메뉴 건너뛰기




Volumn 8, Issue 12, 2013, Pages

Rho associated coiled-coil kinase-1 regulates collagen-induced phosphatidylserine exposure in platelets

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BLOOD CLOTTING FACTOR 10A; COFILIN 1; COLLAGEN; LIM KINASE 1; MYOSIN LIGHT CHAIN; MYOSIN PHOSPHATASE SUBUNIT 1; PHOSPHATASE; PHOSPHATIDYLSERINE; RHO ASSOCIATED COILED COIL KINASE 1; RHO KINASE; UNCLASSIFIED DRUG;

EID: 84892645277     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0084649     Document Type: Article
Times cited : (14)

References (46)
  • 1
    • 0033529620 scopus 로고    scopus 로고
    • Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase
    • doi:10.1126/science.285.5429.895. PubMed: 10436159
    • Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A et al. (1999) Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285: 895-898. doi:10.1126/science.285.5429.895. PubMed: 10436159.
    • (1999) Science , vol.285 , pp. 895-898
    • Maekawa, M.1    Ishizaki, T.2    Boku, S.3    Watanabe, N.4    Fujita, A.5
  • 2
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • doi:10.1038/nature01148. PubMed: 12478284
    • Etienne-Manneville S, Hall A (2002) Rho GTPases in cell biology. Nature 420: 629-635. doi:10.1038/nature01148. PubMed: 12478284.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 3
    • 78649337010 scopus 로고    scopus 로고
    • Differential phosphorylation of myosin light chain (Thr)18 and (Ser)19 and functional implications in platelets
    • PubMed: 20670370
    • Getz TM, Dangelmaier CA, Jin J, Daniel JL, Kunapuli SP. (2010) Differential phosphorylation of myosin light chain (Thr)18 and (Ser)19 and functional implications in platelets. J Thromb Haemost 8: 2283-2293. PubMed: 20670370.
    • (2010) J Thromb Haemost , vol.8 , pp. 2283-2293
    • Getz, T.M.1    Dangelmaier, C.A.2    Jin, J.3    Daniel, J.L.4    Kunapuli, S.P.5
  • 4
    • 0030603119 scopus 로고    scopus 로고
    • ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice
    • doi:10.1016/0014-5793(96)00811-3. PubMed: 8772201
    • Nakagawa O, Fujisawa K, Ishizaki T, Saito Y, Nakao K et al. (1996) ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice. FEBS Lett 392: 189-193. doi:10.1016/0014- 5793(96)00811-3. PubMed: 8772201.
    • (1996) FEBS Lett , vol.392 , pp. 189-193
    • Nakagawa, O.1    Fujisawa, K.2    Ishizaki, T.3    Saito, Y.4    Nakao, K.5
  • 5
    • 77949514452 scopus 로고    scopus 로고
    • Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocyte differentiation
    • doi:10.1371/journal.pone.0008190. PubMed: 19997641
    • Lock FE, Hotchin NA (2009) Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocyte differentiation. PLOS ONE 4: e8190. doi:10.1371/journal.pone.0008190. PubMed: 19997641.
    • (2009) PLOS ONE , vol.4
    • Lock, F.E.1    Hotchin, N.A.2
  • 6
    • 23844442551 scopus 로고    scopus 로고
    • ROCK-I and ROCK-II cooperatively regulate closure of eyelid and ventral body wall in mouse embryo
    • doi:10.1111/j.1365-2443.2005.00882.x. PubMed: 16098146
    • Thumkeo D, Shimizu Y, Sakamoto S, Yamada S, Narumiya S (2005) ROCK-I and ROCK-II cooperatively regulate closure of eyelid and ventral body wall in mouse embryo. Genes Cells 10: 825-834. doi:10.1111/j.1365-2443.2005.00882.x. PubMed: 16098146.
