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  • 1
    Electronic Resource
    Electronic Resource
    Studies in audiogenic seizure susceptibility (1971)
    Springer
    Psychopharmacology 20 (1971), S. 48-56 
    Details
    ISSN: 1432-2072
    Keywords: Audiogenic Seizures ; Biogenic Amines ; Genetics ; Priming
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A genetically heterogeneous (HS) group of mice and a highly inbred strain of mice (C57BL/6) were both shown to become highly susceptible to audiogenic seizures after exposure to acoustic stimulation (priming). In heterogeneous mice the optimal age for priming was 18 days with a test-retest interval of 48 hours. The optimal test-retest interval in C57BL/6 mice primed at 20 days of age was 8 days. One second of priming was found effective in enhancing seizure susceptibility. Drugs known to alter steady state levels of biogenic amines and to change responses of mice genetically predisposed to audiogenic seizures were found to be effective in altering seizure susceptibility from priming, but not effective in altering the priming itself.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00404058
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  • 2
    Electronic Resource
    Electronic Resource
    Post-transcriptional regulation and DNA undermethylation of intracisternal A particle genes in embryonal carcinoma cell lines (1987)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 8 (1987), S. 125-133 
    Details
    ISSN: 0192-253X
    Keywords: retrovirus ; embryonal carcinoma ; embryonic gene ; DNA methylation ; gene expression ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Northern blot analysis and in vitro nuclear transcription assays were performed in order to clarify conflicting reports on the expression of intracisternal A particle (IAP) genes in embryonal carcinoma (EC) cell lines. Results demonstrate that post-transcriptional mechanisms control the final steady-state levels of IAP RNA in EC cells. IAP genes were further found to be undermethylated in IAP-expressing EC cell lines.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020080302
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  • 3
    Electronic Resource
    Electronic Resource
    Control of early gene expression in Dictyostelium (1988)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 9 (1988), S. 337-350 
    Details
    ISSN: 0192-253X
    Keywords: Dictyostelium ; cAMP ; receptor ; gene regulation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have examined the expression of a cAMP pulse-repressed and two cAMP pulse-induced genes in response to cAMP and caffeine under a number of different physiological conditions, and in several classes of developmental mutants altered in cAMP-mediated signal transduction pathways. The data presented help characterize the mutants with regard to early gene expression. Analysis of the data indicates that full induction of the pulse-induced or repression of the pulse-repressed genes requires cycles of activation and adaptation of the cAMP receptor but does not require a rise in intracellular cAMP. Comparison of the results obtained between different mutant classes suggests that repression and activation of the two classes of genes can be uncoupled, implying that different intracellular mechanisms control these processes. In addition, we examined the effects of caffeine and show that it can induce pulse-induced mRNA accumulation in the absence of cAMP.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020090415
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  • 4
    Electronic Resource
    Electronic Resource
    Antibodies directed against a yeast carboxyl-terminal peroxisomal targeting signal specifically recognize peroxisomal proteins from various yeasts (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 721-734 
    Details
    ISSN: 0749-503X
    Keywords: Peroxisomes ; protein tarageting ; Saccharomyces cerevisiae ; Candida tropicalis ; Candida albicans ; Yarrowia lipolytica ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The carboxyl-terminal tripeptide Ala-Lys-Ile is essential for targeting Canadida tropicalis trifunctional enzyme (hydratase-dehydrogenase-epimerase) to peroxisomes of both Candida albicans and Saccharomyces cerevisiae (Aitchison, J. D., Murray, W. W. and Rachubinski, R. A. (1991). J. Biol. Chem. 266, 23197-23203). We investigated the possibility that this tripeptide may act as a general peroxisomal targeting signal (PTS) for other proteins in the yeasts C. tropicalis, C. albicans, Yarrowia lipolytica and S. cerevisiae, and in rat liver. Anti-AKI antibodies raised against the carboxyl-terminal 12 amino acids of trifunctional enzyme were used to search for this PTS in proteins of these yeasts and of rat liver. The anti-AKI antibodies reacted exclusively with multiple peroxisomal proteins from the yeasts C. tropicalis, C. albicans and Y. lipolytica. There was a weak reaction of the antibodies with one peroxisomal protein from S. cerevisiae and no reaction with peroxisomal proteins from rat liver. Antibodies directed against a synthetic peptide containing a carboxyl-terminal Ser-Lys-Leu PTS (Gould, S. J., Krisans, S., Keller, G.-A. and Subramani, S. (1990). J. Cell Biol. 110, 27-34) reacted with multiple peroxisomal proteins of rat liver and with peroxisomal proteins of yeast distinct from those identified with anti-AKI antibodies. These results provide evidence that several peroxisomal proteins of different yeasts contain a PTS antigenically similar to that of C. tropicalis trifunctional enzyme and that this signal is absent from peroxisomal proteins from at least one mammalian system, rat liver.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320080905
