메뉴 건너뛰기




Volumn 169, Issue 3, 2010, Pages 286-293

High-pressure freezing combined with in vivo-DAB-cytochemistry: A novel approach for studies of endocytic compartments

Author keywords

DAB cytochemistry; Electron tomography; Endocytosis; Golgi apparatus; High pressure freezing; trans Golgi network

Indexed keywords

DIAMINOBENZIDINE; HORSERADISH PEROXIDASE; RESIN;

EID: 76749103239     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.10.011     Document Type: Article
Times cited : (9)

References (60)
  • 1
    • 0035239219 scopus 로고    scopus 로고
    • Cryosubstitution of frozen biological specimens in electron microscopy: use and application as an alternative to chemical fixation
    • Bohrmann B., and Kellenberger E. Cryosubstitution of frozen biological specimens in electron microscopy: use and application as an alternative to chemical fixation. Micron 32 (2001) 11-19
    • (2001) Micron , vol.32 , pp. 11-19
    • Bohrmann, B.1    Kellenberger, E.2
  • 2
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino J.S., and Rojas R. Retrograde transport from endosomes to the trans-Golgi network. Nat. Rev. Mol. Cell Biol. 7 (2006) 568-579
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 4
    • 0344993904 scopus 로고    scopus 로고
    • Early endosomes are required for major histocompatibility complex class II transport to peptide-loading compartments
    • Brachet V., Péhau-Arnaudet G., Desaymard C., Raposo G., and Amigorena S. Early endosomes are required for major histocompatibility complex class II transport to peptide-loading compartments. Mol. Biol. Cell 10 (1999) 2891-2904
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2891-2904
    • Brachet, V.1    Péhau-Arnaudet, G.2    Desaymard, C.3    Raposo, G.4    Amigorena, S.5
  • 5
    • 0021352917 scopus 로고
    • Shift of equilibrium density induced by 3,3′-diaminobenzidine cytochemistry: a new procedure for the analysis and purification of peroxidase-containing organelles
    • Courtoy P.J., Quintart J., and Baudhuin P. Shift of equilibrium density induced by 3,3′-diaminobenzidine cytochemistry: a new procedure for the analysis and purification of peroxidase-containing organelles. J. Cell Biol. 98 (1984) 870-876
    • (1984) J. Cell Biol. , vol.98 , pp. 870-876
    • Courtoy, P.J.1    Quintart, J.2    Baudhuin, P.3
  • 6
    • 0024426168 scopus 로고
    • High-pressure freezing for the preservation of biological structure: theory and practice
    • Dahl R., and Staehelin L.A. High-pressure freezing for the preservation of biological structure: theory and practice. J. Electron Microsc. Techn. 13 (1989) 165-174
    • (1989) J. Electron Microsc. Techn. , vol.13 , pp. 165-174
    • Dahl, R.1    Staehelin, L.A.2
  • 8
    • 0025974918 scopus 로고
    • Freeze-substitution and the preservation of diffusible ions
    • Edelmann L. Freeze-substitution and the preservation of diffusible ions. J. Microsc. 161 (1991) 217-228
    • (1991) J. Microsc. , vol.161 , pp. 217-228
    • Edelmann, L.1
  • 9
    • 0029979181 scopus 로고    scopus 로고
    • Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes
    • Futter C.E., Pearse A., Hewlett L.J., and Hopkins C.R. Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes. J. Cell Biol. 132 (1996) 1011-1023
    • (1996) J. Cell Biol. , vol.132 , pp. 1011-1023
    • Futter, C.E.1    Pearse, A.2    Hewlett, L.J.3    Hopkins, C.R.4
  • 11
    • 0142057232 scopus 로고    scopus 로고
    • Freeze-substitution protocols for improved visualisation of membranes in high-pressure frozen samples
