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Volumn 30, Issue 9, 2006, Pages 747-754

Studying cellular architecture in three dimensions with improved resolution: Ta replicas revisited

Author keywords

3D analysis; Cell architecture; Freeze etching; Freeze fracture; Ta replicas

Indexed keywords

PLATINUM; TANTALUM;

EID: 33748424575     PISSN: 10656995     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cellbi.2006.05.006     Document Type: Article
Times cited : (4)

References (65)
  • 2
    • 0344983351 scopus 로고    scopus 로고
    • Volumetric feature extraction and visualization of tomographic molecular imaging
    • Bajaj C., Yu Z., and Auer M. Volumetric feature extraction and visualization of tomographic molecular imaging. J Struct Biol 144 (2003) 132-143
    • (2003) J Struct Biol , vol.144 , pp. 132-143
    • Bajaj, C.1    Yu, Z.2    Auer, M.3
  • 3
    • 11144247761 scopus 로고    scopus 로고
    • A voyage to the inner space of cells
    • Baumeister W. A voyage to the inner space of cells. Prot Sci 14 (2005) 257-269
    • (2005) Prot Sci , vol.14 , pp. 257-269
    • Baumeister, W.1
  • 4
    • 8844226004 scopus 로고    scopus 로고
    • Nuclear pore complex structure and dynamics revealed by cryoelectron tomography
    • Beck M., Förster F., Ecke M., Plitzko J.M., Melchior F., Gerish G., et al. Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science 306 (2004) 1387-1390
    • (2004) Science , vol.306 , pp. 1387-1390
    • Beck, M.1    Förster, F.2    Ecke, M.3    Plitzko, J.M.4    Melchior, F.5    Gerish, G.6
  • 5
    • 0033799507 scopus 로고    scopus 로고
    • A review of the potential and versatility of colloidal gold cytochemical labeling for molecular morphology
    • Bendayan M. A review of the potential and versatility of colloidal gold cytochemical labeling for molecular morphology. Biotech Histochem 75 (2000) 203-242
    • (2000) Biotech Histochem , vol.75 , pp. 203-242
    • Bendayan, M.1
  • 6
    • 0022487317 scopus 로고
    • Structure and composition of the cytoskeleton of nucleated erythrocytes: III. Organization of the cytoskeleton of Bufo marinus erythrocytes as revealed by freeze-dried platinum-carbon replicas and immunofluorescence microscopy
    • Cetonze V.E., Ruben G.C., and Sloboda R.D. Structure and composition of the cytoskeleton of nucleated erythrocytes: III. Organization of the cytoskeleton of Bufo marinus erythrocytes as revealed by freeze-dried platinum-carbon replicas and immunofluorescence microscopy. Cell Motil Cytoskeleton 6 (1986) 376-388
    • (1986) Cell Motil Cytoskeleton , vol.6 , pp. 376-388
    • Cetonze, V.E.1    Ruben, G.C.2    Sloboda, R.D.3
  • 7
    • 0024791737 scopus 로고
    • Preparation of thin, fine-grained, tantalum metal replicas for freeze-fracture electron microscopy
    • Costello M.J., and Escaig J. Preparation of thin, fine-grained, tantalum metal replicas for freeze-fracture electron microscopy. Scanning Microsc Suppl 3 (1989) 189-199
    • (1989) Scanning Microsc Suppl , vol.3 , pp. 189-199
    • Costello, M.J.1    Escaig, J.2
  • 10
    • 0027980117 scopus 로고
    • Structure of intracellular mature vaccinia virus observed by cryoelectron microscopy
    • Dubochet J., Adrian M., Richter K., Garces J., and Wittek R. Structure of intracellular mature vaccinia virus observed by cryoelectron microscopy. J Virol 68 (1994) 1935-1941
    • (1994) J Virol , vol.68 , pp. 1935-1941
    • Dubochet, J.1    Adrian, M.2    Richter, K.3    Garces, J.4    Wittek, R.5
  • 11
    • 0024549988 scopus 로고
