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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
09/08/2002 |
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Data da última atualização: |
28/01/2008 |
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Autoria: |
THORNER, J.; EMR, S. D.; ABELSON, J. N. (ed.). |
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Afiliação: |
University of California; Howard Hughes Medical Institute and School of Medicine, University of California; California Institute of Technology. |
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Título: |
Applications of chimeric genes and hybrid proteins: part C protein-protein interactions and genomics. |
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Ano de publicação: |
2000 |
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Fonte/Imprenta: |
San Diego: Academic Press, 2000. |
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Páginas: |
666 p. |
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Série: |
(Methods in Enzymology, 328). |
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ISBN: |
0-12-182229-X |
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Idioma: |
Inglês |
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Conteúdo: |
High-throughput screening for protein-protein interactions using two-hybrid assay (Gerard Cagney, P. Uetz, S. Fields). LexA-based two-hybrid systems (S. J. Fashena, I. G. Serebriiskii, E. A. Golemis). Interaction mating methods in two-hybrid systems (M. G. Kolonin, J. Zhong, R. L. Finley Júnior). Analysis and identificatio of protein-protein interactions using protein recruitment systems (A. Aronheim, M. Karin). Bacterial two-hybrid system that exploits a cAMP signaling in Escherichia coli (G. Karimova, A. Ullmann, D. Ladant). A green fluorescent protein-based reverse two-hybrid system: application to the characterization of large numbers of potential protein-protein interactions (H. Endoh, A. J. M. Walhout, M. Vidal). Yeast three-hybrid system for detecting lingand-receptor interactions (E. C. Griffith, E. J. Licitra, J. O. Liu). Use of a yeast three-hybrid system to clone bridging proteins (J. Zhang). The yeast tribrid system: cDNA expression clonting of protein interactions dependent on posttranslational modifications (J. P. Kochan, C. Volpers, M. A. Osborne). Mapping protein-protein interaction domains using ordered fragment ladder far-western analysis of hexahistidine-tagged fusion proteins (R. R. Burgess, T. M. Arthur, B. C. Pietz). Mapping specificity determinants for protein-protein association using protein fusions and random peptide libraries (M. B. Yaffe, L. C. Cantley). Selection of genetic agents from random peptide aptamer expression libraries (C. R. Geyer, R. Brent). Detection of protein-protein interactions by protein fragment complementation strategies (S. W. Michnick, I. Remy, François-X, Campbell-Valois, A. Vallée-Bélisle, J. N. Pelletier). Monitoring protein-protein interactions in live mammalian cells by galactosidase complementation (F. M. V. Rossi, B. T. Blakely, C. A. Charlton, H. M. Blau). Green fluorescent protein chimeras to probe protein-protein interactions (S.-H. Park, R. T. Raines). Protein fusions to coiled-coil domains (K. M. Muller, K. M. Arndt, T. Alber). Molecular applications of fusions to leucine zippers (J. D. Rieker, J. C. Hu). Using the yeast three-hybrid system to detect and analyze RNA-protein interactions B. Kraemer, B. Zhang, D. Sengupta, S. Fields, M. Wickens). Principles and applications of a tat-based assay for analysing specific RNA-protein interactions in mammalian cells (B. R. Cullen). Phage display for selection of novel binding peptides (S. S. Sidhu, H. B. Lowman, B. C. Cunningham, J. A. Wells). Selectively infective phage technology (K. M. Arndt, S. Jung, C. Krebber, A. Pluckthun). Use of phage display and transition-sate analogs to select enzyme variants with altered catalytic properties: glutathione transferase as an example (M. Widersten, L. O. Hansson, L. tronstad, B. Mannervik). Selecting and evolving functional proteins in vitro by ribosome display (J. Hanes, L. Jermuts, A. Pluckthun). Yeast surface display for directed evolution of protein expression, affinity, and stability (E. T. Boder, K. D. Wittrup). Methods for in vitro DNA recombination and random chimeragenesis A. A. Volkov, F. H. Arnold). Random chimeragenesis by heteroduplex recombination (A. A. Volkov, Z. Shao, F. H. Arnold). Use of chimeras generated by DNA shuffling: probing structure-function relationships among glutahione transferases (L. O. Hansson, B. Mannervik). protein engineering by expressed protein ligation (U. K. Blaschke, J. Silberstein, T. W. Muir). A systematic and general proteolytic for defining structural and functional domains of proteins (J. Carey). High-throughput expression of fusion proteins (M. S. Nasoff, M. Bergseid, J. P. Hoeffler, J. A. Heyman). Rapid construction of recombinant DNA by the univector plasmid-fusion system (Q. Liu, M. Z. Li, Dou Liu, S. J. Elledge). High-throughput methods for the large-scale analysis of gene function by transposon tagging (A. Kumar, S. A. des Estages, P. S. R. Coelho, G. S. Roeder, M. Snyder). Gateway recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes (A. J. M. Walhouth, G. F. Temple, M. A. Brasch, J. L. Hartley, M. A. lorson, S. van den Heuvel, M. Vidal). Gene trapping methods for the identification and functional analysis of cell surface proteins in mice (W. C. Skarnes). MenosHigh-throughput screening for protein-protein interactions using two-hybrid assay (Gerard Cagney, P. Uetz, S. Fields). LexA-based two-hybrid systems (S. J. Fashena, I. G. Serebriiskii, E. A. Golemis). Interaction mating methods in two-hybrid systems (M. G. Kolonin, J. Zhong, R. L. Finley Júnior). Analysis and identificatio of protein-protein interactions using protein recruitment systems (A. Aronheim, M. Karin). Bacterial two-hybrid system that exploits a cAMP signaling in Escherichia coli (G. Karimova, A. Ullmann, D. Ladant). A green fluorescent protein-based reverse two-hybrid system: application to the characterization of large numbers of potential protein-protein interactions (H. Endoh, A. J. M. Walhout, M. Vidal). Yeast three-hybrid system for detecting lingand-receptor interactions (E. C. Griffith, E. J. Licitra, J. O. Liu). Use of a yeast three-hybrid system to clone bridging proteins (J. Zhang). The yeast tribrid system: cDNA expression clonting of protein interactions dependent on posttranslational modifications (J. P. Kochan, C. Volpers, M. A. Osborne). Mapping protein-protein interaction domains using ordered fragment ladder far-western analysis of hexahistidine-tagged fusion proteins (R. R. Burgess, T. M. Arthur, B. C. Pietz). Mapping specificity determinants for protein-protein association using protein fusions and random peptide libraries (M. B. Yaffe, L. C. Cantley). Selection of genetic agents from random peptide aptamer expression libraries (C. R. Geyer, R.... Mostrar Tudo |
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Palavras-Chave: |
Enzimas; Enzimologia; Interação proteína-proteína; Proteínas. |
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Thesagro: |
Genoma. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 04927nam a2200229 a 4500
001 1008128
005 2008-01-28
008 2000 bl uuuu 00u1 u #d
020 $a0-12-182229-X
100 1 $aTHORNER, J.
245 $aApplications of chimeric genes and hybrid proteins$bpart C protein-protein interactions and genomics.
260 $aSan Diego: Academic Press$c2000
300 $a666 p.
490 $a(Methods in Enzymology, 328).
