Intranet
Acces
Contact
Publications
2008 |
Deddouche, Safia; Matt, Nicolas; Budd, Aidan; Mueller, Stefanie; Kemp, Cordula; Galiana-Arnoux, Delphine; Dostert, Catherine; Antoniewski, Christophe; Hoffmann, Jules A; Imler, Jean-Luc The DExD/Ħ-box helicase Dicer-2 mediates the induction of antiviral activity in drosophila Article de journal Nature Immunology, 9 (12), p. 1425–1432, 2008, ISSN: 1529-2916. Résumé | Liens | BibTeX | Étiquettes: Amino Acid, Animals, Electrophoresis, Fat Body, Gene Expression Regulation, Genetic, Genetically Modified, hoffmann, Humans, imler, M3i, matt, Phylogeny, Polyacrylamide Gel, Reverse Transcriptase Polymerase Chain Reaction, Ribonuclease III, RNA Helicases, Sequence Homology, Transcription, Virus Diseases @article{deddouche_dexd/h-box_2008, title = {The DExD/Ħ-box helicase Dicer-2 mediates the induction of antiviral activity in drosophila}, author = {Safia Deddouche and Nicolas Matt and Aidan Budd and Stefanie Mueller and Cordula Kemp and Delphine Galiana-Arnoux and Catherine Dostert and Christophe Antoniewski and Jules A Hoffmann and Jean-Luc Imler}, doi = {10.1038/ni.1664}, issn = {1529-2916}, year = {2008}, date = {2008-12-01}, journal = {Nature Immunology}, volume = {9}, number = {12}, pages = {1425--1432}, abstract = {Drosophila, like other invertebrates and plants, relies mainly on RNA interference for its defense against viruses. In flies, viral infection also triggers the expression of many genes. One of the genes induced, Vago, encodes a 18-kilodalton cysteine-rich polypeptide. Here we provide genetic evidence that the Vago gene product controlled viral load in the fat body after infection with drosophila C virus. Induction of Vago was dependent on the helicase Dicer-2. Dicer-2 belongs to the same DExD/H-box helicase family as do the RIG-I-like receptors, which sense viral infection and mediate interferon induction in mammals. We propose that this family represents an evolutionary conserved set of sensors that detect viral nucleic acids and direct antiviral responses.}, keywords = {Amino Acid, Animals, Electrophoresis, Fat Body, Gene Expression Regulation, Genetic, Genetically Modified, hoffmann, Humans, imler, M3i, matt, Phylogeny, Polyacrylamide Gel, Reverse Transcriptase Polymerase Chain Reaction, Ribonuclease III, RNA Helicases, Sequence Homology, Transcription, Virus Diseases}, pubstate = {published}, tppubtype = {article} } Drosophila, like other invertebrates and plants, relies mainly on RNA interference for its defense against viruses. In flies, viral infection also triggers the expression of many genes. One of the genes induced, Vago, encodes a 18-kilodalton cysteine-rich polypeptide. Here we provide genetic evidence that the Vago gene product controlled viral load in the fat body after infection with drosophila C virus. Induction of Vago was dependent on the helicase Dicer-2. Dicer-2 belongs to the same DExD/H-box helicase family as do the RIG-I-like receptors, which sense viral infection and mediate interferon induction in mammals. We propose that this family represents an evolutionary conserved set of sensors that detect viral nucleic acids and direct antiviral responses. |
2005 |
Weber, Alexander N R; Moncrieffe, Martin C; Gangloff, Monique; Imler, Jean-Luc; Gay, Nicholas J Ligand-receptor and receptor-receptor interactions act in concert to activate signaling in the Drosophila toll pathway Article de journal The Journal of Biological Chemistry, 280 (24), p. 22793–22799, 2005, ISSN: 0021-9258. Résumé | Liens | BibTeX | Étiquettes: Amino Acid, Animals, Biophysical Phenomena, Biophysics, Body Patterning, Calorimetry, Cell Line, Cell Surface, Cross-Linking Reagents, Cytokines, dimerization, Electrophoresis, Humans, imler, ligands, Luciferases, M3i, Membrane Glycoproteins, Polyacrylamide Gel, Protein Binding, Protein Structure, Receptors, Recombinant Proteins, Sequence Homology, Signal Transduction, Tertiary, Time Factors, Toll-Like