disulfide isomerase is required for thrombus formation but not for hemostasis in mice. Blood 2013 122 1052 1061. doi: 10.1182/blood-2013-03-492504
    • (2013) Blood , vol.122 , pp. 1052-1061
    • Kim, K.1    Hahm, E.2    Li, J.3    Holbrook, L.M.4    Sasikumar, P.5    Stanley, R.G.6    Ushio-Fukai, M.7    Gibbins, J.M.8    Cho, J.9
  • 9
    • 84926669287 scopus 로고    scopus 로고
    • Both platelet- and endothelial cell-derived ERp5 support thrombus formation in a laser-induced mouse model of thrombosis
    • Passam FH, Lin L, Gopal S, Stopa JD, Bellido-Martin L, Huang M, Furie BC, Furie B, Both platelet- and endothelial cell-derived ERp5 support thrombus formation in a laser-induced mouse model of thrombosis. Blood 2015 125 2276 2285. doi: 10.1182/blood-2013-12-547208
    • (2015) Blood , vol.125 , pp. 2276-2285
    • Passam, F.H.1    Lin, L.2    Gopal, S.3    Stopa, J.D.4    Bellido-Martin, L.5    Huang, M.6    Furie, B.C.7    Furie, B.8
  • 10
    • 84888229791 scopus 로고    scopus 로고
    • Platelet-derived ERp57 mediates platelet incorporation into a growing thrombus by regulation of the αiIbβ3 integrin
    • Wang L, Wu Y, Zhou J, Ahmad SS, Mutus B, Garbi N, Hämmerling G, Liu J, Essex DW, Platelet-derived ERp57 mediates platelet incorporation into a growing thrombus by regulation of the αIIbβ3 integrin. Blood 2013 122 3642 3650. doi: 10.1182/blood-2013-06-506691
    • (2013) Blood , vol.122 , pp. 3642-3650
    • Wang, L.1    Wu, Y.2    Zhou, J.3    Ahmad, S.S.4    Mutus, B.5    Garbi, N.6    Hämmerling, G.7    Liu, J.8    Essex, D.W.9
  • 11
    • 84863139700 scopus 로고    scopus 로고
    • The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis
    • Wu Y, Ahmad SS, Zhou J, Wang L, Cully MP, Essex DW, The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis. Blood 2012 119 1737 1746. doi: 10.1182/blood-2011-06-360685
    • (2012) Blood , vol.119 , pp. 1737-1746
    • Wu, Y.1    Ahmad, S.S.2    Zhou, J.3    Wang, L.4    Cully, M.P.5    Essex, D.W.6
  • 12
    • 40549084318 scopus 로고    scopus 로고
    • A critical role for extracellular protein disulfide isomerase during thrombus formation in mice
    • Cho J, Furie BC, Coughlin SR, Furie B, A critical role for extracellular protein disulfide isomerase during thrombus formation in mice. J Clin Invest 2008 118 1123 1131. doi: 10.1172/JCI34134
    • (2008) J Clin Invest , vol.118 , pp. 1123-1131
    • Cho, J.1    Furie, B.C.2    Coughlin, S.R.3    Furie, B.4
  • 14
    • 84880448971 scopus 로고    scopus 로고
    • Extracellular protein disulfide isomerase regulates ligand-binding activity of αmβ2 integrin and neutrophil recruitment during vascular inflammation
    • Hahm E, Li J, Kim K, Huh S, Rogelj S, Cho J, Extracellular protein disulfide isomerase regulates ligand-binding activity of αMβ2 integrin and neutrophil recruitment during vascular inflammation. Blood 2013 121 3789 3800, S1. doi: 10.1182/blood-2012-11-467985
    • (2013) Blood , vol.121 , pp. 3789-3800
    • Hahm, E.1    Li, J.2    Kim, K.3    Huh, S.4    Rogelj, S.5    Cho, J.6
  • 15
    • 0029144477 scopus 로고
    • Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex DW, Chen K, Swiatkowska M, Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 1995 86 2168 2173
    • (1995) Blood , vol.86 , pp. 2168-2173
    • Essex, D.W.1    Chen, K.2    Swiatkowska, M.3
  • 16
    • 84897518813 scopus 로고    scopus 로고
    • Thiol isomerases in thrombus formation
    • Furie B, Flaumenhaft R, Thiol isomerases in thrombus formation. Circ Res 2014 114 1162 1173. doi: 10.1161/CIRCRESAHA.114.301808
