메뉴 건너뛰기




Volumn 537, Issue 7618, 2016, Pages 107-111

An endosomal tether undergoes an entropic collapse to bring vesicles together

Author keywords

[No Author keywords available]

Indexed keywords

EARLY ENDOSOME ANTIGEN 1; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; RAB PROTEIN; RAB5 PROTEIN; UNCLASSIFIED DRUG; GUANOSINE TRIPHOSPHATE; POLYPHOSPHOINOSITIDE; PROTEIN BINDING; SNARE PROTEIN; VESICULAR TRANSPORT PROTEIN;

EID: 84984653623     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature19326     Document Type: Article
Times cited : (105)

References (58)
  • 1
    • 78149306025 scopus 로고    scopus 로고
    • Multisubunit tethering complexes and their role in membrane fusion
    • Bröcker, C., Engelbrecht-Vandré, S. & Ungermann, C. Multisubunit tethering complexes and their role in membrane fusion. Curr. Biol. 20, R943-R952 (2010).
    • (2010) Curr. Biol. , vol.20 , pp. R943-R952
    • Bröcker, C.1    Engelbrecht-Vandré, S.2    Ungermann, C.3
  • 2
    • 78650138725 scopus 로고    scopus 로고
    • An update on transport vesicle tethering
    • Brown, F. C. & Pfeffer, S. R. An update on transport vesicle tethering. Mol. Membr. Biol. 27, 457-461 (2010).
    • (2010) Mol. Membr. Biol. , vol.27 , pp. 457-461
    • Brown, F.C.1    Pfeffer, S.R.2
  • 4
    • 2942755631 scopus 로고    scopus 로고
    • Organelle identity and the organization of membrane traffic
    • Munro, S. Organelle identity and the organization of membrane traffic. Nature Cell Biol. 6, 469-472 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 469-472
    • Munro, S.1
  • 5
    • 0031040763 scopus 로고    scopus 로고
    • Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
    • Mayer, A. & Wickner, W. Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J. Cell Biol. 136, 307-317 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 307-317
    • Mayer, A.1    Wickner, W.2
  • 6
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Christoforidis, S., McBride, H. M., Burgoyne, R. D. & Zerial, M. The Rab5 effector EEA1 is a core component of endosome docking. Nature 397, 621-625 (1999).
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 7
    • 0034635387 scopus 로고    scopus 로고
    • Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes
    • Rubino, M., Miaczynska, M., Lippé, R. & Zerial, M. Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes. J. Biol. Chem. 275, 3745-3748 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3745-3748
    • Rubino, M.1    Miaczynska, M.2    Lippé, R.3    Zerial, M.4
  • 8
    • 84866132236 scopus 로고    scopus 로고
    • Single reconstituted neuronal SNARE complexes zipper in three distinct stages
    • Gao, Y. et al. Single reconstituted neuronal SNARE complexes zipper in three distinct stages. Science 337, 1340-1343 (2012).
    • (2012) Science , vol.337 , pp. 1340-1343
    • Gao, Y.1
  • 9
    • 0037216786 scopus 로고    scopus 로고
    • Measuring distances in supported bilayers by fluorescence interference-contrast microscopy: Polymer supports and SNARE proteins
    • Kiessling, V. & Tamm, L. K. Measuring distances in supported bilayers by fluorescence interference-contrast microscopy: polymer supports and SNARE proteins. Biophys. J. 84, 408-418 (2003).
    • (2003) Biophys. J. , vol.84 , pp. 408-418
    • Kiessling, V.1    Tamm, L.K.2
  • 10
    • 0035930332 scopus 로고    scopus 로고
    • Multivalent endosome targeting by homodimeric EEA1
    • Dumas, J. J. et al. Multivalent endosome targeting by homodimeric EEA1. Mol. Cell 8, 947-958 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 947-958
    • Dumas, J.J.1
  • 11
    • 0033840979 scopus 로고    scopus 로고
    • EEA1, a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts
    • Wilson, J. M. et al. EEA1, a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts. Mol. Biol. Cell 11, 2657-2671 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2657-2671
    • Wilson, J.M.1
  • 12
    • 0032581654 scopus 로고    scopus 로고
    • EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
    • Simonsen, A. et al. EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature 394, 494-498 (1998).