    • The Sendai virus nucleocapsid exists in at least four different helical states
    • Egelman E.H., Wu S.-S., Amrein M., Portner A., and Murti G. The Sendai virus nucleocapsid exists in at least four different helical states. J Virol 63 (1989) 2233-2243
    • (1989) J Virol , vol.63 , pp. 2233-2243
    • Egelman, E.H.1    Wu, S.-S.2    Amrein, M.3    Portner, A.4    Murti, G.5
  • 12
    • 0021337036 scopus 로고
    • Defective vaccinia virus particles in interferon-treated infected cells
    • Esteban M. Defective vaccinia virus particles in interferon-treated infected cells. Virology 133 (1984) 220-227
    • (1984) Virology , vol.133 , pp. 220-227
    • Esteban, M.1
  • 13
    • 0345414562 scopus 로고    scopus 로고
    • An improved algorithm for anisotropic nonlinear diffusion for denoising cryo-tomograms
    • Fernández J.J., and Li S. An improved algorithm for anisotropic nonlinear diffusion for denoising cryo-tomograms. J Struct Biol 144 (2003) 152-161
    • (2003) J Struct Biol , vol.144 , pp. 152-161
    • Fernández, J.J.1    Li, S.2
  • 14
    • 0023714240 scopus 로고
    • Macromolecular dynamics of the cell surface during the formation of coated pits is revealed by fracture-flip
    • Fujimoto K., and Pinto da Silva P. Macromolecular dynamics of the cell surface during the formation of coated pits is revealed by fracture-flip. J Cell Sci 91 (1988) 161-173
    • (1988) J Cell Sci , vol.91 , pp. 161-173
    • Fujimoto, K.1    Pinto da Silva, P.2
  • 15
    • 0027104231 scopus 로고
    • High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores
    • Goldberg M.W., and Allen T.D. High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores. J Cell Biol 119 (1992) 1429-1440
    • (1992) J Cell Biol , vol.119 , pp. 1429-1440
    • Goldberg, M.W.1    Allen, T.D.2
  • 16
    • 0027525230 scopus 로고
    • The nuclear pore complex: three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis
    • Goldberg M.W., and Allen T.D. The nuclear pore complex: three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis. J Cell Sci 106 (1993) 261-274
    • (1993) J Cell Sci , vol.106 , pp. 261-274
    • Goldberg, M.W.1    Allen, T.D.2
  • 17
    • 0034755323 scopus 로고    scopus 로고
    • Structure and assembly of intracellular mature vaccinia virus: isolated particle analysis
    • Griffiths G., Wepf R., Wendt T., Locker J.K., Cyrklaff M., and Ross N. Structure and assembly of intracellular mature vaccinia virus: isolated particle analysis. J Virol 75 (2001) 1034-1055
    • (2001) J Virol , vol.75 , pp. 1034-1055
    • Griffiths, G.1    Wepf, R.2    Wendt, T.3    Locker, J.K.4    Cyrklaff, M.5    Ross, N.6
  • 18
    • 0021693806 scopus 로고
    • High resolution metal replication, quantified by image processing of periodic test specimens
    • Gross H., Müller T., Wildhaber I., and Winkler H. High resolution metal replication, quantified by image processing of periodic test specimens. Ultramicroscopy 16 (1985) 287-304
    • (1985) Ultramicroscopy , vol.16 , pp. 287-304
    • Gross, H.1    Müller, T.2    Wildhaber, I.3    Winkler, H.4
  • 19
    • 0345306753 scopus 로고    scopus 로고
    • Three-dimensional structure of Herpes Simplex Virus from cryo-electron tomography
    • Grünewald K., Desai P., Winkler D.C., Heymann J.B., Belnap D., Baumeister W., et al. Three-dimensional structure of Herpes Simplex Virus from cryo-electron tomography. Science 302 (2003) 1396-1398
    • (2003) Science , vol.302 , pp. 1396-1398
    • Grünewald, K.1    Desai, P.2    Winkler, D.C.3    Heymann, J.B.4    Belnap, D.5    Baumeister, W.6
