메뉴 건너뛰기




Volumn 378, Issue 1, 2008, Pages 44-54

Heterotypic trans-Interaction of LI- and E-Cadherin and Their Localization in Plasmalemmal Microdomains

Author keywords

7D cadherin; adhesion; AFM; cholesterol; enterocyte

Indexed keywords

UVOMORULIN; VASCULAR ENDOTHELIAL CADHERIN;

EID: 41249087636     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.02.023     Document Type: Article
Times cited : (25)

References (59)
  • 1
    • 0035077317 scopus 로고    scopus 로고
    • The cadherin superfamily: diversity in form and function
    • Angst B.D., Marcozzi C., and Magee A.I. The cadherin superfamily: diversity in form and function. J. Cell Sci. 114 (2001) 629-641
    • (2001) J. Cell Sci. , vol.114 , pp. 629-641
    • Angst, B.D.1    Marcozzi, C.2    Magee, A.I.3
  • 2
    • 33845727992 scopus 로고    scopus 로고
    • The cadherin superfamily in neuronal connections and interactions
    • Takeichi M. The cadherin superfamily in neuronal connections and interactions. Nat. Rev., Neurosci. 8 (2007) 11-20
    • (2007) Nat. Rev., Neurosci. , vol.8 , pp. 11-20
    • Takeichi, M.1
  • 3
    • 0031440104 scopus 로고    scopus 로고
    • Molecular and functional analysis of cadherin-based adherens junctions
    • Yap A.S., Brieher W.M., and Gumbiner B.M. Molecular and functional analysis of cadherin-based adherens junctions. Annu. Rev. Cell Dev. Biol. 13 (1997) 119-146
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 119-146
    • Yap, A.S.1    Brieher, W.M.2    Gumbiner, B.M.3
  • 4
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi M. Morphogenetic roles of classic cadherins. Curr. Opin. Cell Biol. 7 (1995) 619-627
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 5
    • 0033103763 scopus 로고    scopus 로고
    • Cadherins and tissue formation: integrating adhesion and signaling
    • Vleminckx K., and Kemler R. Cadherins and tissue formation: integrating adhesion and signaling. BioEssays 21 (1999) 211-220
    • (1999) BioEssays , vol.21 , pp. 211-220
    • Vleminckx, K.1    Kemler, R.2
  • 7
    • 23144442645 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion in morphogenesis
    • Gumbiner B.M. Regulation of cadherin-mediated adhesion in morphogenesis. Nat. Rev., Mol. Cell Biol. 6 (2005) 622-634
    • (2005) Nat. Rev., Mol. Cell Biol. , vol.6 , pp. 622-634
    • Gumbiner, B.M.1
  • 11
    • 0028093281 scopus 로고
    • Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding
    • Pokutta S., Herrenknecht K., Kemler R., and Engel J. Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding. Eur. J. Biochem. 223 (1994) 1019-1026
    • (1994) Eur. J. Biochem. , vol.223 , pp. 1019-1026
    • Pokutta, S.1    Herrenknecht, K.2    Kemler, R.3    Engel, J.4
  • 13
    • 0032953786 scopus 로고    scopus 로고
    • E-cadherin functions as a cis-dimer at the cell-cell adhesive interface in vivo
    • Takeda H., Shimoyama Y., Nagafuchi A., and Hirohashi S. E-cadherin functions as a cis-dimer at the cell-cell adhesive interface in vivo. Nat. Struct. Biol. 6 (1999) 310-312
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 310-312
    • Takeda, H.1    Shimoyama, Y.2    Nagafuchi, A.3    Hirohashi, S.4
  • 14
    • 0021991243 scopus 로고
    • Cell-adhesion molecule uvomorulin is localized in the intermediate junctions of adult intestinal epithelial cells
    • Boller K., Vestweber D., and Kemler R. Cell-adhesion molecule uvomorulin is localized in the intermediate junctions of adult intestinal epithelial cells. J. Cell Biol. 100 (1985) 327-332
