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Volumn 9, Issue 3, 1998, Pages 671-683

PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM domain protein RIL

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; PROTEIN; PROTEIN TYROSINE PHOSPHATASE; TYROSINE;

EID: 0031916105     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.3.671     Document Type: Article
Times cited : (128)

References (61)
  • 2
    • 0030024632 scopus 로고    scopus 로고
    • Specificity of single LIM motifs in targeting and LIM/LIM interactions in situ
    • Arber, S., and Caroni, P. (1996). Specificity of single LIM motifs in targeting and LIM/LIM interactions in situ. Genes Dev. 10, 289-300.
    • (1996) Genes Dev. , vol.10 , pp. 289-300
    • Arber, S.1    Caroni, P.2
  • 3
    • 0028026907 scopus 로고
    • A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases
    • Banville, D., Ahmad, S., Stocco, R., and Shen, S.H. (1994). A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases. J. Biol. Chem. 269, 22320-22327.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22320-22327
    • Banville, D.1    Ahmad, S.2    Stocco, R.3    Shen, S.H.4
  • 4
    • 0027725232 scopus 로고
    • Expanded, a negative regulator of cell proliferation in Drosophila, shows homology to the NF2 tumor suppressor
    • Boedigheimer, M., Bryant, P., and Laughon, A. (1993). Expanded, a negative regulator of cell proliferation in Drosophila, shows homology to the NF2 tumor suppressor. Mech. Dev. 44, 83-84.
    • (1993) Mech. Dev. , vol.44 , pp. 83-84
    • Boedigheimer, M.1    Bryant, P.2    Laughon, A.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alphal-syntrophin mediated by PDZ domains
    • Brenman, J.E., et al. (1996). Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alphal-syntrophin mediated by PDZ domains. Cell 84, 757-767.
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1
  • 7
    • 0027818550 scopus 로고
    • Tumor suppressor genes encoding proteins required for cell interactions and signal transduction in Drosophila
    • Bryant, P.J., Watson, K.L., Justice, R.W., and Woods, D.F. (1993). Tumor suppressor genes encoding proteins required for cell interactions and signal transduction in Drosophila. Development (suppl), 239-249.
    • (1993) Development (Suppl) , pp. 239-249
    • Bryant, P.J.1    Watson, K.L.2    Justice, R.W.3    Woods, D.F.4
  • 8
    • 0028952473 scopus 로고
    • Characterization of a protein tyrosine phosphatase (RIP) expressed at a very early stage of differentiation in both mouse erythroleukemia and embryonal carcinoma cells
    • Chida, D., Kume, T., Mukouyama, Y., Tabata, S., Nomura, N., Thomas, M.L., Watanabe, T., and Oishi, M. (1995). Characterization of a protein tyrosine phosphatase (RIP) expressed at a very early stage of differentiation in both mouse erythroleukemia and embryonal carcinoma cells. FEBS Lett. 358, 233-239.
    • (1995) FEBS Lett. , vol.358 , pp. 233-239
    • Chida, D.1    Kume, T.2    Mukouyama, Y.3    Tabata, S.4    Nomura, N.5    Thomas, M.L.6    Watanabe, T.7    Oishi, M.8
  • 9
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho, K.-O., Hunt, C.A., and Kennedy, M.B. (1992). The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron 9, 929-942.
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.-O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 10
    • 0028895654 scopus 로고
    • Modular binding domains in signal transducing proteins
    • Cohen, G.B., Ren, R., and Baltimore, D. (1995). Modular binding domains in signal transducing proteins. Cell 80, 237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 11
    • 0030778437 scopus 로고    scopus 로고
    • No evidence for involvement of mouse protein-tyrosine phosphatase-BAS-like/Fas-associated phosphatase-1 in Fas-mediated apoptosis
    • Cuppen, E., Nagata, S., Wieringa, B., and Hendriks, W. (1997). No evidence for involvement of mouse protein-tyrosine phosphatase-BAS-like/Fas-associated phosphatase-1 in Fas-mediated apoptosis. J. Biol. Chem. 272, 30215-30220.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30215-30220
    • Cuppen, E.1    Nagata, S.2    Wieringa, B.3    Hendriks, W.4
  • 13
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free mem- Brane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle, D.A., Lee, A., Lewis, J., Kim, E., Sheng, M., and MacKinnon, R. (1996). Crystal structures of a complexed and peptide-free mem- brane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85, 1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 14
    • 0028843736 scopus 로고
    • Asymmetrically distributed PAR-3 protein contributes to cell polarity and spindle alignment in early C. elegans embryos
    • Etemad Moghadam, B., Guo, S., and Kemphues, K.J. (1995). Asymmetrically distributed PAR-3 protein contributes to cell polarity and spindle alignment in early C. elegans embryos. Cell 83, 743-752.
