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Volumn 171, Issue 2, 2010, Pages 154-162

Towards monitoring transport of single cargos across individual nuclear pore complexes by time-lapse atomic force microscopy

Author keywords

Cellular nanomachine; Immuno gold labeling; Nanobiology; Nuclear pore complex (NPC); Nucleocytoplasmic transport; Nucleoporin; Time lapse AFM

Indexed keywords

ANTIBODY; CALCIUM ION; GOLD; NUCLEOPORIN; POLYLYSINE; SILICON;

EID: 77953692666     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.04.004     Document Type: Article
Times cited : (7)

References (59)
  • 1
    • 0027287349 scopus 로고
    • Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey C.W., Radermacher M. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 1993, 122:1-19.
    • (1993) J. Cell Biol. , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 2
    • 0025267751 scopus 로고
    • Small colloidal gold conjugated to Fab fragments or to immunoglobulin-G as high-resolution labels for electron-microscopy - a technical overview
    • Baschong W., Wrigley N.G. Small colloidal gold conjugated to Fab fragments or to immunoglobulin-G as high-resolution labels for electron-microscopy - a technical overview. J. Electron Microsc. Tech. 1990, 14:313-323.
    • (1990) J. Electron Microsc. Tech. , vol.14 , pp. 313-323
    • Baschong, W.1    Wrigley, N.G.2
  • 4
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • Beck M., Lucic V., Forster F., Baumeister W., Medalia O. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 2007, 449:611-615.
    • (2007) Nature , vol.449 , pp. 611-615
    • Beck, M.1    Lucic, V.2    Forster, F.3    Baumeister, W.4    Medalia, O.5
  • 6
    • 0028046781 scopus 로고
    • Towards atomic interpretation of F-actin filament three-dimensional reconstructions
    • Bremer A., Henn C., Goldie K.N., Engel A., Smith P.R., Aebi U. Towards atomic interpretation of F-actin filament three-dimensional reconstructions. J. Mol. Biol. 1994, 242:683-700.
    • (1994) J. Mol. Biol. , vol.242 , pp. 683-700
    • Bremer, A.1    Henn, C.2    Goldie, K.N.3    Engel, A.4    Smith, P.R.5    Aebi, U.6
  • 7
    • 4444291857 scopus 로고    scopus 로고
    • Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane
    • Czajkowsky D.M., Hotze E.M., Shao Z.F., Tweten R.K. Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane. EMBO J. 2004, 23:3206-3215.
    • (2004) EMBO J. , vol.23 , pp. 3206-3215
    • Czajkowsky, D.M.1    Hotze, E.M.2    Shao, Z.F.3    Tweten, R.K.4
  • 8
    • 33845985288 scopus 로고    scopus 로고
    • Fabrication and functionalization of nanochannels by electron-beam-induced silicon oxide deposition
    • Danelon C., Santschi C., Brugger J., Vogel H. Fabrication and functionalization of nanochannels by electron-beam-induced silicon oxide deposition. Langmuir 2006, 22:10711-10715.
    • (2006) Langmuir , vol.22 , pp. 10711-10715
    • Danelon, C.1    Santschi, C.2    Brugger, J.3    Vogel, H.4
  • 9
    • 53749102019 scopus 로고    scopus 로고
    • Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study
    • Dange T., Grünwald D., Grünwald A., Peters R., Kubitscheck U. Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study. J. Cell Biol. 2008, 183:77-86.
    • (2008) J. Cell Biol. , vol.183 , pp. 77-86
    • Dange, T.1    Grünwald, D.2    Grünwald, A.3    Peters, R.4    Kubitscheck, U.5
  • 10
    • 0033787054 scopus 로고    scopus 로고
    • Micromachined interfaces: new approaches in cell immunoisolation and biomolecular separation
    • Desai T.A., Hansford D.J., Ferrari M. Micromachined interfaces: new approaches in cell immunoisolation and biomolecular separation. Biomol. Eng. 2000, 17:23-36.
    • (2000) Biomol. Eng. , vol.17 , pp. 23-36
    • Desai, T.A.1    Hansford, D.J.2    Ferrari, M.3
  • 11
    • 0033602221 scopus 로고    scopus 로고
    • Atomic force microscopy: a forceful way with single molecules
    • Engel A., Gaub H.E., Muller D.J. Atomic force microscopy: a forceful way with single molecules. Curr. Biol. 1999, 9:R133-R136.