    • (1985) J. Cell Biol. , vol.100 , pp. 327-332
    • Boller, K.1    Vestweber, D.2    Kemler, R.3
  • 15
    • 0028206194 scopus 로고
    • Liver-intestine cadherin: molecular cloning and characterization of a novel Ca(2+)-dependent cell adhesion molecule expressed in liver and intestine
    • Berndorff D., Gessner R., Kreft B., Schnoy N., Lajous-Petter A.M., Loch N., et al. Liver-intestine cadherin: molecular cloning and characterization of a novel Ca(2+)-dependent cell adhesion molecule expressed in liver and intestine. J. Cell Biol. 125 (1994) 1353-1369
    • (1994) J. Cell Biol. , vol.125 , pp. 1353-1369
    • Berndorff, D.1    Gessner, R.2    Kreft, B.3    Schnoy, N.4    Lajous-Petter, A.M.5    Loch, N.6
  • 16
    • 0034525594 scopus 로고    scopus 로고
    • Intestinal cell adhesion molecules. Liver-intestine cadherin
    • Gessner R., and Tauber R. Intestinal cell adhesion molecules. Liver-intestine cadherin. Ann. N. Y. Acad. Sci. 915 (2000) 136-143
    • (2000) Ann. N. Y. Acad. Sci. , vol.915 , pp. 136-143
    • Gessner, R.1    Tauber, R.2
  • 17
    • 39849100440 scopus 로고    scopus 로고
    • Adherens and tight junctions: structure, function and connections to the actin cytoskeleton
    • 10.1016/j.bbamem.2007.07.012
    • Hartsock A., and Nelson W.J. Adherens and tight junctions: structure, function and connections to the actin cytoskeleton. Biochim. Biophys. Acta (2007) 10.1016/j.bbamem.2007.07.012
    • (2007) Biochim. Biophys. Acta
    • Hartsock, A.1    Nelson, W.J.2
  • 18
    • 0035006234 scopus 로고    scopus 로고
    • LI-cadherin gene expression during mouse intestinal development
    • Angres B., Kim L., Jung R., Gessner R., and Tauber R. LI-cadherin gene expression during mouse intestinal development. Dev. Dyn. 221 (2001) 182-193
    • (2001) Dev. Dyn. , vol.221 , pp. 182-193
    • Angres, B.1    Kim, L.2    Jung, R.3    Gessner, R.4    Tauber, R.5
  • 19
    • 33746611580 scopus 로고    scopus 로고
    • Unique gene structure and paralogy define the 7D-cadherin family
    • Wendeler M.W., Jung R., Himmelbauer H., and Gessner R. Unique gene structure and paralogy define the 7D-cadherin family. Cell. Mol. Life Sci. 63 (2006) 1564-1573
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 1564-1573
    • Wendeler, M.W.1    Jung, R.2    Himmelbauer, H.3    Gessner, R.4
  • 20
    • 0027445508 scopus 로고
    • Proteins associated with the cytoplasmic surface of adhesion molecules
    • Gumbiner B.M. Proteins associated with the cytoplasmic surface of adhesion molecules. Neuron 11 (1993) 551-564
    • (1993) Neuron , vol.11 , pp. 551-564
    • Gumbiner, B.M.1
  • 21
    • 0027723788 scopus 로고
    • Catenins as mediators of the cytoplasmic functions of cadherins
    • Gumbiner B.M., and McCrea P.D. Catenins as mediators of the cytoplasmic functions of cadherins. J. Cell Sci., Suppl. 17 (1993) 155-158
    • (1993) J. Cell Sci., Suppl. , vol.17 , pp. 155-158
    • Gumbiner, B.M.1    McCrea, P.D.2
  • 22
    • 0027938682 scopus 로고
    • A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated
    • Stappert J., and Kemler R. A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated. Cell Adhes. Commun. 2 (1994) 319-327
    • (1994) Cell Adhes. Commun. , vol.2 , pp. 319-327
    • Stappert, J.1    Kemler, R.2
  • 23
    • 0030892262 scopus 로고    scopus 로고
