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  • 1
    Electronic Resource
    Electronic Resource
    Post-transcriptional transactivation of human retroviral envelope glycoprotein expression by herpes simplex virus Us11 protein (1996)
    [s.l.] : Nature Publishing Group
    Nature 379 (1996), S. 273-277 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] To determine whether Usll protein could substitute for HTLV-I Rex protein, HeLa cells were cotransfected with three different vectors; the first expressing HTLV-I envelope (env) glycoprotein through a non-spliceable primary transcript; the second expressing Tax transcriptional transactivator (tax); ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/379273a0
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  • 2
    Electronic Resource
    Electronic Resource
    In situ hybridization and immuno-electron microscope analyses of the Us11 gene of herpes simplex virus type 1 during transient expression (1996)
    Springer
    Chromosoma 104 (1996), S. 434-444 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The distribution of Us11 RNA and of its encoded protein have been investigated at the ultrastructural level in HeLa cells transiently expressing the Us11 gene of herpes simplex virus type 1. In these transfected cells, Us11 protein accumulates at sites identical to those of lytically infected cells, i.e., in nucleoli and in regions of the cytoplasm that contain ribosomes. Us11 RNA and polyadenylated RNA are scattered over the ribosome-rich areas of the cytoplasm. They also accumulate in the nucleoplasm on clustered ribonucleoprotein (RNP) fibrils but also in clusters of interchromatin granules, some of them contiguous to nucleoli. However they are never found in nucleoli. These data reveal the involvement of interchromatin granules in some steps of Us11 mRNA maturation and/or transport.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00352267
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  • 3
    Electronic Resource
    Electronic Resource
    In situ hybridization and immuno-electron microscope analyses of the Us11 gene of herpes simplex virus type 1 during transient expression (1996)
    Springer
    Chromosoma 104 (1996), S. 434-444 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The distribution of Us11 RNA and of its encoded protein have been investigated at the ultrastructural level in HeLa cells transiently expressing the Us11 gene of herpes simplex virus type 1. In these transfected cells, Us11 protein accumulates at sites identical to those of lytically infected cells, i.e., in nucleoli and in regions of the cytoplasm that contain ribosomes. Us11 RNA and polyadenylated RNA are scattered over the ribosomerich areas of the cytoplasm. They also accumulate in the nucleoplasm on clustered ribonucleoprotein (RNP) fibrils but also in clusters of interchromatin granules, some of them contiguous to nucleoli. However they are never found in nucleoli. These data reveal the involvement of interchromatin granules in some steps of Us11 mRNA maturation and/or transport.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00352267
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  • 4
    Electronic Resource
    Electronic Resource
    Bombyx mori L. Ribosomal proteins: Resolution, nomenclature, molecular weights and in vivo phosphorylation (1981)
    Springer
    Molecular genetics and genomics 182 (1981), S. 273-278 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Bombyx mori L. ribosomal proteins have been analyzed by four related two-dimensional polyacrylamide gel electrophoretic systems (Madjar et al. 1977a). In the small and large subunits are present 32 and 45 proteins, respectively, whose numbering is proposed. No significant differences in composition or migration could be detected between proteins in membranebound ribosomes and free ribosomes. The molecular weights of the proteins vary from 60,000 to less than 10,000. In vivo phosphorylation was investigated by labeling with 32P-orthophosphate. Autoradiograms of four two dimensional gels unambiguously show five labeled ribosomal proteins: S1, S7, L6, L29, and L40.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269670
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  • 5
    Electronic Resource
    Electronic Resource
    Spot position of rat liver ribosomal proteins by four different two-dimensional electrophoreses in polyacrylamide gel (1979)
    Springer
    Molecular genetics and genomics 171 (1979), S. 121-134 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Separation of the proteins from rat liver 40S and 60S ribosomal subunits and polysomes was done in four different two-dimensional polyacrylamide gel electrophoresis systems. The first dimension was run at acidic or basic pH, the second dimension either with sodium dodecyl sulphate or at acidic pH in 18% acrylamide. The position of each individual protein of both subunits and polysomes was determined in each system. This identification resulted from a new method avoiding any previous purification of individual proteins. The new “proposed uniform nomenclature for mammalian ribosomal proteins” (McConkey et al. in press) was used for numbering the proteins in the four systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269998
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  • 6
    Electronic Resource
    Electronic Resource
    Differences in electrophoretic behaviour of eight ribosomal proteins from rat and rabbit tissues and evidence for proteolytic action on liver proteins (1980)
    Springer
    Molecular genetics and genomics 179 (1980), S. 89-101 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Divergence exists between eight ribosomal proteins of rat and rabbit. This is the first time such a divergence has been precisely demonstrated among mammals. In addition, a proteolytic activity, giving the appearance of modified proteins, is observed in the liver of both species but not in rabbit reticulocytes. These results were made possible by a recently developed method. Ribosomal proteins were compared by two-dimensional polyacrylamide gel electrophoresis in four different but related systems. The precise position of each individual protein was established in each of the four systems. Certain ribosomal proteins from different tissues, seemingly identical in one system were found to be different in other systems. Significant differences occurred between proteins of each ribosomal subunit from the two different species. Variation between reticulocyte and liver ribosomal proteins of the rabbit were minor. Several liver proteins of both species change position or disappear and apparently new proteins appear, if appropriate steps are not taken to prevent proteolysis. Differences in behavior of three small subunit and five large subunit proteins are attributable to an evolutionary divergence between the two species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268450