    • Giddings T.H. Freeze-substitution protocols for improved visualisation of membranes in high-pressure frozen samples. J. Microsc. 212 (2003) 53-61
    • (2003) J. Microsc. , vol.212 , pp. 53-61
    • Giddings, T.H.1
  • 12
    • 0002199711 scopus 로고
    • Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins
    • Liener I.E., Sharon N., and Goldstein I.J. (Eds), Academic Press, Orlando
    • Goldstein I.J., and Poretz R.D. Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins. In: Liener I.E., Sharon N., and Goldstein I.J. (Eds). The Lectins: Properties, Functions, and Applications in Biology and Medicine (1986), Academic Press, Orlando 33-247
    • (1986) The Lectins: Properties, Functions, and Applications in Biology and Medicine , pp. 33-247
    • Goldstein, I.J.1    Poretz, R.D.2
  • 14
    • 0013895415 scopus 로고
    • The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique
    • Graham Jr. R.C., and Karnovsky M.J. The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique. J. Histochem. Cytochem. 14 (1966) 291-302
    • (1966) J. Histochem. Cytochem. , vol.14 , pp. 291-302
    • Graham Jr., R.C.1    Karnovsky, M.J.2
  • 15
    • 34247278153 scopus 로고    scopus 로고
    • Rapid freeze-substitution preserves membranes in high-pressure frozen tissue culture cells
    • Hawes P., Netherton C.L., Mueller M., Wileman T., and Monaghan P. Rapid freeze-substitution preserves membranes in high-pressure frozen tissue culture cells. J. Microsc. 226 (2007) 182-189
    • (2007) J. Microsc. , vol.226 , pp. 182-189
    • Hawes, P.1    Netherton, C.L.2    Mueller, M.3    Wileman, T.4    Monaghan, P.5
  • 16
    • 0343526767 scopus 로고    scopus 로고
    • Cryopreparation provides new insight into the effects of Brefeldin A on the structure of the HepG2 Golgi apparatus
    • Hess M.W., Mueller M., Debbage P.L., Vetterlein M., and Pavelka M. Cryopreparation provides new insight into the effects of Brefeldin A on the structure of the HepG2 Golgi apparatus. J. Struct. Biol. 130 (2000) 63-72
    • (2000) J. Struct. Biol. , vol.130 , pp. 63-72
    • Hess, M.W.1    Mueller, M.2    Debbage, P.L.3    Vetterlein, M.4    Pavelka, M.5
  • 17
    • 0027982167 scopus 로고
    • High-pressure freezing of cell suspensions in cellulose capillary tubes
    • Hohenberg H., Mannweiler K., and Mueller M. High-pressure freezing of cell suspensions in cellulose capillary tubes. J. Microsc. 175 (1994) 34-43
    • (1994) J. Microsc. , vol.175 , pp. 34-43
    • Hohenberg, H.1    Mannweiler, K.2    Mueller, M.3
  • 18
    • 69249126071 scopus 로고    scopus 로고
    • Freeze-substitution
    • Cavalier A., Spehner D., and Humbel B. (Eds), CRC Press, Boca Raton
    • Humbel B.M. Freeze-substitution. In: Cavalier A., Spehner D., and Humbel B. (Eds). Handbook of Cryo-preparation Methods for Electron Microscopy (2009), CRC Press, Boca Raton 319-341
    • (2009) Handbook of Cryo-preparation Methods for Electron Microscopy , pp. 319-341
    • Humbel, B.M.1
  • 19
    • 33645244541 scopus 로고    scopus 로고
    • Aclar discs: a versatile substrate for routine high-pressure freezing of mammalian cell monolayers
    • Jiménez N., Humbel B.M., van Donselaar E., Verkleij A.J., and Burger K.N.J. Aclar discs: a versatile substrate for routine high-pressure freezing of mammalian cell monolayers. J. Microsc. 221 (2006) 216-223
    • (2006) J. Microsc. , vol.221 , pp. 216-223
    • Jiménez, N.1    Humbel, B.M.2    van Donselaar, E.3    Verkleij, A.J.4    Burger, K.N.J.5