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  • 5
    Electronic Resource
    Electronic Resource
    RPB7, one of two dissociable subunits of yeast RNA polymerase II, is essential for cell viability (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 295-299 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The Saccharomyces cerevisiae RNA polymerase II subunit gene RPB7 was isolated and sequenced. RPB7 is a single copy gene whose sequence predicts a 19,000 Dalton protein of 171 amino acids. RPB7 is known to dissociate from RNA polymerase II as an RPB4/RPB7 subcomplex in vitro. RPB7 also appears to interact with RNA polymerase II in a manner dependent upon RPB4, since RNA polymerase II purified from cells lacking RPB4 also lacks RPB7. Previous results have demonstrated that deletion of the RPB4 results in slow growth and cold- and temperature-sensitivity. In contrast, deletion of the RPB7 gene revealed that it is essential for cell growth and viability. Loss of both the RPB4 and the RPB7 genes causes lethality. These results suggest that RPB7 contributes to the function of RNA polymerase II in the absence of RPB4 either in a manner independent of its association with the enzyme or by directly binding to the enzyme in a manner independent of its association with RPB4.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090309
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  • 6
    Electronic Resource
    Electronic Resource
    Cloning and sequence of ADP-ribosylation factor 1 (ARF1) from Schizosaccharomyces pombe (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 923-927 
    Details
    ISSN: 0749-503X
    Keywords: ADP-ribosylation factors ; GTP-binding proteins ; Saccharomyces cerevisiae ; 3-amniotriazole ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A gene encoding a homologue of the ADP-ribosylation factor (ARF) family of small GTP binding proteins was cloned from a Schizosaccharomyces pombe cDNA library by a functional screen of suppressors of sensitivity to 3-aminotriazole in a gcn3 null strain of Saccharomyces cerevisiae. Two independent isolates each contained the full coding region of the ARF1 gene. The encoded SpARF1 protein has a predicted molecular weight of 20 618 and is 88% and 79% identical to human and S. cerevisiae ARF1 proteins, respectively. As independent isolates were obtained, this effect of the SpARF1 appears to be a real phenomenon, but cannot currently be easily understood within the context of the evidence for a role(s) for ARF proteins in the protein secretory pathway.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090812
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  • 7
    Electronic Resource
    Electronic Resource
    Mutations sensitizing yeast cells to the start inhibitor nalidixic acid (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 537-547 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; Start ; nalidixic acid ; ERG6 ; ARO7 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The regulatory step Start in the cell cycle of the budding yeast Saccharomyces cerevisiae is inhibited by nalidixic acid (Nal). To study this inhibition, mutations were identified that alter the sensitivity of yeast cells to Nal. Nal-sensitive mutations were sought because the inhibitory effects of Nal on wild-type cells are only transient, and wild-type cells naturally become refractory to Nal. Three complementation groups of Nal-sensitive mutations were found. Mutations in the first complementation group were shown to reside in the ARO7 gene, encoding chorismate mutase; tyrosine and phenylalanine synthesis was inhibited by Nal in these aro7 mutants, whereas wild-type chorismate mutase was unaffected. These aro7 alleles demonstrate ‘recruitment’, by mutation, of an innately indifferent protein to an inhibitor-sensitive form. The Nal-sensitive aro7 mutant cells were used to show that the resumption of Nal-inhibited nuclear activity and cell proliferation takes place while cytoplasmic Nal persists at concentrations inhibitory for the mutant chorismate mutase. Mutations in the second complementation group, nss2 (Nal-supersensitive), increased intracellular Nal concentrations, and may simply alter the permeability of cells to Nal. The third complementation group was found to be the ERG6 gene, previously suggested to encode the ergosterol biosynthetic enzyme sterol methyltransferase. Mutation or deletion of the ERG6 gene had little effect on the inhibition of Start by Nal, but prevented recovery from this inhibition. Mutation of ERG3, encoding another ergosterol biosynthetic enzyme, also caused Nal sensitivity, suggesting that plasma membrane sterol composition, and plasma membrane function, mediates recovery from Nal-mediated inhibition of Start.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320110603
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  • 8
    Electronic Resource
    Electronic Resource