    • (1998) Nature , vol.394 , pp. 494-498
    • Simonsen, A.1
  • 13
    • 77954649564 scopus 로고    scopus 로고
    • Structural basis for Rab GTPase recognition and endosome tethering by the C2H2 zinc finger of early endosomal autoantigen 1 (EEA1)
    • Mishra, A., Eathiraj, S., Corvera, S. & Lambright, D. G. Structural basis for Rab GTPase recognition and endosome tethering by the C2H2 zinc finger of early endosomal autoantigen 1 (EEA1). Proc. Natl Acad. Sci. USA 107, 10866-10871 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 10866-10871
    • Mishra, A.1    Eathiraj, S.2    Corvera, S.3    Lambright, D.G.4
  • 14
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M. & Stock, J. Predicting coiled coils from protein sequences. Science 252, 1162-1164 (1991).
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 15
    • 32144456009 scopus 로고    scopus 로고
    • Paircoil2: Improved prediction of coiled coils from sequence
    • McDonnell, A. V., Jiang, T., Keating, A. E. & Berger, B. Paircoil2: improved prediction of coiled coils from sequence. Bioinformatics 22, 356-358 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 356-358
    • McDonnell, A.V.1    Jiang, T.2    Keating, A.E.3    Berger, B.4
  • 16
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink, J., Ghigo, E., Kalaidzidis, Y. & Zerial, M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 122, 735-749 (2005).
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 18
    • 0030245149 scopus 로고    scopus 로고
    • Radial distribution function of semiflexible polymers
    • Wilhelm, J. & Frey, E. Radial distribution function of semiflexible polymers. Phys. Rev. Lett. 77, 2581-2584 (1996).
    • (1996) Phys. Rev. Lett , vol.77 , pp. 2581-2584
    • Wilhelm, J.1    Frey, E.2
  • 20
    • 0029822793 scopus 로고    scopus 로고
    • GTPase activity of Rab5 acts as a timer for endocytic membrane fusion
    • Rybin, V. et al. GTPase activity of Rab5 acts as a timer for endocytic membrane fusion. Nature 383, 266-269 (1996).
    • (1996) Nature , vol.383 , pp. 266-269
    • Rybin, V.1
  • 21
    • 0026109156 scopus 로고
    • Polymer brushes
    • Milner, S. T. Polymer brushes. Science 251, 905-914 (1991).
    • (1991) Science , vol.251 , pp. 905-914
    • Milner, S.T.1
  • 22
    • 35648983506 scopus 로고    scopus 로고
    • Increased motion and travel, rather than stable docking, characterize the last moments before secretory granule fusion
    • USA
    • Degtyar, V. E., Allersma, M. W., Axelrod, D. & Holz, R. W. Increased motion and travel, rather than stable docking, characterize the last moments before secretory granule fusion. Proc. Natl Acad. Sci. USA 104, 15929-15934 (2007).
    • (2007) Proc. Natl Acad. Sci. , vol.104 , pp. 15929-15934
    • Degtyar, V.E.1    Allersma, M.W.2    Axelrod, D.3    Holz, R.W.4
  • 23
    • 67649470529 scopus 로고    scopus 로고
    • Reconstitution of Rab-and SNARE-dependent membrane fusion by synthetic endosomes
    • Ohya, T. et al. Reconstitution of Rab-and SNARE-dependent membrane fusion by synthetic endosomes. Nature 459, 1091-1097 (2009).
    • (2009) Nature , vol.459 , pp. 1091-1097
    • Ohya, T.1
  • 24
    • 84911428413 scopus 로고    scopus 로고
    • Mammalian CORVET is required for fusion and conversion of distinct early endosome subpopulations
    • Perini, E. D., Schaefer, R., Stöter, M., Kalaidzidis, Y. & Zerial, M. Mammalian CORVET is required for fusion and conversion of distinct early endosome subpopulations. Traffic 15, 1366-1389 (2014).
    • (2014) Traffic , vol.15 , pp. 1366-1389
    • Perini, E.D.1    Schaefer, R.2    Stöter, M.3    Kalaidzidis, Y.4    Zerial, M.5
  • 25
    • 24944540931 scopus 로고    scopus 로고
    • Mesoscale conformational changes in the DNA-repair complex Rad50/Mre11/Nbs1 upon binding DNA
    • Moreno-Herrero, F. et al. Mesoscale conformational changes in the DNA-repair complex Rad50/Mre11/Nbs1 upon binding DNA. Nature 437, 440-443 (2005).
