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  • Articles  (12)
  • Life and Medical Sciences  (12)
  • 1995-1999  (12)
  • 1950-1954
  • 1
    Electronic Resource
    Electronic Resource
    Spinal cord central canal of the German shepherd dog: Morphological, histological, and ultrastructural considerations (1995)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 224 (1995), S. 205-212 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: This study deals with some macroscopical, microscopical, and ultrastructural aspects of the spinal cord central canal of the German shepherd dog. The caudal end of the spinal cord is constituted by the conus medullaris, which may extend to the first sacral vertebra, the terminal ventricle, and the filum terminale. The latter structure is considered as internum (second to third sacral vertebrae) or externum (fifth caudal vertebra), according to its relation to the dura mater. Occasionally, there is a second anchorage which is close to the level of the sixth caudal vertebra. The central canal is surrounded by a ciliated ependymal epithelium, which differs depending upon the levels. The most caudal part of the filum terminale bears a columnar ciliated ependymal epithelium surrounded by two layers of glia and pia mater, which separate the central canal from the subarachnoid space. Microfil injections show a communication between the cavity and the subarachnoid space, as the plastic is able to pass through the ependymal epithelium. At the level of the terminal ventricle there are real separations of the ependymal epithelium, which seem to connect the lumen of the spinal canal with the subarachnoid space. These structures probably constitute one of the drainage pathways of the cerebrospinal fluid. The diameter of the central canal is related to the age of the animal. However, even in very old animals the spinal cord central canal reaches the tip of the filum terminale and remains patent until death. At the ultrastructural level the ependymal cells present villi, located on cytoplasmic projections, cilia, dense mitochondria, and oval nuclei. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1052240209
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  • 2
    Electronic Resource
    Electronic Resource
    Seasonal variation in ovarian histology of the viviparous lizard Sceloporus torquatus torquatus (1995)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 226 (1995), S. 103-119 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Changes in ovarian histology during the reproductive cycle of the viviparous lizard Sceloporus torquatus torquatus are described. In general, the variation in follicular histology observed during the seasonal cycle is similar to that of other lizards. Sceloporus t. torquatus exhibits a cycle in which small, previtellogenic follicles exist in the ovary from December to August. Vitellogenesis occurs between September and November, followed by ovulation from late November to early December. Parturition occurs the following spring. After ovulation, the remaining follicular cells form the corpus luteum and luteolysis did not occur until April-May. Follicular atresia is commonly observed in previtellogenic follicles with polymorphic granulosa, but occurs less frequently in follicles during late vitellogenesis. There are two germinal beds in each ovary. The yolk nucleus is evident in young oocytes as is a vacuolated ooplasma prior to vitellogenesis. Extensive polymorphism is observed in yolk platelets. Mast cells and secretory cells are observed in the thecal layer of the follicular wall as are melanocytes in the ovarian stroma. © 1995 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1052260107
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  • 3
    Electronic Resource
    Electronic Resource
    Overexpression of an epitope- tagged β-tubulin in Chinese hamster ovary cells causes an increase in endogenous α-tubulin synthesis (1995)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 31 (1995), S. 259-272 
    Details
    ISSN: 0886-1544
    Keywords: microtubules ; transfection ; hemagglutinin antigen ; autoregulation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A Chinese hamster β-tubulin cDNA, engineered to express a 9 amino acid epitope from the influenza hemagglutinin antigen (HA), was transfected into Chinese hamster ovary (CHO) cells. The recombinant protein (HAβ1-tubulin) appeared to behave normally by the following criteria: immunofluorescence indicated that HAβ1-tubulin incorporated into all classes of interphase and spindle microtubules as well as microtubule organizing centers. The sensitivity of the cells expressing HAβ1-tubulin to Colcemid and taxol was unchanged. A 210 kD microtubule associated protein (MAP) remained associated with microtubules that incorporate HAβ1-tubulin. The synthesis of both endogenous β-tubulin and HAβ1-tubulin was repressed by colchicine. The HAβ1-tubulin incorporated into microtubules to the same extent as the endogenous β-tubulin, and the overall extent of microtubule