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Volumn 42, Issue 19, 2014, Pages 12306-12321

Protein-responsive ribozyme switches in eukaryotic cells

Author keywords

[No Author keywords available]

Indexed keywords

RIBOZYME; MAGNESIUM; PROTEIN;

EID: 84924945394     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku875     Document Type: Article
Times cited : (41)

References (68)
  • 1
    • 0036272874 scopus 로고    scopus 로고
    • Control of transcription termination in bacteria by RNA-binding proteins that modulate RNA structures
    • Stulke, J. (2002) Control of transcription termination in bacteria by RNA-binding proteins that modulate RNA structures. Arch. Microbiol., 177, 433-440.
    • (2002) Arch. Microbiol. , vol.177 , pp. 433-440
    • Stulke, J.1
  • 2
    • 20444478991 scopus 로고    scopus 로고
    • Riboswitches as versatile gene control elements
    • Tucker, B.J. and Breaker, R.R. (2005) Riboswitches as versatile gene control elements. Curr. Opin. Struct. Biol., 15, 342-348.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 342-348
    • Tucker, B.J.1    Breaker, R.R.2
  • 3
    • 27144527479 scopus 로고    scopus 로고
    • Regulation of bacterial gene expression by riboswitches
    • Winkler, W.C. and Breaker, R.R. (2005) Regulation of bacterial gene expression by riboswitches. Annu. Rev. Microbiol., 59, 487-517.
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 487-517
    • Winkler, W.C.1    Breaker, R.R.2
  • 4
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk, C. and Gold, L. (1990) Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science, 249, 505-510.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 5
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • Ellington, A.D. and Szostak, J.W. (1990) In vitro selection of RNA molecules that bind specific ligands. Nature, 346, 818-822.
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 7
    • 84878740598 scopus 로고    scopus 로고
    • Synthesizing oncogenic signal-processing systems that function as both "signal counters" and "signal blockers" in cancer cells
    • Liu, Y., Huang, W., Zhou, D., Han, Y., Duan, Y., Zhang, X., Zhang, H., Jiang, Z., Gui, Y. and Cai, Z. (2013) Synthesizing oncogenic signal-processing systems that function as both "signal counters" and "signal blockers" in cancer cells. Mol. Biosyst., 9, 1909-1918.
    • (2013) Mol. Biosyst. , vol.9 , pp. 1909-1918
    • Liu, Y.1    Huang, W.2    Zhou, D.3    Han, Y.4    Duan, Y.5    Zhang, X.6    Zhang, H.7    Jiang, Z.8    Gui, Y.9    Cai, Z.10
  • 8
    • 33751016378 scopus 로고    scopus 로고
    • Different modes and potencies of translational repression by sequence-specific RNA-protein interaction at the 5-UTR
    • Nie, M. and Htun, H. (2006) Different modes and potencies of translational repression by sequence-specific RNA-protein interaction at the 5-UTR. Nucleic Acids Res., 34, 5528-5540.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 5528-5540
    • Nie, M.1    Htun, H.2
  • 9
    • 78751632678 scopus 로고    scopus 로고
    • Synthetic human cell fate regulation by protein-driven RNA switches
    • Saito, H., Fujita, Y., Kashida, S., Hayashi, K. and Inoue, T. (2011) Synthetic human cell fate regulation by protein-driven RNA switches. Nat. Commun., 2, 160.