    • (2005) Nature , vol.437 , pp. 440-443
    • Moreno-Herrero, F.1
  • 26
    • 84937460118 scopus 로고    scopus 로고
    • Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly
    • Taylor, K. C. et al. Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly. Proc. Natl Acad. Sci. USA 112, E3806-E3815 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. E3806-E3815
    • Taylor, K.C.1
  • 27
    • 84968796233 scopus 로고    scopus 로고
    • Protein flexibility is required for vesicle tethering at the Golgi
    • Cheung, P. Y., Limouse, C., Mabuchi, H. & Pfeffer, S. R. Protein flexibility is required for vesicle tethering at the Golgi. eLife 4, e12790 (2015).
    • (2015) ELife 4 , pp. e12790
    • Cheung, P.Y.1    Limouse, C.2    Mabuchi, H.3    Pfeffer, S.R.4
  • 28
    • 84925533369 scopus 로고    scopus 로고
    • Structure of human cytoplasmic dynein-2 primed for its power stroke
    • Schmidt, H., Zalyte, R., Urnavicius, L. & Carter, A. P. Structure of human cytoplasmic dynein-2 primed for its power stroke. Nature 518, 435-438 (2015).
    • (2015) Nature , vol.518 , pp. 435-438
    • Schmidt, H.1    Zalyte, R.2    Urnavicius, L.3    Carter, A.P.4
  • 29
    • 62049083505 scopus 로고    scopus 로고
    • Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding
    • Kon, T. et al. Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding. Nature Struct. Mol. Biol. 16, 325-333 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 325-333
    • Kon, T.1
  • 30
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
    • Sheffield, P., Garrard, S. & Derewenda, Z. Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein Expr. Purif. 15, 34-39 (1999).
    • (1999) Protein Expr. Purif. , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 31
    • 4444351852 scopus 로고    scopus 로고
    • Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5
    • Delprato, A., Merithew, E. & Lambright, D. G. Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5. Cell 118, 607-617 (2004).
    • (2004) Cell , vol.118 , pp. 607-617
    • Delprato, A.1    Merithew, E.2    Lambright, D.G.3
  • 32
    • 17344377424 scopus 로고    scopus 로고
    • A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
    • Horiuchi, H. et al. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell 90, 1149-1159 (1997).
    • (1997) Cell , vol.90 , pp. 1149-1159
    • Horiuchi, H.1
  • 33
    • 84857131736 scopus 로고    scopus 로고
    • Structural basis for membrane targeting by the MVB12-associated -prism domain of the human ESCRT-I MVB12 subunit
    • Boura, E. & Hurley, J. H. Structural basis for membrane targeting by the MVB12-associated -prism domain of the human ESCRT-I MVB12 subunit. Proc. Natl Acad. Sci. USA 109, 1901-1906 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 1901-1906
    • Boura, E.1    Hurley, J.H.2
  • 35
    • 84872033669 scopus 로고    scopus 로고
    • Analyzing membrane remodeling and fission using supported bilayers with excess membrane reservoir
    • Neumann, S., Pucadyil, T. J. & Schmid, S. L. Analyzing membrane remodeling and fission using supported bilayers with excess membrane reservoir. Nature Protocols 8, 213-222 (2013).
    • (2013) Nature Protocols , vol.8 , pp. 213-222
    • Neumann, S.1    Pucadyil, T.J.2    Schmid, S.L.3
  • 36
    • 57649238675 scopus 로고    scopus 로고
    • Real-time visualization of dynamin-catalyzed membrane fission and vesicle release
    • Pucadyil, T. J. & Schmid, S. L. Real-time visualization of dynamin-catalyzed membrane fission and vesicle release. Cell 135, 1263-1275 (2008).
    • (2008) Cell , vol.135 , pp. 1263-1275
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 37
    • 84895436450 scopus 로고    scopus 로고
    • Segmentation and quantification of subcellular structures in fluorescence microscopy images using Squassh
    • Rizk, A. et al. Segmentation and quantification of subcellular structures in fluorescence microscopy images using Squassh. Nature Protocols 9, 586-596 (2014).