    • (1999) Curr. Biol. , vol.9
    • Engel, A.1    Gaub, H.E.2    Muller, D.J.3
  • 12
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: nucleocytoplasmic transport and beyond
    • Fahrenkrog B., Aebi U. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat. Rev. Mol. Cell Biol. 2003, 4:757-766.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 13
    • 0033924809 scopus 로고    scopus 로고
    • Comparative spatial localization of protein-A-tagged and authentic yeast nuclear pore complex proteins by immunogold electron microscopy
    • Fahrenkrog B., Aris J.P., Hurt E.C., Pante N., Aebi U. Comparative spatial localization of protein-A-tagged and authentic yeast nuclear pore complex proteins by immunogold electron microscopy. J. Struct. Biol. 2000, 129:295-305.
    • (2000) J. Struct. Biol. , vol.129 , pp. 295-305
    • Fahrenkrog, B.1    Aris, J.P.2    Hurt, E.C.3    Pante, N.4    Aebi, U.5
  • 14
    • 0036968863 scopus 로고    scopus 로고
    • Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex
    • Fahrenkrog B., Maco B., Fager A.M., Koser J., Sauder U., Ullman K.S., Aebi U. Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex. J. Struct. Biol. 2002, 140:254-267.
    • (2002) J. Struct. Biol. , vol.140 , pp. 254-267
    • Fahrenkrog, B.1    Maco, B.2    Fager, A.M.3    Koser, J.4    Sauder, U.5    Ullman, K.S.6    Aebi, U.7
  • 15
    • 73249130542 scopus 로고    scopus 로고
    • Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture
    • Frenkiel-Krispin D., Maco B., Aebi U., Medalia O. Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture. J. Mol. Biol. 2010, 395:578-586.
    • (2010) J. Mol. Biol. , vol.395 , pp. 578-586
    • Frenkiel-Krispin, D.1    Maco, B.2    Aebi, U.3    Medalia, O.4
  • 16
    • 0003051583 scopus 로고
    • Controlled nucleation for regulation of particle-size in monodisperse gold suspensions
    • Frens G. Controlled nucleation for regulation of particle-size in monodisperse gold suspensions. Nat. Phys. Sci. 1973, 241:20-22.
    • (1973) Nat. Phys. Sci. , vol.241 , pp. 20-22
    • Frens, G.1
  • 17
    • 0029869424 scopus 로고    scopus 로고
    • The nuclear pore complex and lamina: three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy
    • Goldberg M.W., Allen T.D. The nuclear pore complex and lamina: three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy. J. Mol. Biol. 1996, 257:848-865.
    • (1996) J. Mol. Biol. , vol.257 , pp. 848-865
    • Goldberg, M.W.1    Allen, T.D.2
  • 18
  • 19
    • 0033593012 scopus 로고    scopus 로고
    • Varieties of imaging with scanning probe microscopes
    • Hansma H.G. Varieties of imaging with scanning probe microscopes. Proc. Natl. Acad. Sci. USA 1999, 96:14678-14680.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14678-14680
    • Hansma, H.G.1
  • 20
    • 84960604029 scopus 로고
    • Imaging and nanodissection of individual supercoiled plasmids by atomic force microscopy
    • Henderson E. Imaging and nanodissection of individual supercoiled plasmids by atomic force microscopy. Nucl. Acids Res. 1992, 20:445-447.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 445-447
    • Henderson, E.1
  • 21
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • Hinshaw J.E., Carragher B.O., Milligan R.A. Architecture and design of the nuclear pore complex. Cell 1992, 69:1133-1141.
    • (1992) Cell , vol.69 , pp. 1133-1141
    • Hinshaw, J.E.1    Carragher, B.O.2    Milligan, R.A.3
  • 22
    • 0035135778 scopus 로고    scopus 로고
    • Poly(L-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces: surface-analytical characterization and resistance to serum and fibrinogen adsorption
    • Huang N.P., Michel R., Voros J., Textor M., Hofer R., Rossi A., Elbert D.L., Hubbell J.A., Spencer N.D. Poly(L-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces: surface-analytical characterization and resistance to serum and fibrinogen adsorption. Langmuir 2001, 17:489-498.