  • 20
    • 0036013787 scopus 로고    scopus 로고
    • Routine preparation of air-dried negatively stained and unstained specimens on holey carbon support films: a review of applications
    • Harris J.R., and Scheffler D. Routine preparation of air-dried negatively stained and unstained specimens on holey carbon support films: a review of applications. Micron 33 (2002) 461-480
    • (2002) Micron , vol.33 , pp. 461-480
    • Harris, J.R.1    Scheffler, D.2
  • 21
    • 0141865704 scopus 로고    scopus 로고
    • Untangling desmosomal knots with electron tomography
    • He W., Cowen P., and Stokes D.L. Untangling desmosomal knots with electron tomography. Science 302 (2003) 109-113
    • (2003) Science , vol.302 , pp. 109-113
    • He, W.1    Cowen, P.2    Stokes, D.L.3
  • 24
    • 12344274281 scopus 로고    scopus 로고
    • Cryo-electron tomography reveals the cytoskeletal structure of Spiroplasma melliferum
    • Kürner J., Frangakis A.S., and Baumeister W. Cryo-electron tomography reveals the cytoskeletal structure of Spiroplasma melliferum. Science 307 (2005) 436-438
    • (2005) Science , vol.307 , pp. 436-438
    • Kürner, J.1    Frangakis, A.S.2    Baumeister, W.3
  • 25
    • 29844451883 scopus 로고    scopus 로고
    • Cryo-electron tomography and fluorescence microscopy of unicellular algae in vitreous cryosections
    • Leis A., Andrees L., Gruska M., Al-Amoudi A., Sartori A., Dubochet J., et al. Cryo-electron tomography and fluorescence microscopy of unicellular algae in vitreous cryosections. Microsc Microanal 11 Suppl. 2 (2005) 330CD
    • (2005) Microsc Microanal , vol.11 , Issue.SUPPL. 2
    • Leis, A.1    Andrees, L.2    Gruska, M.3    Al-Amoudi, A.4    Sartori, A.5    Dubochet, J.6
  • 26
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lučić V., Förster F., and Baumeister W. Structural studies by electron tomography: from cells to molecules. Annu Rev Biochem 74 (2005) 833-865
    • (2005) Annu Rev Biochem , vol.74 , pp. 833-865
    • Lučić, V.1    Förster, F.2    Baumeister, W.3
  • 27
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationship in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh M.J., Mastronarde D.N., Buttle K.F., Howell K.E., and McIntosh J.R. Organellar relationship in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc Natl Acad Sci U S A 98 (2000) 2399-2406
    • (2000) Proc Natl Acad Sci U S A , vol.98 , pp. 2399-2406
    • Marsh, M.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5
  • 28
    • 0009222122 scopus 로고    scopus 로고
    • Amplification methods for the immunolocalization of rare molecules in cells and tissues
    • Mayer G., and Bendayan M. Amplification methods for the immunolocalization of rare molecules in cells and tissues. Prog Histochem Cytochem 36 (2001) 3-85
    • (2001) Prog Histochem Cytochem , vol.36 , pp. 3-85
    • Mayer, G.1    Bendayan, M.2
  • 29
    • 11844305068 scopus 로고    scopus 로고
    • New views of cells in 3D: an introduction to electron tomography
    • McIntosh R., Nicastro D., and Mastronarde D. New views of cells in 3D: an introduction to electron tomography. Trends Cell Biol 15 (2005) 43-51
    • (2005) Trends Cell Biol , vol.15 , pp. 43-51
    • McIntosh, R.1    Nicastro, D.2    Mastronarde, D.3
  • 31
    • 0142025252 scopus 로고    scopus 로고
    • Cryoimmobilization and three-dimensional visualization of C. elegans ultrastructure
    • Muller-Reichert T., Hohenberg H., O'Toole E.T., and McDonald K. Cryoimmobilization and three-dimensional visualization of C. elegans ultrastructure. J Microsc 212 (2003) 71-80
