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1
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27644552994
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Review: advances in functional protein microarray technology
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Bertone P., and Snyder M. Review: advances in functional protein microarray technology. FEBS J 272 (2005) 5400-5411
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(2005)
FEBS J
, vol.272
, pp. 5400-5411
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Bertone, P.1
Snyder, M.2
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2
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10644223453
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Review: quantitative protein profiling using protein arrays
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Barry R., and Soloviev M. Review: quantitative protein profiling using protein arrays. Proteomics 4 (2004) 3717-3726
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(2004)
Proteomics
, vol.4
, pp. 3717-3726
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Barry, R.1
Soloviev, M.2
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4
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0034665455
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Design of high-throughput methods of protein production for structural biology
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Stevens R.C. Design of high-throughput methods of protein production for structural biology. Struct Fold Des 8 (2000) R177-R185
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(2000)
Struct Fold Des
, vol.8
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Stevens, R.C.1
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5
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33749533435
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Cell-free protein synthesis at high temperatures using the lysate of a hyperthermophile
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In contrast to systems operating at moderate temperatures, this paper reports preparation of a cell-free lysate operative at high temperatures, from the hyperthermophilic archaeon, Thermococcus kodakaraensis. With this in vitro translation system, active chitinase was produced at temperatures between 40 and 80 °C (optimum 65 °C). A system for coupled transcription and translation at high temperatures, using a combination of T. kodakaraensis lysate and thermostable T7 RNA polymerase, was also developed.
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Endoh T., Kanai T., Sato Y.T., Liu D.V., Yoshikawa K., Atomi H., and Imanaka T. Cell-free protein synthesis at high temperatures using the lysate of a hyperthermophile. J Biotechnol 126 (2006) 186-195. In contrast to systems operating at moderate temperatures, this paper reports preparation of a cell-free lysate operative at high temperatures, from the hyperthermophilic archaeon, Thermococcus kodakaraensis. With this in vitro translation system, active chitinase was produced at temperatures between 40 and 80 °C (optimum 65 °C). A system for coupled transcription and translation at high temperatures, using a combination of T. kodakaraensis lysate and thermostable T7 RNA polymerase, was also developed.
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(2006)
J Biotechnol
, vol.126
, pp. 186-195
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Endoh, T.1
Kanai, T.2
Sato, Y.T.3
Liu, D.V.4
Yoshikawa, K.5
Atomi, H.6
Imanaka, T.7
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6
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33846204799
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A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins
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The authors developed an efficient system derived from a monoclonal antibody-producing hybridoma for cell-free synthesis of glycoproteins. It was successfully used to produce a biologically active, multichain glycoprotein (human choriogonadotropin).
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Mikami S., Kobayashi T., Yokoyama S., and Imataka H. A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins. J Biotechnol 127 (2006) 65-78. The authors developed an efficient system derived from a monoclonal antibody-producing hybridoma for cell-free synthesis of glycoproteins. It was successfully used to produce a biologically active, multichain glycoprotein (human choriogonadotropin).
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(2006)
J Biotechnol
, vol.127
, pp. 65-78
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Mikami, S.1
Kobayashi, T.2
Yokoyama, S.3
Imataka, H.4
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7
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0037052966
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Site-specific and temporally controlled initiation of DNA replication in a human cell-free system
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Keller C., Hyrien O., Knippers R., and Krude T. Site-specific and temporally controlled initiation of DNA replication in a human cell-free system. Nucleic Acids Res 30 (2001) 2114-2123
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(2001)
Nucleic Acids Res
, vol.30
, pp. 2114-2123
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Keller, C.1
Hyrien, O.2
Knippers, R.3
Krude, T.4
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8
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0036250652
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Reprogrammed gene expression in a somatic cell-free extract
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Landsverk H.B., Hakelien A.M., Kuntziger T., Robl J.M., Skalhegg B.S., and Collas P. Reprogrammed gene expression in a somatic cell-free extract. EMBO Rep 3 (2002) 384-389
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(2002)
EMBO Rep
, vol.3
, pp. 384-389
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Landsverk, H.B.1
Hakelien, A.M.2
Kuntziger, T.3
Robl, J.M.4
Skalhegg, B.S.5
Collas, P.6
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9
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37249021351
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A systematic approach for testing expression of human full-length proteins in cell-free expression systems
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The authors compared cell free expression in E. coli and wheat germ systems for a subset of 87 full-length human proteins which, out of 960 evaluated in a pre-screen, showed no product in E. coli in vivo. Through appropriate optimisations, a success rate of 93% was achieved in vitro. Wheat germ expression with a two compartment system emerged as the method of choice for high yield of soluble proteins.