    • (1995) Cell , vol.83 , pp. 743-752
    • Etemad Moghadam, B.1    Guo, S.2    Kemphues, K.J.3
  • 15
    • 0030293766 scopus 로고    scopus 로고
    • Protein-protein interactions: PDZ domain networks
    • Fanning, A.S., and Anderson, J.M. (1996). Protein-protein interactions: PDZ domain networks. Curr. Biol. 6, 1385-1388.
    • (1996) Curr. Biol. , vol.6 , pp. 1385-1388
    • Fanning, A.S.1    Anderson, J.M.2
  • 17
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni, J.V., and Neel, B.G. (1993). Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal. Biochem. 220, 179-187.
    • (1993) Anal. Biochem. , vol.220 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 18
    • 15844375659 scopus 로고    scopus 로고
    • LIMK-1 hemizygosity implicated in impaired visuospatial constructive cognition
    • Frangiskakis, J.M., et al. (1996). LIMK-1 hemizygosity implicated in impaired visuospatial constructive cognition. Cell 86, 59-69.
    • (1996) Cell , vol.86 , pp. 59-69
    • Frangiskakis, J.M.1
  • 19
    • 0030296378 scopus 로고    scopus 로고
    • Synaptic proteins and the assembly of synaptic junctions
    • Garner, C.C. (1996). Synaptic proteins and the assembly of synaptic junctions. Trends Cell Biol. 6, 429-433.
    • (1996) Trends Cell Biol. , vol.6 , pp. 429-433
    • Garner, C.C.1
  • 20
    • 0029978023 scopus 로고    scopus 로고
    • Clustering membrane proteins: It's all coming together with the PSD-95/SAP90 protein family
    • Gomperts, S.N. (1996). Clustering membrane proteins: it's all coming together with the PSD-95/SAP90 protein family. Cell 84, 659-662.
    • (1996) Cell , vol.84 , pp. 659-662
    • Gomperts, S.N.1
  • 21
    • 0024283936 scopus 로고
    • A versatile in vivo and in vitro eukaryotic expression vector for protein engineering
    • Green, S., Issemann, I., and Sheer, E. (1988). A versatile in vivo and in vitro eukaryotic expression vector for protein engineering. Nucleic Acids Res. 26, 369.
    • (1988) Nucleic Acids Res. , vol.26 , pp. 369
    • Green, S.1    Issemann, I.2    Sheer, E.3
  • 22
    • 0027437850 scopus 로고
    • Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2
    • Gyuris, J., Golemis, E., Chertkov, H., and Brent, R. (1993). Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 75, 791-803.
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemis, E.2    Chertkov, H.3    Brent, R.4
  • 23
    • 0029816885 scopus 로고    scopus 로고
    • Solution structure of a naturally occurring zinc-peptide complex demonstrates that the N-terminal zinc-binding module of the Lasp-1 LIM domain is an independent folding unit
    • Hammarstrom, A., Berndt, K.D., Sillard, R., Adermann, K., and Otting, G. (1996). Solution structure of a naturally occurring zinc-peptide complex demonstrates that the N-terminal zinc-binding module of the Lasp-1 LIM domain is an independent folding unit. Biochemistry 35, 12723-12732.
    • (1996) Biochemistry , vol.35 , pp. 12723-12732
    • Hammarstrom, A.1    Berndt, K.D.2    Sillard, R.3    Adermann, K.4    Otting, G.5
  • 24
    • 0030576521 scopus 로고    scopus 로고
    • Peptide-surface association: The case of PDZ and PTB domains
    • Harrison, S.C. (1996). Peptide-surface association: the case of PDZ and PTB domains. Cell 86, 341-343.
    • (1996) Cell , vol.86 , pp. 341-343
    • Harrison, S.C.1
  • 26
    • 0030067804 scopus 로고    scopus 로고
    • The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins
    • Hoskins, R., Hajnal, A.F., Harp, S.A., and Kim, S.K. (1996). The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins. Development 122, 97-111.
    • (1996) Development , vol.122 , pp. 97-111
    • Hoskins, R.1    Hajnal, A.F.2    Harp, S.A.3    Kim, S.K.4
  • 27
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter, T. (1995). Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80, 225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 28
    • 0030041409 scopus 로고    scopus 로고
    • PTPN13, a Fasassociated protein tyrosine phosphatase, is located on the long arm of chromosome 4 at band q21.3
    • Inazawa, J., Ariyama, T., Abe, T., Druck, T., Ohta, M., Huebner, K., Yanagisawa, J., Reed, J.C., and Sato, T. (1996). PTPN13, a Fasassociated protein tyrosine phosphatase, is located on the long arm of chromosome 4 at band q21.3. Genomics 32, 240-242.
