메뉴 건너뛰기




Volumn 388, Issue 6, 2007, Pages 561-568

Anti-innexin 2 aptamers specifically inhibit the heterologous interaction of the innexin 2 and innexin 3 carboxyl-termini in vitro

Author keywords

Aptamer; Drosophila; Gap junctions; In vitro selection; Innexin 2; Innexin 3

Indexed keywords

APTAMER; INNEXIN 2; INNEXIN 3; PROTEIN; RNA; UNCLASSIFIED DRUG;

EID: 34249995953     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2007.074     Document Type: Article
Times cited : (8)

References (54)
  • 2
    • 0035853435 scopus 로고    scopus 로고
    • The carboxyl-terminal domain regulates the unitary conductance and voltage dependence of connexin40 gap junction channels
    • Anumonwo, J.M., Taffet, S.M., Gu, H., Chanson, M., Moreno, A.P., and Delmar, M. (2001). The carboxyl-terminal domain regulates the unitary conductance and voltage dependence of connexin40 gap junction channels. Circ. Res. 88, 666-673.
    • (2001) Circ. Res , vol.88 , pp. 666-673
    • Anumonwo, J.M.1    Taffet, S.M.2    Gu, H.3    Chanson, M.4    Moreno, A.P.5    Delmar, M.6
  • 3
    • 0036558284 scopus 로고    scopus 로고
    • The Drosophila gap junction channel gene innexin 2 controls foregut development in response to Wingless signalling
    • Bauer, R., Lehmann, C., Fuss, B., Eckardt, F., and Hoch, M. (2002). The Drosophila gap junction channel gene innexin 2 controls foregut development in response to Wingless signalling. J. Cell Sci. 115, 1859-1867.
    • (2002) J. Cell Sci , vol.115 , pp. 1859-1867
    • Bauer, R.1    Lehmann, C.2    Fuss, B.3    Eckardt, F.4    Hoch, M.5
  • 4
    • 0347126500 scopus 로고    scopus 로고
    • Cellular distribution of innexin 1 and 2 gap junctional channel proteins in epithelia of the Drosophila embryo
    • Bauer, R., Martini, J., Lehmann, C., and Hoch, M. (2003). Cellular distribution of innexin 1 and 2 gap junctional channel proteins in epithelia of the Drosophila embryo. Cell Commun. Adhes. 10, 221-225.
    • (2003) Cell Commun. Adhes , vol.10 , pp. 221-225
    • Bauer, R.1    Martini, J.2    Lehmann, C.3    Hoch, M.4
  • 5
    • 2542471450 scopus 로고    scopus 로고
    • Gap junction channel protein innexin 2 is essential for epithelial morphogenesis in the Drosophila embryo
    • Bauer, R., Lehmann, C., Martini, J., Eckardt, F., and Hoch, M. (2004). Gap junction channel protein innexin 2 is essential for epithelial morphogenesis in the Drosophila embryo. Mol. Biol. Cell 15, 2992-3004.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2992-3004
    • Bauer, R.1    Lehmann, C.2    Martini, J.3    Eckardt, F.4    Hoch, M.5
  • 6
    • 19644398654 scopus 로고    scopus 로고
    • Intercellular communication: The Drosophila innexin multiprotein family of gap junction proteins
    • Bauer, R., Loer, B., Ostrowski, K., Martini, J., Weimbs, A., Lechner, H., and Hoch, M. (2005). Intercellular communication: the Drosophila innexin multiprotein family of gap junction proteins. Chem. Biol. 12, 515-526.
    • (2005) Chem. Biol , vol.12 , pp. 515-526
    • Bauer, R.1    Loer, B.2    Ostrowski, K.3    Martini, J.4    Weimbs, A.5    Lechner, H.6    Hoch, M.7
  • 7
    • 33646091506 scopus 로고    scopus 로고
    • DE-cadherin, a core component of the adherens junction complex modifies subcellular localization of the Drosophila gap junction protein innexin2
    • Bauer, R., Weimbs, A., Lechner, H., and Hoch, M. (2006). DE-cadherin, a core component of the adherens junction complex modifies subcellular localization of the Drosophila gap junction protein innexin2. Cell Commun. Adhes. 13, 103-114.