Receptors, Ultracentrifugation @article{weber_ligand-receptor_2005, title = {Ligand-receptor and receptor-receptor interactions act in concert to activate signaling in the Drosophila toll pathway}, author = {Alexander N R Weber and Martin C Moncrieffe and Monique Gangloff and Jean-Luc Imler and Nicholas J Gay}, doi = {10.1074/jbc.M502074200}, issn = {0021-9258}, year = {2005}, date = {2005-01-01}, journal = {The Journal of Biological Chemistry}, volume = {280}, number = {24}, pages = {22793--22799}, abstract = {In Drosophila, the signaling pathway mediated by the Toll receptor is critical for the establishment of embryonic dorso-ventral pattern and for innate immune responses to bacterial and fungal pathogens. Toll is activated by high affinity binding of the cytokine Spätzle, a dimeric ligand of the cystine knot family. In vertebrates, a related family of Toll-like receptors play a critical role in innate immune responses. Despite the importance of this family of receptors, little is known about the biochemical events that lead to receptor activation and signaling. Here, we show that Spätzle binds to the N-terminal region of Toll and, using biophysical methods, that the binding is complex. The two binding events that cause formation of the cross-linked complex are non-equivalent: the first Toll ectodomain binds Spätzle with an affinity 3-fold higher than the second molecule suggesting that pathway activation involves negative cooperativity. We further show that the Toll ectodomains are able to form low affinity dimers in solution and that juxtamembrane sequences of Toll are critical for the activation or derepression of the pathway. These results, taken together, suggest a mechanism of signal transduction that requires both ligand-receptor and receptor-receptor interactions.}, keywords = {Amino Acid, Animals, Biophysical Phenomena, Biophysics, Body Patterning, Calorimetry, Cell Line, Cell Surface, Cross-Linking Reagents, Cytokines, dimerization, Electrophoresis, Humans, imler, ligands, Luciferases, M3i, Membrane Glycoproteins, Polyacrylamide Gel, Protein Binding, Protein Structure, Receptors, Recombinant Proteins, Sequence Homology, Signal Transduction, Tertiary, Time Factors, Toll-Like Receptors, Ultracentrifugation}, pubstate = {published}, tppubtype = {article} } In Drosophila, the signaling pathway mediated by the Toll receptor is critical for the establishment of embryonic dorso-ventral pattern and for innate immune responses to bacterial and fungal pathogens. Toll is activated by high affinity binding of the cytokine Spätzle, a dimeric ligand of the cystine knot family. In vertebrates, a related family of Toll-like receptors play a critical role in innate immune responses. Despite the importance of this family of receptors, little is known about the biochemical events that lead to receptor activation and signaling. Here, we show that Spätzle binds to the N-terminal region of Toll and, using biophysical methods, that the binding is complex. The two binding events that cause formation of the cross-linked complex are non-equivalent: the first Toll ectodomain binds Spätzle with an affinity 3-fold higher than the second molecule suggesting that pathway activation involves negative cooperativity. We further show that the Toll ectodomains are able to form low affinity dimers in solution and that juxtamembrane sequences of Toll are critical for the activation or derepression of the pathway. These results, taken together, suggest a mechanism of signal transduction that requires both ligand-receptor and receptor-receptor interactions. |
2004 |