    • (2005) Genes Cells , vol.10 , pp. 825-834
    • Thumkeo, D.1    Shimizu, Y.2    Sakamoto, S.3    Yamada, S.4    Narumiya, S.5
  • 7
    • 78650415748 scopus 로고    scopus 로고
    • Signaling during platelet adhesion and activation
    • PubMed: 21071698
    • Li Z, Delaney MK, O'Brien KA, Du X. (2010) Signaling during platelet adhesion and activation. Arterioscler Thromb Vasc Biol 30: 2341-2349. PubMed: 21071698.
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , pp. 2341-2349
    • Li, Z.1    Delaney, M.K.2    O'Brien, K.A.3    Du, X.4
  • 8
    • 0026331861 scopus 로고
    • Collagen-induced exposure of anionic phospholipid in platelets and platelet-derived microparticles
    • PubMed: 1662206
    • Thiagarajan P, Tait JF (1991) Collagen-induced exposure of anionic phospholipid in platelets and platelet-derived microparticles. J Biol Chem 266: 24302-24307. PubMed: 1662206.
    • (1991) J Biol Chem , vol.266 , pp. 24302-24307
    • Thiagarajan, P.1    Tait, J.F.2
  • 9
    • 0035045208 scopus 로고    scopus 로고
    • Platelet adhesion enhances the glycoprotein VI-dependent procoagulant response: Involvement of p38 MAP kinase and calpain
    • doi:10.1161/01.ATV.21.4.618. PubMed: 11304481
    • Siljander P, Farndale RW, Feijge MA, Comfurius P, Kos S et al. (2001) Platelet adhesion enhances the glycoprotein VI-dependent procoagulant response: Involvement of p38 MAP kinase and calpain. Arterioscler Thromb Vasc Biol 21: 618-627. doi:10.1161/01.ATV.21.4.618. PubMed: 11304481.
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 618-627
    • Siljander, P.1    Farndale, R.W.2    Feijge, M.A.3    Comfurius, P.4    Kos, S.5
  • 10
    • 78649460021 scopus 로고    scopus 로고
    • Platelet senescence and phosphatidylserine exposure
    • doi:10.1111/j.1537-2995.2010.02676.x. PubMed: 20456701
    • Dasgupta SK, Argaiz ER, Mercado JE, Maul HO, Garza J et al. (2010) Platelet senescence and phosphatidylserine exposure. Transfusion 50: 2167-2175. doi:10.1111/j.1537-2995.2010.02676.x. PubMed: 20456701.
    • (2010) Transfusion , vol.50 , pp. 2167-2175
    • Dasgupta, S.K.1    Argaiz, E.R.2    Mercado, J.E.3    Maul, H.O.4    Garza, J.5
  • 11
    • 0033214045 scopus 로고    scopus 로고
    • Platelet shape change is mediated by both calcium-dependent and -independent signaling pathways. Role of p160 Rho-associated coiled-coil-containing protein kinase in platelet shape change
    • doi:10.1074/jbc.274.40.28293. PubMed: 10497186
    • Paul BZ, Daniel JL, Kunapuli SP (1999) Platelet shape change is mediated by both calcium-dependent and -independent signaling pathways. Role of p160 Rho-associated coiled-coil-containing protein kinase in platelet shape change. J Biol Chem 274: 28293-28300. doi:10.1074/jbc.274.40.28293. PubMed: 10497186.
    • (1999) J Biol Chem , vol.274 , pp. 28293-28300
    • Paul, B.Z.1    Daniel, J.L.2    Kunapuli, S.P.3
  • 12
    • 0033593667 scopus 로고    scopus 로고
    • Activation of G12/G13 results in shape change and Rho/Rho-kinase-mediated myosin light chain phosphorylation in mouse platelets
    • doi:10.1083/jcb.144.4.745. PubMed: 10037795
    • Klages B, Brandt U, Simon MI, Schultz G, Offermanns S (1999) Activation of G12/G13 results in shape change and Rho/Rho-kinase-mediated myosin light chain phosphorylation in mouse platelets. J Cell Biol 144: 745-754. doi:10.1083/jcb.144.4.745. PubMed: 10037795.