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  • 7
    Electronic Resource
    Electronic Resource
    Ribosome and protein synthesis modifications after infection of human epidermoid carcinoma cells with herpes simplex virus type 1 (1990)
    Springer
    Molecular genetics and genomics 220 (1990), S. 377-388 
    Details
    ISSN: 1617-4623
    Keywords: Ribosome ; Protein phosphorylation ; Shut off ; HSV-1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Modifications of ribosomes have been investigated in human epidermoid carcinoma-2 cells at different stages of herpes simplex virus type 1 infection. Very early in infection, there is an increase in ribosomal protein S6 phosphorylation even in the absence of serum. The same result is obtained in the presence of actinomycin D. At early infection time, ribosomal proteins S2, S3a and Sa are newly phosphorylated. At early and early-late times, three phosphorylated non-ribosomal proteins (v1, v2 and v3) are differently associated temporally to ribosomes. Analyses of proteins extracted from 40S subunits, 80S ribosomes and polysomes show that v1 and v2 are distributed differently among the different ribosomal populations. S6 phosphopeptides were found to be identical after serum stimulation and after viral infection. In every case phosphoserine and phosphothreonine were identified in S6. Only phosphoserine was found in other phosphorylated proteins. Our results indicate that herpes simplex virus type 1 is able to modify pre-existing ribosomes: (i) by stimulating a pre-existing kinase for S6 phosphorylation even in the absence of serum and of viral genome expression; (ii) by inducing new specific kinase activity(ies); and (iii) by association of new, phosphorylated proteins to ribosomes. These ribosomal modifications are correlated with changes in protein synthesis, as shown by two-dimensional electrophoretic analyses of newly synthesized 35S-labelled proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00391742
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  • 8
    Electronic Resource
    Electronic Resource
    Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1317-1322 
    Details
    ISSN: 0173-0835
    Keywords: Herpes simplex virus ; Us11 ; phosphorylation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The Us11 protein is a true late gene product of herpes simplex virus type 1 (HSV-1), whose exact function is unknown but which exhibits RNA-binding properties and which is phosphorylated on serine residues. In order to determine whether the Us11 protein is phosphorylated by cellular kinase(s) or by virally encoded kinase(s), the Us11 gene has been cloned and transiently expressed in HeLa cells. In addition, HeLa-derived cell lines have been selected for their ability to express Us11 protein constitutively. 32P-Labeling and analysis by two-dimensional electrophoresis of transiently and constitutively expressed Us11 protein demonstrated that, indeed, multiple phosphorylation of the protein occurs in absence of HSV-1 genome expression, indicating that the protein behaves as a natural substrate for cellular kinase(s). In addition, a sequence heterogeneity of the Us11 protein, due to a difference in the number of SPREPR repeats, has been characterized between different strains of HSV-1.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601216
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  • 9
    Electronic Resource
    Electronic Resource
    Precise quantitation of chloramphenicol acetyl transferase reporter mRNA by competitive polymerase chain reaction (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 1292-1294 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A strategy, based on competitive polymerase chain reaction (PCR) after reverse transcription, was developed to quantitate mRNA of the E. coli chloramphenicol acetyl transferase (CAT) gene. Precise quantitation of this rare mRNA is achieved by co-amplification of a constant amount of the complementary DNA (cDNA) with successive dilutions of a competitive DNA template of known concentration and with the use of the same primers. The unique EcoRI site located in the CAT coding sequence has been abolished in the competitive DNA. The two oligonucleotide primers used are both located in the CAT coding sequence at equal distance from the EcoRI site. After amplification, the PCR products from the cDNA to be quantified and from the competitor DNA are discriminated by EcoRI digestion, followed by separation of the resulting fragments by agarose gel electrophoresis. DNA amplified from the target cDNA is the only DNA digested by EcoRI into two fragments of identical size co-migrating in an agarose gel. After ethidium bromide staining, comparison of the intensity of fluorescence of the resulting bands in a competition series permits us to estimate precisely the amount of CAT cDNA and therefore of the mRNA to be quantified.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401197
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  • 10
    Electronic Resource
    Electronic Resource
    Very alkaline immobilized pH gradients for two-dimensional electrophoresis of ribosomal and nuclear proteins (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 328-337 
    Details
    ISSN: 0173-0835
    Keywords: Alkaline proteins ; Histones ; Immobilized pH gradient ; Nuclear proteins ; Ribosomal proteins ; Two-dimensional polyacrylamide gel electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Basic proteins normally lost by the cathodic drift of carrier ampholyte focusing, or separated by NEPHGE with limited reproducibility, could be well separated by two-dimensional (2-D) electrophoresis under equilibrium conditions using immobilized pH gradients (IPGs) 4-10 and 6-10 using a previously published protocol (Görg et al., Electrophoresis 1988, 9, 531-546). In the present study we have extended the pH gradient to pH 12 with IPGs 8-12, 9-12 and 10-12 for the analysis of very basic proteins. Different optimization steps with respect to pH engineering, gel composition and running conditions, such as substitution of acrylamide by dimethylacrylamide and addition of isopropanol with and without methylcellulose to the IPG rehydration solution (in order to suppress the reverse electroosmotic flow) were necessary to obtain highly reproducible 2-D patterns of ribosomal proteins from HeLa cells and mouse liver. Histones from chicken erythrocyte nuclei as well as total cell extracts of erythrocytes were also successfully separated under steady-state conditions. Due to the selectivity of isoelectric focusing in IPG 9-12, where the more acidic proteins abandon the gel, the tedious procedure of nuclei preparation prior to histone extraction can be omitted.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180306
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