de la Pena-Lefebvre, Garcia P; Chanseaud, Y; Tamby, M C; Reinbolt, J; Batteux, F; Allanore, Y; Kahan, A; Meyer, O; Benveniste, O; Boyer, O; Guillevin, L; Boissier, M C; Mouthon, L IgG reactivity with a 100-kDa tissue and endothelial cell antigen identified as topoisomerase 1 distinguishes between limited and diffuse systemic sclerosis patients Article de journal Clin Immunol, 111 (3), p. 241-51, 2004, (1521-6616 Journal Article). Résumé | BibTeX | Étiquettes: Aged, Assay, Autoantibodies/*analysis, Blotting, Cells/*immunology, Centromere/immunology, DNA, EHRESMANN, Electrophoresis, Endothelial, Enzyme-Linked, Female, G/analysis, Gel, Gov't, Human, I/*immunology, Immunoglobulin, Immunosorbent, M/analysis, Male, Middle, Non-U.S., Polyacrylamide, Scleroderma, Support, Systemic/*immunology, Topoisomerases, Type, Western @article{, title = {IgG reactivity with a 100-kDa tissue and endothelial cell antigen identified as topoisomerase 1 distinguishes between limited and diffuse systemic sclerosis patients}, author = { P. Garcia de la Pena-Lefebvre and Y. Chanseaud and M. C. Tamby and J. Reinbolt and F. Batteux and Y. Allanore and A. Kahan and O. Meyer and O. Benveniste and O. Boyer and L. Guillevin and M. C. Boissier and L. Mouthon}, year = {2004}, date = {2004-01-01}, journal = {Clin Immunol}, volume = {111}, number = {3}, pages = {241-51}, abstract = {We have analyzed antibody (Ab) reactivities of patients with limited systemic sclerosis (SSc) and anti-centromere Ab, patients with diffuse SSc and anti-topoisomerase 1 (anti-topo 1) Ab, patients with diffuse SSc without anti-topo 1 or anti-centromere Ab and age- and gender-matched healthy controls with normal human tissue and endothelial cell (EC) antigens. IgG reactivities with tissue antigens differed significantly between patients with anti-topo 1 Ab and patients with anti-centromere Ab. One 100-kDa band identified as topoisomerase 1 in macrovascular and microvascular EC extracts was recognized by IgG from patients with anti-topo 1 Ab and 50% of patients without specific Ab. IgG from patients with limited SSc and anti-centromere Ab, but not those of other patients or controls specifically recognized a 80-kDa band only in microvascular EC. Our results indicate that Ab from patients with limited or diffuse SSc with or without anti-topo 1 Ab exhibit specific and mutually exclusive reactivity patterns.}, note = {1521-6616 Journal Article}, keywords = {Aged, Assay, Autoantibodies/*analysis, Blotting, Cells/*immunology, Centromere/immunology, DNA, EHRESMANN, Electrophoresis, Endothelial, Enzyme-Linked, Female, G/analysis, Gel, Gov't, Human, I/*immunology, Immunoglobulin, Immunosorbent, M/analysis, Male, Middle, Non-U.S., Polyacrylamide, Scleroderma, Support, Systemic/*immunology, Topoisomerases, Type, Western}, pubstate = {published}, tppubtype = {article} } We have analyzed antibody (Ab) reactivities of patients with limited systemic sclerosis (SSc) and anti-centromere Ab, patients with diffuse SSc and anti-topoisomerase 1 (anti-topo 1) Ab, patients with diffuse SSc without anti-topo 1 or anti-centromere Ab and age- and gender-matched healthy controls with normal human tissue and endothelial cell (EC) antigens. IgG reactivities with tissue antigens differed significantly between patients with anti-topo 1 Ab and patients with anti-centromere Ab. One 100-kDa band identified as topoisomerase 1 in macrovascular and microvascular EC extracts was recognized by IgG from patients with anti-topo 1 Ab and 50% of patients without specific Ab. IgG from patients with limited SSc and anti-centromere Ab, but not those of other patients or controls specifically recognized a 80-kDa band only in microvascular EC. Our results indicate that Ab from patients with limited or diffuse SSc with or without anti-topo 1 Ab exhibit specific and mutually exclusive reactivity patterns. |
1999 |
