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Volumn 279, Issue 2, 2002, Pages 188-201

Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens

Author keywords

Basement membrane; Cell adhesion; Epithelial mesenchymal interactions; Laminin; Nidogen

Indexed keywords

ALPHA6 INTEGRIN; ANTIBODY; COLLAGEN TYPE 4; ENTACTIN; FIBULIN; INTEGRIN; LAMININ; MESSENGER RNA; NIDOGEN 1; NIDOGEN 2; PERLECAN; PROTEIN; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 3; VERY LATE ACTIVATION ANTIGEN 6;

EID: 0036405396     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2002.5611     Document Type: Article
Times cited : (97)

References (58)
  • 2
    • 0030087944 scopus 로고    scopus 로고
    • Supramolecular assembly of basement membranes
    • Timpl, R., and Brown, J. (1996). Supramolecular assembly of basement membranes. BioEssays 18, 123-132.
    • (1996) BioEssays , vol.18 , pp. 123-132
    • Timpl, R.1    Brown, J.2
  • 3
    • 0033808066 scopus 로고    scopus 로고
    • Still more complexity in mammalian basement membranes
    • Erickson, A. C., and Couchman, J. R. (2000). Still more complexity in mammalian basement membranes. J. Histochem. Cytochem. 48, 1291-1306.
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 1291-1306
    • Erickson, A.C.1    Couchman, J.R.2
  • 4
    • 0034952050 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1
    • Hopf, M., Göhring, W., Ries, A., Timpl, R., and Hohenester, E. (2001). Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1. Nat. Struct. Biol. 8, 634-640.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 634-640
    • Hopf, M.1    Göhring, W.2    Ries, A.3    Timpl, R.4    Hohenester, E.5
  • 5
    • 0035476687 scopus 로고    scopus 로고
    • Structural basis for the high-affinity interaction of nidogen-1 with immunoglobulin-like domain 3 of perlecan
    • Kvansakul, M., Hopf, M., Ries, A., Timpl, R., and Hohenester, E. (2001). Structural basis for the high-affinity interaction of nidogen-1 with immunoglobulin-like domain 3 of perlecan. EMBO J. 20, 5342-5346.
    • (2001) EMBO J. , vol.20 , pp. 5342-5346
    • Kvansakul, M.1    Hopf, M.2    Ries, A.3    Timpl, R.4    Hohenester, E.5
  • 6
    • 0034791903 scopus 로고    scopus 로고
    • Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal anti-bodies
    • Ries, A., Göhring, W., Fox, J. W. Timpl, R., and Sasaki, T. (2001). Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal anti-bodies. Eur. J. Biochem. 268, 5119-5128.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5119-5128
    • Ries, A.1    Göhring, W.2    Fox, J.W.3    Timpl, R.4    Sasaki, T.5
  • 7
    • 0027286695 scopus 로고
    • A single EGF-like motif of laminin is responsible for high affinity nidogen binding
    • Mayer, U., Nischt, R., Pöschl, E., Mann, K., Fukuda, K., Gerl, M., Yamada, Y., and Timpl, R. (1993). A single EGF-like motif of laminin is responsible for high affinity nidogen binding. EMBO J. 12, 1879-1885.
    • (1993) EMBO J. , vol.12 , pp. 1879-1885
    • Mayer, U.1    Nischt, R.2    Pöschl, E.3    Mann, K.4    Fukuda, K.5    Gerl, M.6    Yamada, Y.7    Timpl, R.8
  • 8
    • 0028074247 scopus 로고
    • Two non-contiguous regions contribute to nidogen binding to a single EGF-like motif of the laminin γ1 chain
    • Pöschl, E., Fox, J. W., Block, D., Mayer, U., and Timpl, R. (1994). Two non-contiguous regions contribute to nidogen binding to a single EGF-like motif of the laminin γ1 chain. EMBO J. 13, 3741-3747.
    • (1994) EMBO J. , vol.13 , pp. 3741-3747
    • Pöschl, E.1    Fox, J.W.2    Block, D.3    Mayer, U.4    Timpl, R.5
  • 9
    • 0029790892 scopus 로고    scopus 로고
    • Site-directed mutagenesis and structural interpretation of the nidogen binding site of the laminin γ1 chain
    • Pöschl, E., Mayer, U., Stetefeld, J., Baumgartner, R., Holak, T. A., Huber, R., and Timpl, R. (1996). Site-directed mutagenesis and structural interpretation of the nidogen binding site of the laminin γ1 chain. EMBO J. 15, 5154-5159.