    • LI-cadherin-mediated cell-cell adhesion does not require cytoplasmic interactions
    • Kreft B., Berndorff D., Bottinger A., Finnemann S., Wedlich D., Hortsch M., et al. LI-cadherin-mediated cell-cell adhesion does not require cytoplasmic interactions. J. Cell Biol. 136 (1997) 1109-1121
    • (1997) J. Cell Biol. , vol.136 , pp. 1109-1121
    • Kreft, B.1    Berndorff, D.2    Bottinger, A.3    Finnemann, S.4    Wedlich, D.5    Hortsch, M.6
  • 24
    • 0029980542 scopus 로고    scopus 로고
    • Structural basis of calcium-induced E-cadherin rigidification and dimerization
    • Nagar B., Overduin M., Ikura M., and Rini J.M. Structural basis of calcium-induced E-cadherin rigidification and dimerization. Nature 380 (1996) 360-364
    • (1996) Nature , vol.380 , pp. 360-364
    • Nagar, B.1    Overduin, M.2    Ikura, M.3    Rini, J.M.4
  • 25
    • 0033119626 scopus 로고    scopus 로고
    • A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation
    • Pertz O., Bozic D., Koch A.W., Fauser C., Brancaccio A., and Engel J. A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation. EMBO J. 18 (1999) 1738-1747
    • (1999) EMBO J. , vol.18 , pp. 1738-1747
    • Pertz, O.1    Bozic, D.2    Koch, A.W.3    Fauser, C.4    Brancaccio, A.5    Engel, J.6
  • 26
    • 0032102397 scopus 로고    scopus 로고
    • Structure-function analysis of cell adhesion by neural (N-) cadherin
    • Tamura K., Shan W.S., Hendrickson W.A., Colman D.R., and Shapiro L. Structure-function analysis of cell adhesion by neural (N-) cadherin. Neuron 20 (1998) 1153-1163
    • (1998) Neuron , vol.20 , pp. 1153-1163
    • Tamura, K.1    Shan, W.S.2    Hendrickson, W.A.3    Colman, D.R.4    Shapiro, L.5
  • 28
    • 0031149109 scopus 로고    scopus 로고
    • Lateral clustering of the adhesive ectodomain: a fundamental determinant of cadherin function
    • Yap A.S., Brieher W.M., Pruschy M., and Gumbiner B.M. Lateral clustering of the adhesive ectodomain: a fundamental determinant of cadherin function. Curr. Biol. 7 (1997) 308-315
    • (1997) Curr. Biol. , vol.7 , pp. 308-315
    • Yap, A.S.1    Brieher, W.M.2    Pruschy, M.3    Gumbiner, B.M.4
  • 29
    • 34249656371 scopus 로고    scopus 로고
    • Intestinal LI-cadherin acts as a Ca(2+)-dependent adhesion switch
    • Wendeler M.W., Drenckhahn D., Gessner R., and Baumgartner W. Intestinal LI-cadherin acts as a Ca(2+)-dependent adhesion switch. J. Mol. Biol. 370 (2007) 220-230
    • (2007) J. Mol. Biol. , vol.370 , pp. 220-230
    • Wendeler, M.W.1    Drenckhahn, D.2    Gessner, R.3    Baumgartner, W.4
  • 31
    • 0035069677 scopus 로고    scopus 로고
    • Direct measurements of multiple adhesive alignments and unbinding trajectories between cadherin extracellular domains
    • Sivasankar S., Gumbiner B., and Leckband D. Direct measurements of multiple adhesive alignments and unbinding trajectories between cadherin extracellular domains. Biophys. J. 80 (2001) 1758-1768
    • (2001) Biophys. J. , vol.80 , pp. 1758-1768
    • Sivasankar, S.1    Gumbiner, B.2    Leckband, D.3
  • 32
    • 0037013927 scopus 로고    scopus 로고
    • Fast dissociation kinetics between individual E-cadherin fragments revealed by flow chamber analysis
    • Perret E., Benoliel A.M., Nassoy P., Pierres A., Delmas V., Thiery J.P., et al. Fast dissociation kinetics between individual E-cadherin fragments revealed by flow chamber analysis. EMBO J. 21 (2002) 2537-2546