    • (2006) Cell Commun. Adhes , vol.13 , pp. 103-114
    • Bauer, R.1    Weimbs, A.2    Lechner, H.3    Hoch, M.4
  • 8
    • 0033616819 scopus 로고    scopus 로고
    • Cytoplasmic RNA modulators of an inside-out signal-transduction cascade
    • Blind, M., Kolanus, W., and Famulok, M. (1999). Cytoplasmic RNA modulators of an inside-out signal-transduction cascade. Proc. Natl. Acad. Sci. USA 96, 3606-3610.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3606-3610
    • Blind, M.1    Kolanus, W.2    Famulok, M.3
  • 10
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell, R.C. and Joyce, G.F. (1992). Randomization of genes by PCR mutagenesis. PCR Methods Appl. 2, 28-33.
    • (1992) PCR Methods Appl , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 14
    • 11144285441 scopus 로고    scopus 로고
    • Selection of stable RNA molecules that can regulate the channel-opening equilibrium of the membrane-bound γ-aminobutyric acid receptor
    • Cui, Y., Rajasethupathy, P., and Hess, G.P. (2004). Selection of stable RNA molecules that can regulate the channel-opening equilibrium of the membrane-bound γ-aminobutyric acid receptor. Biochemistry 43, 16442-16449.
    • (2004) Biochemistry , vol.43 , pp. 16442-16449
    • Cui, Y.1    Rajasethupathy, P.2    Hess, G.P.3
  • 15
    • 0347364648 scopus 로고    scopus 로고
    • A tenascin-C aptamer identified by tumor cell SELEX: Systematic evolution of ligands by exponential enrichment
    • Daniels, D.A., Chen, H., Hicke, B.J., Swiderek, K.M., and Gold, L. (2003). A tenascin-C aptamer identified by tumor cell SELEX: systematic evolution of ligands by exponential enrichment. Proc. Natl. Acad. Sci. USA 100, 15416-15421.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15416-15421
    • Daniels, D.A.1    Chen, H.2    Hicke, B.J.3    Swiderek, K.M.4    Gold, L.5
  • 18
    • 12344306475 scopus 로고    scopus 로고
    • Intramers and aptamers: Applications in protein-function analyses and potential for drug screening
    • Famulok, M. and Mayer, G. (2005). Intramers and aptamers: applications in protein-function analyses and potential for drug screening. ChemBioChem 6, 19-26.
    • (2005) ChemBioChem , vol.6 , pp. 19-26
    • Famulok, M.1    Mayer, G.2
  • 19
    • 0036843787 scopus 로고    scopus 로고
    • In vivo-applied functional RNAs as tools in proteomics and genomics research
    • Famulok, M. and Verma, S. (2002). In vivo-applied functional RNAs as tools in proteomics and genomics research. Trends Biotechnol. 20, 462-466.
    • (2002) Trends Biotechnol , vol.20 , pp. 462-466
    • Famulok, M.1    Verma, S.2
  • 20
    • 13144252170 scopus 로고    scopus 로고
    • The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein
    • Giepmans, B.N. and Moolenaar, W.H. (1998). The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein. Curr. Biol. 8, 931-934.
    • (1998) Curr. Biol , vol.8 , pp. 931-934
    • Giepmans, B.N.1    Moolenaar, W.H.2
  • 21
    • 0035754494 scopus 로고    scopus 로고
    • Connexin-43 interactions with ZO-1 and α- and β-tubulin
    • Giepmans, B.N., Verlaan, I., and Moolenaar, W.H. (2001). Connexin-43 interactions with ZO-1 and α- and β-tubulin. Cell Commun. Adhes. 8, 219-223.
    • (2001) Cell Commun. Adhes , vol.8 , pp. 219-223
    • Giepmans, B.N.1    Verlaan, I.2    Moolenaar, W.H.3
  • 22
    • 0032445969 scopus 로고    scopus 로고
    • RNA aptamers that specifically bind to the Ras-binding domain of Raf-1
    • Kimoto, M., Sakamoto, K., Shirouzu, M., Hirao, I., and Yokoyama, S. (1998). RNA aptamers that specifically bind to the Ras-binding domain of Raf-1. FEBS Lett. 441, 322-326.