    • (1996) EMBO J. , vol.15 , pp. 5154-5159
    • Pöschl, E.1    Mayer, U.2    Stetefeld, J.3    Baumgartner, R.4    Holak, T.A.5    Huber, R.6    Timpl, R.7
  • 10
    • 0031059074 scopus 로고    scopus 로고
    • Importance of nidogen binding to laminin γ1 for branching epithelial morphogenesis of the submandibular gland
    • Kadoya, Y., Salmivirta, K., Talts, J. F., Kadoya, K., Mayer, U., Timpl, R., and Ekblom, P. (1997). Importance of nidogen binding to laminin γ1 for branching epithelial morphogenesis of the submandibular gland. Development 124, 683-691.
    • (1997) Development , vol.124 , pp. 683-691
    • Kadoya, Y.1    Salmivirta, K.2    Talts, J.F.3    Kadoya, K.4    Mayer, U.5    Timpl, R.6    Ekblom, P.7
  • 13
    • 0036333442 scopus 로고    scopus 로고
    • Specific ablation of the nidogen-binding site in the laminin γ1 chain interferes with kidney and lung development
    • Willem, M., Miosge, N., Halfter, W., Smyth, N., Jannetti, I., Burghart, E., Timpl, R., and Mayer, U. (2002). Specific ablation of the nidogen-binding site in the laminin γ1 chain interferes with kidney and lung development. Development 129, 2711-2722.
    • (2002) Development , vol.129 , pp. 2711-2722
    • Willem, M.1    Miosge, N.2    Halfter, W.3    Smyth, N.4    Jannetti, I.5    Burghart, E.6    Timpl, R.7    Mayer, U.8
  • 14
    • 0033730457 scopus 로고    scopus 로고
    • Nidogen is not essential and not required for normal collagen IV localization in C. elegans
    • Kang, S. H., and Kramer, J. M. (2000). Nidogen is not essential and not required for normal collagen IV localization in C. elegans. Mol. Biol. Cell. 11, 3911-3923.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 3911-3923
    • Kang, S.H.1    Kramer, J.M.2
  • 15
    • 0034616141 scopus 로고    scopus 로고
    • Positioning of longitudinal nerves in C. elegans by nidogen
    • Kim, S., and Wadsworth, W. G. (2000). Positioning of longitudinal nerves in C. elegans by nidogen. Science 288, 150-154.
    • (2000) Science , vol.288 , pp. 150-154
    • Kim, S.1    Wadsworth, W.G.2
  • 17
    • 0036785584 scopus 로고    scopus 로고
    • Gene structure and functional analysis of the mouse nidogen-2 gene: Nidogen-2 is not essential for basement membrane formation in mice
    • in press
    • Schymeinsky, J., Nedbal, S., Miosge, N., Pöschl, E., Rao, C., Beier, D. R., Skarnes, D. R., Timpl, R., and Bader, B. L. (2002). Gene structure and functional analysis of the mouse nidogen-2 gene: Nidogen-2 is not essential for basement membrane formation in mice. Mol. Cell Biol. (in press).
    • (2002) Mol. Cell Biol.
    • Schymeinsky, J.1    Nedbal, S.2    Miosge, N.3    Pöschl, E.4    Rao, C.5    Beier, D.R.6    Skarnes, D.R.7    Timpl, R.8    Bader, B.L.9
  • 18
    • 0034063444 scopus 로고    scopus 로고
    • Ultrastructural colocalization of nidogen-1 and nidogen-2 with laminin-1 in murine kidney basement membranes
    • Miosge, N., Köhter, F., Heinemann, S., Kohfeldt, E., Herken, R., and Timpl, R. (2000). Ultrastructural colocalization of nidogen-1 and nidogen-2 with laminin-1 in murine kidney basement membranes. Histochem. Cell. Biol. 113, 115-124.
    • (2000) Histochem. Cell. Biol. , vol.113 , pp. 115-124
    • Miosge, N.1    Köhter, F.2    Heinemann, S.3    Kohfeldt, E.4    Herken, R.5    Timpl, R.6
  • 19
    • 0032508461 scopus 로고    scopus 로고
    • Nidogen-2: A new basement membrane protein with diverse binding properties
    • Kohfeldt, E., Sasaki, T., Göhring, W., and Timpl, R. (1998). Nidogen-2: A new basement membrane protein with diverse binding properties. J. Mol. Biol. 282, 99-109.