    • (1999) J Cell Biol , vol.144 , pp. 745-754
    • Klages, B.1    Brandt, U.2    Simon, M.I.3    Schultz, G.4    Offermanns, S.5
  • 13
    • 0033562781 scopus 로고    scopus 로고
    • Agonist-induced regulation of myosin phosphatase activity in human platelets through activation of Rho-kinase
    • PubMed: 10233893
    • Suzuki Y, Yamamoto M, Wada H, Ito M, Nakano T et al. (1999) Agonist-induced regulation of myosin phosphatase activity in human platelets through activation of Rho-kinase. Blood 93: 3408-3417. PubMed: 10233893.
    • (1999) Blood , vol.93 , pp. 3408-3417
    • Suzuki, Y.1    Yamamoto, M.2    Wada, H.3    Ito, M.4    Nakano, T.5
  • 14
    • 0033835125 scopus 로고    scopus 로고
    • ADP-induced platelet shape change: An investigation of the signalling pathways involved and their dependence on the method of platelet preparation
    • doi:10.1080/09537100050129305. PubMed: 11030463
    • Wilde JI, Retzer M, Siess W, Watson SP (2000) ADP-induced platelet shape change: an investigation of the signalling pathways involved and their dependence on the method of platelet preparation. Platelets 11: 286-295. doi:10.1080/09537100050129305. PubMed: 11030463.
    • (2000) Platelets , vol.11 , pp. 286-295
    • Wilde, J.I.1    Retzer, M.2    Siess, W.3    Watson, S.P.4
  • 15
    • 36549040859 scopus 로고    scopus 로고
    • The selectivity of protein kinase inhibitors: A further update
    • doi:10.1042/BJ20070797. PubMed: 17850214
    • Bain J, Plater L, Elliott M, Shpiro N, Hastie CJ et al. (2007) The selectivity of protein kinase inhibitors: a further update. Biochem J 408: 297-315. doi:10.1042/BJ20070797. PubMed: 17850214.
    • (2007) Biochem J , vol.408 , pp. 297-315
    • Bain, J.1    Plater, L.2    Elliott, M.3    Shpiro, N.4    Hastie, C.J.5
  • 16
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • doi:10.1042/0264-6021:3510095. PubMed: 10998351
    • Davies SP, Reddy H, Caivano M, Cohen P (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 351: 95-105. doi:10.1042/0264-6021:3510095. PubMed: 10998351.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 17
    • 67651095943 scopus 로고    scopus 로고
    • Rho kinase-1 mediates cardiac fibrosis by regulating fibroblast precursor cell differentiation
    • doi:10.1093/cvr/cvp135. PubMed: 19406912
    • Haudek SB, Gupta D, Dewald O, Schwartz RJ, Wei L et al. (2009) Rho kinase-1 mediates cardiac fibrosis by regulating fibroblast precursor cell differentiation. Cardiovasc Res 83: 511-518. doi:10.1093/cvr/cvp135. PubMed: 19406912.
    • (2009) Cardiovasc Res , vol.83 , pp. 511-518
    • Haudek, S.B.1    Gupta, D.2    Dewald, O.3    Schwartz, R.J.4    Wei, L.5
  • 18
    • 33744473805 scopus 로고    scopus 로고
    • Targeted deletion of ROCK1 protects the heart against pressure overload by inhibiting reactive fibrosis
    • doi:10.1096/fj.05-5129com. PubMed: 16675849
    • Zhang YM, Bo J, Taffet GE, Chang J, Shi J et al. (2006) Targeted deletion of ROCK1 protects the heart against pressure overload by inhibiting reactive fibrosis. FASEB J 20: 916-925. doi:10.1096/fj.05-5129com. PubMed: 16675849.