    • (2014) Circ Res , vol.114 , pp. 1162-1173
    • Furie, B.1    Flaumenhaft, R.2
  • 17
    • 75149147568 scopus 로고    scopus 로고
    • Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation
    • Holbrook LM, Watkins NA, Simmonds AD, Jones CI, Ouwehand WH, Gibbins JM, Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation. Br J Haematol 2010 148 627 637. doi: 10.1111/j.1365-2141.2009.07994.x
    • (2010) Br J Haematol , vol.148 , pp. 627-637
    • Holbrook, L.M.1    Watkins, N.A.2    Simmonds, A.D.3    Jones, C.I.4    Ouwehand, W.H.5    Gibbins, J.M.6
  • 19
    • 73949086509 scopus 로고    scopus 로고
    • Platelet protein disulfide isomerase is localized in the dense tubular system and does not become surface expressed after activation
    • van Nispen Tot Pannerden HE, van Dijk SM, Du V, Heijnen HF, Platelet protein disulfide isomerase is localized in the dense tubular system and does not become surface expressed after activation. Blood 2009 114 4738 4740. doi: 10.1182/blood-2009-03-210450
    • (2009) Blood , vol.114 , pp. 4738-4740
    • Van Nispen, T.1    Pannerden, H.E.2    Van Dijk, S.M.3    Du, V.4    Heijnen, H.F.5
  • 21
    • 18544374500 scopus 로고    scopus 로고
    • The actin cytoskeleton differentially regulates platelet alpha-granule and dense-granule secretion
    • Flaumenhaft R, Dilks JR, Rozenvayn N, Monahan-Earley RA, Feng D, Dvorak AM, The actin cytoskeleton differentially regulates platelet alpha-granule and dense-granule secretion. Blood 2005 105 3879 3887. doi: 10.1182/blood-2004-04-1392
    • (2005) Blood , vol.105 , pp. 3879-3887
    • Flaumenhaft, R.1    Dilks, J.R.2    Rozenvayn, N.3    Monahan-Earley, R.A.4    Feng, D.5    Dvorak, A.M.6
  • 22
    • 0031027591 scopus 로고    scopus 로고
    • Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin
    • Betz A, Okamoto M, Benseler F, Brose N, Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin. J Biol Chem 1997 272 2520 2526
    • (1997) J Biol Chem , vol.272 , pp. 2520-2526
    • Betz, A.1    Okamoto, M.2    Benseler, F.3    Brose, N.4
  • 23
    • 10744224641 scopus 로고    scopus 로고
    • Munc13-4 is essential for cytolytic granules fusion and is mutated in a form of familial hemophagocytic lymphohistiocytosis (FHL3
    • Feldmann J, Callebaut I, Raposo G, Munc13-4 is essential for cytolytic granules fusion and is mutated in a form of familial hemophagocytic lymphohistiocytosis (FHL3). Cell 2003 115 461 473
    • (2003) Cell , vol.115 , pp. 461-473
    • Feldmann, J.1    Callebaut, I.2    Raposo, G.3
  • 24
    • 29044447583 scopus 로고    scopus 로고
    • UNC-13 interaction with syntaxin is required for synaptic transmission
    • Madison JM, Nurrish S, Kaplan JM, UNC-13 interaction with syntaxin is required for synaptic transmission. Curr Biol 2005 15 2236 2242. doi: 10.1016/j.cub.2005.10.049
    • (2005) Curr Biol , vol.15 , pp. 2236-2242
    • Madison, J.M.1    Nurrish, S.2    Kaplan, J.M.3
  • 25
    • 77956519683 scopus 로고    scopus 로고
    • Munc13-4 is a limiting factor in the pathway required for platelet granule release and hemostasis
    • Ren Q, Wimmer C, Chicka MC, Ye S, Ren Y, Hughson FM, Whiteheart SW, Munc13-4 is a limiting factor in the pathway required for platelet granule release and hemostasis. Blood 2010 116 869 877. doi: 10.1182/blood-2010-02-270934
    • (2010) Blood , vol.116 , pp. 869-877
    • Ren, Q.1    Wimmer, C.2    Chicka, M.C.3    Ye, S.4    Ren, Y.5    Hughson, F.M.6    Whiteheart, S.W.7