    • (1998) FEBS Lett , vol.441 , pp. 322-326
    • Kimoto, M.1    Sakamoto, K.2    Shirouzu, M.3    Hirao, I.4    Yokoyama, S.5
  • 23
    • 0031010402 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB
    • Klug, S.J., Hüttenhofer, A., Kromayer, M., and Famulok, M. (1997). In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB. Proc. Natl. Acad. Sci. USA 94, 6676-6681.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6676-6681
    • Klug, S.J.1    Hüttenhofer, A.2    Kromayer, M.3    Famulok, M.4
  • 24
    • 0031183804 scopus 로고    scopus 로고
    • Isolation and characterization of 2′-fluoro-, 2′-amino-, and 2′-fluoro-/amino-modified RNA ligands to human IFN-γ that inhibit receptor binding
    • Kubik, M.F., Bell, C., Fitzwater, T., Watson, S.R., and Tasset, D.M. (1997). Isolation and characterization of 2′-fluoro-, 2′-amino-, and 2′-fluoro-/amino-modified RNA ligands to human IFN-γ that inhibit receptor binding. J. Immunol. 159, 259-267.
    • (1997) J. Immunol , vol.159 , pp. 259-267
    • Kubik, M.F.1    Bell, C.2    Fitzwater, T.3    Watson, S.R.4    Tasset, D.M.5
  • 25
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • Kumar, N.M. and Gilula, N.B. (1996). The gap junction communication channel. Cell 84, 381-388.
    • (1996) Cell , vol.84 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 26
    • 33745427413 scopus 로고    scopus 로고
    • Heteromerization of innexin gap junction proteins regulates epithelial tissue organization in Drosophila
    • Lehmann, C., Lechner, H., Loer, B., Knieps, M., Herrmann, S., Famulok, M., Bauer, R., and Hoch, M. (2006). Heteromerization of innexin gap junction proteins regulates epithelial tissue organization in Drosophila. Mol. Biol. Cell 17, 1676-1685.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1676-1685
    • Lehmann, C.1    Lechner, H.2    Loer, B.3    Knieps, M.4    Herrmann, S.5    Famulok, M.6    Bauer, R.7    Hoch, M.8
  • 27
    • 0028641549 scopus 로고
    • Modified RNA sequence pools for in vitro selection
    • Lin, Y., Qiu, Q., Gill, S.C., and Jayasena, S.D. (1994). Modified RNA sequence pools for in vitro selection. Nucleic Acids Res. 22, 5229-5234.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5229-5234
    • Lin, Y.1    Qiu, Q.2    Gill, S.C.3    Jayasena, S.D.4
  • 28
    • 1942438659 scopus 로고    scopus 로고
    • Incorporation of connexins into plasma membranes and gap junctions
    • Martin, P.E. and Evans, W.H. (2004). Incorporation of connexins into plasma membranes and gap junctions. Cardiovasc. Res. 62, 378-387.
    • (2004) Cardiovasc. Res , vol.62 , pp. 378-387
    • Martin, P.E.1    Evans, W.H.2
  • 30
    • 0029062420 scopus 로고
    • In vitro selection of RNA ligands to substance P
    • Nieuwlandt, D., Wecker, M., and Gold, L. (1995). In vitro selection of RNA ligands to substance P. Biochemistry 34, 5651-5659.
    • (1995) Biochemistry , vol.34 , pp. 5651-5659
    • Nieuwlandt, D.1    Wecker, M.2    Gold, L.3
  • 31
    • 0031012128 scopus 로고    scopus 로고
    • Potent 2′-amino-, and 2′-fluoro-2′-deoxyribonucleotide RNA inhibitors of keratinocyte growth factor
    • Pagratis, N.C., Bell, C., Chang, Y.-F., Jennings, S., Fitzwater, T., Jellinek, D., and Dang, C. (1997). Potent 2′-amino-, and 2′-fluoro-2′-deoxyribonucleotide RNA inhibitors of keratinocyte growth factor. Nat. Biotechnol. 15, 68-73.
    • (1997) Nat. Biotechnol , vol.15 , pp. 68-73
    • Pagratis, N.C.1    Bell, C.2    Chang, Y.-F.3    Jennings, S.4    Fitzwater, T.5    Jellinek, D.6    Dang, C.7
  • 32
    • 24744466474 scopus 로고    scopus 로고
    • Aptamers against extracellular targets for in vivo applications
    • Pestourie, C., Tavitian, B., and Duconge, F. (2005). Aptamers against extracellular targets for in vivo applications. Biochimie 87, 921-930.