    • (1998) J. Mol. Biol. , vol.282 , pp. 99-109
    • Kohfeldt, E.1    Sasaki, T.2    Göhring, W.3    Timpl, R.4
  • 20
    • 0031820133 scopus 로고    scopus 로고
    • Entactin-2: A new member of basement membrane protein with high homology to entactin/nidogen
    • Kimura, N., Toyoshima, T., Kojima, T., and Shimane, M. (1998). Entactin-2: A new member of basement membrane protein with high homology to entactin/nidogen. Exp. Cell. Res. 241, 36-45.
    • (1998) Exp. Cell. Res. , vol.241 , pp. 36-45
    • Kimura, N.1    Toyoshima, T.2    Kojima, T.3    Shimane, M.4
  • 22
    • 0029584361 scopus 로고
    • Binding of mouse and human fibulin-2 to extracellular matrix ligands
    • Sasaki, T., Pan, T.-C., Chu, M.-L., and Timpl, R. (1995). Binding of mouse and human fibulin-2 to extracellular matrix ligands. J. Mol. Biol. 254, 892-899.
    • (1995) J. Mol. Biol. , vol.254 , pp. 892-899
    • Sasaki, T.1    Pan, T.-C.2    Chu, M.-L.3    Timpl, R.4
  • 23
    • 0033082328 scopus 로고    scopus 로고
    • Recombinant domain IV of perlecan binds nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin
    • Hopf, M., Göhring, W., Kohfeldt, E., Yamada, Y., and Timpl, R. (1999). Recombinant domain IV of perlecan binds nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin. Eur. J. Biochem. 259, 917-925.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 917-925
    • Hopf, M.1    Göhring, W.2    Kohfeldt, E.3    Yamada, Y.4    Timpl, R.5
  • 24
    • 0023377705 scopus 로고
    • Laminin-nidogen complex: Extraction with chelating agents and structural chracterization
    • Paulsson, M., Aumailley, M., Deutzmann, R., Timpl, R., Beck, K., and Engel, J. (1987). Laminin-nidogen complex: Extraction with chelating agents and structural chracterization. Eur. J. Biochem. 166, 11-19.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 11-19
    • Paulsson, M.1    Aumailley, M.2    Deutzmann, R.3    Timpl, R.4    Beck, K.5    Engel, J.6
  • 25
    • 0025881189 scopus 로고
    • Characterization of a type IV collagen major cell binding site with affinity to the α1β1 and α2β1 integrins
    • Vandenberg, P., Kern, A., Ries, A., Lückenbill-Edds, L., Mann, K., and Kühn, K. (1991). Characterization of a type IV collagen major cell binding site with affinity to the α1β1 and α2β1 integrins. J. Cell. Biol. 113, 1475-1483.
    • (1991) J. Cell. Biol. , vol.113 , pp. 1475-1483
    • Vandenberg, P.1    Kern, A.2    Ries, A.3    Lückenbill-Edds, L.4    Mann, K.5    Kühn, K.6
  • 26
    • 0028149335 scopus 로고
    • Binding of purified collagen receptors (α1β1, α2β1) and RGD-dependent integrins to laminins and laminin fragments
    • Pfaff, M., Göhring, W., Brown, J. C., and Timpl, R. (1994). Binding of purified collagen receptors (α1β1, α2β1) and RGD-dependent integrins to laminins and laminin fragments. Eur. J. Biochem. 225, 975-984.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 975-984
    • Pfaff, M.1    Göhring, W.2    Brown, J.C.3    Timpl, R.4
  • 27
    • 0030804282 scopus 로고    scopus 로고
    • Properties of the extracellular calcium binding module of the proteoglycan testican
    • Kohfeldt, E., Maurer, P., Vannahme, C., and Timpl, R. (1997). Properties of the extracellular calcium binding module of the proteoglycan testican. FEBS Lett. 414, 557-561.