Lamberty, M; Ades, S; Uttenweiler-Joseph, S; Brookhart, G; Bushey, D; Hoffmann, Jules A; Bulet, Philippe Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity Article de journal J. Biol. Chem., 274 (14), p. 9320–9326, 1999, ISSN: 0021-9258. Résumé | BibTeX | Étiquettes: Amino Acid, Animals, Antifungal Agents, Capillary, Chromatography, Defensins, Electrophoresis, Escherichia coli, Hemolymph, High Pressure Liquid, hoffmann, Insect Proteins, Larva, Lepidoptera, M3i, Micrococcus luteus, Proteins, Sequence Homology @article{lamberty_insect_1999, title = {Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity}, author = {M Lamberty and S Ades and S Uttenweiler-Joseph and G Brookhart and D Bushey and Jules A Hoffmann and Philippe Bulet}, issn = {0021-9258}, year = {1999}, date = {1999-04-01}, journal = {J. Biol. Chem.}, volume = {274}, number = {14}, pages = {9320--9326}, abstract = {Lepidoptera have been reported to produce several antibacterial peptides in response to septic injury. However, in marked contrast to other insect groups, no inducible antifungal molecules had been described so far in this insect order. Surprisingly, also cysteine-rich antimicrobial peptides, which predominate in the antimicrobial defense of other insects, had not been discovered in Lepidoptera. Here we report the isolation from the hemolymph of immune induced larvae of the lepidopteran Heliothis virescens of a cysteine-rich molecule with exclusive antifungal activity. We have fully characterized this antifungal molecule, which has significant homology with the insect defensins, a large family of antibacterial peptides directed against Gram-positive strains. Interestingly, the novel peptide shows also similarities with the antifungal peptide drosomycin from Drosophila. Thus, Lepidoptera appear to have built their humoral immune response against bacteria on cecropins and attacins. In addition, we report that Lepidoptera have conferred antifungal properties to the well conserved structure of antibacterial insect defensins through amino acid replacements.}, keywords = {Amino Acid, Animals, Antifungal Agents, Capillary, Chromatography, Defensins, Electrophoresis, Escherichia coli, Hemolymph, High Pressure Liquid, hoffmann, Insect Proteins, Larva, Lepidoptera, M3i, Micrococcus luteus, Proteins, Sequence Homology}, pubstate = {published}, tppubtype = {article} } Lepidoptera have been reported to produce several antibacterial peptides in response to septic injury. However, in marked contrast to other insect groups, no inducible antifungal molecules had been described so far in this insect order. Surprisingly, also cysteine-rich antimicrobial peptides, which predominate in the antimicrobial defense of other insects, had not been discovered in Lepidoptera. Here we report the isolation from the hemolymph of immune induced larvae of the lepidopteran Heliothis virescens of a cysteine-rich molecule with exclusive antifungal activity. We have fully characterized this antifungal molecule, which has significant homology with the insect defensins, a large family of antibacterial peptides directed against Gram-positive strains. Interestingly, the novel peptide shows also similarities with the antifungal peptide drosomycin from Drosophila. Thus, Lepidoptera appear to have built their humoral immune response against bacteria on cecropins and attacins. In addition, we report that Lepidoptera have conferred antifungal properties to the well conserved structure of antibacterial insect defensins through amino acid replacements. |
1994 |
Santos, M A; el-Adlouni, C; Cox, A D; Luz, J M; Keith, G; Tuite, M F Transfer RNA profiling: a new method for the identification of pathogenic Candida species Article de journal Yeast, 10 (5), p. 625-36, 1994, (0749-503x Journal Article). Résumé | BibTeX | Étiquettes: Candida/classification/*genetics/pathogenicity, Electrophoresis, Fungal, Gel, Genetic, Gov't, Markers, Non-U.S., Polyacrylamide, RNA, Support, Transfer/*analysis @article{, title = {Transfer RNA profiling: a new method for the identification of pathogenic Candida species}, author = { M. A. Santos and C. el-Adlouni and A. D. Cox and J. M. Luz and G. Keith and M. F. Tuite}, year = {1994}, date = {1994-01-01}, journal = {Yeast}, volume = {10}, number = {5}, pages = {625-36}, abstract = {A new molecular taxonomic method applicable to the