    • (2014) Nature Protocols , vol.9 , pp. 586-596
    • Rizk, A.1
  • 38
    • 84855457001 scopus 로고    scopus 로고
    • Intrinsic tethering activity of endosomal Rab proteins
    • Lo, S. Y. et al. Intrinsic tethering activity of endosomal Rab proteins. Nature Struct. Mol. Biol. 19, 40-47 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.19 , pp. 40-47
    • Lo, S.Y.1
  • 39
    • 0018852410 scopus 로고
    • Rotary shadowing of extended molecules dried from glycerol
    • Tyler, J. M. & Branton, D. Rotary shadowing of extended molecules dried from glycerol. J. Ultrastruct. Res. 71, 95-102 (1980).
    • (1980) J. Ultrastruct. Res. , vol.71 , pp. 95-102
    • Tyler, J.M.1    Branton, D.2
  • 40
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • Gittes, F., Mickey, B., Nettleton, J. & Howard, J. Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J. Cell Biol. 120, 923-934 (1993).
    • (1993) J. Cell Biol. , vol.120 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 41
    • 84959210452 scopus 로고    scopus 로고
    • Condensin Smc2-Smc4 dimers are flexible and dynamic
    • Eeftens, J. M. et al. Condensin Smc2-Smc4 dimers are flexible and dynamic. Cell Reports 14, 1813-1818 (2016).
    • (2016) Cell Reports , vol.14 , pp. 1813-1818
    • Eeftens, J.M.1
  • 42
    • 84903877478 scopus 로고    scopus 로고
    • Easyworm: An open-source software tool to determine the mechanical properties of worm-like chains
    • Lamour, G., Kirkegaard, J. B., Li, H., Knowles, T. P. & Gsponer, J. Easyworm: an open-source software tool to determine the mechanical properties of worm-like chains. Source Code Biol. Med. 9, 16 (2014).
    • (2014) Source Code Biol. Med. , vol.9 , pp. 16
    • Lamour, G.1    Kirkegaard, J.B.2    Li, H.3    Knowles, T.P.4    Gsponer, J.5
  • 43
    • 0030596081 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA deposited onto mica: Equilibration versus kinetic trapping studied by statistical polymer chain analysis
    • Rivetti, C., Guthold, M. & Bustamante, C. Scanning force microscopy of DNA deposited onto mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis. J. Mol. Biol. 264, 919-932 (1996).
    • (1996) J. Mol. Biol. , vol.264 , pp. 919-932
    • Rivetti, C.1    Guthold, M.2    Bustamante, C.3
  • 44
    • 28844445045 scopus 로고    scopus 로고
    • Scaling exponents and probability distributions of DNA end-to-end distance
    • Valle, F., Favre, M., De Los Rios, P., Rosa, A. & Dietler, G. Scaling exponents and probability distributions of DNA end-to-end distance. Phys. Rev. Lett. 95, 158105 (2005).
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 158105
    • Valle, F.1    Favre, M.2    De Los Rios, P.3    Rosa, A.4    Dietler, G.5
  • 45
    • 84961770691 scopus 로고    scopus 로고
    • Mechanisms of backtrack recovery by RNA polymerases i and II
    • USA
    • Lisica, A. et al. Mechanisms of backtrack recovery by RNA polymerases I and II. Proc. Natl Acad. Sci. USA 113, 2946-2951 (2016).
    • (2016) Proc. Natl Acad. Sci. , vol.113 , pp. 2946-2951
    • Lisica, A.1
  • 47
    • 67749129301 scopus 로고    scopus 로고
    • Quantifying noise in optical tweezers by allan variance
    • Czerwinski, F., Richardson, A. C. & Oddershede, L. B. Quantifying noise in optical tweezers by allan variance. Opt. Express 17, 13255-13269 (2009).
    • (2009) Opt. Express , vol.17 , pp. 13255-13269
    • Czerwinski, F.1    Richardson, A.C.2    Oddershede, L.B.3
  • 48
    • 77957166880 scopus 로고    scopus 로고
    • Power spectrum analysis with least-squares fitting: Amplitude bias and its elimination, with application to optical tweezers and atomic force microscope cantilevers
    • Nørrelykke, S. F. & Flyvbjerg, H. Power spectrum analysis with least-squares fitting: amplitude bias and its elimination, with application to optical tweezers and atomic force microscope cantilevers. Rev. Sci. Instrum. 81, 075103 (2010).