  • 20
    • 57749196733 scopus 로고    scopus 로고
    • Tracing the retrograde route in protein trafficking
    • Johannes L., and Popoff V. Tracing the retrograde route in protein trafficking. Cell 135 (2008) 1175-1187
    • (2008) Cell , vol.135 , pp. 1175-1187
    • Johannes, L.1    Popoff, V.2
  • 21
    • 35848931005 scopus 로고    scopus 로고
    • Analysis of de novo Golgi complex formation after enzyme-based inactivation
    • Jollivet F., Raposo G., Dimitrov A., Sougrat R., Goud B., and Perez F. Analysis of de novo Golgi complex formation after enzyme-based inactivation. Mol. Biol. Cell 18 (2007) 4637-4647
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4637-4647
    • Jollivet, F.1    Raposo, G.2    Dimitrov, A.3    Sougrat, R.4    Goud, B.5    Perez, F.6
  • 22
    • 69249084367 scopus 로고    scopus 로고
    • BAL-TEC HPM 010 high-pressure freezing machine
    • Cavalier A., Spehner D., and Humbel B. (Eds), CRC Press, Boca Raton
    • Kaech A. BAL-TEC HPM 010 high-pressure freezing machine. In: Cavalier A., Spehner D., and Humbel B. (Eds). Handbook of Cryo-preparation Methods for Electron Microscopy (2009), CRC Press, Boca Raton 101-128
    • (2009) Handbook of Cryo-preparation Methods for Electron Microscopy , pp. 101-128
    • Kaech, A.1
  • 23
    • 0005648680 scopus 로고
    • Cryofixation of dynamic processes in cells and organelles
    • Steinbrecht R.A., and Zierold K. (Eds), Springer-Verlag, Berlin, Heidelberg
    • Knoll G., Verkleij A.J., and Plattner H. Cryofixation of dynamic processes in cells and organelles. In: Steinbrecht R.A., and Zierold K. (Eds). Cryotechniques in Biological Electron Microscopy (1987), Springer-Verlag, Berlin, Heidelberg 258-271
    • (1987) Cryotechniques in Biological Electron Microscopy , pp. 258-271
    • Knoll, G.1    Verkleij, A.J.2    Plattner, H.3
  • 24
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: functional insights from the normal rat kidney cell
    • Ladinsky M.S., Mastronarde D.N., McIntosh J.R., Howell K.E., and Staehelin L.A. Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J. Cell Biol. 144 (1999) 1135-1149
    • (1999) J. Cell Biol. , vol.144 , pp. 1135-1149
    • Ladinsky, M.S.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4    Staehelin, L.A.5
  • 26
    • 48749089692 scopus 로고    scopus 로고
    • Cryo-electron tomography of cells: connecting structure and function
    • Lucić V., Leis A., and Baumeister W. Cryo-electron tomography of cells: connecting structure and function. Histochem. Cell Biol. 130 (2008) 185-196
    • (2008) Histochem. Cell Biol. , vol.130 , pp. 185-196
    • Lucić, V.1    Leis, A.2    Baumeister, W.3
  • 27
    • 20544476675 scopus 로고    scopus 로고
    • Lessons from tomographic studies of the mammalian Golgi
    • Marsh B.J. Lessons from tomographic studies of the mammalian Golgi. Biochem. Biophys. Acta 1744 (2005) 273-292
    • (2005) Biochem. Biophys. Acta , vol.1744 , pp. 273-292
    • Marsh, B.J.1
  • 28
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh B.J., Mastronarde D.N., Buttle K.F., Howell K.E., and McIntosh J.R. Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc. Nat. Acad. Sci. USA 98 (2001) 2399-2406
    • (2001) Proc. Nat. Acad. Sci. USA , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5
  • 29
    • 27744497309 scopus 로고    scopus 로고
    • Epoxy resin as fixative during freeze-substitution
    • Matsko N., and Mueller M. Epoxy resin as fixative during freeze-substitution. J. Struct. Biol. 152 (2005) 92-103
