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Volumn 7, Issue , 2017, Pages

Annexin-A5 organized in 2D-network at the plasmalemma eases human trophoblast fusion

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CATENIN; BETA CATENIN; CADHERIN; CDH1 PROTEIN, HUMAN; CTNNB1 PROTEIN, HUMAN; LIPOCORTIN 5; SMALL INTERFERING RNA;

EID: 85011982469     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep42173     Document Type: Article
Times cited : (30)

References (53)
  • 1
    • 0022426155 scopus 로고
    • The fusion of myoblasts
    • Wakelam, M. The fusion of myoblasts. Biochem J 15, 1-12 (1985).
    • (1985) Biochem J , vol.15 , pp. 1-12
    • Wakelam, M.1
  • 3
    • 37049245766 scopus 로고
    • Morphogenesis of syncytiotrophoblast in vivo: An autoradiographic demonstration
    • Midgley, A., Pierce, G., Denau, G. & Gosling, J. Morphogenesis of syncytiotrophoblast in vivo: an autoradiographic demonstration. Science 141, 350-351 (1963).
    • (1963) Science , vol.141 , pp. 350-351
    • Midgley, A.1    Pierce, G.2    Denau, G.3    Gosling, J.4
  • 4
    • 0021285529 scopus 로고
    • Monocytes from circulating blood fuse in vitro with purified osteoclasts in primary culture
    • Zambonin Zallone, A., Teti, A. & Primavera, M. Monocytes from circulating blood fuse in vitro with purified osteoclasts in primary culture. J Cell Sci 66, 335-342 (1984).
    • (1984) J Cell Sci , vol.66 , pp. 335-342
    • Zambonin Zallone, A.1    Teti, A.2    Primavera, M.3
  • 5
    • 84924334828 scopus 로고    scopus 로고
    • Review: An overview of molecular events occurring in human trophoblast fusion
    • Gerbaud, P. & Pidoux, G. Review: An overview of molecular events occurring in human trophoblast fusion. Placenta 36 Suppl 1, S35-42, doi: 10.1016/j.placenta.2014.12.015 (2015).
    • (2015) Placenta , vol.36 , pp. S35-S42
    • Gerbaud, P.1    Pidoux, G.2
  • 6
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik, L. V. & Kozlov, M. M. Membrane hemifusion: crossing a chasm in two leaps. Cell 123, 375-382, doi: 10.1016/j. cell.2005.10.015 (2005).
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 7
    • 79960937293 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of mammalian cell fusion
    • Zhou, X. & Platt, J. L. Molecular and cellular mechanisms of mammalian cell fusion. Adv Exp Med Biol 713, 33-64, doi: 10.1007/978- 94-007-0763-4-4 (2011).
    • (2011) Adv Exp Med Biol , vol.713 , pp. 33-64
    • Zhou, X.1    Platt, J.L.2
  • 8
    • 14044274774 scopus 로고    scopus 로고
    • Expression of connexins during differentiation and regeneration of skeletal muscle: Functional relevance of connexin43
    • Araya, R. et al. Expression of connexins during differentiation and regeneration of skeletal muscle: functional relevance of connexin43. J Cell Sci 118, 27-37, doi: 10.1242/jcs.01553 (2005).
    • (2005) J Cell Sci , vol.118 , pp. 27-37
    • Araya, R.1
  • 9
    • 84913609111 scopus 로고    scopus 로고
    • A PKA-ezrin-connexin 43 signaling complex controls gap junction communication and thereby trophoblast cell fusion
    • Pidoux, G. et al. A PKA-ezrin-connexin 43 signaling complex controls gap junction communication and thereby trophoblast cell fusion. J Cell Sci 127, 4172-4185, doi: 10.1242/jcs.149609 (2014).
    • (2014) J Cell Sci , vol.127 , pp. 4172-4185
    • Pidoux, G.1
  • 10
    • 0002079737 scopus 로고    scopus 로고
    • Extravillous trophoblast in the human placenta
    • Kaufmann, P. & Castellucci, M. Extravillous trophoblast in the human placenta. Placenta 18, 21-65, doi: 10.1016/S0143- 4004(97)80079-3 (1997).