    • (2002) EMBO J. , vol.21 , pp. 2537-2546
    • Perret, E.1    Benoliel, A.M.2    Nassoy, P.3    Pierres, A.4    Delmas, V.5    Thiery, J.P.6
  • 33
    • 33750323506 scopus 로고    scopus 로고
    • Similarities between heterophilic and homophilic cadherin adhesion
    • Prakasam A.K., Maruthamuthu V., and Leckband D.E. Similarities between heterophilic and homophilic cadherin adhesion. Proc. Natl. Acad. Sci. USA 103 (2006) 15434-15439
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15434-15439
    • Prakasam, A.K.1    Maruthamuthu, V.2    Leckband, D.E.3
  • 35
    • 0037444477 scopus 로고    scopus 로고
    • Cadherin function probed by laser tweezer and single molecule fluorescence in vascular endothelial cells
    • Baumgartner W., Schutz G.J., Wiegand J., Golenhofen N., and Drenckhahn D. Cadherin function probed by laser tweezer and single molecule fluorescence in vascular endothelial cells. J. Cell Sci. 116 (2003) 1001-1011
    • (2003) J. Cell Sci. , vol.116 , pp. 1001-1011
    • Baumgartner, W.1    Schutz, G.J.2    Wiegand, J.3    Golenhofen, N.4    Drenckhahn, D.5
  • 36
    • 0348010286 scopus 로고    scopus 로고
    • Ca2+ dependency of N-cadherin function probed by laser tweezer and atomic force microscopy
    • Baumgartner W., Golenhofen N., Grundhofer N., Wiegand J., and Drenckhahn D. Ca2+ dependency of N-cadherin function probed by laser tweezer and atomic force microscopy. J. Neurosci. 23 (2003) 11008-11014
    • (2003) J. Neurosci. , vol.23 , pp. 11008-11014
    • Baumgartner, W.1    Golenhofen, N.2    Grundhofer, N.3    Wiegand, J.4    Drenckhahn, D.5
  • 37
    • 34748902244 scopus 로고    scopus 로고
    • Imaging and force spectroscopy on desmoglein 1 using atomic force microscopy reveal multivalent Ca(2+)-dependent, low-affinity trans-interaction
    • Waschke J., Menendez-Castro C., Bruggeman P., Koob R., Amagai M., Gruber H.J., et al. Imaging and force spectroscopy on desmoglein 1 using atomic force microscopy reveal multivalent Ca(2+)-dependent, low-affinity trans-interaction. J. Membr. Biol. 216 (2007) 83-92
    • (2007) J. Membr. Biol. , vol.216 , pp. 83-92
    • Waschke, J.1    Menendez-Castro, C.2    Bruggeman, P.3    Koob, R.4    Amagai, M.5    Gruber, H.J.6
  • 38
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell G.I. Models for the specific adhesion of cells to cells. Science 200 (1978) 618-627
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 39
    • 1542299041 scopus 로고    scopus 로고
    • Ksp-cadherin is a functional cell-cell adhesion molecule related to LI-cadherin
    • Wendeler M.W., Praus M., Jung R., Hecking M., Metzig C., and Gessner R. Ksp-cadherin is a functional cell-cell adhesion molecule related to LI-cadherin. Exp. Cell Res. 294 (2004) 345-355
    • (2004) Exp. Cell Res. , vol.294 , pp. 345-355
    • Wendeler, M.W.1    Praus, M.2    Jung, R.3    Hecking, M.4    Metzig, C.5    Gessner, R.6
  • 40
    • 0022493456 scopus 로고
    • Identification and characterization of brush-border membrane-bound neutral metalloendopeptidases from rat small intestine
    • Song I.S., Yoshioka M., Erickson R.H., Miura S., Guan D., and Kim Y.S. Identification and characterization of brush-border membrane-bound neutral metalloendopeptidases from rat small intestine. Gastroenterology 91 (1986) 1234-1242
    • (1986) Gastroenterology , vol.91 , pp. 1234-1242
    • Song, I.S.1    Yoshioka, M.2    Erickson, R.H.3    Miura, S.4    Guan, D.5    Kim, Y.S.6