    • (2011) Nat. Commun. , vol.2 , pp. 160
    • Saito, H.1    Fujita, Y.2    Kashida, S.3    Hayashi, K.4    Inoue, T.5
  • 11
    • 0032477882 scopus 로고    scopus 로고
    • A translational repression assay procedure (TRAP) for RNA-protein interactions in vivo
    • Paraskeva, E., Atzberger, A. and Hentze, M.W. (1998) A translational repression assay procedure (TRAP) for RNA-protein interactions in vivo. Proc. Natl. Acad. Sci. U.S.A. , 95, 951-956.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 951-956
    • Paraskeva, E.1    Atzberger, A.2    Hentze, M.W.3
  • 12
    • 0028070676 scopus 로고
    • Proteins binding to 5' untranslated region sites: A general mechanism for translational regulation of mRNAs in human and yeast cells
    • Stripecke, R., Oliveira, C.C., McCarthy, J.E. and Hentze, M.W. (1994) Proteins binding to 5' untranslated region sites: A general mechanism for translational regulation of mRNAs in human and yeast cells. Mol. Cell. Biol., 14, 5898-5909.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5898-5909
    • Stripecke, R.1    Oliveira, C.C.2    McCarthy, J.E.3    Hentze, M.W.4
  • 13
    • 78649429678 scopus 로고    scopus 로고
    • Reprogramming cellular behavior with RNA controllers responsive to endogenous proteins
    • Culler, S.J., Hoff, K.G. and Smolke, C.D. (2010) Reprogramming cellular behavior with RNA controllers responsive to endogenous proteins. Science, 330, 1251-1255.
    • (2010) Science , vol.330 , pp. 1251-1255
    • Culler, S.J.1    Hoff, K.G.2    Smolke, C.D.3
  • 14
    • 84875464082 scopus 로고    scopus 로고
    • A versatile cis-blocking and trans-activation strategy for ribozyme characterization
    • Kennedy, A.B., Liang, J.C. and Smolke, C.D. (2013) A versatile cis-blocking and trans-activation strategy for ribozyme characterization. Nucleic Acids Res., 41, e41.
    • (2013) Nucleic Acids Res. , vol.41 , pp. e41
    • Kennedy, A.B.1    Liang, J.C.2    Smolke, C.D.3
  • 15
    • 84874216535 scopus 로고    scopus 로고
    • A yeast-based rapid prototype platform for gene control elements in mammalian cells
    • Wei, K.Y., Chen, Y.Y. and Smolke, C.D. (2013) A yeast-based rapid prototype platform for gene control elements in mammalian cells. Biotechnol. Bioeng., 110, 1201-1210.
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 1201-1210
    • Wei, K.Y.1    Chen, Y.Y.2    Smolke, C.D.3
  • 16
    • 0023663396 scopus 로고
    • Self-cleavage of plus and minus RNAs of a virusoid and a structural model for the active sites
    • Forster, A.C. and Symons, R.H. (1987) Self-cleavage of plus and minus RNAs of a virusoid and a structural model for the active sites. Cell, 49, 211-220.
    • (1987) Cell , vol.49 , pp. 211-220
    • Forster, A.C.1    Symons, R.H.2
  • 18
    • 35448990907 scopus 로고    scopus 로고
    • A modular and extensible RNA-based gene-regulatory platform for engineering cellular function
    • Win, M.N. and Smolke, C.D. (2007) A modular and extensible RNA-based gene-regulatory platform for engineering cellular function. Proc. Natl. Acad. Sci. U.S.A. , 104, 14283-14288.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 14283-14288
    • Win, M.N.1    Smolke, C.D.2
  • 19
    • 54249113318 scopus 로고    scopus 로고
    • Higher-order cellular information processing with synthetic RNA devices
    • Win, M.N. and Smolke, C.D. (2008) Higher-order cellular information processing with synthetic RNA devices. Science, 322, 456-460.
    • (2008) Science , vol.322 , pp. 456-460
    • Win, M.N.1    Smolke, C.D.2
  • 20
    • 84862167101 scopus 로고    scopus 로고
    • High-throughput enzyme evolution in Saccharomyces cerevisiae using a synthetic RNA switch
    • Michener, J.K. and Smolke, C.D. (2012) High-throughput enzyme evolution in Saccharomyces cerevisiae using a synthetic RNA switch. Metab. Eng., 14, 306-316.