    • (2003) J Microsc , vol.212 , pp. 71-80
    • Muller-Reichert, T.1    Hohenberg, H.2    O'Toole, E.T.3    McDonald, K.4
  • 33
    • 23844480674 scopus 로고    scopus 로고
    • Key Golgi factors for structural and functional maturation of Bunyamwera virus
    • Novoa R.R., Calderita G., Cabezas P., Elliott R.M., and Risco C. Key Golgi factors for structural and functional maturation of Bunyamwera virus. J Virol 79 (2005) 10852-10863
    • (2005) J Virol , vol.79 , pp. 10852-10863
    • Novoa, R.R.1    Calderita, G.2    Cabezas, P.3    Elliott, R.M.4    Risco, C.5
  • 34
    • 14544300928 scopus 로고    scopus 로고
    • Virus factories: associations of cell organelles for viral replication and morphogenesis
    • Novoa R.R., Calderita G., Arranz R., Fontana J., Granzow H., and Risco C. Virus factories: associations of cell organelles for viral replication and morphogenesis. Biol Cell 97 (2005) 147-172
    • (2005) Biol Cell , vol.97 , pp. 147-172
    • Novoa, R.R.1    Calderita, G.2    Arranz, R.3    Fontana, J.4    Granzow, H.5    Risco, C.6
  • 35
    • 0025306106 scopus 로고
    • High-resolution surface views of human lymphocytes during camping of CD4 and HLA antigens as revealed by immunogold fracture-flip
    • Pavan A., Mancini P., Lucania G., Frati L., Torrisi M.R., and Pinto da Silva P. High-resolution surface views of human lymphocytes during camping of CD4 and HLA antigens as revealed by immunogold fracture-flip. J Cell Sci 96 (1990) 151-157
    • (1990) J Cell Sci , vol.96 , pp. 151-157
    • Pavan, A.1    Mancini, P.2    Lucania, G.3    Frati, L.4    Torrisi, M.R.5    Pinto da Silva, P.6
  • 36
    • 0018608313 scopus 로고
    • Scanning electron microscopy at macromolecular resolution in low energy mode on biological specimens coated with ultra thin metal films
    • Peters K.R. Scanning electron microscopy at macromolecular resolution in low energy mode on biological specimens coated with ultra thin metal films. Scanning Electron Microsc 2 (1979) 133-148
    • (1979) Scanning Electron Microsc , vol.2 , pp. 133-148
    • Peters, K.R.1
  • 37
    • 0022270453 scopus 로고
    • Working at higher magnifications in scanning electron microscopy with secondary and backscattered electrons on metal coated biological specimens and imaging macromolecular cell membrane structures
    • Peters K.R. Working at higher magnifications in scanning electron microscopy with secondary and backscattered electrons on metal coated biological specimens and imaging macromolecular cell membrane structures. Scanning Electron Microsc 4 (1985) 1519-1544
    • (1985) Scanning Electron Microsc , vol.4 , pp. 1519-1544
    • Peters, K.R.1
  • 38
    • 0022531252 scopus 로고
    • Rationale for the application of thin, continuous metal films in high magnification electron microscopy
    • Peters K.R. Rationale for the application of thin, continuous metal films in high magnification electron microscopy. J Microsc 142 (1986) 25-34
    • (1986) J Microsc , vol.142 , pp. 25-34
    • Peters, K.R.1
  • 39
    • 0010434348 scopus 로고
    • Topology, dynamics, and molecular cytochemistry of integral membrane proteins: a freeze-fracture view
    • Harris J.R., and Horne R.W. (Eds), Academic Press
    • Pinto da Silva P. Topology, dynamics, and molecular cytochemistry of integral membrane proteins: a freeze-fracture view. In: Harris J.R., and Horne R.W. (Eds). Electron microscopy of proteins (1987), Academic Press 2-38
    • (1987) Electron microscopy of proteins , pp. 2-38