    • (2006) FASEB J , vol.20 , pp. 916-925
    • Zhang, Y.M.1    Bo, J.2    Taffet, G.E.3    Chang, J.4    Shi, J.5
  • 19
    • 33748089036 scopus 로고    scopus 로고
    • Lactadherin binding and phosphatidylserine expression on cell surface-comparison with annexin A5
    • doi:10.1016/j.lab.2006.03.006. PubMed: 16887494
    • Dasgupta SK, Guchhait P, Thiagarajan P (2006) Lactadherin binding and phosphatidylserine expression on cell surface-comparison with annexin A5. Transl Res 148: 19-25. doi:10.1016/j.lab.2006.03.006. PubMed: 16887494.
    • (2006) Transl Res , vol.148 , pp. 19-25
    • Dasgupta, S.K.1    Guchhait, P.2    Thiagarajan, P.3
  • 20
    • 0025006126 scopus 로고
    • Binding of annexin V/placental anticoagulant protein I to platelets. Evidence for phosphatidylserine exposure in the procoagulant response of activated platelets
    • PubMed: 2145274
    • Thiagarajan P, Tait JF (1990) Binding of annexin V/placental anticoagulant protein I to platelets. Evidence for phosphatidylserine exposure in the procoagulant response of activated platelets. J Biol Chem 265: 17420-17423. PubMed: 2145274.
    • (1990) J Biol Chem , vol.265 , pp. 17420-17423
    • Thiagarajan, P.1    Tait, J.F.2
  • 21
    • 80051606228 scopus 로고    scopus 로고
    • Bcl-xL-inhibitory BH3 mimetics can induce a transient thrombocytopathy that undermines the hemostatic function of platelets
    • doi:10.1182/blood-2011-04-347849. PubMed: 21673344
    • Schoenwaelder SM, Jarman KE, Gardiner EE, Hua M, Qiao J et al. (2011) Bcl-xL-inhibitory BH3 mimetics can induce a transient thrombocytopathy that undermines the hemostatic function of platelets. Blood 118: 1663-1674. doi:10.1182/blood-2011-04-347849. PubMed: 21673344.
    • (2011) Blood , vol.118 , pp. 1663-1674
    • Schoenwaelder, S.M.1    Jarman, K.E.2    Gardiner, E.E.3    Hua, M.4    Qiao, J.5
  • 22
    • 57549094163 scopus 로고    scopus 로고
    • Differential role of von Willebrand factor and P-selectin on microvascular thrombosis in endotoxemia
    • doi:10.1161/ATVBAHA.108.175679. PubMed: 18802014
    • Patel KN, Soubra SH, Bellera RV, Dong JF, McMullen CA et al. (2008) Differential role of von Willebrand factor and P-selectin on microvascular thrombosis in endotoxemia. Arterioscler Thromb Vasc Biol 28: 2225-2230. doi:10.1161/ATVBAHA.108.175679. PubMed: 18802014.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 2225-2230
    • Patel, K.N.1    Soubra, S.H.2    Bellera, R.V.3    Dong, J.F.4    McMullen, C.A.5
  • 23
    • 84863779713 scopus 로고    scopus 로고
    • Inhibition of interdomain motion in g-actin by the natural product latrunculin: A molecular dynamics study
    • PubMed: 22488806
    • Rennebaum S, Caflisch A. (2012) Inhibition of interdomain motion in g-actin by the natural product latrunculin: a molecular dynamics study. Proteins 80: 1998-2008. PubMed: 22488806.
    • (2012) Proteins , vol.80 , pp. 1998-2008
    • Rennebaum, S.1    Caflisch, A.2
  • 24
    • 77954900213 scopus 로고    scopus 로고
    • Roles of platelet STIM1 and Orai1 in glycoprotein VI- and thrombin-dependent procoagulant activity and thrombus formation
    • PubMed: 20519511
    • Gilio K, van Kruchten R, Braun A, Berna-Erro A, Feijge MA et al. (2010) Roles of platelet STIM1 and Orai1 in glycoprotein VI- and thrombin-dependent procoagulant activity and thrombus formation. J Biol Chem 285: 23629-23638. PubMed: 20519511.