    • (2012) Metab. Eng. , vol.14 , pp. 306-316
    • Michener, J.K.1    Smolke, C.D.2
  • 21
    • 77952679687 scopus 로고    scopus 로고
    • Genetic control of mammalian T-cell proliferation with synthetic RNA regulatory systems
    • Chen, Y.Y., Jensen, M.C. and Smolke, C.D. (2010) Genetic control of mammalian T-cell proliferation with synthetic RNA regulatory systems. Proc. Natl. Acad. Sci. U.S.A. , 107, 8531-8536.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 8531-8536
    • Chen, Y.Y.1    Jensen, M.C.2    Smolke, C.D.3
  • 22
    • 84881408628 scopus 로고    scopus 로고
    • Dynamically reshaping signaling networks to program cell fate via genetic controllers
    • Galloway, K.E., Franco, E. and Smolke, C.D. (2013) Dynamically reshaping signaling networks to program cell fate via genetic controllers. Science, 341, 1235005.
    • (2013) Science , vol.341 , pp. 1235005
    • Galloway, K.E.1    Franco, E.2    Smolke, C.D.3
  • 23
    • 84869070585 scopus 로고    scopus 로고
    • A high-throughput, quantitative cell-based screen for efficient tailoring of RNA device activity
    • Liang, J.C., Chang, A. L., Kennedy, A. B. and Smolke, C. D. (2012) A high-throughput, quantitative cell-based screen for efficient tailoring of RNA device activity. Nucleic Acids Res. 40, e154.
    • (2012) Nucleic Acids Res. , vol.40 , pp. e154
    • Liang, J.C.1    Chang, A.L.2    Kennedy, A.B.3    Smolke, C.D.4
  • 24
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • Myszka, D.G. (1999) Improving biosensor analysis. J. Mol. Recognit., 12, 279-284.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 279-284
    • Myszka, D.G.1
  • 25
    • 0032702275 scopus 로고    scopus 로고
    • Affinity analysis of non-steady-state data obtained under mass transport limited conditions using BIAcore technology
    • Karlsson, R. (1999) Affinity analysis of non-steady-state data obtained under mass transport limited conditions using BIAcore technology. J. Mol. Recognit., 12, 285-292.
    • (1999) J. Mol. Recognit. , vol.12 , pp. 285-292
    • Karlsson, R.1
  • 26
    • 0034581194 scopus 로고    scopus 로고
    • Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE
    • Myszka, D.G. (2000) Kinetic, equilibrium, and thermodynamic analysis of macromolecular interactions with BIACORE. Methods Enzymol., 323, 325-340.
    • (2000) Methods Enzymol. , vol.323 , pp. 325-340
    • Myszka, D.G.1
  • 27
    • 0036351172 scopus 로고    scopus 로고
    • Kinetic studies of RNA-protein interactions using surface plasmon resonance
    • Katsamba, P.S., Park, S. and Laird-Offringa, I.A. (2002) Kinetic studies of RNA-protein interactions using surface plasmon resonance. Methods, 26, 95-104.
    • (2002) Methods , vol.26 , pp. 95-104
    • Katsamba, P.S.1    Park, S.2    Laird-Offringa, I.A.3
  • 29
    • 79952362042 scopus 로고    scopus 로고
    • The glmS riboswitch integrates signals from activating and inhibitory metabolites in vivo
    • Watson, P.Y. and Fedor, M.J. (2011) The glmS riboswitch integrates signals from activating and inhibitory metabolites in vivo. Nat. Struct. Mol. Biol., 18, 359-363.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 359-363
    • Watson, P.Y.1    Fedor, M.J.2
  • 30
    • 41949098095 scopus 로고    scopus 로고
    • Improved aptazyme design and in vivo screening enable riboswitching in bacteria
    • Wieland, M. and Hartig, J.S. (2008) Improved aptazyme design and in vivo screening enable riboswitching in bacteria. Angew. Chem. Int. Ed. Engl., 47, 2604-2607.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 2604-2607
    • Wieland, M.1    Hartig, J.S.2
  • 33
    • 33744955253 scopus 로고    scopus 로고
    • The regulatory roles of the galactose permease and kinase in the induction response of the GAL network in Saccharomyces cerevisiae
    • Hawkins, K.M. and Smolke, C.D. (2006) The regulatory roles of the galactose permease and kinase in the induction response of the GAL network in Saccharomyces cerevisiae. J. Biol. Chem., 281, 13485-13492.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13485-13492
    • Hawkins, K.M.1    Smolke, C.D.2
  • 34
    • 34347206860 scopus 로고    scopus 로고
    • High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method
    • Gietz, R.D. and Schiestl, R.H. (2007) High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method. Nat. Protoc., 2, 31-34.