identification of medically important Candida species and other yeast species has been developed. It is based on the electrophoretic pattern of total tRNA samples (a 'tRNA profile') isolated from Candida species and generated using high-resolution semi-denaturing urea-polyacrylamide gel electrophoresis and methylene blue staining. Species-specific tRNA profiles for the species C. albicans, C. tropicalis, C. parapsilosis, C. guilliermondii, C. glabrata and Pichia guilliermondii were obtained. Detailed studies with the major human pathogen of the Candida genus, C. albicans, demonstrated that the tRNA profile for a given species was both reproducible and strain-independent; seven different C. albicans strains generated identical tRNA profiles. Minor strain-specific heterogeneities in the tRNA profiles of C. guilliermondii and C. parapsilosis were detected, but in neither case did they significantly alter the species-specific diagnostic tRNA profile. The potential of this method in clarifying taxonomic anomalies was demonstrated by the finding that Type I and Type II strains of C. stellatoidea generate very different tRNA profiles, with that of a Type II strain being identical to the C. albicans tRNA profile. This method offers a number of advantages over current electrophoretic karyotype methods for species identification, both within the Candida genus and with yeast species in general.}, note = {0749-503x Journal Article}, keywords = {Candida/classification/*genetics/pathogenicity, Electrophoresis, Fungal, Gel, Genetic, Gov't, Markers, Non-U.S., Polyacrylamide, RNA, Support, Transfer/*analysis}, pubstate = {published}, tppubtype = {article} } A new molecular taxonomic method applicable to the identification of medically important Candida species and other yeast species has been developed. It is based on the electrophoretic pattern of total tRNA samples (a 'tRNA profile') isolated from Candida species and generated using high-resolution semi-denaturing urea-polyacrylamide gel electrophoresis and methylene blue staining. Species-specific tRNA profiles for the species C. albicans, C. tropicalis, C. parapsilosis, C. guilliermondii, C. glabrata and Pichia guilliermondii were obtained. Detailed studies with the major human pathogen of the Candida genus, C. albicans, demonstrated that the tRNA profile for a given species was both reproducible and strain-independent; seven different C. albicans strains generated identical tRNA profiles. Minor strain-specific heterogeneities in the tRNA profiles of C. guilliermondii and C. parapsilosis were detected, but in neither case did they significantly alter the species-specific diagnostic tRNA profile. The potential of this method in clarifying taxonomic anomalies was demonstrated by the finding that Type I and Type II strains of C. stellatoidea generate very different tRNA profiles, with that of a Type II strain being identical to the C. albicans tRNA profile. This method offers a number of advantages over current electrophoretic karyotype methods for species identification, both within the Candida genus and with yeast species in general. |
1993 |
Pochart, P; Agoutin, B; Fix, C; Keith, G; Heyman, T A very poorly expressed tRNA(Ser) is highly concentrated together with replication primer initiator tRNA(Met) in the yeast Ty1 virus-like particles Article de journal Nucleic Acids Res, 21 (7), p. 1517-21, 1993, (0305-1048 Journal Article). Résumé | BibTeX | Étiquettes: &, Acid, Base, cerevisiae/metabolism, Conformation, Data, development, DNA, Electrophoresis, Elements/*physiology, Gel, Met/metabolism, Molecular, Nucleic, Retroviridae/*growth, RNA, Saccharomyces, Sequence, Ser/*metabolism, Transfer, Transposable, Two-Dimensional, Viral/*metabolism @article{, title = {A very poorly expressed tRNA(Ser) is highly concentrated together with replication primer initiator tRNA(Met) in the yeast Ty1 virus-like particles}, author = { P. Pochart and B. Agoutin and C. Fix