    Yeast sequencing reports. Isolation of phosphoribosylpyrophosphate synthetase (PRS1) gene from Candida albicans (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 1295-1302 
    Details
    ISSN: 0749-503X
    Keywords: Candida albicans ; PRS1 ; phosphoribosylpyrophosphate synthetase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have isolated a 3·7 kb EcoR1 fragment from a genomic library of Candida albicans which displayed a 65% level of identity with the PRS gene family (PRS) of Saccharomyces cerevisiae. The PRS gene encodes a phosphoribosylpyrophosphate (PRPP) synthetase of S. cerevisiae, which catalyses the synthesis of purines, pyrimidines, and amino acids such as histidine and tryptophan. By Northern analyses, we observed that the entire 3·7 kb EcoR1 fragment as well as a 1·1 kb KpnI-SacI internal fragment of the 3·7 kb EcoR1 fragment hybridized to the same 1.4 kb transcript. An internal 2·6 kb KpnI fragment was subcloned and sequenced. A deduced sequence of 321 amino acids representing a polypeptide of 35·2 kDa was determined. A FASTA search indicated that the C. albicans PRS (Ca PRS1) had an overall homology at the amino acid level of 91% with the S. cerevisiae PRS3. Putative transcriptional start and termination sequences as well as a cation-binding, PRPP synthetase signature sequence were identified. Ca PRS1 was localized to chromosome 2 of the C. albicans genome. Low stringency hybridizations indicates that the organism may possess multiple PRS genes. The function of these genes in nitrogen signaling is discussed. The Ca PRS1 sequence submitted to the EMBL data library is available under Accession Number U23934.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320111310
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  • 9
    Electronic Resource
    Electronic Resource
    Rapid identification and characterization of peroxisomal assembly mutants in Yarrowia lipolytica (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 507-517 
    Details
    ISSN: 0749-503X
    Keywords: Peroxisome ; immunofluorescence ; PTS-1 ; electroporation ; yeast ; targeting ; biogenesis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We describe the isolation and characterization of peroxisomal assembly mutants in the genetically manipulable yeast Yarrowia lipolytica (pay mutants). These mutants were initially identified as oleic acid-non-utilizers by their inability to grow on oleic acid, the utilization of which requires peroxisomal β-oxidation enzymes. Identification of a subset of oleic acid-non-utilizers as pay mutants was obtained by a rapid immunofluorescence procedure using antibodies to the peroxisomal targeting signal Ser-Lys-Leu-CO2H. Punctate structures characteristic of peroxisomes were not detected in pay mutants using this technique. This rapid identification by immunofluorescence should be generally applicable to the selection of peroxisomal assembly mutants in other yeasts. To take advantage of the pay mutant system, we constructed a genomic library in the autonomously replicating vector pINA445 and developed an efficient and rapid electroporation procedure for the functional complementation of these mutants. We have been successful in functionally complementing two independent pay mutants. Molecular analysis of these and other complementing genes will allow for characterization of some of the cellular elements involved in peroxisomal assembly.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090506
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  • 10
    Electronic Resource
    Electronic Resource
    Identification of a putative histidine kinase two-component phosphorelay gene (CaHK1) in Candida albicans (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 665-674 
    Details
    ISSN: 0749-503X
    Keywords: histidine kinase ; phosphorylation ; signal transduction ; gene ; two-component ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have cloned and analysed the sequence of a putative histidine kinase, two-component gene (CaHK1) from Candida albicans. This gene encodes a 2471 amino acid protein (Cahk1p) with an estimated molecular mass of 281·8 kDa. A homology search of Cahk1p with other proteins in the databases showed that Cahk1p exhibits the greatest homology at its C-terminus with both the sensor and regulator components of prokaryotic and eukaryotic two-component histidine kinases. A further analysis of this homology showed that the Cahk1p possessed both sensor and regulator domains in the same polypeptide. Also, Cahk1p is likely to be a soluble protein. The sensor kinase domain of Cahk1p contains conserved motifs that are characteristic of all histidine kinase proteins, including the putative histidine which is believed to be autophosphorylated during activation, ATP binding motifs and others (F- and N-motifs), with unknown function. The Cahk1p regulator domain also contains conserved aspartate and lysine residues and the putative aspartate, which is secondarily phosphorylated by the autophosphorylated histidine. Finally, according to the codon usage frequency of the CaHK1 gene in comparison with other genes from C. albicans, there would appear to be a low level of expression of the gene. The accession number for the described sequence is AF013273, as filed in the EMBL/GenBank/DDBJ database. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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