    • (1997) Placenta , vol.18 , pp. 21-65
    • Kaufmann, P.1    Castellucci, M.2
  • 12
    • 0002922470 scopus 로고
    • (eds C. W. Redman, I. L. Sargent & P. M. Starkey),Blackwell Scientific Publication
    • Eaton, B. & Contractor, S. In The human placenta (eds C. W. Redman, I. L. Sargent & P. M. Starkey) 471-503 (Blackwell Scientific Publication, 1993).
    • (1993) The Human Placenta , pp. 471-503
    • Eaton, B.1    Contractor, S.2
  • 13
    • 0022527203 scopus 로고
    • Purification characterization, and in vitro differenciation of cytotrophoblasts from human term placentae
    • Kliman, H., Nestler, J., Sermasi, E., Sanger, J. & Strauss, J. III Purification, characterization, and in vitro differenciation of cytotrophoblasts from human term placentae. Endocrinology 118, 1567-1582 (1986).
    • (1986) Endocrinology , vol.118 , pp. 1567-1582
    • Kliman, H.1    Nestler, J.2    Sermasi, E.3    Sanger, J.4    Strauss, J.5
  • 14
    • 4444294976 scopus 로고    scopus 로고
    • Apoptosis in the trophoblast-role of apoptosis in placental morphogenesis
    • Huppertz, B. & Kingdom, J. C. Apoptosis in the trophoblast-role of apoptosis in placental morphogenesis. J Soc Gynecol Investig 11, 353-362, doi: 10.1016/j.jsgi.2004.06.002 (2004).
    • (2004) J Soc Gynecol Investig , vol.11 , pp. 353-362
    • Huppertz, B.1    Kingdom, J.C.2
  • 15
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke, V. & Moss, S. E. Annexins: from structure to function. Physiol Rev 82, 331-371, doi: 10.1152/physrev.00030.2001 (2002).
    • (2002) Physiol Rev , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 16
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: Linking Ca2+ signalling to membrane dynamics
    • Gerke, V., Creutz, C. E. & Moss, S. E. Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol 6, 449-461, doi: 10.1038/nrm1661 (2005).
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 17
    • 84924498439 scopus 로고    scopus 로고
    • Review: Annexin-A5 and cell membrane repair
    • Bouter, A. et al. Review: Annexin-A5 and cell membrane repair. Placenta 36 Suppl 1, S43-49, doi: 10.1016/j.placenta.2015.01.193 (2015).
    • (2015) Placenta , vol.36 , pp. S43-S49
    • Bouter, A.1
  • 18
    • 27744522668 scopus 로고    scopus 로고
    • On the kinetics of adsorption and two-dimensional self-assembly of annexin A5 on supported lipid bilayers
    • Richter, R. P., Him, J. L., Tessier, B., Tessier, C. & Brisson, A. R. On the kinetics of adsorption and two-dimensional self-assembly of annexin A5 on supported lipid bilayers. Biophys J 89, 3372-3385, doi: 10.1529/biophysj.105.064337 (2005).
    • (2005) Biophys J , vol.89 , pp. 3372-3385
    • Richter, R.P.1    Him, J.L.2    Tessier, B.3    Tessier, C.4    Brisson, A.R.5
  • 19
    • 77954578642 scopus 로고    scopus 로고
    • Role of Annexin A1 in mouse myoblast cell differentiation
    • Bizzarro, V. et al. Role of Annexin A1 in mouse myoblast cell differentiation. J Cell Physiol 224, 757-765, doi: 10.1002/jcp.22178 (2010).
    • (2010) J Cell Physiol , vol.224 , pp. 757-765
    • Bizzarro, V.1
  • 20
    • 84872079429 scopus 로고    scopus 로고
    • Extracellular annexins and dynamin are important for sequential steps in myoblast fusion
    • Leikina, E. et al. Extracellular annexins and dynamin are important for sequential steps in myoblast fusion. J Cell Biol 200, 109-123, doi: 10.1083/jcb.201207012 (2013).