    • (2001) Langmuir , vol.17 , pp. 489-498
    • Huang, N.P.1    Michel, R.2    Voros, J.3    Textor, M.4    Hofer, R.5    Rossi, A.6    Elbert, D.L.7    Hubbell, J.A.8    Spencer, N.D.9
  • 25
    • 0344550524 scopus 로고    scopus 로고
    • Quantitative topographical analysis of nuclear pore complex function using scanning force microscopy
    • Jaggi R.D., Franco-Obregon A., Ensslin K. Quantitative topographical analysis of nuclear pore complex function using scanning force microscopy. Biophys. J. 2003, 85:4093-4098.
    • (2003) Biophys. J. , vol.85 , pp. 4093-4098
    • Jaggi, R.D.1    Franco-Obregon, A.2    Ensslin, K.3
  • 26
    • 0026323478 scopus 로고
    • Toward a more complete 3-D structure of the nuclear pore complex
    • Jarnik M., Aebi U. Toward a more complete 3-D structure of the nuclear pore complex. J. Struct. Biol. 1991, 107:291-308.
    • (1991) J. Struct. Biol. , vol.107 , pp. 291-308
    • Jarnik, M.1    Aebi, U.2
  • 28
    • 33749504719 scopus 로고    scopus 로고
    • Single hepatitis-B virus core capsid binding to individual nuclear pore complexes in HeLa cells
    • Lill Y., Lill M.A., Fahrenkrog B., Schwarz-Herion K., Paulillo S., Aebi U., Hecht B. Single hepatitis-B virus core capsid binding to individual nuclear pore complexes in HeLa cells. Biophys. J. 2006, 91:3123-3130.
    • (2006) Biophys. J. , vol.91 , pp. 3123-3130
    • Lill, Y.1    Lill, M.A.2    Fahrenkrog, B.3    Schwarz-Herion, K.4    Paulillo, S.5    Aebi, U.6    Hecht, B.7
  • 29
    • 31344455700 scopus 로고    scopus 로고
    • From the trap to the basket: getting to the bottom of the nuclear pore complex
    • Lim R.Y., Aebi U., Stoffler D. From the trap to the basket: getting to the bottom of the nuclear pore complex. Chromosoma 2006, 115:15-26.
    • (2006) Chromosoma , vol.115 , pp. 15-26
    • Lim, R.Y.1    Aebi, U.2    Stoffler, D.3
  • 32
    • 0031017249 scopus 로고    scopus 로고
    • Visualization of supercoiled DNA with atomic force microscopy in situ
    • Lyubchenko Y.L., Shlyakhtenko L.S. Visualization of supercoiled DNA with atomic force microscopy in situ. Proc. Natl. Acad. Sci. USA 1997, 94:496-501.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 496-501
    • Lyubchenko, Y.L.1    Shlyakhtenko, L.S.2
  • 33
    • 33745512678 scopus 로고    scopus 로고
    • Nuclear pore complex structure and plasticity revealed by electron and atomic force microscopy
    • Maco B., Fahrenkrog B., Huang N.-P., Aebi U. Nuclear pore complex structure and plasticity revealed by electron and atomic force microscopy. Method. Mol. Biol. 2006, 322:273-288.
    • (2006) Method. Mol. Biol. , vol.322 , pp. 273-288
    • Maco, B.1    Fahrenkrog, B.2    Huang, N.-P.3    Aebi, U.4
  • 35
    • 32944468077 scopus 로고    scopus 로고
    • Nuclear side conformational changes in the nuclear pore complex following calcium release from the nuclear membrane
    • Mooren O.L., Erickson E.S., Moore-Nichols D., Dunn R.C. Nuclear side conformational changes in the nuclear pore complex following calcium release from the nuclear membrane. Phys. Biol. 2004, 1:125-134.
    • (2004) Phys. Biol. , vol.1 , pp. 125-134
    • Mooren, O.L.1    Erickson, E.S.2    Moore-Nichols, D.3    Dunn, R.C.4
  • 37
    • 0029797940 scopus 로고    scopus 로고
    • Sequential binding of import ligands to distinct nucleopore regions during their nuclear import
    • Pante N., Aebi U. Sequential binding of import ligands to distinct nucleopore regions during their nuclear import. Science 1996, 273:1729-1732.