    • (2005) J. Struct. Biol. , vol.152 , pp. 92-103
    • Matsko, N.1    Mueller, M.2
  • 31
    • 2442640305 scopus 로고    scopus 로고
    • Predicting function from structure: 3D structure studies of the mammalian Golgi complex
    • Mogelsvang S., Marsh B.J., Ladinsky M.S., and Howell K.E. Predicting function from structure: 3D structure studies of the mammalian Golgi complex. Traffic 5 (2004) 338-345
    • (2004) Traffic , vol.5 , pp. 338-345
    • Mogelsvang, S.1    Marsh, B.J.2    Ladinsky, M.S.3    Howell, K.E.4
  • 32
    • 0032412495 scopus 로고    scopus 로고
    • High-pressure freezing for immunocytochemistry
    • Monaghan P., Perusinghe N., and Mueller M. High-pressure freezing for immunocytochemistry. J. Microsc. 192 (1998) 248-258
    • (1998) J. Microsc. , vol.192 , pp. 248-258
    • Monaghan, P.1    Perusinghe, N.2    Mueller, M.3
  • 33
    • 0005355225 scopus 로고
    • Recent progress in high pressure-freezing
    • Moor H. Recent progress in high pressure-freezing. J. Electron Microsc. 35 (1986) 1961-1964
    • (1986) J. Electron Microsc. , vol.35 , pp. 1961-1964
    • Moor, H.1
  • 34
    • 0002133971 scopus 로고
    • Theory and practice of high pressure freezing
    • Steinbrecht R.A., and Zierold K. (Eds), Springer-Verlag, Berlin, Heidelberg
    • Moor H. Theory and practice of high pressure freezing. In: Steinbrecht R.A., and Zierold K. (Eds). Cryotechniques in Biological Electron Microscopy (1987), Springer-Verlag, Berlin, Heidelberg 175-191
    • (1987) Cryotechniques in Biological Electron Microscopy , pp. 175-191
    • Moor, H.1
  • 35
    • 0142088974 scopus 로고    scopus 로고
    • Influence of aldehyde fixation on the morphology of endosomes and lysosomes: quantitative analysis and electron tomography
    • Murk J.L.A.N., Posthuma G., Koster A.J., Geuze H.J., Verkleij A.J., Kleijmeer M.J., and Humbel B.M. Influence of aldehyde fixation on the morphology of endosomes and lysosomes: quantitative analysis and electron tomography. J. Microsc. 212 (2003) 81-90
    • (2003) J. Microsc. , vol.212 , pp. 81-90
    • Murk, J.L.A.N.1    Posthuma, G.2    Koster, A.J.3    Geuze, H.J.4    Verkleij, A.J.5    Kleijmeer, M.J.6    Humbel, B.M.7
  • 36
    • 0023517021 scopus 로고
    • Functional morphology of the Golgi apparatus
    • Pavelka M. Functional morphology of the Golgi apparatus. Adv. Anat. Embryol. Cell Biol. 106 (1987) 1-94
    • (1987) Adv. Anat. Embryol. Cell Biol. , vol.106 , pp. 1-94
    • Pavelka, M.1
  • 39
    • 39749142542 scopus 로고    scopus 로고
    • Retrograde traffic in the biosynthetic-secretory route
    • Pavelka M., Neumüller J., and Ellinger A. Retrograde traffic in the biosynthetic-secretory route. Histochem. Cell Biol. 129 (2008) 277-288
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 277-288
    • Pavelka, M.1    Neumüller, J.2    Ellinger, A.3
  • 40
    • 76749100430 scopus 로고
    • Current trends in the electron microscopic analysis of dynamic processes in the field of cell and molecular biology
    • Plattner H. (Ed), CRC Press, Boca Raton
    • Plattner H. Current trends in the electron microscopic analysis of dynamic processes in the field of cell and molecular biology. In: Plattner H. (Ed). Electron Microscopy of Subcellular Dynamics (1989), CRC Press, Boca Raton 1-11
    • (1989) Electron Microscopy of Subcellular Dynamics , pp. 1-11
    • Plattner, H.1
  • 42
    • 0033581015 scopus 로고    scopus 로고
    • Functional early endosomes are required for maturation of major histocompatibility complex class II molecules in human B lymphoblastoid cells