    • (2013) J Cell Biol , vol.200 , pp. 109-123
    • Leikina, E.1
  • 21
    • 84924431318 scopus 로고    scopus 로고
    • Annexin-A5 promotes membrane resealing in human trophoblasts
    • Carmeille, R. et al. Annexin-A5 promotes membrane resealing in human trophoblasts. Biochim Biophys Acta, doi: 10.1016/j. bbamcr.2014.12.038 (2015).
    • (2015) Biochim Biophys Acta
    • Carmeille, R.1
  • 22
    • 79953796350 scopus 로고    scopus 로고
    • Annexin-A5 assembled into two-dimensional arrays promotes cell membrane repair
    • Bouter, A. et al. Annexin-A5 assembled into two-dimensional arrays promotes cell membrane repair. Nature communications 2, 270, doi: 10.1038/ncomms1270 (2011).
    • (2011) Nature Communications , vol.2 , pp. 270
    • Bouter, A.1
  • 23
    • 0031565732 scopus 로고    scopus 로고
    • Structural analysis of junctions formed between lipid membranes and several annexins by cryo-electron microscopy
    • Lambert, O., Gerke, V., Bader, M. F., Porte, F. & Brisson, A. Structural analysis of junctions formed between lipid membranes and several annexins by cryo-electron microscopy. J Mol Biol 272, 42-55, doi: 10.1006/jmbi.1997.1183 (1997).
    • (1997) J Mol Biol , vol.272 , pp. 42-55
    • Lambert, O.1    Gerke, V.2    Bader, M.F.3    Porte, F.4    Brisson, A.5
  • 24
    • 0026008734 scopus 로고
    • E-cadherin expression during the differentiation of human trophoblasts
    • Coutifaris, C. et al. E-cadherin expression during the differentiation of human trophoblasts. Development 113, 767-777 (1991).
    • (1991) Development , vol.113 , pp. 767-777
    • Coutifaris, C.1
  • 25
    • 33745627481 scopus 로고    scopus 로고
    • Annexin A4 self-association modulates general membrane protein mobility in living cells
    • Piljic, A. & Schultz, C. Annexin A4 self-association modulates general membrane protein mobility in living cells. Mol Biol Cell 17, 3318-3328, doi: 10.1091/mbc.E06-01-0041 (2006).
    • (2006) Mol Biol Cell , vol.17 , pp. 3318-3328
    • Piljic, A.1    Schultz, C.2
  • 26
    • 0344222161 scopus 로고    scopus 로고
    • Influence of annexin v on the structure and dynamics of phosphatidylcholine/phosphatidylserine bilayers: A fluorescence and NMR study
    • Saurel, O., Cezanne, L., Milon, A., Tocanne, J. F. & Demange, P. Influence of annexin V on the structure and dynamics of phosphatidylcholine/phosphatidylserine bilayers: a fluorescence and NMR study. Biochemistry 37, 1403-1410, doi: 10.1021/ bi971484n (1998).
    • (1998) Biochemistry , vol.37 , pp. 1403-1410
    • Saurel, O.1    Cezanne, L.2    Milon, A.3    Tocanne, J.F.4    Demange, P.5
  • 27
    • 84904234456 scopus 로고    scopus 로고
    • Ionomycin causes susceptibility to phospholipase A2 while temperature-induced increases in membrane fluidity fail: Possible involvement of actin fragmentation
    • Gibbons, E. et al. Ionomycin causes susceptibility to phospholipase A2 while temperature-induced increases in membrane fluidity fail: possible involvement of actin fragmentation. Biochim Biophys Acta 1838, 2607-2614, doi: 10.1016/j.bbamem.2014.05.028 (2014).
    • (2014) Biochim Biophys Acta , vol.1838 , pp. 2607-2614
    • Gibbons, E.1
  • 28
    • 0033604454 scopus 로고    scopus 로고
    • Calcium influx triggers the sequential proteolysis of extracellular and cytoplasmic domains of E-cadherin, leading to loss of beta-catenin from cell-cell contacts
    • Ito, K. et al. Calcium influx triggers the sequential proteolysis of extracellular and cytoplasmic domains of E-cadherin, leading to loss of beta-catenin from cell-cell contacts. Oncogene 18, 7080-7090, doi: 10.1038/sj.onc.1203191 (1999).