    • (2010) J Biol Chem , vol.285 , pp. 23629-23638
    • Gilio, K.1    Van Kruchten, R.2    Braun, A.3    Berna-Erro, A.4    Feijge, M.A.5
  • 25
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • doi: 10.1016/0092-8674(95)90370-4. PubMed: 7536630
    • Nobes CD, Hall A (1995) Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81: 53-62. doi: 10.1016/0092-8674(95)90370-4. PubMed: 7536630.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 26
    • 72949093138 scopus 로고    scopus 로고
    • Platelet response heterogeneity in thrombus formation
    • PubMed: 19967145
    • Munnix IC, Cosemans JM, Auger JM, Heemskerk JW (2009) Platelet response heterogeneity in thrombus formation. Thromb Haemost 102: 1149-1156. PubMed: 19967145.
    • (2009) Thromb Haemost , vol.102 , pp. 1149-1156
    • Munnix, I.C.1    Cosemans, J.M.2    Auger, J.M.3    Heemskerk, J.W.4
  • 27
    • 0027999286 scopus 로고
    • Scott syndrome: A disorder of platelet coagulant activity
    • PubMed: 7831576
    • Weiss HJ (1994) Scott syndrome: a disorder of platelet coagulant activity. Semin Hematol 31: 312-319. PubMed: 7831576.
    • (1994) Semin Hematol , vol.31 , pp. 312-319
    • Weiss, H.J.1
  • 29
    • 60249091217 scopus 로고    scopus 로고
    • R93W mutation in Orai1 causes impaired calcium influx in platelets
    • doi:10.1182/blood-2008-08-174516. PubMed: 18952890
    • Bergmeier W, Oh-Hora M, McCarl CA, Roden RC, Bray PF et al. (2009) R93W mutation in Orai1 causes impaired calcium influx in platelets. Blood 113: 675-678. doi:10.1182/blood-2008-08-174516. PubMed: 18952890.
    • (2009) Blood , vol.113 , pp. 675-678
    • Bergmeier, W.1    Oh-Hora, M.2    McCarl, C.A.3    Roden, R.C.4    Bray, P.F.5
  • 30
    • 84871860558 scopus 로고    scopus 로고
    • TMEM16F forms a Ca2+-activated cation channel required for lipid scrambling in platelets during blood coagulation
    • doi:10.1016/j.cell.2012.07.036. PubMed: 23021219
    • Yang H, Kim A, David T, Palmer D, Jin T et al. (2012) TMEM16F forms a Ca2+-activated cation channel required for lipid scrambling in platelets during blood coagulation. Cell 151: 111-122. doi:10.1016/j.cell.2012.07.036. PubMed: 23021219.
    • (2012) Cell , vol.151 , pp. 111-122
    • Yang, H.1    Kim, A.2    David, T.3    Palmer, D.4    Jin, T.5
  • 31
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • doi: 10.1038/nature09583. PubMed: 21107324
    • Suzuki J, Umeda M, Sims PJ, Nagata S. (2010) Calcium-dependent phospholipid scrambling by TMEM16F. Nature 468: 834-838. doi: 10.1038/nature09583. PubMed: 21107324.
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1    Umeda, M.2    Sims, P.J.3    Nagata, S.4
  • 32
    • 33947227522 scopus 로고    scopus 로고
    • Programmed anuclear cell death delimits platelet life span
    • doi:10.1016/j.cell.2007.01.037. PubMed: 17382885
    • Mason KD, Carpinelli MR, Fletcher JI, Collinge JE, Hilton AA et al. (2007) Programmed anuclear cell death delimits platelet life span. Cell 128: 1173-1186. doi:10.1016/j.cell.2007.01.037. PubMed: 17382885.
    • (2007) Cell , vol.128 , pp. 1173-1186
    • Mason, K.D.1    Carpinelli, M.R.2    Fletcher, J.I.3    Collinge, J.E.4    Hilton, A.A.5
  • 33
    • 84856603735 scopus 로고    scopus 로고
    • Bcl-xL-inhibitory BH3 mimetics (ABT-737 or ABT-263) and the modulation of cytosolic calcium flux and platelet function
    • author reply: 22308285
    • Schoenwaelder SM, Jackson SP. (2012) Bcl-xL-inhibitory BH3 mimetics (ABT-737 or ABT-263) and the modulation of cytosolic calcium flux and platelet function. Blood 119: 1320-1322; author reply: 22308285.