    • (2007) Nat. Protoc. , vol.2 , pp. 31-34
    • Gietz, R.D.1    Schiestl, R.H.2
  • 36
    • 0032242421 scopus 로고    scopus 로고
    • The limits of specificity: An experimental analysis with RNA aptamers to MS2 coat protein variants
    • Hirao, I., Spingola, M., Peabody, D. and Ellington, A.D. (1998) The limits of specificity: An experimental analysis with RNA aptamers to MS2 coat protein variants. Mol. Divers., 4, 75-89.
    • (1998) Mol. Divers. , vol.4 , pp. 75-89
    • Hirao, I.1    Spingola, M.2    Peabody, D.3    Ellington, A.D.4
  • 37
    • 0034650498 scopus 로고    scopus 로고
    • RNA aptamers for the MS2 bacteriophage coat protein and the wild-type RNA operator have similar solution behaviour
    • Parrott, A.M., Lago, H., Adams, C.J., Ashcroft, A.E., Stonehouse, N.J. and Stockley, P.G. (2000) RNA aptamers for the MS2 bacteriophage coat protein and the wild-type RNA operator have similar solution behaviour. Nucleic Acids Res., 28, 489-497.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 489-497
    • Parrott, A.M.1    Lago, H.2    Adams, C.J.3    Ashcroft, A.E.4    Stonehouse, N.J.5    Stockley, P.G.6
  • 38
    • 0025300971 scopus 로고
    • Use of synthetic oligoribonucleotides to probe RNA-protein interactions in the MS2 translational operator complex
    • Talbot, S.J., Goodman, S., Bates, S.R., Fishwick, C.W. and Stockley, P.G. (1990) Use of synthetic oligoribonucleotides to probe RNA-protein interactions in the MS2 translational operator complex. Nucleic Acids Res., 18, 3521-3528.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3521-3528
    • Talbot, S.J.1    Goodman, S.2    Bates, S.R.3    Fishwick, C.W.4    Stockley, P.G.5
  • 40
    • 54749153656 scopus 로고    scopus 로고
    • Capturing hammerhead ribozyme structures in action by modulating general base catalysis
    • Chi, Y.I., Martick, M., Lares, M., Kim, R., Scott, W.G. and Kim, S.H. (2008) Capturing hammerhead ribozyme structures in action by modulating general base catalysis. PLoS Biol., 6, e234.