    • (2005) Biochimie , vol.87 , pp. 921-930
    • Pestourie, C.1    Tavitian, B.2    Duconge, F.3
  • 34
    • 0035012765 scopus 로고    scopus 로고
    • Innexins get into the gap
    • Phelan, P. and Starich, T.A. (2001). Innexins get into the gap. Bioessays, 23, 388-396.
    • (2001) Bioessays , vol.23 , pp. 388-396
    • Phelan, P.1    Starich, T.A.2
  • 35
    • 0026337408 scopus 로고
    • Kinetic characterization of ribonuclease-resistant 2′-modified hammerhead ribozymes
    • Pieken, W.A., Olsen, D.B., Benseler, F., Aurup, H., and Eckstein, F. (1991). Kinetic characterization of ribonuclease-resistant 2′-modified hammerhead ribozymes. Science 253, 314-317.
    • (1991) Science , vol.253 , pp. 314-317
    • Pieken, W.A.1    Olsen, D.B.2    Benseler, F.3    Aurup, H.4    Eckstein, F.5
  • 38
    • 0037180804 scopus 로고    scopus 로고
    • A ribozyme composed of only two different nucleotides
    • Reader, J.S. and Joyce, G.F. (2002). A ribozyme composed of only two different nucleotides. Nature 420, 841-844.
    • (2002) Nature , vol.420 , pp. 841-844
    • Reader, J.S.1    Joyce, G.F.2
  • 39
    • 33748164764 scopus 로고    scopus 로고
    • RNA aptamers selectively modulate protein recruitment to the cytoplasmic domain of β-secretase BACE1 in vitro
    • Rentmeister, A., Bill, A., Wahle, T., Walter, J., and Famulok, M. (2006). RNA aptamers selectively modulate protein recruitment to the cytoplasmic domain of β-secretase BACE1 in vitro. RNA 12, 1650-1660.
    • (2006) RNA , vol.12 , pp. 1650-1660
    • Rentmeister, A.1    Bill, A.2    Wahle, T.3    Walter, J.4    Famulok, M.5
  • 40
    • 0033581938 scopus 로고    scopus 로고
    • A ribozyme that lacks cytidine
    • Rogers, J. and Joyce, G.F. (1999). A ribozyme that lacks cytidine. Nature 402, 323-325.
    • (1999) Nature , vol.402 , pp. 323-325
    • Rogers, J.1    Joyce, G.F.2
  • 41
    • 0035032445 scopus 로고    scopus 로고
    • The effect of cytidine on the structure and function of an RNA ligase ribozyme
    • Rogers, J. and Joyce, G.F. (2001). The effect of cytidine on the structure and function of an RNA ligase ribozyme. RNA 7, 395-404.
    • (2001) RNA , vol.7 , pp. 395-404
    • Rogers, J.1    Joyce, G.F.2
  • 42
    • 0032493654 scopus 로고    scopus 로고
    • 2′- Fluoropyrimidine RNA-based aptamers to the 165-amino acid form of vascular endothelial growth factor (VEGF165). Inhibition of receptor binding and VEGF-induced vascular permeability through interactions requiring the exon 7-encoded domain
    • Ruckman, J., Green, L.S., Beeson, J., Waugh, S., Gillette, W.L., Henninger, D.D., Claesson, W.L., and Janjic, N. (1998). 2′- Fluoropyrimidine RNA-based aptamers to the 165-amino acid form of vascular endothelial growth factor (VEGF165). Inhibition of receptor binding and VEGF-induced vascular permeability through interactions requiring the exon 7-encoded domain. J. Biol. Chem. 273, 20556-20567.
    • (1998) J. Biol. Chem , vol.273 , pp. 20556-20567
    • Ruckman, J.1    Green, L.S.2    Beeson, J.3    Waugh, S.4    Gillette, W.L.5    Henninger, D.D.6    Claesson, W.L.7    Janjic, N.8
  • 43
    • 0037035519 scopus 로고    scopus 로고
    • Connexin family members target to lipid raft domains and interact with caveolin-1
    • Schubert, A.L., Schubert, W., Spray, D.C., and Lisanti, M.P. (2002). Connexin family members target to lipid raft domains and interact with caveolin-1. Biochemistry 41, 5754-5764.