and G. Keith and T. Heyman}, year = {1993}, date = {1993-01-01}, journal = {Nucleic Acids Res}, volume = {21}, number = {7}, pages = {1517-21}, abstract = {The analysis of the tRNAs associated to the virus-like particles produced by the Ty1 element revealed the specific packaging of three major tRNA species, in about equal amounts: the replication primer initiator tRNA(Met), the tRNA(Ser)AGA and a tRNA undetected until now as an expressed species in yeast. The latter tRNA is coded by the already described tDNA(Ser)GCT. This tRNA is enriched more than 150 fold in the particles as compared to its content in total cellular tRNA where it represents less than 0.1% (initiator tRNA(Met) and tRNA(Ser)AGA being 11 and 4 fold enriched respectively). This tRNA is the only species coded by the tDNA(Ser)GCT gene which is found in three copies per genome since no other corresponding expressed tRNA could be detected. This gene is thus very poorly expressed. The high concentration of tRNA(Ser)GCU in the particles compared to its very low cellular content led us to consider its possible implication in Ty specific processes.}, note = {0305-1048 Journal Article}, keywords = {&, Acid, Base, cerevisiae/metabolism, Conformation, Data, development, DNA, Electrophoresis, Elements/*physiology, Gel, Met/metabolism, Molecular, Nucleic, Retroviridae/*growth, RNA, Saccharomyces, Sequence, Ser/*metabolism, Transfer, Transposable, Two-Dimensional, Viral/*metabolism}, pubstate = {published}, tppubtype = {article} } The analysis of the tRNAs associated to the virus-like particles produced by the Ty1 element revealed the specific packaging of three major tRNA species, in about equal amounts: the replication primer initiator tRNA(Met), the tRNA(Ser)AGA and a tRNA undetected until now as an expressed species in yeast. The latter tRNA is coded by the already described tDNA(Ser)GCT. This tRNA is enriched more than 150 fold in the particles as compared to its content in total cellular tRNA where it represents less than 0.1% (initiator tRNA(Met) and tRNA(Ser)AGA being 11 and 4 fold enriched respectively). This tRNA is the only species coded by the tDNA(Ser)GCT gene which is found in three copies per genome since no other corresponding expressed tRNA could be detected. This gene is thus very poorly expressed. The high concentration of tRNA(Ser)GCU in the particles compared to its very low cellular content led us to consider its possible implication in Ty specific processes. |
1992 |
Nothwang, H G; Coux, O; Keith, G; Silva-Pereira, I; Scherrer, K The major RNA in prosomes of HeLa cells and duck erythroblasts is tRNA(Lys,3) Article de journal Nucleic Acids Res, 20 (8), p. 1959-65, 1992, (0305-1048 Journal Article). Résumé | BibTeX | Étiquettes: Animals, Base, Blotting, Cells, Data, Ducks, effects, Electrophoresis, Erythroblasts, Gel, Gov't, Hela, Human, Lys/*analysis/metabolism, Molecular, Non-U.S., Northern, Nucleotidyltransferases/metabolism, Ribonucleoproteins/*chemistry/drug, RNA, Sequence, Support, Transfer, Two-Dimensional, Zinc/pharmacology @article{, title = {The major RNA in prosomes of HeLa cells and duck erythroblasts is tRNA(Lys,3)}, author = { H. G. Nothwang and O. Coux and G. Keith and I. Silva-Pereira and K. Scherrer}, year = {1992}, date = {1992-01-01}, journal = {Nucleic Acids Res}, volume = {20}, number = {8}, pages = {1959-65}, abstract = {Two-dimensional gel electrophoresis of HeLa cell prosomal RNAs, 3'-end labeled by RNA ligase, revealed one prominent spot. Determination of a partial sequence at the 3'-end indicated full homology to the 18 nucleotides at the 3'-end of tRNA(Lys,3) from rabbit, the bovine and the human species. An oligonucleotide complementary to the 3'-end of tRNA(Lys,3) hybridized on Northern blots with prosomal RNA from both HeLa cells and duck erythroblasts. In two-dimensional PAGE, the major pRNA of HeLa cells co-migrated with bovine tRNA(Lys,3). Reconstitution of the CCA 3'-end of RNA from both human and duck prosomes, by tRNA-nucleotidyl-transferase, confirmed the tRNA character of this type of RNA. Furthermore, it revealed at least one additional tRNA band about 85 nt long among the prosomal RNA from both species. Finally, confirming an original property of prosomal RNA, we show that in vitro synthesized tRNA(Lys,3) hybridizes stably to duck globin mRNA, and to poly(A)(+)- and poly(A)(-)-RNA from HeLa cells.