    • (2008) PLoS Biol. , vol.6 , pp. e234
    • Chi, Y.I.1    Martick, M.2    Lares, M.3    Kim, R.4    Scott, W.G.5    Kim, S.H.6
  • 41
    • 2442626706 scopus 로고    scopus 로고
    • Incorporating chemical modification constraints into a dynamic programming algorithm for prediction of RNA secondary structure
    • Mathews, D.H., Disney, M.D., Childs, J.L., Schroeder, S.J., Zuker, M. and Turner, D.H. (2004) Incorporating chemical modification constraints into a dynamic programming algorithm for prediction of RNA secondary structure. Proc. Natl. Acad. Sci. U.S.A., 101, 7287-7292.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7287-7292
    • Mathews, D.H.1    Disney, M.D.2    Childs, J.L.3    Schroeder, S.J.4    Zuker, M.5    Turner, D.H.6
  • 42
    • 0043009734 scopus 로고    scopus 로고
    • Sequence elements outside the hammerhead ribozyme catalytic core enable intracellular activity
    • Khvorova, A., Lescoute, A., Westhof, E. and Jayasena, S.D. (2003) Sequence elements outside the hammerhead ribozyme catalytic core enable intracellular activity. Nat. Struct. Biol., 10, 708-712.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 708-712
    • Khvorova, A.1    Lescoute, A.2    Westhof, E.3    Jayasena, S.D.4
  • 43
    • 84897481365 scopus 로고    scopus 로고
    • Kinetic and equilibrium binding characterization of aptamers to small molecules using a label-free, sensitive, and scalable platform
    • Chang, A.L., McKeague, M., Liang, J.C. and Smolke, C.D. (2014) Kinetic and equilibrium binding characterization of aptamers to small molecules using a label-free, sensitive, and scalable platform. Anal. Chem., 86, 3273-3278.
    • (2014) Anal. Chem. , vol.86 , pp. 3273-3278
    • Chang, A.L.1    McKeague, M.2    Liang, J.C.3    Smolke, C.D.4
  • 44
    • 84901804745 scopus 로고    scopus 로고
    • Quantitative analysis of RNA-protein interactions on a massively parallel array reveals biophysical and evolutionary landscapes
    • Buenrostro, J.D., Araya, C.L., Chircus, L.M., Layton, C.J., Chang, H.Y., Snyder, M.P. and Greenleaf, W.J. (2014) Quantitative analysis of RNA-protein interactions on a massively parallel array reveals biophysical and evolutionary landscapes. Nat. Biotechnol., 32, 562-568.
    • (2014) Nat. Biotechnol. , vol.32 , pp. 562-568
    • Buenrostro, J.D.1    Araya, C.L.2    Chircus, L.M.3    Layton, C.J.4    Chang, H.Y.5    Snyder, M.P.6    Greenleaf, W.J.7
  • 46
    • 7044272278 scopus 로고    scopus 로고
    • The crystal structure of a high affinity RNA stem-loop complexed with the bacteriophage MS2 capsid: Further challenges in the modeling of ligand-RNA interactions
    • Horn, W.T., Convery, M.A., Stonehouse, N.J., Adams, C.J., Liljas, L., Phillips, S.E. and Stockley, P.G. (2004) The crystal structure of a high affinity RNA stem-loop complexed with the bacteriophage MS2 capsid: Further challenges in the modeling of ligand-RNA interactions. RNA, 10, 1776-1782.
    • (2004) RNA , vol.10 , pp. 1776-1782
    • Horn, W.T.1    Convery, M.A.2    Stonehouse, N.J.3    Adams, C.J.4    Liljas, L.5    Phillips, S.E.6    Stockley, P.G.7
  • 48
    • 0024264659 scopus 로고
    • Ribonucleoprotein complexes of R17 coat protein and a translational operator analog
    • Beckett, D. and Uhlenbeck, O.C. (1988) Ribonucleoprotein complexes of R17 coat protein and a translational operator analog. J. Mol. Biol., 204, 927-938.
    • (1988) J. Mol. Biol. , vol.204 , pp. 927-938
    • Beckett, D.1    Uhlenbeck, O.C.2
  • 49
    • 0014202486 scopus 로고
    • Ribonucleoprotein complexes formed between bacteriophage MS2 RNA and MS2 protein in vitro
    • Sugiyama, T., Hebert, R.R. and Hartman, K.A. (1967) Ribonucleoprotein complexes formed between bacteriophage MS2 RNA and MS2 protein in vitro. J. Mol. Biol., 25, 455-463.