    • (1997) FEBS Lett. , vol.414 , pp. 557-561
    • Kohfeldt, E.1    Maurer, P.2    Vannahme, C.3    Timpl, R.4
  • 28
    • 0024460533 scopus 로고
    • Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV
    • Aumailley, M., Wiedemann, H., Mann, K., and Timpl, R. (1989). Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV. Eur. J. Biochem. 184, 241-248.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 241-248
    • Aumailley, M.1    Wiedemann, H.2    Mann, K.3    Timpl, R.4
  • 29
    • 0032126693 scopus 로고    scopus 로고
    • Mapping of the binding of platelet-derived growth factor to distinct domains of the basement membrane proteins BM-40 and perlecan and distinction from the BM-40 collagen-binding epitope
    • Göhring, W., Sasaki, T., Heldin, C.-H., and Timpl, R. (1998). Mapping of the binding of platelet-derived growth factor to distinct domains of the basement membrane proteins BM-40 and perlecan and distinction from the BM-40 collagen-binding epitope. Eur. J. Biochem. 255, 60-66.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 60-66
    • Göhring, W.1    Sasaki, T.2    Heldin, C.-H.3    Timpl, R.4
  • 30
    • 0024559992 scopus 로고
    • Cell attachment properties of collagen type VI and Arg-Gly-Asp dependent binding to its α2(IV) and α3(IV) chains
    • Aumailley, M., Mann, K., von der Mark, K., and Timpl, R. (1989). Cell attachment properties of collagen type VI and Arg-Gly-Asp dependent binding to its α2(IV) and α3(IV) chains. Exp. Cell. Res. 181, 463-474.
    • (1989) Exp. Cell. Res. , vol.181 , pp. 463-474
    • Aumailley, M.1    Mann, K.2    Von der Mark, K.3    Timpl, R.4
  • 31
    • 0027324217 scopus 로고
    • Structural basis of β1 integrin-mediated cell adhesion to a large heparan sulphate proteoglycan from basement membranes
    • Battaglia, C., Aumailley, M., Mann, K., Mayer, U., and Timpl, R. (1993). Structural basis of β1 integrin-mediated cell adhesion to a large heparan sulphate proteoglycan from basement membranes. Eur. J. Cell. Biol. 61, 92-99.
    • (1993) Eur. J. Cell. Biol. , vol.61 , pp. 92-99
    • Battaglia, C.1    Aumailley, M.2    Mann, K.3    Mayer, U.4    Timpl, R.5
  • 32
    • 0020011438 scopus 로고
    • Antibodies to collagens and procollagens
    • Timpl, R. (1982). Antibodies to collagens and procollagens. Methods Enzymol. 82, 472-498.
    • (1982) Methods Enzymol. , vol.82 , pp. 472-498
    • Timpl, R.1
  • 33
    • 0032850748 scopus 로고    scopus 로고
    • Angiogenesis inhibitor endostatin is a distinct component of elastic fibers in vessel walls
    • Miosge, N., Sasaki, T., and Timpl, R. (1999). Angiogenesis inhibitor endostatin is a distinct component of elastic fibers in vessel walls. FASEB J. 13, 1743-1750.
    • (1999) FASEB J. , vol.13 , pp. 1743-1750
    • Miosge, N.1    Sasaki, T.2    Timpl, R.3
  • 34
    • 4244028214 scopus 로고
    • Amino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for laminin, collagen IV and cells
    • Mann, K., Deutzmann, R., Aumailley, M., Timpl, R., Raimondi, L., Yamada, Y., Pan, T., Conway, D., and Chu, M.-L. (1989). Amino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for laminin, collagen IV and cells. EMBO J. 12, 1879-1885.
    • (1989) EMBO J. , vol.12 , pp. 1879-1885
    • Mann, K.1    Deutzmann, R.2    Aumailley, M.3    Timpl, R.4    Raimondi, L.5    Yamada, Y.6    Pan, T.7    Conway, D.8    Chu, M.-L.9
  • 35
    • 0030669942 scopus 로고    scopus 로고
    • Differential expression of laminin α chains during murine tooth development
    • Salmivirta, K., Sorokin, L. M., and Ekblom, P. (1997). Differential expression of laminin α chains during murine tooth development. Dev. Dyn. 210, 206-215.
    • (1997) Dev. Dyn. , vol.210 , pp. 206-215
    • Salmivirta, K.1    Sorokin, L.M.2    Ekblom, P.3
  • 36
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986). A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14, 4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 37
    • 0024228420 scopus 로고
    • Amino acid sequence and domain structure of entactin: Homology with epidermal growth factor precursor and low density lipoprotein receptor
    • Durkin, M. E., Chakravarti, S., Bartos, B. B., Liu, S.-H., Friedman, R. L., and Chung, A. (1988). Amino acid sequence and domain structure of entactin: Homology with epidermal growth factor precursor and low density lipoprotein receptor. J. Cell. Biol. 107, 2749-2756.