    • Pinto da Silva, P.1
  • 40
    • 0014804933 scopus 로고
    • Membrane splitting in freeze-etching. Covalently labelled ferritin as a membrane marker
    • Pinto da Silva P., and Branton D. Membrane splitting in freeze-etching. Covalently labelled ferritin as a membrane marker. J Cell Biol 45 (1970) 598-605
    • (1970) J Cell Biol , vol.45 , pp. 598-605
    • Pinto da Silva, P.1    Branton, D.2
  • 41
    • 0019824681 scopus 로고
    • Freeze-fracture cytochemistry: localization of wheat-germ agglutinin and concanavalin A binding sites on freeze-fractured pancreatic cells
    • Pinto da Silva P., Torrisi M.R., and Kachar B. Freeze-fracture cytochemistry: localization of wheat-germ agglutinin and concanavalin A binding sites on freeze-fractured pancreatic cells. J Cell Biol 91 (1981) 361-372
    • (1981) J Cell Biol , vol.91 , pp. 361-372
    • Pinto da Silva, P.1    Torrisi, M.R.2    Kachar, B.3
  • 43
    • 0027408009 scopus 로고
    • Binding of bacterial endotoxins to the macrophage surface: visualization by fracture-flip and immunocytochemistry
    • Risco C., and Pinto da Silva P. Binding of bacterial endotoxins to the macrophage surface: visualization by fracture-flip and immunocytochemistry. J Histochem Cytochem 41 (1993) 601-608
    • (1993) J Histochem Cytochem , vol.41 , pp. 601-608
    • Risco, C.1    Pinto da Silva, P.2
  • 44
    • 0029038230 scopus 로고
    • Cellular functions during activation and damage by pathogens: immunogold studies of the interaction of bacterial endotoxins with target cells
    • Risco C., and Pinto da Silva P. Cellular functions during activation and damage by pathogens: immunogold studies of the interaction of bacterial endotoxins with target cells. Microsc Res Tech 31 (1995) 141-158
    • (1995) Microsc Res Tech , vol.31 , pp. 141-158
    • Risco, C.1    Pinto da Silva, P.2
  • 45
    • 7144261712 scopus 로고    scopus 로고
    • The fracture-flip technique reveals new structural features of the Escherichia coli cell wall
    • Risco C., and Pinto da Silva P. The fracture-flip technique reveals new structural features of the Escherichia coli cell wall. J Microsc 189 (1998) 213-218
    • (1998) J Microsc , vol.189 , pp. 213-218
    • Risco, C.1    Pinto da Silva, P.2
  • 46
    • 0028353574 scopus 로고
    • Type II pneumocytes revisited: intracellular membranous systems, surface characteristics, and lamellar body secretion
    • Risco C., Romero C., Bosch M.A., and Pinto da Silva P. Type II pneumocytes revisited: intracellular membranous systems, surface characteristics, and lamellar body secretion. Lab Invest 70 (1994) 407-417
    • (1994) Lab Invest , vol.70 , pp. 407-417
    • Risco, C.1    Romero, C.2    Bosch, M.A.3    Pinto da Silva, P.4
  • 47
    • 0036149942 scopus 로고    scopus 로고
    • Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly
    • Risco C., Rodríguez J.R., López-Iglesias C., Carrascosa J.L., Esteban M., and Rodríguez D. Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly. J Virol 76 (2002) 1839-1855
    • (2002) J Virol , vol.76 , pp. 1839-1855
    • Risco, C.1    Rodríguez, J.R.2    López-Iglesias, C.3    Carrascosa, J.L.4    Esteban, M.5    Rodríguez, D.6
  • 48
    • 22544445888 scopus 로고    scopus 로고
    • Lipid droplets gain PAT family proteins by interactions with specialized plasma membrane domains
    • Robenek H., Robenek M.J., Buers I., Lorkowski S., Hofnagel O., Troyer D., et al. Lipid droplets gain PAT family proteins by interactions with specialized plasma membrane domains. J Biol Chem 280 (2005) 26330-26338