    • (1967) J. Mol. Biol. , vol.25 , pp. 455-463
    • Sugiyama, T.1    Hebert, R.R.2    Hartman, K.A.3
  • 50
    • 0029143235 scopus 로고
    • Mutants of the bacteriophage MS2 coat protein that alter its cooperative binding to RNA
    • LeCuyer, K.A., Behlen, L.S. and Uhlenbeck, O.C. (1995) Mutants of the bacteriophage MS2 coat protein that alter its cooperative binding to RNA. Biochemistry, 34, 10600-10606.
    • (1995) Biochemistry , vol.34 , pp. 10600-10606
    • LeCuyer, K.A.1    Behlen, L.S.2    Uhlenbeck, O.C.3
  • 52
    • 33746228126 scopus 로고    scopus 로고
    • Tertiary contacts distant from the active site prime a ribozyme for catalysis
    • Martick, M. and Scott, W.G. (2006) Tertiary contacts distant from the active site prime a ribozyme for catalysis. Cell, 126, 309-320.
    • (2006) Cell , vol.126 , pp. 309-320
    • Martick, M.1    Scott, W.G.2
  • 53
    • 46849108485 scopus 로고    scopus 로고
    • Catalytic diversity of extended hammerhead ribozymes
    • Shepotinovskaya, I.V. and Uhlenbeck, O.C. (2008) Catalytic diversity of extended hammerhead ribozymes. Biochemistry, 47, 7034-7042.
    • (2008) Biochemistry , vol.47 , pp. 7034-7042
    • Shepotinovskaya, I.V.1    Uhlenbeck, O.C.2
  • 54
    • 0034652185 scopus 로고    scopus 로고
    • Relationship between total and free cellular Mg(2+) during metabolic stimulation of rat cardiac myocytes and perfused hearts
    • Fatholahi, M., LaNoue, K., Romani, A. and Scarpa, A. (2000) Relationship between total and free cellular Mg(2+) during metabolic stimulation of rat cardiac myocytes and perfused hearts. Arch. Biochem. Biophys., 374, 395-401.
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 395-401
    • Fatholahi, M.1    LaNoue, K.2    Romani, A.3    Scarpa, A.4
  • 55
    • 0032962840 scopus 로고    scopus 로고
    • Na+-dependent regulation of the free Mg2+ concentration in neuropile glial cells and P neurones of the leech Hirudo medicinalis
    • Hintz, K., Gunzel, D. and Schlue, W.R. (1999) Na+-dependent regulation of the free Mg2+ concentration in neuropile glial cells and P neurones of the leech Hirudo medicinalis. Pflugers Arch., 437, 354-362.
    • (1999) Pflugers Arch. , vol.437 , pp. 354-362
    • Hintz, K.1    Gunzel, D.2    Schlue, W.R.3
  • 56
    • 0026036451 scopus 로고
    • Methods for measurement of intracellular magnesium: NMR and fluorescence
    • London, R.E. (1991) Methods for measurement of intracellular magnesium: NMR and fluorescence. Annu. Rev. Physiol., 53, 241-258.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 241-258
    • London, R.E.1
  • 57
    • 0030725135 scopus 로고    scopus 로고
    • Free magnesium concentration in isolated rabbit hearts subjected to high dose isoproterenol infusion: A 31P NMR study
    • Mottet, I., Goudemant, J.F., Francaux, M., Demeure, R. and Sturbois, X. (1997) Free magnesium concentration in isolated rabbit hearts subjected to high dose isoproterenol infusion: A 31P NMR study. Can. J. Physiol. Pharmacol., 75, 1015-1021.
    • (1997) Can. J. Physiol. Pharmacol. , vol.75 , pp. 1015-1021
    • Mottet, I.1    Goudemant, J.F.2    Francaux, M.3    Demeure, R.4    Sturbois, X.5
  • 58
    • 0030761409 scopus 로고    scopus 로고
    • Mutations in PTEN are frequent in endometrial carcinoma but rare in other common gynecological malignancies
    • Tashiro, H., Blazes, M.S., Wu, R., Cho, K.R., Bose, S., Wang, S.I., Li, J., Parsons, R. and Ellenson, L.H. (1997) Mutations in PTEN are frequent in endometrial carcinoma but rare in other common gynecological malignancies. Cancer Res., 57, 3935-3940.