    • (1999) Oncogene , vol.18 , pp. 7080-7090
    • Ito, K.1
  • 29
    • 44849115958 scopus 로고    scopus 로고
    • A two-tiered mechanism for stabilization and immobilization of E-cadherin
    • Cavey, M., Rauzi, M., Lenne, P. F. & Lecuit, T. A two-tiered mechanism for stabilization and immobilization of E-cadherin. Nature 453, 751-756, doi: 10.1038/nature06953 (2008).
    • (2008) Nature , vol.453 , pp. 751-756
    • Cavey, M.1    Rauzi, M.2    Lenne, P.F.3    Lecuit, T.4
  • 30
    • 0027933860 scopus 로고
    • The expression of the placental anticoagulant protein, annexin V, by villous trophoblasts: Immunolocalization and in vitro regulation
    • Krikun, G. et al. The expression of the placental anticoagulant protein, annexin V, by villous trophoblasts: immunolocalization and in vitro regulation. Placenta 15, 601-612 (1994).
    • (1994) Placenta , vol.15 , pp. 601-612
    • Krikun, G.1
  • 31
    • 0035037491 scopus 로고    scopus 로고
    • Alpha-, beta-, gamma-catenin, and p120(CTN) expression during the terminal differentiation and fusion of human mononucleate cytotrophoblasts in vitro and in vivo
    • Getsios, S., Chen, G. T. & MacCalman, C. D. alpha-, beta-, gamma-catenin, and p120(CTN) expression during the terminal differentiation and fusion of human mononucleate cytotrophoblasts in vitro and in vivo. Molecular reproduction and development 59, 168-177, doi: 10.1002/mrd.1019 (2001).
    • (2001) Molecular Reproduction and Development , vol.59 , pp. 168-177
    • Getsios, S.1    Chen, G.T.2    MacCalman, C.D.3
  • 32
    • 43549116086 scopus 로고    scopus 로고
    • Extracellular annexin A5: Functions of phosphatidylserine-binding and two-dimensional crystallization
    • van Genderen, H. O., Kenis, H., Hofstra, L., Narula, J. & Reutelingsperger, C. P. Extracellular annexin A5: functions of phosphatidylserine-binding and two-dimensional crystallization. Biochim Biophys Acta 1783, 953-963, doi: 10.1016/j. bbamcr.2008.01.030 (2008).
    • (2008) Biochim Biophys Acta 1783 , pp. 953-963
    • Van Genderen, H.O.1    Kenis, H.2    Hofstra, L.3    Narula, J.4    Reutelingsperger, C.P.5
  • 33
    • 40749113644 scopus 로고    scopus 로고
    • Contribution of annexin 2 to the architecture of mature endothelial adherens junctions
    • Heyraud, S. et al. Contribution of annexin 2 to the architecture of mature endothelial adherens junctions. Mol Cell Biol 28, 1657-1668, doi: 10.1128/MCB.00695-07 (2008).
    • (2008) Mol Cell Biol , vol.28 , pp. 1657-1668
    • Heyraud, S.1
  • 34
    • 2342586664 scopus 로고    scopus 로고
    • Measurement of the affinity and cooperativity of annexin V-membrane binding under conditions of low membrane occupancy
    • Tait, J. F., Gibson, D. F. & Smith, C. Measurement of the affinity and cooperativity of annexin V-membrane binding under conditions of low membrane occupancy. Anal Biochem 329, 112-119, doi: 10.1016/j.ab.2004.02.043 (2004).
    • (2004) Anal Biochem , vol.329 , pp. 112-119
    • Tait, J.F.1    Gibson, D.F.2    Smith, C.3
  • 35
    • 0026514824 scopus 로고
    • Microdomains of high calcium concentration in a presynaptic terminal
    • Llinas, R., Sugimori, M. & Silver, R. B. Microdomains of high calcium concentration in a presynaptic terminal. Science 256, 677-679 (1992).