  • 31
    • 0031860328 scopus 로고    scopus 로고
    • Inverse immunostaining pattern for synthesized versus endocytosed alpha-granule proteins in human bone marrow megakaryocytes
    • de Larouzière V, Brouland JP, Souni F, Drouet L, Cramer E, Inverse immunostaining pattern for synthesized versus endocytosed alpha-granule proteins in human bone marrow megakaryocytes. Br J Haematol 1998 101 618 625
    • (1998) Br J Haematol , vol.101 , pp. 618-625
    • De Larouzière, V.1    Brouland, J.P.2    Souni, F.3    Drouet, L.4    Cramer, E.5
  • 32
    • 84868609117 scopus 로고    scopus 로고
    • Mechanism of platelet dense granule biogenesis: Study of cargo transport and function of Rab32 and Rab38 in a model system
    • Ambrosio AL, Boyle JA, Di Pietro SM, Mechanism of platelet dense granule biogenesis: study of cargo transport and function of Rab32 and Rab38 in a model system. Blood 2012 120 4072 4081. doi: 10.1182/blood-2012-04-420745
    • (2012) Blood , vol.120 , pp. 4072-4081
    • Ambrosio, A.L.1    Boyle, J.A.2    Di Pietro, S.M.3
  • 33
    • 65849360502 scopus 로고    scopus 로고
    • Platelet alpha-granules: Basic biology and clinical correlates
    • Blair P, Flaumenhaft R, Platelet alpha-granules: basic biology and clinical correlates. Blood Rev 2009 23 177 189. doi: 10.1016/j.blre.2009.04.001
    • (2009) Blood Rev , vol.23 , pp. 177-189
    • Blair, P.1    Flaumenhaft, R.2
  • 34
    • 0032055178 scopus 로고    scopus 로고
    • Multivesicular bodies are an intermediate stage in the formation of platelet alpha-granules
    • Heijnen HF, Debili N, Vainchencker W, Breton-Gorius J, Geuze HJ, Sixma JJ, Multivesicular bodies are an intermediate stage in the formation of platelet alpha-granules. Blood 1998 91 2313 2325
    • (1998) Blood , vol.91 , pp. 2313-2325
    • Heijnen, H.F.1    Debili, N.2    Vainchencker, W.3    Breton-Gorius, J.4    Geuze, H.J.5    Sixma, J.J.6
  • 35
    • 0023333472 scopus 로고
    • Isolation of an endocytic compartment from A431 cells using a density modification procedure employing a receptor-specific monoclonal antibody complexed with colloidal gold
    • Beardmore J, Howell KE, Miller K, Hopkins CR, Isolation of an endocytic compartment from A431 cells using a density modification procedure employing a receptor-specific monoclonal antibody complexed with colloidal gold. J Cell Sci 1987 87 pt 4 495 506
    • (1987) J Cell Sci , vol.87 , Issue.PT4 , pp. 495-506
    • Beardmore, J.1    Howell, K.E.2    Miller, K.3    Hopkins, C.R.4
  • 36
    • 79960903114 scopus 로고    scopus 로고
    • Mutations in NBEAL2, encoding a BEACH protein, cause gray platelet syndrome
    • Kahr WH, Hinckley J, Li L, Mutations in NBEAL2, encoding a BEACH protein, cause gray platelet syndrome. Nat Genet 2011 43 738 740. doi: 10.1038/ng.884
    • (2011) Nat Genet , vol.43 , pp. 738-740
    • Kahr, W.H.1    Hinckley, J.2    Li, L.3
  • 37
    • 84907755883 scopus 로고    scopus 로고
    • Granule-mediated release of sphingosine-1-phosphate by activated platelets
    • Jonnalagadda D, Sunkara M, Morris AJ, Whiteheart SW, Granule-mediated release of sphingosine-1-phosphate by activated platelets. Biochim Biophys Acta 2014 1841 1581 1589. doi: 10.1016/j.bbalip.2014.08.013
    • (2014) Biochim Biophys Acta , vol.1841 , pp. 1581-1589
    • Jonnalagadda, D.1    Sunkara, M.2    Morris, A.J.3    Whiteheart, S.W.4
  • 38
    • 35548992274 scopus 로고    scopus 로고