    • (2010) Rev. Sci. Instrum. , vol.81 , pp. 075103
    • Nørrelykke, S.F.1    Flyvbjerg, H.2
  • 49
    • 84871961490 scopus 로고    scopus 로고
    • Optimal detection of changepoints with a linear computational cost
    • Killick, R., Fearnhead, P. & Eckley, I. A. Optimal detection of changepoints with a linear computational cost. J. Am. Stat. Assoc. 107, 1590-1598 (2012).
    • (2012) J. Am. Stat. Assoc. , vol.107 , pp. 1590-1598
    • Killick, R.1    Fearnhead, P.2    Eckley, I.A.3
  • 50
    • 84868565776 scopus 로고    scopus 로고
    • Force spectroscopy with dual-trap optical tweezers: Molecular stiffness measurements and coupled fluctuations analysis
    • Ribezzi-Crivellari, M. & Ritort, F. Force spectroscopy with dual-trap optical tweezers: molecular stiffness measurements and coupled fluctuations analysis. Biophys J. 103, 1919-1928 (2012).
    • (2012) Biophys J. , vol.103 , pp. 1919-1928
    • Ribezzi-Crivellari, M.1    Ritort, F.2
  • 51
    • 11744311356 scopus 로고
    • Statistical mechanics of supercoiled DNA
    • Marko, J. F. & Siggia, E. D. Statistical mechanics of supercoiled DNA. Phys. Rev. E 52, 2912-2938 (1995).
    • (1995) Phys. Rev. e , vol.52 , pp. 2912-2938
    • Marko, J.F.1    Siggia, E.D.2
  • 52
    • 84887010498 scopus 로고    scopus 로고
    • Genome engineering using the CRISPR-Cas9 system
    • Ran, F. A. et al. Genome engineering using the CRISPR-Cas9 system. Nature Protocols 8, 2281-2308 (2013).
    • (2013) Nature Protocols , vol.8 , pp. 2281-2308
    • Ran, F.A.1
  • 53
    • 42949095911 scopus 로고    scopus 로고
    • BAC TransgeneOmics: A high-throughput method for exploration of protein function in mammals
    • Poser, I. et al. BAC TransgeneOmics: a high-throughput method for exploration of protein function in mammals. Nature Methods 5, 409-415 (2008).
    • (2008) Nature Methods , vol.5 , pp. 409-415
    • Poser, I.1
  • 54
    • 84980327273 scopus 로고    scopus 로고
    • APPL endosomes are not obligatory endocytic intermediates but act as stable cargo-sorting compartments
    • Kalaidzidis, I. et al. APPL endosomes are not obligatory endocytic intermediates but act as stable cargo-sorting compartments. J. Cell Biol. 211, 123-144 (2015).
    • (2015) J. Cell Biol. , vol.211 , pp. 123-144
    • Kalaidzidis, I.1
  • 55
    • 34247568898 scopus 로고    scopus 로고
    • The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis
    • Peplowska, K., Markgraf, D. F., Ostrowicz, C. W., Bange, G. & Ungermann, C. The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev. Cell 12, 739-750 (2007).
    • (2007) Dev. Cell , vol.12 , pp. 739-750
    • Peplowska, K.1    Markgraf, D.F.2    Ostrowicz, C.W.3    Bange, G.4    Ungermann, C.5
  • 56
    • 77949424084 scopus 로고    scopus 로고
    • Systems survey of endocytosis by multiparametric image analysis
    • Collinet, C. et al. Systems survey of endocytosis by multiparametric image analysis. Nature 464, 243-249 (2010).
    • (2010) Nature , vol.464 , pp. 243-249
    • Collinet, C.1
  • 57
    • 84880304273 scopus 로고    scopus 로고
    • Image-based analysis of lipid nanoparticle-mediated siRNA delivery, intracellular trafficking and endosomal escape
    • Gilleron, J. et al. Image-based analysis of lipid nanoparticle-mediated siRNA delivery, intracellular trafficking and endosomal escape. Nature Biotechnol. 31, 638-646 (2013).
    • (2013) Nature Biotechnol , vol.31 , pp. 638-646
    • Gilleron, J.1
  • 58
    • 84945283561 scopus 로고    scopus 로고
    • Kidney organoids from human iPS cells contain multiple lineages and model human nephrogenesis
    • Takasato, M. et al. Kidney organoids from human iPS cells contain multiple lineages and model human nephrogenesis. Nature 526, 564-568 (2015).
    • (2015) Nature , vol.526 , pp. 564-568
    • Takasato, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.