    • (1988) J. Cell. Biol. , vol.107 , pp. 2749-2756
    • Durkin, M.E.1    Chakravarti, S.2    Bartos, B.B.3    Liu, S.-H.4    Friedman, R.L.5    Chung, A.6
  • 38
    • 0027410419 scopus 로고
    • Analysis of sequence requirements for protein tyrosine sulfation
    • Rosenquist, G. L., and Nicholas, H. B., Jr. (1993). Analysis of sequence requirements for protein tyrosine sulfation. Protein Sci. 2, 215-222.
    • (1993) Protein Sci. , vol.2 , pp. 215-222
    • Rosenquist, G.L.1    Nicholas H.B., Jr.2
  • 39
    • 0026725843 scopus 로고
    • The receptor for basement membrane glycoprotein entactin is the integrin α3β1
    • Dedhar, S., Jewell, K., Roijani, M., and Gray, V. (1992). The receptor for basement membrane glycoprotein entactin is the integrin α3β1. J. Biol. Chem. 267, 18908-18914.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18908-18914
    • Dedhar, S.1    Jewell, K.2    Roijani, M.3    Gray, V.4
  • 40
    • 0029072783 scopus 로고
    • Two distinct cell attachment sites in entactin are revealed by amino acid substitutions and deletion of the RGD sequence in the cysteine-rich epidermal growth factor repeat 2
    • Dong, L.-J., Hsieh, J.-C., and Chung, A. E. (1995). Two distinct cell attachment sites in entactin are revealed by amino acid substitutions and deletion of the RGD sequence in the cysteine-rich epidermal growth factor repeat 2. J. Biol. Chem. 270, 15838-15843.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15838-15843
    • Dong, L.-J.1    Hsieh, J.-C.2    Chung, A.E.3
  • 41
    • 0029805953 scopus 로고    scopus 로고
    • Domain-specific interactions between entactin and neutrophil integrins. G2 domain ligation of integrin α3β1 and E domain ligation of the leukocyte response integrin signal for different responses
    • Gresham, H. D., Graham, I. L., Griffin, G. L., Hsieh, J.-C., Dong, L.-J., Chung, A. E., and Senior, R. M. (1996). Domain-specific interactions between entactin and neutrophil integrins. G2 domain ligation of integrin α3β1 and E domain ligation of the leukocyte response integrin signal for different responses. J. Biol. Chem. 271, 30587-30594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30587-30594
    • Gresham, H.D.1    Graham, I.L.2    Griffin, G.L.3    Hsieh, J.-C.4    Dong, L.-J.5    Chung, A.E.6    Senior, R.M.7
  • 42
    • 0027422810 scopus 로고
    • Downregulation of tenascin expression by glucocorticoids in bone marrow stromal cells and in fibroblasts
    • Ekblom, M., Fässler, R., Thomasini-Johansson, B., Nilsson, K., and Ekblom, P. (1993). Downregulation of tenascin expression by glucocorticoids in bone marrow stromal cells and in fibroblasts. J. Cell. Biol. 123, 1037-1045.
    • (1993) J. Cell. Biol. , vol.123 , pp. 1037-1045
    • Ekblom, M.1    Fässler, R.2    Thomasini-Johansson, B.3    Nilsson, K.4    Ekblom, P.5
  • 43
    • 0032491379 scopus 로고    scopus 로고
    • An extracellular β-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursors, and extracellular matrix components
    • Springer, T. A. (1998). An extracellular β-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursors, and extracellular matrix components. J. Mol. Biol. 283, 837-862.
    • (1998) J. Mol. Biol. , vol.283 , pp. 837-862
    • Springer, T.A.1
  • 44
    • 0023924807 scopus 로고
    • Human laminin B2 chain: Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains
    • Pikkarainen, T., Kallunki, T., and Tryggvason, K. (1988). Human laminin B2 chain: Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains. J. Biol. Chem. 263, 6751-6758.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6751-6758
    • Pikkarainen, T.1    Kallunki, T.2    Tryggvason, K.3
  • 45
    • 0030919488 scopus 로고    scopus 로고
    • The laminin α chains: Expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel α3 isoform
    • Miner, J. H., Patton, B. L., Lentz, S. I., Gilbert, D. J., Snider, W. D., Jenkins, N. A., Copeland, N. G., and Sanes, J. R. (1997). The laminin α chains: Expression, developmental transitions, and chromosomal locations of α1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel 33 isoform. J. Cell. Biol. 137, 685-701.