  • 41
    • 0036977859 scopus 로고    scopus 로고
    • Plasmalemmal concentration and affinity of mouse vascular endothelial cadherin, VE-cadherin
    • Baumgartner W., and Drenckhahn D. Plasmalemmal concentration and affinity of mouse vascular endothelial cadherin, VE-cadherin. Eur. Biophys. J. 31 (2002) 532-538
    • (2002) Eur. Biophys. J. , vol.31 , pp. 532-538
    • Baumgartner, W.1    Drenckhahn, D.2
  • 42
    • 0037148522 scopus 로고    scopus 로고
    • Cadherin-mediated cell sorting not determined by binding or adhesion specificity
    • Niessen C.M., and Gumbiner B.M. Cadherin-mediated cell sorting not determined by binding or adhesion specificity. J. Cell Biol. 156 (2002) 389-399
    • (2002) J. Cell Biol. , vol.156 , pp. 389-399
    • Niessen, C.M.1    Gumbiner, B.M.2
  • 43
    • 0027273236 scopus 로고
    • Defining E-cadherin-associated protein complexes in epithelial cells: plakoglobin, beta- and gamma-catenin are distinct components
    • Piepenhagen P.A., and Nelson W.J. Defining E-cadherin-associated protein complexes in epithelial cells: plakoglobin, beta- and gamma-catenin are distinct components. J. Cell Sci. 104 (1993) 751-762
    • (1993) J. Cell Sci. , vol.104 , pp. 751-762
    • Piepenhagen, P.A.1    Nelson, W.J.2
  • 44
    • 0028981208 scopus 로고
    • Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm D.L., Koslov E.R., Kebriaei P., Cianci C.D., and Morrow J.S. Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proc. Natl. Acad. Sci. USA 92 (1995) 8813-8817
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8813-8817
    • Rimm, D.L.1    Koslov, E.R.2    Kebriaei, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 45
    • 2542515342 scopus 로고    scopus 로고
    • Phylogenetic origin of LI-cadherin revealed by protein and gene structure analysis
    • Jung R., Wendeler M.W., Danevad M., Himmelbauer H., and Gessner R. Phylogenetic origin of LI-cadherin revealed by protein and gene structure analysis. Cell. Mol. Life Sci. 61 (2004) 1157-1166
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1157-1166
    • Jung, R.1    Wendeler, M.W.2    Danevad, M.3    Himmelbauer, H.4    Gessner, R.5
  • 46
    • 0026940189 scopus 로고
    • Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions
    • Tsukita S., Tsukita S., Nagafuchi A., and Yonemura S. Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions. Curr. Opin. Cell Biol. 4 (1992) 834-839
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 834-839
    • Tsukita, S.1    Tsukita, S.2    Nagafuchi, A.3    Yonemura, S.4
  • 47
    • 28344433073 scopus 로고    scopus 로고
    • Deconstructing the cadherin-catenin-actin complex
    • Yamada S., Pokutta S., Drees F., Weis W.I., and Nelson W.J. Deconstructing the cadherin-catenin-actin complex. Cell 123 (2005) 889-901
    • (2005) Cell , vol.123 , pp. 889-901
    • Yamada, S.1    Pokutta, S.2    Drees, F.3    Weis, W.I.4    Nelson, W.J.5
  • 48
    • 0036228856 scopus 로고    scopus 로고
    • Transmembrane cooperative linkage in cellular adhesion
    • Baumgartner W., and Drenckhahn D. Transmembrane cooperative linkage in cellular adhesion. Eur. J. Cell Biol. 81 (2002) 161-168
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 161-168
    • Baumgartner, W.1    Drenckhahn, D.2
  • 49
    • 0019795864 scopus 로고
    • Junctional complexes in fetal rat small intestine during morphogenesis