520 $aHigh-throughput screening for protein-protein interactions using two-hybrid assay (Gerard Cagney, P. Uetz, S. Fields). LexA-based two-hybrid systems (S. J. Fashena, I. G. Serebriiskii, E. A. Golemis). Interaction mating methods in two-hybrid systems (M. G. Kolonin, J. Zhong, R. L. Finley Júnior). Analysis and identificatio of protein-protein interactions using protein recruitment systems (A. Aronheim, M. Karin). Bacterial two-hybrid system that exploits a cAMP signaling in Escherichia coli (G. Karimova, A. Ullmann, D. Ladant). A green fluorescent protein-based reverse two-hybrid system: application to the characterization of large numbers of potential protein-protein interactions (H. Endoh, A. J. M. Walhout, M. Vidal). Yeast three-hybrid system for detecting lingand-receptor interactions (E. C. Griffith, E. J. Licitra, J. O. Liu). Use of a yeast three-hybrid system to clone bridging proteins (J. Zhang). The yeast tribrid system: cDNA expression clonting of protein interactions dependent on posttranslational modifications (J. P. Kochan, C. Volpers, M. A. Osborne). Mapping protein-protein interaction domains using ordered fragment ladder far-western analysis of hexahistidine-tagged fusion proteins (R. R. Burgess, T. M. Arthur, B. C. Pietz). Mapping specificity determinants for protein-protein association using protein fusions and random peptide libraries (M. B. Yaffe, L. C. Cantley). Selection of genetic agents from random peptide aptamer expression libraries (C. R. Geyer, R. Brent). Detection of protein-protein interactions by protein fragment complementation strategies (S. W. Michnick, I. Remy, François-X, Campbell-Valois, A. Vallée-Bélisle, J. N. Pelletier). Monitoring protein-protein interactions in live mammalian cells by galactosidase complementation (F. M. V. Rossi, B. T. Blakely, C. A. Charlton, H. M. Blau). Green fluorescent protein chimeras to probe protein-protein interactions (S.-H. Park, R. T. Raines). Protein fusions to coiled-coil domains (K. M. Muller, K. M. Arndt, T. Alber). Molecular applications of fusions to leucine zippers (J. D. Rieker, J. C. Hu). Using the yeast three-hybrid system to detect and analyze RNA-protein interactions B. Kraemer, B. Zhang, D. Sengupta, S. Fields, M. Wickens). Principles and applications of a tat-based assay for analysing specific RNA-protein interactions in mammalian cells (B. R. Cullen). Phage display for selection of novel binding peptides (S. S. Sidhu, H. B. Lowman, B. C. Cunningham, J. A. Wells). Selectively infective phage technology (K. M. Arndt, S. Jung, C. Krebber, A. Pluckthun). Use of phage display and transition-sate analogs to select enzyme variants with altered catalytic properties: glutathione transferase as an example (M. Widersten, L. O. Hansson, L. tronstad, B. Mannervik). Selecting and evolving functional proteins in vitro by ribosome display (J. Hanes, L. Jermuts, A. Pluckthun). Yeast surface display for directed evolution of protein expression, affinity, and stability (E. T. Boder, K. D. Wittrup). Methods for in vitro DNA recombination and random chimeragenesis A. A. Volkov, F. H. Arnold). Random chimeragenesis by heteroduplex recombination (A. A. Volkov, Z. Shao, F. H. Arnold). Use of chimeras generated by DNA shuffling: probing structure-function relationships among glutahione transferases (L. O. Hansson, B. Mannervik). protein engineering by expressed protein ligation (U. K. Blaschke, J. Silberstein, T. W. Muir). A systematic and general proteolytic for defining structural and functional domains of proteins (J. Carey). High-throughput expression of fusion proteins (M. S. Nasoff, M. Bergseid, J. P. Hoeffler, J. A. Heyman). Rapid construction of recombinant DNA by the univector plasmid-fusion system (Q. Liu, M. Z. Li, Dou Liu, S. J. Elledge). High-throughput methods for the large-scale analysis of gene function by transposon tagging (A. Kumar, S. A. des Estages, P. S. R. Coelho, G. S. Roeder, M. Snyder). Gateway recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes (A. J. M. Walhouth, G. F. Temple, M. A. Brasch, J. L. Hartley, M. A. lorson, S. van den Heuvel, M. Vidal). Gene trapping methods for the identification and functional analysis of cell surface proteins in mice (W. C. Skarnes).
650 $aGenoma
653 $aEnzimas
653 $aEnzimologia
653 $aInteração proteína-proteína
653 $aProteínas
700 1 $aEMR, S. D.
700 1 $aABELSON, J. N.
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Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
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