    • (2002) Biochemistry , vol.41 , pp. 5754-5764
    • Schubert, A.L.1    Schubert, W.2    Spray, D.C.3    Lisanti, M.P.4
  • 44
    • 1642407845 scopus 로고    scopus 로고
    • Regulation of connexin biosynthesis, assembly, gap junction formation, and removal
    • Segretain, D. and Falk, M.M. (2004). Regulation of connexin biosynthesis, assembly, gap junction formation, and removal. Biochim. Biophys. Acta 1662, 3-21.
    • (2004) Biochim. Biophys. Acta , vol.1662 , pp. 3-21
    • Segretain, D.1    Falk, M.M.2
  • 45
    • 0033621140 scopus 로고    scopus 로고
    • RNA aptamers as effective protein antagonists in a multicellular organism
    • Shi, H., Hoffman, B.E., and Lis, J.T. (1999). RNA aptamers as effective protein antagonists in a multicellular organism. Proc. Natl. Acad. Sci. USA 96, 10033-10038.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10033-10038
    • Shi, H.1    Hoffman, B.E.2    Lis, J.T.3
  • 46
    • 1942438964 scopus 로고    scopus 로고
    • Gap junctions and the connexin protein family
    • Söhl, G. and Willecke, K. (2004). Gap junctions and the connexin protein family. Cardiovasc. Res. 62, 228-232.
    • (2004) Cardiovasc. Res , vol.62 , pp. 228-232
    • Söhl, G.1    Willecke, K.2
  • 47
    • 11144230049 scopus 로고    scopus 로고
    • Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1
    • Sorgen, P.L., Duffy, H.S., Sahoo, P., Coombs, W., Delmar, M., and Spray, D.C. (2004). Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. J. Biol. Chem. 279, 54695-54701.
    • (2004) J. Biol. Chem , vol.279 , pp. 54695-54701
    • Sorgen, P.L.1    Duffy, H.S.2    Sahoo, P.3    Coombs, W.4    Delmar, M.5    Spray, D.C.6
  • 48
    • 0029091457 scopus 로고
    • A mutant T7 RNA polymerase as a DNA polymerase
    • Sousa, R. and Padilla, R. (1995). A mutant T7 RNA polymerase as a DNA polymerase. EMBO J. 14, 4609-4621.
    • (1995) EMBO J , vol.14 , pp. 4609-4621
    • Sousa, R.1    Padilla, R.2
  • 49
    • 0035001466 scopus 로고    scopus 로고
    • Streptavidin aptamers: Affinity tags for the study of RNAs and ribonucleoproteins
    • Srisawat, C. and Engelke, D.R. (2001). Streptavidin aptamers: affinity tags for the study of RNAs and ribonucleoproteins. RNA 7, 632-641.
    • (2001) RNA , vol.7 , pp. 632-641
    • Srisawat, C.1    Engelke, D.R.2
  • 52
    • 0035910415 scopus 로고    scopus 로고
    • c-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes
    • Toyofuku, T., Akamatsu, Y., Zhang, H., Kuzuya, T., Tada, M., and Hori, M. (2001). c-Src regulates the interaction between connexin-43 and ZO-1 in cardiac myocytes. J. Biol. Chem. 276, 1780-1788.
    • (2001) J. Biol. Chem , vol.276 , pp. 1780-1788
    • Toyofuku, T.1    Akamatsu, Y.2    Zhang, H.3    Kuzuya, T.4    Tada, M.5    Hori, M.6
  • 53
    • 0030844452 scopus 로고    scopus 로고
    • Selection of RNA aptamers that bind specifically to the NS3 protease of hepatitis C virus
    • Urvil, P.T., Kakiuchi, N., Zhou, D.M., Shimotohno, K., Kumar, P.K., and Nishikawa, S. (1997). Selection of RNA aptamers that bind specifically to the NS3 protease of hepatitis C virus. Eur. J. Biochem. 248, 130-138.
    • (1997) Eur. J. Biochem , vol.248 , pp. 130-138
    • Urvil, P.T.1    Kakiuchi, N.2    Zhou, D.M.3    Shimotohno, K.4    Kumar, P.K.5    Nishikawa, S.6
  • 54
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. (2003). Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31, 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.