    • Subfractionation and purification of intracellular granule-structures of human platelets: An improved method based on magnetic sorting
    • Niessen J, Jedlitschky G, Grube M, Bien S, Strobel U, Ritter CA, Greinacher A, Kroemer HK, Subfractionation and purification of intracellular granule-structures of human platelets: an improved method based on magnetic sorting. J Immunol Methods 2007 328 89 96. doi: 10.1016/j.jim.2007.08.010
    • (2007) J Immunol Methods , vol.328 , pp. 89-96
    • Niessen, J.1    Jedlitschky, G.2    Grube, M.3    Bien, S.4    Strobel, U.5    Ritter, C.A.6    Greinacher, A.7    Kroemer, H.K.8
  • 39
    • 84865623640 scopus 로고    scopus 로고
    • Protein secretion and the endoplasmic reticulum
    • Benham AM, Protein secretion and the endoplasmic reticulum. Cold Spring Harb Perspect Biol 2012 4 a012872. doi: 10.1101/cshperspect.a012872
    • (2012) Cold Spring Harb Perspect Biol , vol.4 , pp. a012872
    • Benham, A.M.1
  • 40
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • Caramelo JJ, Parodi AJ, Getting in and out from calnexin/calreticulin cycles. J Biol Chem 2008 283 10221 10225. doi: 10.1074/jbc.R700048200
    • (2008) J Biol Chem , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 41
    • 0035884517 scopus 로고    scopus 로고
    • All three splice variants of the human sarco/endoplasmic reticulum Ca2+-ATPase 3 gene are translated to proteins: A study of their co-expression in platelets and lymphoid cells
    • Kovács T, Felföldi F, Papp B, Pászty K, Bredoux R, Enyedi A, Enouf J, All three splice variants of the human sarco/endoplasmic reticulum Ca2+-ATPase 3 gene are translated to proteins: a study of their co-expression in platelets and lymphoid cells. Biochem J 2001 358 pt 3 559 568
    • (2001) Biochem J , vol.358 , Issue.PT3 , pp. 559-568
    • Kovács, T.1    Felföldi, F.2    Papp, B.3    Pászty, K.4    Bredoux, R.5    Enyedi, A.6    Enouf, J.7
  • 42
    • 84901599553 scopus 로고    scopus 로고
    • A draft map of the human proteome
    • Kim MS, Pinto SM, Getnet D, A draft map of the human proteome. Nature 2014 509 575 581. doi: 10.1038/nature13302
    • (2014) Nature , vol.509 , pp. 575-581
    • Kim, M.S.1    Pinto, S.M.2    Getnet, D.3
  • 44
    • 33748791716 scopus 로고    scopus 로고
    • Interaction of STIM1 with endogenously expressed human canonical TRP1 upon depletion of intracellular Ca2+ stores
    • López JJ, Salido GM, Pariente JA, Rosado JA, Interaction of STIM1 with endogenously expressed human canonical TRP1 upon depletion of intracellular Ca2+ stores. J Biol Chem 2006 281 28254 28264. doi: 10.1074/jbc.M604272200
    • (2006) J Biol Chem , vol.281 , pp. 28254-28264
    • López, J.J.1    Salido, G.M.2    Pariente, J.A.3    Rosado, J.A.4
  • 45
    • 0032829103 scopus 로고    scopus 로고
    • New anti-actin drugs in the study of the organization and function of the actin cytoskeleton
    • Spector I, Braet F, Shochet NR, Bubb MR, New anti-actin drugs in the study of the organization and function of the actin cytoskeleton. Microsc Res Tech 1999 47 18 37. doi: 10.1002/(SICI)1097-0029(19991001)47:1<18::AID-JEMT3>3.0.CO;2-E
    • (1999) Microsc Res Tech , vol.47 , pp. 18-37
    • Spector, I.1    Braet, F.2    Shochet, N.R.3    Bubb, M.R.4
  • 46
    • 84964698105 scopus 로고    scopus 로고
    • Platelet dense granule secretion defects may obscure α-granule secretion mechanisms: Evidence from Munc13-4-deficient platelets
    • Harper MT, van den Bosch MT, Hers I, Poole AW, Platelet dense granule secretion defects may obscure α-granule secretion mechanisms: evidence from Munc13-4-deficient platelets. Blood 2015 125 3034 3036. doi: 10.1182/blood-2014-12-618439