    • (1996) Science , vol.273 , pp. 1729-1732
    • Pante, N.1    Aebi, U.2
  • 38
    • 0027931054 scopus 로고
    • Interactions and three-dimensional localization of a group of nuclear pore complex proteins
    • Pante N., Bastos R., McMorrow I., Burke B., Aebi U. Interactions and three-dimensional localization of a group of nuclear pore complex proteins. J. Cell Biol. 1994, 126:603-617.
    • (1994) J. Cell Biol. , vol.126 , pp. 603-617
    • Pante, N.1    Bastos, R.2    McMorrow, I.3    Burke, B.4    Aebi, U.5
  • 39
    • 28844458899 scopus 로고
    • Isoelectric points of solid oxides solid hydroxides and aqueous hydroxo complex systems
    • Parks G.A. Isoelectric points of solid oxides solid hydroxides and aqueous hydroxo complex systems. Chem. Rev. 1965, 65:177.
    • (1965) Chem. Rev. , vol.65 , pp. 177
    • Parks, G.A.1
  • 40
    • 25844440748 scopus 로고    scopus 로고
    • Effects of ionic strength and surface charge on protein adsorption at PEGylated surfaces
    • Pasche S., Voros J., Griesser H.J., Spencer N.D., Textor M. Effects of ionic strength and surface charge on protein adsorption at PEGylated surfaces. J Phys. Chem. B 2005, 109:17545-17552.
    • (2005) J Phys. Chem. B , vol.109 , pp. 17545-17552
    • Pasche, S.1    Voros, J.2    Griesser, H.J.3    Spencer, N.D.4    Textor, M.5
  • 41
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt R., Holzenburg A., Buhle E.L., Jarnik M., Engel A., Aebi U. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 1990, 110:883-894.
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle, E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 42
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M., Gautel M., Oesterhelt F., Fernandez J.M., Gaub H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 1997, 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 43
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: composition, architecture, and transport mechanism
    • Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., et al. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 2000, 148:635-651.
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5
  • 45
    • 0018650401 scopus 로고
    • Digital image-processing - SEMPER system
    • Saxton W.O., Pitt T.J., Horner M. Digital image-processing - SEMPER system. Ultramicroscopy 1979, 4:343-353.
    • (1979) Ultramicroscopy , vol.4 , pp. 343-353
    • Saxton, W.O.1    Pitt, T.J.2    Horner, M.3
  • 46
    • 0028986125 scopus 로고
    • Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • Schabert F.A., Henn C., Engel A. Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science 1995, 268:92-94.
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 47
    • 33646598418 scopus 로고    scopus 로고
    • Plugs in nuclear pores: transcripts in early oocyte development identified with nanotechniques
    • Schlune A., Shahin V., Enss K., Schillers H., Oberleithner H. Plugs in nuclear pores: transcripts in early oocyte development identified with nanotechniques. J. Cell Biochem. 2006, 98:567-576.
    • (2006) J. Cell Biochem. , vol.98 , pp. 567-576
    • Schlune, A.1    Shahin, V.2    Enss, K.3    Schillers, H.4    Oberleithner, H.5
  • 48
    • 0035976603 scopus 로고    scopus 로고
    • Real-time single-molecule imaging of the infection pathway of an adeno-associated virus
    • Seisenberger G., Ried M.U., Endress T., Buning H., Hallek M., Brauchle C. Real-time single-molecule imaging of the infection pathway of an adeno-associated virus. Science 2001, 294:1929-1932.
    • (2001) Science , vol.294 , pp. 1929-1932
    • Seisenberger, G.1    Ried, M.U.2    Endress, T.3    Buning, H.4    Hallek, M.5    Brauchle, C.6
  • 49
    • 0033151769 scopus 로고    scopus 로고
    • The nuclear pore complex: from molecular architecture to functional dynamics
    • Stoffler D., Fahrenkrog B., Aebi U. The nuclear pore complex: from molecular architecture to functional dynamics. Curr. Opin. Cell Biol. 1999, 11:391-401.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 391-401
    • Stoffler, D.1    Fahrenkrog, B.2    Aebi, U.3
  • 50
    • 0343415750 scopus 로고    scopus 로고
    • Imaging biological matter across dimensions: from cells to molecules and atoms
    • Stoffler D., Steinmetz M.O., Aebi U. Imaging biological matter across dimensions: from cells to molecules and atoms. FASEB J. 1999, 13(Suppl. 2):S195-S200.