}, note = {0305-1048 Journal Article}, keywords = {Animals, Base, Blotting, Cells, Data, Ducks, effects, Electrophoresis, Erythroblasts, Gel, Gov't, Hela, Human, Lys/*analysis/metabolism, Molecular, Non-U.S., Northern, Nucleotidyltransferases/metabolism, Ribonucleoproteins/*chemistry/drug, RNA, Sequence, Support, Transfer, Two-Dimensional, Zinc/pharmacology}, pubstate = {published}, tppubtype = {article} } Two-dimensional gel electrophoresis of HeLa cell prosomal RNAs, 3'-end labeled by RNA ligase, revealed one prominent spot. Determination of a partial sequence at the 3'-end indicated full homology to the 18 nucleotides at the 3'-end of tRNA(Lys,3) from rabbit, the bovine and the human species. An oligonucleotide complementary to the 3'-end of tRNA(Lys,3) hybridized on Northern blots with prosomal RNA from both HeLa cells and duck erythroblasts. In two-dimensional PAGE, the major pRNA of HeLa cells co-migrated with bovine tRNA(Lys,3). Reconstitution of the CCA 3'-end of RNA from both human and duck prosomes, by tRNA-nucleotidyl-transferase, confirmed the tRNA character of this type of RNA. Furthermore, it revealed at least one additional tRNA band about 85 nt long among the prosomal RNA from both species. Finally, confirming an original property of prosomal RNA, we show that in vitro synthesized tRNA(Lys,3) hybridizes stably to duck globin mRNA, and to poly(A)(+)- and poly(A)(-)-RNA from HeLa cells. |
1974 |
Goltzené, F; Hoffmann, Jules A Control of haemolymph protein synthesis and oocyte maturation by the corpora allata in female adults of locusta migratoria (Orthoptera): role of the blood-forming tissue Article de journal Gen. Comp. Endocrinol., 22 (4), p. 489–498, 1974, ISSN: 0016-6480. BibTeX | Étiquettes: Animals, Disc, Electrophoresis, Female, Grasshoppers, Hematopoietic System, Hemolymph, hoffmann, M3i, Ovum, Protein Biosynthesis, Radiation Effects @article{goltzene_control_1974, title = {Control of haemolymph protein synthesis and oocyte maturation by the corpora allata in female adults of locusta migratoria (Orthoptera): role of the blood-forming tissue}, author = {F Goltzené and Jules A Hoffmann}, issn = {0016-6480}, year = {1974}, date = {1974-04-01}, journal = {Gen. Comp. Endocrinol.}, volume = {22}, number = {4}, pages = {489--498}, keywords = {Animals, Disc, Electrophoresis, Female, Grasshoppers, Hematopoietic System, Hemolymph, hoffmann, M3i, Ovum, Protein Biosynthesis, Radiation Effects}, pubstate = {published}, tppubtype = {article} } |
1973 |
Koolman, J; Hoffmann, Jules A; Karlson, P Sulphage esters as inactivation products of ecdysone in Locusta migratoria Article de journal Hoppe-Seyler's Z. Physiol. Chem., 354 (9), p. 1043–1048, 1973, ISSN: 0018-4888. BibTeX | Étiquettes: Animals, Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, hoffmann, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, M3i, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium @article{koolman_sulphage_1973, title = {Sulphage esters as inactivation products of ecdysone in Locusta migratoria}, author = {J Koolman and Jules A Hoffmann and P Karlson}, issn = {0018-4888}, year = {1973}, date = {1973-09-01}, journal = {Hoppe-Seyler's Z. Physiol. Chem.}, volume = {354}, number = {9}, pages = {1043--1048}, keywords = {Animals, Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, hoffmann, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, M3i, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium}, pubstate = {published}, tppubtype = {article} } |