    • Madara J.L., Neutra M.R., and Trier J.S. Junctional complexes in fetal rat small intestine during morphogenesis. Dev. Biol. 86 (1981) 170-178
    • (1981) Dev. Biol. , vol.86 , pp. 170-178
    • Madara, J.L.1    Neutra, M.R.2    Trier, J.S.3
  • 50
    • 0027613979 scopus 로고
    • Heterotypic cellular cooperation in gut morphogenesis and differentiation
    • Simon-Assmann P., and Kedinger M. Heterotypic cellular cooperation in gut morphogenesis and differentiation. Semin. Cell Biol. 4 (1993) 221-230
    • (1993) Semin. Cell Biol. , vol.4 , pp. 221-230
    • Simon-Assmann, P.1    Kedinger, M.2
  • 51
    • 0028806001 scopus 로고
    • Mouse R-cadherin: expression during the organogenesis of pancreas and gastrointestinal tract
    • Sjodin A., Dahl U., and Semb H. Mouse R-cadherin: expression during the organogenesis of pancreas and gastrointestinal tract. Exp. Cell Res. 221 (1995) 413-425
    • (1995) Exp. Cell Res. , vol.221 , pp. 413-425
    • Sjodin, A.1    Dahl, U.2    Semb, H.3
  • 53
    • 0036144678 scopus 로고    scopus 로고
    • Global gene expression analysis of gastric cancer by oligonucleotide microarrays
    • Hippo Y., Taniguchi H., Tsutsumi S., Machida N., Chong J.M., Fukayama M., et al. Global gene expression analysis of gastric cancer by oligonucleotide microarrays. Cancer Res. 62 (2002) 233-240
    • (2002) Cancer Res. , vol.62 , pp. 233-240
    • Hippo, Y.1    Taniguchi, H.2    Tsutsumi, S.3    Machida, N.4    Chong, J.M.5    Fukayama, M.6
  • 55
    • 0037085531 scopus 로고    scopus 로고
    • Rho and rho kinase modulation of barrier properties: cultured endothelial cells and intact microvessels of rats and mice
    • Adamson R.H., Curry F.E., Adamson G., Liu B., Jiang Y., Aktories K., et al. Rho and rho kinase modulation of barrier properties: cultured endothelial cells and intact microvessels of rats and mice. J. Physiol. 539 (2002) 295-308
    • (2002) J. Physiol. , vol.539 , pp. 295-308
    • Adamson, R.H.1    Curry, F.E.2    Adamson, G.3    Liu, B.4    Jiang, Y.5    Aktories, K.6
  • 56
    • 0036210084 scopus 로고    scopus 로고
    • Expression and induction of the stress protein alpha-B-crystallin in vascular endothelial cells
    • Golenhofen N., Ness W., Wawrousek E.F., and Drenckhahn D. Expression and induction of the stress protein alpha-B-crystallin in vascular endothelial cells. Histochem. Cell Biol. 117 (2002) 203-209
    • (2002) Histochem. Cell Biol. , vol.117 , pp. 203-209
    • Golenhofen, N.1    Ness, W.2    Wawrousek, E.F.3    Drenckhahn, D.4
  • 57
  • 58
    • 0035984386 scopus 로고    scopus 로고
    • An expectation-maximisation algorithm for the deconvolution of the intrinsic distribution of single molecule's parameters
    • Baumgartner W., and Drenckhahn D. An expectation-maximisation algorithm for the deconvolution of the intrinsic distribution of single molecule's parameters. Comput. Chem. 26 (2002) 321-326
    • (2002) Comput. Chem. , vol.26 , pp. 321-326
    • Baumgartner, W.1    Drenckhahn, D.2
  • 59
    • 0033973107 scopus 로고    scopus 로고
    • Data analysis of interaction forces measured with the atomic force microscope
    • Baumgartner W., Hinterdorfer P., and Schindler H. Data analysis of interaction forces measured with the atomic force microscope. Ultramicroscopy 82 (2000) 85-95
    • (2000) Ultramicroscopy , vol.82 , pp. 85-95
    • Baumgartner, W.1    Hinterdorfer, P.2    Schindler, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.