    • (1999) FASEB J. , vol.13 , Issue.SUPPL. 2
    • Stoffler, D.1    Steinmetz, M.O.2    Aebi, U.3
  • 51
    • 0033537992 scopus 로고    scopus 로고
    • Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy
    • Stoffler D., Goldie K.N., Feja B., Aebi U. Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy. J. Mol. Biol. 1999, 287:741-752.
    • (1999) J. Mol. Biol. , vol.287 , pp. 741-752
    • Stoffler, D.1    Goldie, K.N.2    Feja, B.3    Aebi, U.4
  • 52
    • 0037453221 scopus 로고    scopus 로고
    • Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport
    • Stoffler D., Feja B., Fahrenkrog B., Walz J., Typke D., Aebi U. Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J. Mol. Biol. 2003, 328:119-130.
    • (2003) J. Mol. Biol. , vol.328 , pp. 119-130
    • Stoffler, D.1    Feja, B.2    Fahrenkrog, B.3    Walz, J.4    Typke, D.5    Aebi, U.6
  • 53
    • 33947281541 scopus 로고    scopus 로고
    • Developing scanning probe-based nanodevices-stepping out of the laboratory into the clinic
    • Stolz M., Aebi U., Stoffler D. Developing scanning probe-based nanodevices-stepping out of the laboratory into the clinic. Nanomedicine 2007, 3:53-62.
    • (2007) Nanomedicine , vol.3 , pp. 53-62
    • Stolz, M.1    Aebi, U.2    Stoffler, D.3
  • 54
    • 0033767765 scopus 로고    scopus 로고
    • Monitoring biomolecular interactions by time-lapse atomic force microscopy
    • Stolz M., Stoffler D., Aebi U., Goldsbury C. Monitoring biomolecular interactions by time-lapse atomic force microscopy. J. Struct. Biol. 2000, 131:171-180.
    • (2000) J. Struct. Biol. , vol.131 , pp. 171-180
    • Stolz, M.1    Stoffler, D.2    Aebi, U.3    Goldsbury, C.4
  • 55
    • 2142765353 scopus 로고    scopus 로고
    • Dynamic elastic modulus of porcine articular cartilage determined at two different levels of tissue organization by indentation-type atomic force microscopy
    • Stolz M., Raiteri R., Daniels A.U., VanLandingham M.R., Baschong W., Aebi U. Dynamic elastic modulus of porcine articular cartilage determined at two different levels of tissue organization by indentation-type atomic force microscopy. Biophys. J. 2004, 86:3269-3283.
    • (2004) Biophys. J. , vol.86 , pp. 3269-3283
    • Stolz, M.1    Raiteri, R.2    Daniels, A.U.3    VanLandingham, M.R.4    Baschong, W.5    Aebi, U.6
  • 56
    • 0031193343 scopus 로고    scopus 로고
    • The atomic force microscope as a new microdissecting tool for the generation of genetic probes
    • Thalhammer S., Stark R.W., Muller S., Wienberg J., Heckl W.M. The atomic force microscope as a new microdissecting tool for the generation of genetic probes. J. Struct. Biol. 1997, 119:232-237.
    • (1997) J. Struct. Biol. , vol.119 , pp. 232-237
    • Thalhammer, S.1    Stark, R.W.2    Muller, S.3    Wienberg, J.4    Heckl, W.M.5
  • 58
    • 0033014673 scopus 로고    scopus 로고
    • Conformational changes of the in situ nuclear pore complex
    • Wang H., Clapham D.E. Conformational changes of the in situ nuclear pore complex. Biophys. J. 1999, 77:241-247.
    • (1999) Biophys. J. , vol.77 , pp. 241-247
    • Wang, H.1    Clapham, D.E.2
  • 59
    • 0031604505 scopus 로고    scopus 로고
    • Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications
    • Yang Q., Rout M.P., Akey C.W. Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol. Cell 1998, 1:223-234.
    • (1998) Mol. Cell , vol.1 , pp. 223-234
    • Yang, Q.1    Rout, M.P.2    Akey, C.W.3


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