    • (2005) J Biol Chem , vol.280 , pp. 26330-26338
    • Robenek, H.1    Robenek, M.J.2    Buers, I.3    Lorkowski, S.4    Hofnagel, O.5    Troyer, D.6
  • 49
    • 0030847417 scopus 로고    scopus 로고
    • Enhanced maintenance and retroviral transduction of primitive hematopoietic progenitor cells using a novel three-dimensional system
    • Rosenzweig M., Pykett M., Marks D.F., and Johnson R.P. Enhanced maintenance and retroviral transduction of primitive hematopoietic progenitor cells using a novel three-dimensional system. Gene Ther 4 (1997) 928-936
    • (1997) Gene Ther , vol.4 , pp. 928-936
    • Rosenzweig, M.1    Pykett, M.2    Marks, D.F.3    Johnson, R.P.4
  • 50
    • 0024313954 scopus 로고
    • Ultrathin (1 nm) vertically shadowed platinum-carbon replicas for imaging individual molecules in freeze-etched biological DNA and material science metal and plastic specimens
    • Ruben G.C. Ultrathin (1 nm) vertically shadowed platinum-carbon replicas for imaging individual molecules in freeze-etched biological DNA and material science metal and plastic specimens. J Electron Microsc Tech 13 (1989) 335-354
    • (1989) J Electron Microsc Tech , vol.13 , pp. 335-354
    • Ruben, G.C.1
  • 51
    • 0028358351 scopus 로고
    • High resolution platinum-carbon replication of freeze-dried basement membrane
    • Ruben G.C., and Yurchenco P.D. High resolution platinum-carbon replication of freeze-dried basement membrane. Microsc Res Tech 28 (1994) 13-28
    • (1994) Microsc Res Tech , vol.28 , pp. 13-28
    • Ruben, G.C.1    Yurchenco, P.D.2
  • 52
  • 53
    • 23944469458 scopus 로고    scopus 로고
    • Coexistence of multivalent and monovalent TCRs explains high sensitivity and wide range of response
    • Schamel W.W.A., Arechaga I., Risueño R.M., van Santen H.M., Cabezas P., Risco C., et al. Coexistence of multivalent and monovalent TCRs explains high sensitivity and wide range of response. J Exp Med 202 (2005) 493-503
    • (2005) J Exp Med , vol.202 , pp. 493-503
    • Schamel, W.W.A.1    Arechaga, I.2    Risueño, R.M.3    van Santen, H.M.4    Cabezas, P.5    Risco, C.6
  • 54
    • 0025970532 scopus 로고
    • Structure of the mitochondrial creatine kinase octamer: high-resolution shadowing and image averaging of single molecules and formation of linear filaments under specific staining conditions
    • Schnyder T., Gross H., Winkler H., Eppenberger H.M., and Wallimann T. Structure of the mitochondrial creatine kinase octamer: high-resolution shadowing and image averaging of single molecules and formation of linear filaments under specific staining conditions. J Cell Biol 112 (1991) 95-101
    • (1991) J Cell Biol , vol.112 , pp. 95-101
    • Schnyder, T.1    Gross, H.2    Winkler, H.3    Eppenberger, H.M.4    Wallimann, T.5
  • 55
    • 0026098503 scopus 로고
    • Freeze-fracture cytochemistry: a simplified guide and update on developments
    • Severs N.J. Freeze-fracture cytochemistry: a simplified guide and update on developments. J Microsc 161 (1991) 109-134
    • (1991) J Microsc , vol.161 , pp. 109-134
    • Severs, N.J.1
  • 56
    • 0016992413 scopus 로고
    • High-resolution metal replication of macromolecules
    • Slayter H.S. High-resolution metal replication of macromolecules. Ultramicroscopy 1 (1976) 341-357
    • (1976) Ultramicroscopy , vol.1 , pp. 341-357
    • Slayter, H.S.1
  • 57
    • 0028048497 scopus 로고
    • Serial section electron tomography: a method for three-dimensional reconstruction of large structures