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Langlais C., Guilleaume B., Wermke N., Scheuermann T., Ebert L., Labaer J., and Korn B. A systematic approach for testing expression of human full-length proteins in cell-free expression systems. BMC Biotechnol 7 (2007) 64. The authors compared cell free expression in E. coli and wheat germ systems for a subset of 87 full-length human proteins which, out of 960 evaluated in a pre-screen, showed no product in E. coli in vivo. Through appropriate optimisations, a success rate of 93% was achieved in vitro. Wheat germ expression with a two compartment system emerged as the method of choice for high yield of soluble proteins.
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(2007)
BMC Biotechnol
, vol.7
, pp. 64
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Langlais, C.1
Guilleaume, B.2
Wermke, N.3
Scheuermann, T.4
Ebert, L.5
Labaer, J.6
Korn, B.7
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10
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23044504786
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Protein synthesis by pure translation systems
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Shimizu Y., Kanamori T., and Ueda T. Protein synthesis by pure translation systems. Methods 36 (2005) 299-304
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(2005)
Methods
, vol.36
, pp. 299-304
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Shimizu, Y.1
Kanamori, T.2
Ueda, T.3
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11
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33748546619
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Protein-protein interaction analysis by C-terminally specific fluorescence labeling and fluorescence cross-correlation spectroscopy
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The authors present a cell free system containing diluted puromycin derivatised with biotin, together with either Cy5 or RhG fluorophores. The expressed labelled proteins are purified via the biotin to provide fluorophore-labeled proteins for interaction studies by FCCS.
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Oyama R., Takashima H., Yonezawa M., Doi N., Miyamoto-Sato E., Kinjo M., and Yanagawa H. Protein-protein interaction analysis by C-terminally specific fluorescence labeling and fluorescence cross-correlation spectroscopy. Nucleic Acids Res 4 (2006) e102. The authors present a cell free system containing diluted puromycin derivatised with biotin, together with either Cy5 or RhG fluorophores. The expressed labelled proteins are purified via the biotin to provide fluorophore-labeled proteins for interaction studies by FCCS.
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(2006)
Nucleic Acids Res
, vol.4
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Oyama, R.1
Takashima, H.2
Yonezawa, M.3
Doi, N.4
Miyamoto-Sato, E.5
Kinjo, M.6
Yanagawa, H.7
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12
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33748311913
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N-Labelled proteins by cell-free protein synthesis
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Ozawa K., Wu P.S., Dixon N.E., and Otting G. N-Labelled proteins by cell-free protein synthesis. FEBS J 273 (2006) 4154-4159
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(2006)
FEBS J
, vol.273
, pp. 4154-4159
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Ozawa, K.1
Wu, P.S.2
Dixon, N.E.3
Otting, G.4
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13
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1842477047
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Cell-free protein expression and functional assay in nanowell chip format
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Angenendt P., Nyarsik L., Szaflarski W., Glökler J., Nierhaus K.H., Lehrach H., Cahill D.J., and Lueking A. Cell-free protein expression and functional assay in nanowell chip format. Anal Chem 76 (2004) 1844-1849
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(2004)
Anal Chem
, vol.76
, pp. 1844-1849
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Angenendt, P.1
Nyarsik, L.2
Szaflarski, W.3
Glökler, J.4
Nierhaus, K.H.5
Lehrach, H.6
Cahill, D.J.7
Lueking, A.8
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14
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4644269746
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High-throughput cell-free systems for synthesis of functionally active proteins
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Spirin A. High-throughput cell-free systems for synthesis of functionally active proteins. Trends Biotechnol 22 (2004) 538-545
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(2004)
Trends Biotechnol
, vol.22
, pp. 538-545
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Spirin, A.1
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15
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23244440886
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An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates
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Calhoun K., and Swartz J.R. An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates. Biotechnol Prog 21 (2005) 1146-1153
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(2005)
Biotechnol Prog
, vol.21
, pp. 1146-1153
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Calhoun, K.1
Swartz, J.R.2
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16
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33751502407
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Enhanced cell-free protein expression by fusion with immunoglobulin Cκ domain
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A novel strategy is reported for promoting synthesis of 'difficult-to-express' proteins in the E. coli cell free system, through C-terminal fusion of the constant domain of human immunoglobulin κ light chain (Cκ). Four proteins (two single-chain antibody fragments, a GTP-binding protein and FK506 binding protein) all showed highly enhanced expression as Cκ fusions.