    • (1997) Cancer Res. , vol.57 , pp. 3935-3940
    • Tashiro, H.1    Blazes, M.S.2    Wu, R.3    Cho, K.R.4    Bose, S.5    Wang, S.I.6    Li, J.7    Parsons, R.8    Ellenson, L.H.9
  • 59
    • 18144443291 scopus 로고    scopus 로고
    • Regulation of intracellular free Mg2+ concentration in isolated rat hearts via beta-adrenergic and muscarinic receptors
    • Watanabe, J., Nakayama, S., Matsubara, T. and Hotta, N. (1998) Regulation of intracellular free Mg2+ concentration in isolated rat hearts via beta-adrenergic and muscarinic receptors. J. Mol. Cell. Cardiol., 30, 2307-2318.
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 2307-2318
    • Watanabe, J.1    Nakayama, S.2    Matsubara, T.3    Hotta, N.4
  • 61
    • 35248825969 scopus 로고    scopus 로고
    • A method for measuring intracellular free magnesium concentration in platelets using flow cytometry
    • Fox, C.H., Timm, E.A. Jr., Smith, S.J., Touyz, R.M., Bush, E.G. and Wallace, P.K. (2007) A method for measuring intracellular free magnesium concentration in platelets using flow cytometry. Magnes. Res., 20, 200-207.
    • (2007) Magnes. Res. , vol.20 , pp. 200-207
    • Fox, C.H.1    Timm, E.A.2    Smith, S.J.3    Touyz, R.M.4    Bush, E.G.5    Wallace, P.K.6
  • 62
    • 0036315896 scopus 로고    scopus 로고
    • Intracellular magnesium and magnesium buffering
    • Grubbs, R.D. (2002) Intracellular magnesium and magnesium buffering. Biometals, 15, 251-259.
    • (2002) Biometals , vol.15 , pp. 251-259
    • Grubbs, R.D.1
  • 63
    • 34250807710 scopus 로고    scopus 로고
    • The maximal size of protein to diffuse through the nuclear pore is larger than 60kDa
    • Wang, R. and Brattain, M.G. (2007) The maximal size of protein to diffuse through the nuclear pore is larger than 60kDa. FEBS Lett., 581, 3164-3170.
    • (2007) FEBS Lett. , vol.581 , pp. 3164-3170
    • Wang, R.1    Brattain, M.G.2
  • 64
    • 0021716406 scopus 로고
    • A short amino acid sequence able to specify nuclear location
    • Kalderon, D., Roberts, B.L., Richardson, W.D. and Smith, A.E. (1984) A short amino acid sequence able to specify nuclear location. Cell, 39, 499-509.
    • (1984) Cell , vol.39 , pp. 499-509
    • Kalderon, D.1    Roberts, B.L.2    Richardson, W.D.3    Smith, A.E.4
  • 65
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., Meinkoth, J.L., Tsien, R.Y. and Taylor, S.S. (1995) Identification of a signal for rapid export of proteins from the nucleus. Cell, 82, 463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 66
    • 0036799597 scopus 로고    scopus 로고
    • RNA recognition site of PP7 coat protein
    • Lim, F. and Peabody, D.S. (2002) RNA recognition site of PP7 coat protein. Nucleic Acids Res., 30, 4138-4144.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4138-4144
    • Lim, F.1    Peabody, D.S.2
  • 67
    • 37849019313 scopus 로고    scopus 로고
    • Structural basis for the coevolution of a viral RNA-protein complex
    • Chao, J.A., Patskovsky, Y., Almo, S.C. and Singer, R.H. (2008) Structural basis for the coevolution of a viral RNA-protein complex. Nat. Struct. Mol. Biol., 15, 103-105.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 103-105
    • Chao, J.A.1    Patskovsky, Y.2    Almo, S.C.3    Singer, R.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.