    • (1996) Genomics , vol.32 , pp. 240-242
    • Inazawa, J.1    Ariyama, T.2    Abe, T.3    Druck, T.4    Ohta, M.5    Huebner, K.6    Yanagisawa, J.7    Reed, J.C.8    Sato, T.9
  • 29
    • 0028812412 scopus 로고
    • Expression of RIL, a novel LIM domain gene, is down-regulated in Hras-transformed cells and restored in phenotypic revertants
    • Kiess, M., Scharm, B., Aguzzi, A., Hajnal, A., Klemenz, R., Schwarte Waldhoff, I., and Schafer, R. (1995). Expression of RIL, a novel LIM domain gene, is down-regulated in Hras-transformed cells and restored in phenotypic revertants. Oncogene 20, 61-68.
    • (1995) Oncogene , vol.20 , pp. 61-68
    • Kiess, M.1    Scharm, B.2    Aguzzi, A.3    Hajnal, A.4    Klemenz, R.5    Schwarte Waldhoff, I.6    Schafer, R.7
  • 30
    • 0028882810 scopus 로고
    • Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases
    • Kim, E., Niethammer, M., Rothschild, A., Jan, Y.N., and Sheng, M. (1995). Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases. Nature 378, 85-88.
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1    Niethammer, M.2    Rothschild, A.3    Jan, Y.N.4    Sheng, M.5
  • 31
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H.C., Schenker, L.T., Kennedy, M.B., and Seeburg, P.H. (1995). Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269, 1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 32
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon, M.A., Ferguson, K.M., and Schlessinger, J. (1996). PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85, 621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 33
    • 0028040007 scopus 로고
    • Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats
    • Maekawa, K., Imagawa, N., Nagamatsu, M., and Harada, S. (1994). Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats. FEBS Lett, 337, 200-206.
    • (1994) FEBS Lett , vol.337 , pp. 200-206
    • Maekawa, K.1    Imagawa, N.2    Nagamatsu, M.3    Harada, S.4
  • 34
    • 0028299432 scopus 로고
    • "Zip codes" direct intracellular protein tyrosine phosphatases to the correct cellular "address."
    • Mauro, L.J., and Dixon, J.E. (1994). "Zip codes" direct intracellular protein tyrosine phosphatases to the correct cellular "address." Trends Biochem. Sci. 79, 151-155.
    • (1994) Trends Biochem. Sci. , vol.79 , pp. 151-155
    • Mauro, L.J.1    Dixon, J.E.2
  • 35
    • 0028987993 scopus 로고
    • Canoe encodes a novel protein containing a GLGF/DHR motif and functions with notch and scabrous in common developmental pathways in Drosovhila
    • Miyamoto, H., Nihonmatsu, I., Kondo, S., Ueda, R., Togashi, S., Hirata, K., Ikegami, Y., and Yamamoto, D. (1995). Canoe encodes a novel protein containing a GLGF/DHR motif and functions with notch and scabrous in common developmental pathways in Drosovhila. Genes Dev. 9, 612-625.
    • (1995) Genes Dev. , vol.9 , pp. 612-625
    • Miyamoto, H.1    Nihonmatsu, I.2    Kondo, S.3    Ueda, R.4    Togashi, S.5    Hirata, K.6    Ikegami, Y.7    Yamamoto, D.8
  • 37
    • 0029946167 scopus 로고    scopus 로고
    • Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
    • Niethammer, M., Kim, E., and Sheng, M. (1996). Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J. Neurosci. 16, 2157-2163.