    • (1992) Science , vol.256 , pp. 677-679
    • Llinas, R.1    Sugimori, M.2    Silver, R.B.3
  • 36
    • 0034764237 scopus 로고    scopus 로고
    • Transient expression of phosphatidylserine at cell-cell contact areas is required for myotube formation
    • van den Eijnde, S. M. et al. Transient expression of phosphatidylserine at cell-cell contact areas is required for myotube formation. J Cell Sci 114, 3631-3642 (2001).
    • (2001) J Cell Sci , vol.114 , pp. 3631-3642
    • Van Den Eijnde, S.M.1
  • 37
    • 77949567598 scopus 로고    scopus 로고
    • Decreased annexin A5 mRNA placental expression in pregnancies complicated by fetal growth restriction
    • Sifakis, S. et al. Decreased annexin A5 mRNA placental expression in pregnancies complicated by fetal growth restriction. Thrombosis research 125, 326-331, doi: 10.1016/j.thromres.2009.11.033 (2010).
    • (2010) Thrombosis Research , vol.125 , pp. 326-331
    • Sifakis, S.1
  • 38
    • 0033971192 scopus 로고    scopus 로고
    • Immunohistochemical study of annexin v expression in placentae of preeclampsia
    • doi: 10206
    • Shu, F. et al. Immunohistochemical study of annexin V expression in placentae of preeclampsia. Gynecol Obstet Invest 49, 17-23, doi: 10206 (2000).
    • (2000) Gynecol Obstet Invest , vol.49 , pp. 17-23
    • Shu, F.1
  • 39
    • 84893949557 scopus 로고    scopus 로고
    • Reduced ANXA5 mRNA and protein expression in pregnancies complicated by preeclampsia
    • Gourvas, V. et al. Reduced ANXA5 mRNA and protein expression in pregnancies complicated by preeclampsia. Thrombosis research 133, 495-500, doi: 10.1016/j.thromres.2013.12.027 (2014).
    • (2014) Thrombosis Research , vol.133 , pp. 495-500
    • Gourvas, V.1
  • 40
    • 34249885877 scopus 로고    scopus 로고
    • Biochemical characterization and modulation of LH/CG-receptor during human trophoblast differentiation
    • Pidoux, G. et al. Biochemical characterization and modulation of LH/CG-receptor during human trophoblast differentiation. J Cell Physiol 212, 26-35, doi: 10.1002/jcp.20995 (2007).
    • (2007) J Cell Physiol , vol.212 , pp. 26-35
    • Pidoux, G.1
  • 41
    • 77952603166 scopus 로고    scopus 로고
    • ZO-1 is involved in trophoblastic cell differentiation in human placenta
    • Pidoux, G. et al. ZO-1 is involved in trophoblastic cell differentiation in human placenta. Am J Physiol Cell Physiol 298, C1517-1526, doi: 10.1152/ajpcell.00484.2008 (2010).
    • (2010) Am J Physiol Cell Physiol , vol.298 , pp. C1517-1526
    • Pidoux, G.1
  • 42
    • 84904555134 scopus 로고    scopus 로고
    • Differential labeling of cell-surface and internalized proteins after antibody feeding of live cultured neurons
    • Carrodus, N. L., Teng, K. S., Munro, K. M., Kennedy, M. J. & Gunnersen, J. M. Differential labeling of cell-surface and internalized proteins after antibody feeding of live cultured neurons. J Vis Exp. e51139, doi: 10.3791/51139 (2014).
    • (2014) J Vis Exp
    • Carrodus, N.L.1    Teng, K.S.2    Munro, K.M.3    Kennedy, M.J.4    Gunnersen, J.M.5
  • 43
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl
    • Martin, S. J. et al. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl. The Journal of experimental medicine 182, 1545-1556 (1995).
    • (1995) The Journal of Experimental Medicine , vol.182 , pp. 1545-1556
    • Martin, S.J.1
  • 44
    • 0031985647 scopus 로고    scopus 로고
    • Annexin V-affinity assay: A review on an apoptosis detection system based on phosphatidylserine exposure
    • van Engeland, M., Nieland, L. J., Ramaekers, F. C., Schutte, B. & Reutelingsperger, C. P. Annexin V-affinity assay: a review on an apoptosis detection system based on phosphatidylserine exposure. Cytometry 31, 1-9 (1998).