    • (1997) J. Cell. Biol. , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6    Copeland, N.G.7    Sanes, J.R.8
  • 47
    • 0027279422 scopus 로고
    • Genes coding for basement membrane glycoproteins laminin, nidogen and collagen IV are differentially expressed in the nervous system and by epithelial, endothelial and mesenchymal cells of the mouse embryo
    • Thomas, T., and Dziadek, M. (1993). Genes coding for basement membrane glycoproteins laminin, nidogen and collagen IV are differentially expressed in the nervous system and by epithelial, endothelial and mesenchymal cells of the mouse embryo. Exp. Cell. Res. 208, 54-67.
    • (1993) Exp. Cell. Res. , vol.208 , pp. 54-67
    • Thomas, T.1    Dziadek, M.2
  • 49
    • 0034108469 scopus 로고    scopus 로고
    • Nidogen-1 regulates laminin-1-dependent mammary-specific gene expression
    • Pujuguet, P., Simian, M., Law, J., Timpl, R., Werb, Z., and Bissell, M. J. (2000). Nidogen-1 regulates laminin-1-dependent mammary-specific gene expression. J. Cell. Sci. 113, 849-858.
    • (2000) J. Cell. Sci. , vol.113 , pp. 849-858
    • Pujuguet, P.1    Simian, M.2    Law, J.3    Timpl, R.4    Werb, Z.5    Bissell, M.J.6
  • 50
  • 53
    • 0030587609 scopus 로고    scopus 로고
    • Development of aortic vessel wall as defined by vascular smooth muscle and extracellular matrix markers
    • Hungerford, J. E., Owens, G. K., Argraves, W. S., and Little, C. D. (1996). Development of aortic vessel wall as defined by vascular smooth muscle and extracellular matrix markers. Dev. Biol. 178, 375-392.
    • (1996) Dev. Biol. , vol.178 , pp. 375-392
    • Hungerford, J.E.1    Owens, G.K.2    Argraves, W.S.3    Little, C.D.4
  • 54
    • 0029935171 scopus 로고    scopus 로고
    • Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo
    • Zhang, H.-Y., Timpl, R., Sasaki, T., Chu, M.-L., and Ekblom, P. (1996). Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo. Dev. Dyn. 205, 348-364.
    • (1996) Dev. Dyn. , vol.205 , pp. 348-364
    • Zhang, H.-Y.1    Timpl, R.2    Sasaki, T.3    Chu, M.-L.4    Ekblom, P.5
  • 55
    • 0034802720 scopus 로고    scopus 로고
    • Perinatal lethality and endothelial cell abnormalities in several vessel compartments of fibulin-1-deficient mice
    • Kostka, G., Giltay, R., Bloch, W., Addicks, K., Timpl, R., Fässler, R., and Chu, M.-L. (2001). Perinatal lethality and endothelial cell abnormalities in several vessel compartments of fibulin-1-deficient mice. Mol. Cell. Biol. 20, 7025-7034.
    • (2001) Mol. Cell. Biol. , vol.20 , pp. 7025-7034
    • Kostka, G.1    Giltay, R.2    Bloch, W.3    Addicks, K.4    Timpl, R.5    Fässler, R.6    Chu, M.-L.7
  • 58
    • 0035824882 scopus 로고    scopus 로고
    • Short arm region of laminin-5 γ2 chain: Structure, mechanisms of processing and binding to heparin and proteins
    • Sasaki, T., Göhring, W., Mann, K., Brakebusch, C., Yamada, Y., Fässler, R., and Timpl, R. (2001). Short arm region of laminin-5 γ2 chain: Structure, mechanisms of processing and binding to heparin and proteins. J. Mol. Biol. 314, 761-763.
    • (2001) J. Mol. Biol. , vol.314 , pp. 761-763
    • Sasaki, T.1    Göhring, W.2    Mann, K.3    Brakebusch, C.4    Yamada, Y.5    Fässler, R.6    Timpl, R.7


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