    • Pond L., and Watts C. Functional early endosomes are required for maturation of major histocompatibility complex class II molecules in human B lymphoblastoid cells. J. Biol. Chem. 274 (1999) 18049-18054
    • (1999) J. Biol. Chem. , vol.274 , pp. 18049-18054
    • Pond, L.1    Watts, C.2
  • 44
    • 0025910689 scopus 로고
    • Rapid-freezing cytochemistry: preservation of tubular lysosomes and enzyme activity
    • Robinson J.M., and Karnovsky M.J. Rapid-freezing cytochemistry: preservation of tubular lysosomes and enzyme activity. J. Histochem. Cytochem. 39 (1991) 787-792
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 787-792
    • Robinson, J.M.1    Karnovsky, M.J.2
  • 45
    • 20744450629 scopus 로고    scopus 로고
    • Delivery into cells: lessons learned from plant and bacterial toxins
    • Sandvig K., and Van Deurs B. Delivery into cells: lessons learned from plant and bacterial toxins. Gene Ther. 12 (2005) 865-872
    • (2005) Gene Ther. , vol.12 , pp. 865-872
    • Sandvig, K.1    Van Deurs, B.2
  • 47
    • 34548020973 scopus 로고    scopus 로고
    • Correlative light and electron microscopy using immunolabeled resin sections
    • Schwarz H., and Humbel B.M. Correlative light and electron microscopy using immunolabeled resin sections. Methods Mol. Biol. 369 (2007) 229-256
    • (2007) Methods Mol. Biol. , vol.369 , pp. 229-256
    • Schwarz, H.1    Humbel, B.M.2
  • 48
    • 40649107390 scopus 로고    scopus 로고
    • The combination of chemical fixation procedures with high pressure freezing and freeze substitution preserves highly labile tissue ultrastructure for electron tomography applications
    • Sosinsky G.E., Crum J., Jones Y.Z., Lanman J., Smarr B., Terada M., Martone M.E., Deerinck T.J., Johnson J.E., and Ellisman M.H. The combination of chemical fixation procedures with high pressure freezing and freeze substitution preserves highly labile tissue ultrastructure for electron tomography applications. J. Struct. Biol. 161 (2008) 359-371
    • (2008) J. Struct. Biol. , vol.161 , pp. 359-371
    • Sosinsky, G.E.1    Crum, J.2    Jones, Y.Z.3    Lanman, J.4    Smarr, B.5    Terada, M.6    Martone, M.E.7    Deerinck, T.J.8    Johnson, J.E.9    Ellisman, M.H.10
  • 49
    • 0002743936 scopus 로고
    • Freeze-substitution and freeze-drying
    • Steinbrecht R.A., and Zierold K. (Eds), Springer-Verlag, Berlin, Heidelberg
    • Steinbrecht R.A., and Müller M. Freeze-substitution and freeze-drying. In: Steinbrecht R.A., and Zierold K. (Eds). Cryotechniques in Biological Electron Microscopy (1987), Springer-Verlag, Berlin, Heidelberg 149-172
    • (1987) Cryotechniques in Biological Electron Microscopy , pp. 149-172
    • Steinbrecht, R.A.1    Müller, M.2
  • 50
    • 0029610381 scopus 로고
    • Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex
    • Stinchcombe J.C., Nomoto H., Cutler D.F., and Hopkins C.R. Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex. J. Cell Biol. 131 (1995) 1387-1401
    • (1995) J. Cell Biol. , vol.131 , pp. 1387-1401
    • Stinchcombe, J.C.1    Nomoto, H.2    Cutler, D.F.3    Hopkins, C.R.4
  • 51
    • 0030047961 scopus 로고    scopus 로고
    • A novel class of clathrin-coated vesicles budding from endosomes
    • Stoorvogel W., Oorschot V., and Geuze H.J. A novel class of clathrin-coated vesicles budding from endosomes. J. Cell Biol. 132 (1996) 21-33
    • (1996) J. Cell Biol. , vol.132 , pp. 21-33