    • Soto G.E., Young S.J., Martone M.E., Deerinck T.J., Lamont S., Carragher B.O., et al. Serial section electron tomography: a method for three-dimensional reconstruction of large structures. Neuroimage 1 (1994) 230-243
    • (1994) Neuroimage , vol.1 , pp. 230-243
    • Soto, G.E.1    Young, S.J.2    Martone, M.E.3    Deerinck, T.J.4    Lamont, S.5    Carragher, B.O.6
  • 58
    • 0037333340 scopus 로고    scopus 로고
    • The next ice age: cryo-electron tomography of intact cells
    • Steven A.C., and Aebi U. The next ice age: cryo-electron tomography of intact cells. Trends Cell Biol 13 (2003) 107-110
    • (2003) Trends Cell Biol , vol.13 , pp. 107-110
    • Steven, A.C.1    Aebi, U.2
  • 59
    • 0019362246 scopus 로고
    • Single bacteriorhodopsin molecules revealed on both surfaces of freeze-dried and heavy metal-decorated purple membranes
    • Studer D., Moor H., and Gross H. Single bacteriorhodopsin molecules revealed on both surfaces of freeze-dried and heavy metal-decorated purple membranes. J Cell Biol 90 (1981) 153-159
    • (1981) J Cell Biol , vol.90 , pp. 153-159
    • Studer, D.1    Moor, H.2    Gross, H.3
  • 60
    • 0035462162 scopus 로고    scopus 로고
    • A new approach for cryofixation by high-pressure freezing
    • Studer D., Graber W., Al-Amoudi A., and Eggli P. A new approach for cryofixation by high-pressure freezing. J Microsc 203 (2001) 285-294
    • (2001) J Microsc , vol.203 , pp. 285-294
    • Studer, D.1    Graber, W.2    Al-Amoudi, A.3    Eggli, P.4
  • 61
    • 3042548142 scopus 로고    scopus 로고
    • Three-dimensional electron microscopy at molecular resolution
    • Subramaniam S., and Milne J.L.S. Three-dimensional electron microscopy at molecular resolution. Annu Rev Biophys Biomol Struct 33 (2004) 141-155
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 141-155
    • Subramaniam, S.1    Milne, J.L.S.2
  • 62
    • 0018279121 scopus 로고
    • Freeze-fracture morphology of biological membranes
    • Verkleij A.J., and Ververgaert P.H. Freeze-fracture morphology of biological membranes. Biochim Biophys Acta 515 (1978) 303-327
    • (1978) Biochim Biophys Acta , vol.515 , pp. 303-327
    • Verkleij, A.J.1    Ververgaert, P.H.2
  • 63
    • 0034105981 scopus 로고    scopus 로고
    • Expression of GM3 microdomains on the surfaces of murine fibroblasts correlates with inhibition of cell proliferation
    • Visco V., Lucania G., Sansolini T., Dolo V., Garofalo T., Sorice M., et al. Expression of GM3 microdomains on the surfaces of murine fibroblasts correlates with inhibition of cell proliferation. Histochem Cell Biol 113 (2000) 43-50
    • (2000) Histochem Cell Biol , vol.113 , pp. 43-50
    • Visco, V.1    Lucania, G.2    Sansolini, T.3    Dolo, V.4    Garofalo, T.5    Sorice, M.6
  • 64
    • 0142120565 scopus 로고    scopus 로고
    • Recent progress in freeze-fracturing of high-pressure frozen samples
    • Walther P. Recent progress in freeze-fracturing of high-pressure frozen samples. J Microsc 212 (2003) 34-43
    • (2003) J Microsc , vol.212 , pp. 34-43
    • Walther, P.1
  • 65
    • 0025734160 scopus 로고
    • Platinum/iridium/carbon: a high resolution shadowing material for TEM, STM, and SEM of biological macromolecular structures
    • Wepf R., Amrein M., Bürkliand U., and Gross H. Platinum/iridium/carbon: a high resolution shadowing material for TEM, STM, and SEM of biological macromolecular structures. J Microsc 163 (1991) 51-64
    • (1991) J Microsc , vol.163 , pp. 51-64
    • Wepf, R.1    Amrein, M.2    Bürkliand, U.3    Gross, H.4


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