    • (1996) J. Neurosci. , vol.16 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 38
    • 0029594144 scopus 로고
    • Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs
    • Okano, I., Hiraoka, J., Otera, H., Nunoue, K., Ohashi, K., Iwashita, S., Hirai, M., and Mizuno, K. (1995). Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs. J. Biol. Chem. 270, 31321-31330.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31321-31330
    • Okano, I.1    Hiraoka, J.2    Otera, H.3    Nunoue, K.4    Ohashi, K.5    Iwashita, S.6    Hirai, M.7    Mizuno, K.8
  • 39
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. (1995). Protein modules and signalling networks. Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 41
    • 0028902098 scopus 로고
    • DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins
    • Ponting, C.P., and Phillips, C. (1995). DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins. Trends Biochem. Sci. 20, 102-103.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 102-103
    • Ponting, C.P.1    Phillips, C.2
  • 42
    • 0028003644 scopus 로고
    • Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins
    • Saras, J., Claesson Welsh, L., Heldin, C.H., and Gonez, L.J. (1994). Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins. J. Biol. Chem. 269, 24082-24089.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24082-24089
    • Saras, J.1    Claesson Welsh, L.2    Heldin, C.H.3    Gonez, L.J.4
  • 43
    • 0030772973 scopus 로고    scopus 로고
    • Characterization of the interactions between PDZ domains of the protein-tyrosine phosphatase PTPL1 and the carboxyl-terminal tail of Fas
    • Saras, J., Engström, U., Gonez, L.J., and Heldin, C.H. (1997a). Characterization of the interactions between PDZ domains of the protein-tyrosine phosphatase PTPL1 and the carboxyl-terminal tail of Fas. J. Biol. Chem. 272, 20979-20981.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20979-20981
    • Saras, J.1    Engström, U.2    Gonez, L.J.3    Heldin, C.H.4
  • 44
    • 0030763619 scopus 로고    scopus 로고
    • A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1
    • Saras, J., Franzen, P., Aspenstrom, P., Hellman, U., Gonez, L.J., and Heldin, C.H. (1997b). A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1. J. Biol. Chem. 272, 24333-24338.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24333-24338
    • Saras, J.1    Franzen, P.2    Aspenstrom, P.3    Hellman, U.4    Gonez, L.J.5    Heldin, C.H.6
  • 45
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with Fas
    • Sato, T., Irie, S., Kitada, S., and Reed, J.C. (1995). FAP-1: a protein tyrosine phosphatase that associates with Fas. Science 268, 411-415.
    • (1995) Science , vol.268 , pp. 411-415
    • Sato, T.1    Irie, S.2    Kitada, S.3    Reed, J.C.4
  • 46
    • 0030995719 scopus 로고    scopus 로고
    • The neuronal nitric oxide synthase PDZ motif binds to -GDXV* carboxyterminal sequences
    • Schepens, J., Cuppen, E., Wieringa, B., and Hendriks, W. (1997). The neuronal nitric oxide synthase PDZ motif binds to -GDXV* carboxyterminal sequences. FEBS Lett. 409, 53-56.
    • (1997) FEBS Lett. , vol.409 , pp. 53-56
    • Schepens, J.1    Cuppen, E.2    Wieringa, B.3    Hendriks, W.4
  • 47
    • 0000507749 scopus 로고
    • ed. M.O. Dayhoff, Washington, DC: National Biomedical Research Foundation
    • Schwartz, R.M., and Dayhoff, M.O. (1979). In: Atlas of Protein Sequence and Structure, ed. M.O. Dayhoff, Washington, DC: National Biomedical Research Foundation, 353-358.
    • (1979) Atlas of Protein Sequence and Structure , pp. 353-358
    • Schwartz, R.M.1    Dayhoff, M.O.2
  • 48
    • 0029019297 scopus 로고
    • The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions
    • Serra Pages, C., Kedersha, N.L., Fazikas, L., Medley, Q., Debant, A., and Streuli, M. (1995). The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions. EMBO J. 14, 2827-2838.
    • (1995) EMBO J. , vol.14 , pp. 2827-2838
    • Serra Pages, C.1    Kedersha, N.L.2    Fazikas, L.3    Medley, Q.4    Debant, A.5    Streuli, M.6
  • 49
    • 0029664550 scopus 로고    scopus 로고
    • 2+ channel by INAD in Drosophila photoreceptors
    • 2+ channel by INAD in Drosophila photoreceptors. Neuron 16, 991-998.
    • (1996) Neuron , vol.16 , pp. 991-998
    • Shieh, B.H.1    Zhu, M.Y.2
  • 50
    • 0029993728 scopus 로고    scopus 로고
    • LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction
    • Simske, J.S., Kaech, S.M., Harp, S.A., and Kim, S.K. (1996). LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction. Cell 85, 195-204.
    • (1996) Cell , vol.85 , pp. 195-204
    • Simske, J.S.1    Kaech, S.M.2    Harp, S.A.3    Kim, S.K.4
  • 51
    • 0028875162 scopus 로고
    • Recognition and specificity in protein tyrosine kinase mediated signalling
    • Songyang, Z., and Cantley, L.Z. (1995). Recognition and specificity in protein tyrosine kinase mediated signalling. Trends Biochem. Sci. 20, 470-475.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 470-475
    • Songyang, Z.1    Cantley, L.Z.2
  • 54
    • 0028178391 scopus 로고
    • Dishevelled is required during wingless signaling to establish both cell polarity and cell identity
    • Theisen, H., Purcell, J., Bennett, M., Kansagara, D., Syed, A., and Marsh, J.L. (1994). Dishevelled is required during wingless signaling to establish both cell polarity and cell identity. Development 120, 347-360.