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Palmer E., Liu H., Khan F., Taussig M.J., and He M. Enhanced cell-free protein expression by fusion with immunoglobulin Cκ domain. Protein Sci 15 (2006) 2842-2846. A novel strategy is reported for promoting synthesis of 'difficult-to-express' proteins in the E. coli cell free system, through C-terminal fusion of the constant domain of human immunoglobulin κ light chain (Cκ). Four proteins (two single-chain antibody fragments, a GTP-binding protein and FK506 binding protein) all showed highly enhanced expression as Cκ fusions.
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(2006)
Protein Sci
, vol.15
, pp. 2842-2846
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Palmer, E.1
Liu, H.2
Khan, F.3
Taussig, M.J.4
He, M.5
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17
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0035430843
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Single step generation of protein arrays from DNA by cell-free expression and in situ immobilisation (PISA method)
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He M., and Taussig M.J. Single step generation of protein arrays from DNA by cell-free expression and in situ immobilisation (PISA method). Nucleic Acids Res 29 (2001) e73
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(2001)
Nucleic Acids Res
, vol.29
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He, M.1
Taussig, M.J.2
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18
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33646540098
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A double-His tag with high affinity binding for protein immobilisation, purification, and detection on Ni-NTA surfaces
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6 antibodies and a variety of Ni-NTA conjugates in western blotting, ELISA and protein arrays. It was applied in single-step protein immobilisation and purification from crude mixtures.
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6 antibodies and a variety of Ni-NTA conjugates in western blotting, ELISA and protein arrays. It was applied in single-step protein immobilisation and purification from crude mixtures.
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(2006)
Anal Chem
, vol.78
, pp. 3072-3079
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Khan, F.1
He, M.2
Taussig, M.J.3
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19
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33747782971
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6-tagged single framework recombinant antibody fragments
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6-tag (ref. 18 above), significantly improved binding to Ni-NTA-coated surfaces. This enabled non-purified probes to be applied directly to the surface, eliminating pre-purification before the immobilisation, and created better long-term functional on-chip stability.
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6-tag (ref. 18 above), significantly improved binding to Ni-NTA-coated surfaces. This enabled non-purified probes to be applied directly to the surface, eliminating pre-purification before the immobilisation, and created better long-term functional on-chip stability.
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(2006)
Proteomics
, vol.6
, pp. 4227-4234
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Steinhauer, C.1
Wingren, C.2
Khan, F.3
He, M.4
Taussig, M.J.5
Borrebaeck, C.A.6
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20
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0037332583
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DiscernArray technology: a cell-free method for the generation of protein arrays from PCR DNA
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He M., and Taussig M.J. DiscernArray technology: a cell-free method for the generation of protein arrays from PCR DNA. J Immunol Methods 274 (2003) 265-270
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(2003)
J Immunol Methods
, vol.274
, pp. 265-270
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He, M.1
Taussig, M.J.2
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21
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33749243012
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Generation of high density protein microarrays by cell-free in situ expression of unpurified PCR products
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This describes in situ production of protein microarrays by a multiple spotting technique, first spotting PCR DNA and then the cell free system on top, and allowing cell free transcription and translation to occur in each spot. Protein yields were analysed. The method was adapted to high throughput library expression and demonstrated with 384 randomly chosen clones. Protein microarrays with up to 13,000 spots per slide can be generated in situ.