assembly in transfected cells was unchanged. Finally, trasfected cells had normal growth rates and morphologies. When effects on endogenous tubulin production were measured, it was found that expression of the HAβ1-tubulin reduced the synthesis of endogenous wild-type β-tubulin but increased the synthesis of α-tubulin. At steady state, a small increase in total tubulin consistent with the increased synthesis of α-tubulin was found. The results indicate that expression of excess exogenous β-tubulin perturbs the synthesis of endogenous α-tubulin in a manner that is not easily explained by current models of tubulin regulation. The changes in tubulin synthesis along with degradation of excess tubulin subunits may reflect mechanisms that exist to ensure coordinate levels of α- and β-tubulin for assembly. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970310403
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  • 4
    Electronic Resource
    Electronic Resource
    Order-disorder in T, T′, and T* phase: Superconductors and related materials (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 30 (1995), S. 193-207 
    Details
    ISSN: 1059-910X
    Keywords: Superconductivity ; n-type superconductors ; Nonstoichiometry ; Superconducting oxides ; T, T′ ; T* structures ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: After reviewing microstructural studies on superconducting materials showing T, T′, and T* structural types, results are presented on the microstructure of some n-type superconductors and related materials prepared with accurate control of the oxygen stoichiometry. Electron microscopy is used to describe the ordering of interstitial oxygen defects in T-type La2NiO4+δ leading to the formation of the n = 2 term of a homologous series with the general formula La8nNi4nO16n+1. Structural transitions and superstructure formation in the Pr2-x-yCexSryCuO4-δ system are reported, where T, T′:;, and T* phases are isolated as a function of both Ce and Sr content. © 1995 Wiley-Liss, Inc.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070300302
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  • 5
    Electronic Resource
    Electronic Resource
    Role of amino acid-induced changes in ion fluxes in the regulation of hepatic protein synthesis (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 163 (1995), S. 277-284 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Alanine is a powerful stimulator of hepatic protein synthesis whose mechanism of action has not yet been ascertained. The present work aimed to elucidate whether rate changes in ion fluxes accompanying the transport of this amino acid could play a role in the stimulation of protein synthesis. In perfused livers, the utilization of alanine produced a net uptake of K+ of 1.5 μMol/min/liver, a progressively increasing efflux of Ca2+ to reach a maximum of 0.9 μMol/min/liver, and alkalization of the extracellular medium. Inhibition of Na+/K+ exchange by ouabain reversed only the uptake of K+, indicating that this is the main way for the efflux of Na+ cotransported with alanine. In isolated hepatocytes, the uptake of alanine increased the intracellular content of K+ and the cell volume. The following observations suggest that these changes, and not an increased intracellular concentration of Na+, are associated with the stimulation of protein synthesis: 1) Ouabain inhibited the alanine stimulation of L-[3H]-valine incorporation into protein without altering the basal rate of protein labeling; 2) ouabain had no effects on alanine uptake indicating that Na+ influx is not involved in the alanine stimulation of protein synthesis; 3) disruption of Na+ gradient across the plasma membrane by specific ionophores, monensin and gramicidin D, inhibited both basal and alanine-stimulated protein synthesis, but substitution of extracellular Na+ by K+ did not prevent the stimulatory action of alanine. The observation that hypotonic buffer enhanced protein synthesis to the same degree than alanine in liver cells indicates that alanine-induced cell swelling could be sufficient to stimulate protein synthesis. © 1995 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041630208
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  • 6
    Electronic Resource
    Electronic Resource
    DNA Sequence Analysis of a 23 002 bp DNA Fragment of the Right Arm of Saccharomyces cerevisiae Chromosome VII (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 13 (1997), S. 357-363 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; yeast genome ; genome sequencing ; chromosome VII ; QCR9 ; UBR1 ; TYS1 ; TFG1 ; HGH1 ; BUB1 ; tRNALeu3 ; tRNATrp ; tRNALys1 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the sequence of a 23 002 bp fragment located on the right arm of Saccharomyces cerevisiae chromosome VII. Analysis of this region revealed 14 complete open reading frames (ORFs) with more than 300 base pairs. Six of them correspond to previously known genes. G7164 is the QCR9 gene coding for subunit 9 of the cytochrome c reductase; G7168 is