    • (1994) Development , vol.120 , pp. 347-360
    • Theisen, H.1    Purcell, J.2    Bennett, M.3    Kansagara, D.4    Syed, A.5    Marsh, J.L.6
  • 55
    • 0027380638 scopus 로고
    • Submembranous junctional plaque proteins include potential tumor suppressor molecules
    • Tsukita, S., Itoh, M., Nagafuchi, A., Yonemura, S., and Tsukita, S. (1993). Submembranous junctional plaque proteins include potential tumor suppressor molecules. J. Cell Biol. 123, 1049-1053.
    • (1993) J. Cell Biol. , vol.123 , pp. 1049-1053
    • Tsukita, S.1    Itoh, M.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, S.5
  • 56
    • 0029814674 scopus 로고    scopus 로고
    • The gene (PTPN13) encoding the protein tyrosine phosphatase PTP-BL/PTP-BAS is located in mouse chromosome region 5E/F and human chromosome region 4q21
    • van den Maagdenberg, A.M., Olde Weghuis, D., Rijss, J., Merkx, G.F., Wieringa, B., Geurts van Kessel, A., and Hendriks, W.J. (1996). The gene (PTPN13) encoding the protein tyrosine phosphatase PTP-BL/PTP-BAS is located in mouse chromosome region 5E/F and human chromosome region 4q21. Cytogenet. Cell Genet. 74, 153-155.
    • (1996) Cytogenet. Cell Genet. , vol.74 , pp. 153-155
    • Van den Maagdenberg, A.M.1    Olde Weghuis, D.2    Rijss, J.3    Merkx, G.F.4    Wieringa, B.5    Geurts van Kessel, A.6    Hendriks, W.J.7
  • 57
    • 0028800393 scopus 로고
    • Cloning of a rat cDNA encoding a novel LIM domain protein with high homology to rat RIL
    • Wang, H., Harrison Shostak, D.C., Lemasters, J.J., and Herman, B. (1995). Cloning of a rat cDNA encoding a novel LIM domain protein with high homology to rat RIL. Gene 265, 267-271.
    • (1995) Gene , vol.265 , pp. 267-271
    • Wang, H.1    Harrison Shostak, D.C.2    Lemasters, J.J.3    Herman, B.4
  • 58
    • 0027768992 scopus 로고
    • ZO-1, DlgA and PSD-95/ SAP90: Homologous proteins in tight, septate and synaptic cell junctions
    • Woods, D.F., and Bryant, P.J. (1993). ZO-1, DlgA and PSD-95/ SAP90: homologous proteins in tight, septate and synaptic cell junctions. Mech. Dev. 44, 85-89.
    • (1993) Mech. Dev. , vol.44 , pp. 85-89
    • Woods, D.F.1    Bryant, P.J.2
  • 59
    • 0029819449 scopus 로고    scopus 로고
    • Dig protein is required for junction structure, cell polarity, and proliferation control in Drosophila epithelia
    • Woods, D.F., Hough, C., Peel, D., Callaini, G., and Bryant, P.J. (1996). Dig protein is required for junction structure, cell polarity, and proliferation control in Drosophila epithelia. J. Cell Biol. 134, 1469-1482.
    • (1996) J. Cell Biol. , vol.134 , pp. 1469-1482
    • Woods, D.F.1    Hough, C.2    Peel, D.3    Callaini, G.4    Bryant, P.J.5
  • 60
    • 0028061406 scopus 로고
    • LIM domain recognition of a tyrosine-containing tight turn
    • Wu, R.Y., and Gill, G.N. (1994). LIM domain recognition of a tyrosine-containing tight turn. J. Biol. Chem. 269, 25085-25090.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25085-25090
    • Wu, R.Y.1    Gill, G.N.2
  • 61
    • 0030827949 scopus 로고    scopus 로고
    • Actinin-associated LIM protein: Identification of a domain interaction between PDZ and spectrin-like repeat motifs
    • Xia, H., Winokur, ST., Kuo, W., Altherr, M.R., and Bredt, D.S. (1997). Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs. J. Cell Biol. 139, 507-515.
    • (1997) J. Cell Biol. , vol.139 , pp. 507-515
    • Xia, H.1    Winokur, S.T.2    Kuo, W.3    Altherr, M.R.4    Bredt, D.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.