    • (2012) Blood , vol.119 , pp. 1320-1322
    • Schoenwaelder, S.M.1    Jackson, S.P.2
  • 34
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • doi:10.1146/annurev.cellbio.15.1.185. PubMed: 10611961
    • Bamburg JR (1999) Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu Rev Cell Dev Biol 15: 185-230. doi:10.1146/annurev.cellbio.15.1.185. PubMed: 10611961.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 35
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • doi:10.1046/j.1365-2443.1996.05005.x. PubMed: 9078368
    • Moriyama K, Iida K, Yahara I (1996) Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1: 73-86. doi:10.1046/j.1365-2443.1996.05005.x. PubMed: 9078368.
    • (1996) Genes Cells , vol.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 36
    • 47549090623 scopus 로고    scopus 로고
    • Structure of the actin-depolymerizing factor homology domain in complex with actin
    • doi:10.1083/jcb.200803100. PubMed: 18625842
    • Paavilainen VO, Oksanen E, Goldman A, Lappalainen P (2008) Structure of the actin-depolymerizing factor homology domain in complex with actin. J Cell Biol 182: 51-59. doi:10.1083/jcb.200803100. PubMed: 18625842.
    • (2008) J Cell Biol , vol.182 , pp. 51-59
    • Paavilainen, V.O.1    Oksanen, E.2    Goldman, A.3    Lappalainen, P.4
  • 37
    • 48049098171 scopus 로고    scopus 로고
    • Cofilin increases the bending flexibility of actin filaments: Implications for severing and cell mechanics
    • doi:10.1016/j.jmb.2008.05.055. PubMed: 18617188
    • McCullough BR, Blanchoin L, Martiel JL, De la Cruz EM (2008) Cofilin increases the bending flexibility of actin filaments: implications for severing and cell mechanics. J Mol Biol 381: 550-558. doi:10.1016/j.jmb.2008.05.055. PubMed: 18617188.
    • (2008) J Mol Biol , vol.381 , pp. 550-558
    • McCullough, B.R.1    Blanchoin, L.2    Martiel, J.L.3    De La Cruz, E.M.4
  • 38
    • 77956607977 scopus 로고    scopus 로고
    • ADF/n-cofilin-dependent actin turnover determines platelet formation and sizing
    • doi:10.1182/blood-2010-03-274340. PubMed: 20530287
    • Bender M, Eckly A, Hartwig JH, Elvers M, Pleines I et al. (2010) ADF/n-cofilin-dependent actin turnover determines platelet formation and sizing. Blood 116: 1767-1775. doi:10.1182/blood-2010-03-274340. PubMed: 20530287.
    • (2010) Blood , vol.116 , pp. 1767-1775
    • Bender, M.1    Eckly, A.2    Hartwig, J.H.3    Elvers, M.4    Pleines, I.5
  • 39
    • 0021909324 scopus 로고
    • Phospholipid asymmetry in human erythrocyte ghosts
    • doi:10.1002/jcp.1041230209. PubMed: 2579962
    • Williamson P, Algarin L, Bateman J, Choe HR, Schlegel RA (1985) Phospholipid asymmetry in human erythrocyte ghosts. J Cell Physiol 123: 209-214. doi:10.1002/jcp.1041230209. PubMed: 2579962.
    • (1985) J Cell Physiol , vol.123 , pp. 209-214
    • Williamson, P.1    Algarin, L.2    Bateman, J.3    Choe, H.R.4    Schlegel, R.A.5
  • 40
    • 0035895971 scopus 로고    scopus 로고
    • Regulation of phosphatidylserine transbilayer redistribution by store-operated Ca2+ entry: Role of actin cytoskeleton
    • doi:10.1074/jbc.M007924200. PubMed: 11076944
    • Kunzelmann-Marche C, Freyssinet JM, Martínez MC (2001) Regulation of phosphatidylserine transbilayer redistribution by store-operated Ca2+ entry: role of actin cytoskeleton. J Biol Chem 276: 5134-5139. doi:10.1074/jbc. M007924200. PubMed: 11076944.