    • (1998) Cytometry , vol.31 , pp. 1-9
    • Van Engeland, M.1    Nieland, L.J.2    Ramaekers, F.C.3    Schutte, B.4    Reutelingsperger, C.P.5
  • 45
    • 84869496214 scopus 로고    scopus 로고
    • Live-cell imaging shows apoptosis initiates locally and propagates as a wave throughout syncytiotrophoblasts in primary cultures of human placental villous trophoblasts
    • Longtine, M. S., Barton, A., Chen, B. & Nelson, D. M. Live-cell imaging shows apoptosis initiates locally and propagates as a wave throughout syncytiotrophoblasts in primary cultures of human placental villous trophoblasts. Placenta 33, 971-976, doi: 10.1016/j. placenta.2012.09.013 (2012).
    • (2012) Placenta , vol.33 , pp. 971-976
    • Longtine, M.S.1    Barton, A.2    Chen, B.3    Nelson, D.M.4
  • 46
    • 35548940414 scopus 로고    scopus 로고
    • Human placental development is impaired by abnormal human chorionic gonadotropin signaling in trisomy 21 pregnancies
    • Pidoux, G. et al. Human placental development is impaired by abnormal human chorionic gonadotropin signaling in trisomy 21 pregnancies. Endocrinology 148, 5403-5413, doi: 10.1210/en.2007-0589 (2007).
    • (2007) Endocrinology , vol.148 , pp. 5403-5413
    • Pidoux, G.1
  • 47
    • 84941356650 scopus 로고    scopus 로고
    • Formaldehyde Crosses the Human Placenta and Affects Human Trophoblast Differentiation and Hormonal Functions
    • Pidoux, G. et al. Formaldehyde Crosses the Human Placenta and Affects Human Trophoblast Differentiation and Hormonal Functions. PloS one 10, e0133506, doi: 10.1371/journal.pone.0133506 (2015).
    • (2015) PloS One , vol.10
    • Pidoux, G.1
  • 48
    • 0037205418 scopus 로고    scopus 로고
    • Lateral dimerization of the E-cadherin extracellular domain is necessary but not sufficient for adhesive activity
    • Ozawa, M. Lateral dimerization of the E-cadherin extracellular domain is necessary but not sufficient for adhesive activity. J Biol Chem 277, 19600-19608, doi: 10.1074/jbc.M202029200 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 19600-19608
    • Ozawa, M.1
  • 49
    • 77954599053 scopus 로고    scopus 로고
    • P62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • Jain, A. et al. p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. J Biol Chem 285, 22576-22591, doi: 10.1074/jbc.M110.118976 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 22576-22591
    • Jain, A.1
  • 50
    • 85053361346 scopus 로고    scopus 로고
    • Spatiotemporal regulation of cAMP signaling controls the human trophoblast fusion
    • Gerbaud, P., Tasken, K. & Pidoux, G. Spatiotemporal regulation of cAMP signaling controls the human trophoblast fusion. Front Pharmacol 6, 202, doi: 10.3389/fphar.2015.00202 (2015).
    • (2015) Front Pharmacol , vol.6 , Issue.202
    • Gerbaud, P.1    Tasken, K.2    Pidoux, G.3
  • 51
    • 84893836000 scopus 로고    scopus 로고
    • Recycling endosome tubule morphogenesis from sorting endosomes requires the kinesin motor KIF13A
    • Delevoye, C. et al. Recycling endosome tubule morphogenesis from sorting endosomes requires the kinesin motor KIF13A. Cell Rep 6, 445-454, doi: 10.1016/j.celrep.2014.01.002 (2014).
    • (2014) Cell Rep , vol.6 , pp. 445-454
    • Delevoye, C.1
  • 52
    • 76249091081 scopus 로고    scopus 로고
    • Patch-based nonlocal functional for denoising fluorescence microscopy image sequences
    • Boulanger, J. et al. Patch-based nonlocal functional for denoising fluorescence microscopy image sequences. IEEE Trans Med Imaging 29, 442-454, doi: 10.1109/TMI.2009.2033991 (2010).
    • (2010) IEEE Trans Med Imaging , vol.29 , pp. 442-454
    • Boulanger, J.1


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