    • (2015) Blood , vol.125 , pp. 3034-3036
    • Harper, M.T.1    Van Den Bosch, M.T.2    Hers, I.3    Poole, A.W.4
  • 47
    • 31044443970 scopus 로고    scopus 로고
    • The biogenesis of platelets from megakaryocyte proplatelets
    • Patel SR, Hartwig JH, Italiano JE Jr, The biogenesis of platelets from megakaryocyte proplatelets. J Clin Invest 2005 115 3348 3354. doi: 10.1172/JCI26891
    • (2005) J Clin Invest , vol.115 , pp. 3348-3354
    • Patel, S.R.1    Hartwig, J.H.2    Italiano, J.E.3
  • 50
    • 79953304059 scopus 로고    scopus 로고
    • STIM1 and STIM2 are located in the acidic Ca2+ stores and associates with orai1 upon depletion of the acidic stores in human platelets
    • Zbidi H, Jardin I, Woodard GE, Lopez JJ, Berna-Erro A, Salido GM, Rosado JA, STIM1 and STIM2 are located in the acidic Ca2+ stores and associates with Orai1 upon depletion of the acidic stores in human platelets. J Biol Chem 2011 286 12257 12270. doi: 10.1074/jbc.M110.190694
    • (2011) J Biol Chem , vol.286 , pp. 12257-12270
    • Zbidi, H.1    Jardin, I.2    Woodard, G.E.3    Lopez, J.J.4    Berna-Erro, A.5    Salido, G.M.6    Rosado, J.A.7
  • 51
    • 84961537493 scopus 로고    scopus 로고
    • Platelet hyaluronidase-2: An enzyme that translocates to the surface upon activation to function in extracellular matrix degradation
    • Albeiroti S, Ayasoufi K, Hill DR, Shen B, de la Motte CA, Platelet hyaluronidase-2: an enzyme that translocates to the surface upon activation to function in extracellular matrix degradation. Blood 2015 125 1460 1469. doi: 10.1182/blood-2014-07-590513
    • (2015) Blood , vol.125 , pp. 1460-1469
    • Albeiroti, S.1    Ayasoufi, K.2    Hill, D.R.3    Shen, B.4    De La Motte, C.A.5
  • 52
    • 80255123366 scopus 로고    scopus 로고
    • Modulation of STIM1 and capacitative Ca2+ entry by the endoplasmic reticulum luminal oxidoreductase ERp57
    • Prins D, Groenendyk J, Touret N, Michalak M, Modulation of STIM1 and capacitative Ca2+ entry by the endoplasmic reticulum luminal oxidoreductase ERp57. EMBO Rep 2011 12 1182 1188. doi: 10.1038/embor.2011.173
    • (2011) EMBO Rep , vol.12 , pp. 1182-1188
    • Prins, D.1    Groenendyk, J.2    Touret, N.3    Michalak, M.4
  • 54
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman JE, Warren G, Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr Biol 1994 4 220 233
    • (1994) Curr Biol , vol.4 , pp. 220-233
    • Rothman, J.E.1    Warren, G.2
  • 57
    • 0033520421 scopus 로고    scopus 로고
    • The platelet cytoskeleton regulates the affinity of the integrin alpha(IIb)beta(3) for fibrinogen
    • Bennett JS, Zigmond S, Vilaire G, Cunningham ME, Bednar B, The platelet cytoskeleton regulates the affinity of the integrin alpha(IIb)beta(3) for fibrinogen. J Biol Chem 1999 274 25301 25307
    • (1999) J Biol Chem , vol.274 , pp. 25301-25307
    • Bennett, J.S.1    Zigmond, S.2    Vilaire, G.3    Cunningham, M.E.4    Bednar, B.5
  • 58
    • 84920283235 scopus 로고    scopus 로고
    • Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease
    • Flaumenhaft R, Furie B, Zwicker JI, Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease. Arterioscler Thromb Vasc Biol 2015 35 16 23. doi: 10.1161/ATVBAHA.114.303410
    • (2015) Arterioscler Thromb Vasc Biol , vol.35 , pp. 16-23
    • Flaumenhaft, R.1    Furie, B.2    Zwicker, J.I.3


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