    • (2001) J Biol Chem , vol.276 , pp. 5134-5139
    • Kunzelmann-Marche, C.1    Freyssinet, J.M.2    Martínez, M.C.3
  • 41
    • 0037133206 scopus 로고    scopus 로고
    • Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability
    • doi:10.1073/pnas.042688399. PubMed: 11830646
    • Manno S, Takakuwa Y, Mohandas N (2002) Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability. Proc Natl Acad Sci U S A 99: 1943-1948. doi:10.1073/pnas.042688399. PubMed: 11830646.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1943-1948
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 42
    • 0031048791 scopus 로고    scopus 로고
    • Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
    • doi:10.1126/science.275.5304.1308. PubMed: 9036856
    • Amano M, Chihara K, Kimura K, Fukata Y, Nakamura N et al. (1997) Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science 275: 1308-1311. doi:10.1126/science.275.5304.1308. PubMed: 9036856.
    • (1997) Science , vol.275 , pp. 1308-1311
    • Amano, M.1    Chihara, K.2    Kimura, K.3    Fukata, Y.4    Nakamura, N.5
  • 43
    • 69249215416 scopus 로고    scopus 로고
    • Actin-induced perturbation of PS lipid-cholesterol interaction: A possible mechanism of cytoskeleton-based regulation of membrane organization
    • doi:10.1016/j.jsb.2009.04.001. PubMed: 19366633
    • Garg S, Tang JX, Rühe J, Naumann CA (2009) Actin-induced perturbation of PS lipid-cholesterol interaction: A possible mechanism of cytoskeleton-based regulation of membrane organization. J Struct Biol 168: 11-20. doi:10.1016/j.jsb.2009.04.001. PubMed: 19366633.
    • (2009) J Struct Biol , vol.168 , pp. 11-20
    • Garg, S.1    Tang, J.X.2    Rühe, J.3    Naumann, C.A.4
  • 44
    • 0028038109 scopus 로고
    • Reversible binding kinetics of a cytoskeletal protein at the erythrocyte submembrane
    • doi:10.1016/S0006-3495(94)80604-6. PubMed: 7811947
    • Stout AL, Axelrod D (1994) Reversible binding kinetics of a cytoskeletal protein at the erythrocyte submembrane. Biophys J 67: 1324-1334. doi:10.1016/S0006-3495(94)80604-6. PubMed: 7811947.
    • (1994) Biophys J , vol.67 , pp. 1324-1334
    • Stout, A.L.1    Axelrod, D.2
  • 45
    • 70349638633 scopus 로고    scopus 로고
    • 4.1R-deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins
    • doi:10.3324/haematol.2009.006585. PubMed: 19794081
    • Jeremy KP, Plummer ZE, Head DJ, Madgett TE, Sanders KL et al. (2009) 4.1R-deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins. Haematologica 94: 1354-1361. doi:10.3324/haematol.2009.006585. PubMed: 19794081.
    • (2009) Haematologica , vol.94 , pp. 1354-1361
    • Jeremy, K.P.1    Plummer, Z.E.2    Head, D.J.3    Madgett, T.E.4    Sanders, K.L.5
  • 46
    • 84871274666 scopus 로고    scopus 로고
    • Shedding of phosphatidylserine from developing erythroid cells involves microtubule depolymerization and affects membrane lipid composition
    • PubMed: 22825717
    • Freikman I, Ringel I, Fibach E. (2012) Shedding of phosphatidylserine from developing erythroid cells involves microtubule depolymerization and affects membrane lipid composition. J Membr Biol 245: 779-787. PubMed: 22825717.
    • (2012) J Membr Biol , vol.245 , pp. 779-787
    • Freikman, I.1    Ringel, I.2    Fibach, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.