    • Stoorvogel, W.1    Oorschot, V.2    Geuze, H.J.3
  • 53
    • 54049097431 scopus 로고    scopus 로고
    • Electron microscopy of high pressure frozen samples: bridging the gap between cellular ultrastructure and atomic resolution
    • Studer D., Humbel B.M., and Chiquet M. Electron microscopy of high pressure frozen samples: bridging the gap between cellular ultrastructure and atomic resolution. Histochem. Cell Biol. 130 (2008) 877-889
    • (2008) Histochem. Cell Biol. , vol.130 , pp. 877-889
    • Studer, D.1    Humbel, B.M.2    Chiquet, M.3
  • 54
    • 34548229482 scopus 로고    scopus 로고
    • Alternate routes for drug delivery to the cell interior: pathways to the Golgi apparatus and endoplasmic reticulum
    • Tarrago-Trani M.T., and Storrie B. Alternate routes for drug delivery to the cell interior: pathways to the Golgi apparatus and endoplasmic reticulum. Adv. Drug Deliv. Rev. 59 (2007) 782-797
    • (2007) Adv. Drug Deliv. Rev. , vol.59 , pp. 782-797
    • Tarrago-Trani, M.T.1    Storrie, B.2
  • 55
    • 0023239830 scopus 로고
    • Delivery of internalized ricin from endosomes to cisternal Golgi elements is a discontinuous, temperature-sensitive process
    • van Deurs B., Petersen O.W., Olsnes S., and Sandvig K. Delivery of internalized ricin from endosomes to cisternal Golgi elements is a discontinuous, temperature-sensitive process. Exp. Cell Res. 171 (1986) 137-152
    • (1986) Exp. Cell Res. , vol.171 , pp. 137-152
    • van Deurs, B.1    Petersen, O.W.2    Olsnes, S.3    Sandvig, K.4
  • 56
    • 69249090017 scopus 로고    scopus 로고
    • High-pressure freezing LEICA EMPACT
    • Cavalier A., Spehner D., and Humbel B. (Eds), CRC Press, Boca Raton
    • Vanhecke D., and Studer D. High-pressure freezing LEICA EMPACT. In: Cavalier A., Spehner D., and Humbel B. (Eds). Handbook of Cryo-preparation Methods for Electron Microscopy (2009), CRC Press, Boca Raton 129-156
    • (2009) Handbook of Cryo-preparation Methods for Electron Microscopy , pp. 129-156
    • Vanhecke, D.1    Studer, D.2
  • 57
    • 42649111676 scopus 로고    scopus 로고
    • Moving EM: the rapid transfer system as a new tool for correlative light and electron microscopy and high throughout for high-pressure freezing
    • Verkade P. Moving EM: the rapid transfer system as a new tool for correlative light and electron microscopy and high throughout for high-pressure freezing. J. Microsc. 230 (2008) 317-328
    • (2008) J. Microsc. , vol.230 , pp. 317-328
    • Verkade, P.1
  • 59
    • 0041328515 scopus 로고    scopus 로고
    • Brefeldin A-regulated retrograde transport into the endoplasmic reticulum of internalised wheat germ agglutinin
    • Vetterlein M., Niapir M., Ellinger A., Neumüller J., and Pavelka M. Brefeldin A-regulated retrograde transport into the endoplasmic reticulum of internalised wheat germ agglutinin. Histochem. Cell Biol. 120 (2003) 121-128
    • (2003) Histochem. Cell Biol. , vol.120 , pp. 121-128
    • Vetterlein, M.1    Niapir, M.2    Ellinger, A.3    Neumüller, J.4    Pavelka, M.5
  • 60
    • 6344256207 scopus 로고    scopus 로고
    • Binding and uptake of wheat germ agglutinin-grafted PLGA-nanospheres by Caco-2 monolayers
    • Weissenböck A., Bogner E., Wirth M., and Gabor F. Binding and uptake of wheat germ agglutinin-grafted PLGA-nanospheres by Caco-2 monolayers. Pharmac. Res. 21 (2004) 1917-1923
    • (2004) Pharmac. Res. , vol.21 , pp. 1917-1923
    • Weissenböck, A.1    Bogner, E.2    Wirth, M.3    Gabor, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.