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Angenendt P., Kreutzberger J., Glokler J., and Hoheisel J.D. Generation of high density protein microarrays by cell-free in situ expression of unpurified PCR products. Mol Cell Proteomics 5 (2006) 1658-1666. This describes in situ production of protein microarrays by a multiple spotting technique, first spotting PCR DNA and then the cell free system on top, and allowing cell free transcription and translation to occur in each spot. Protein yields were analysed. The method was adapted to high throughput library expression and demonstrated with 384 randomly chosen clones. Protein microarrays with up to 13,000 spots per slide can be generated in situ.
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(2006)
Mol Cell Proteomics
, vol.5
, pp. 1658-1666
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Angenendt, P.1
Kreutzberger, J.2
Glokler, J.3
Hoheisel, J.D.4
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22
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3042757210
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Self-assembling protein mircoarrays
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This paper describes the NAPPA technique for converting DNA arrays into protein arrays, in which immobilised plasmids encoding fusion proteins are used as templates for on-chip protein synthesis by cell free transcription and translation. The proteins are captured by antibody, cospotted with the plasmid and directed against the fusion tag. As well as demonstrating protein microarray production, pairwise interaction studies with 29 human replication initiation proteins were performed.
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Ramachandran N., Hainsworth E., Bhullar B., Eisenstein S., Rosen B., Lau A.Y., Walter J.C., and LaBaer J. Self-assembling protein mircoarrays. Science 305 (2004) 86-90. This paper describes the NAPPA technique for converting DNA arrays into protein arrays, in which immobilised plasmids encoding fusion proteins are used as templates for on-chip protein synthesis by cell free transcription and translation. The proteins are captured by antibody, cospotted with the plasmid and directed against the fusion tag. As well as demonstrating protein microarray production, pairwise interaction studies with 29 human replication initiation proteins were performed.
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(2004)
Science
, vol.305
, pp. 86-90
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Ramachandran, N.1
Hainsworth, E.2
Bhullar, B.3
Eisenstein, S.4
Rosen, B.5
Lau, A.Y.6
Walter, J.C.7
LaBaer, J.8
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24
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0030817279
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RNA-peptide fusions for the in vitro selection of peptides and proteins
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Roberts R.W., and Szostak J.W. RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc Natl Acad Sci U S A 94 (1997) 12297-12302
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(1997)
Proc Natl Acad Sci U S A
, vol.94
, pp. 12297-12302
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Roberts, R.W.1
Szostak, J.W.2
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25
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33749863636
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Protein chip fabrication by capture of nascent polypeptides
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Thie authors performed on-chip production of protein microarrays from modified in vitro transcribed mRNA immobilised on the chip surface. Cell free translation was performed on the slide, during which a puromycin-oligonucleotide, hybridised to the mRNA, displaced the full length nascent protein, both linking it to the mRNA and trapping it on the surface. The mRNA was then removed enzymatically. The method produced arrays with well-defined spots of GST and functional transcription factors.
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Tao S.-C., and Zhu H. Protein chip fabrication by capture of nascent polypeptides. Nat Biotechnol 24 (2006) 1253-1254. Thie authors performed on-chip production of protein microarrays from modified in vitro transcribed mRNA immobilised on the chip surface. Cell free translation was performed on the slide, during which a puromycin-oligonucleotide, hybridised to the mRNA, displaced the full length nascent protein, both linking it to the mRNA and trapping it on the surface. The mRNA was then removed enzymatically. The method produced arrays with well-defined spots of GST and functional transcription factors.
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(2006)
Nat Biotechnol
, vol.24
, pp. 1253-1254
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Tao, S.-C.1
Zhu, H.2
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26
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33845654360
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Solid-phase translation and RNA-protein fusion: a novel approach for folding quality control and direct immobilisation of proteins using anchored mRNA
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A similar, 'RNA array to protein array' approach to that of ref. [25] using modified mRNA-protein fusion and exemplified with GFP and a functional enzyme, aldehyde reductase.
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Biyani M., Husimi Y., and Nemoto N. Solid-phase translation and RNA-protein fusion: a novel approach for folding quality control and direct immobilisation of proteins using anchored mRNA. Nucleic Acids Res 34 (2006) e140. A similar, 'RNA array to protein array' approach to that of ref. [25] using modified mRNA-protein fusion and exemplified with GFP and a functional enzyme, aldehyde reductase.
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(2006)
Nucleic Acids Res
, vol.34
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Biyani, M.1
Husimi, Y.2
Nemoto, N.3
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