UBR1, encoding an ubiquitin protein ligase; G7522 is the TYS1 gene, which encodes for the tyrosyl tRNA synthetase; G7526 is TFG1, the gene coding for the RNA polymerase transcription initiation factor TFIIF (factor G); G7538 is the gene HGH1 which encodes a protein related to the mammalian HMG1 and HMG2 proteins. G7542 is the BUB1 gene which encodes a ser/thr protein kinase involved in spindle assembly during the cell cycle. One of the ORFs, G7553, shares significant homologies with the gene UTR2 from S. cerevisiae. None of the seven remaining ORFs shows similarity to any of the sequences within the public databases. Three ORFs are internal ORFs of the above-described known genes, and two small ORFs are completely contained in larger ORFs on the complementary strand, and therefore probably do not correspond to real genes. This region also contains three genes specifying tRNAs for Leu, Lys and Trp, and several LTR elements. The sequence described in this paper has been deposited in the EMBL data library under the Accession Number X99074. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 3 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    Isolation and Characterization of the KlHEM1 Gene in Kluyveromyces lactis (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 13 (1997), S. 961-971 
    Details
    ISSN: 0749-503X
    Keywords: Kluyveromyces lactis ; HEM1 ; 5-aminolevulinate synthase ; transcription regulation ; heme-responsive element ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The KlHEM1 gene from Kluyveromyces lactis encodes a functional 5-aminolevulinate synthase (δALA synthase), as confirmed by complementation of a hem1 mutant Saccharomyces cerevisiae strain, homology search, and detection of a 2·3 kb transcript. The gene is highly homologous to the ScHEM1 gene, and the sequence of the promoter region contains a complex combination of putative regulatory signals. Some of them are related to phospholipid biosynthesis, glycolytic metabolism, and regulation by carbon source. Transcription of KlHEM1 increased significantly in response to limited oxygen, and only slightly with the change from repressed (glucose) to derepressed conditions (glycerol). The δALA synthase from K. lactis contains, in the amino-terminal region, two heme-responsive elements that are not present in the protein from Saccharomyces cerevisiae. The complete nucleotide sequence has been entered in the EMBL data library under Accession Number X92944. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 6 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    Isolation and sequence analysis of the orotidine-5'-phosphate decarboxylase gene (URA3) of Candida utilis. Comparison with the OMP decarboxylase gene family (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 1399-1406 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; Candida utilis ; URA3 ; orotidine 5′-monophosphate decarboxylase ; transformation system ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The URA3 gene of Candida utilis encoding orotidine-5′-phosphate decarboxylase enzyme was isolated by complementation in Escherichia coli pyrF mutation. The deduced amino-acid sequence is highly similar to that of the Ura3 proteins from other yeast and fungal species. An extensive analysis of the family of orotidine-5′-phosphate decarboxylase is shown. The URA3 gene of C. utilis was able to complement functionally the ura3 mutation of Saccharomyces cerevisiae. The sequence presented here has been deposited in the EMBL data library under Accession Number Y12660. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    VII. Yeast sequencing reports. The complete sequence of a 9000 bp fragment of the right arm of Saccharomyces cerevisiae chromosome VII contains four previously unknown open reading frames (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 11 (1995), S. 1087-1091 
    Details
    ISSN: 0749-503X
    Keywords: yeast genome ; chromosome VII ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the sequence of a 9000 bp fragment from the right arm of Saccharomyces cerevisiae chromosome VII. Analysis of the sequence revealed four complete previously unknown open reading frames, which were named G7587, G7589, G7591 and G7594 following standard rules for provisional nomenclature. Outstanding features of some of these proteins were the homology of the putative protein coded by G7589 with proteins involved in transcription regulation and the transmembrane domains predicted in the putative protein coded by G7591. The sequence reported has been deposited in the EMBL data library under Accession Number X82775.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320111110
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  • 10
    Electronic Resource
    Electronic Resource
    A rapid and reliable method for metabolite extraction in yeast using boiling buffered ethanol (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 13 (1997), S. 1347-1355 
    Details
    ISSN: 0749-503X
    Keywords: yeast metabolism ; metabolite extraction ; metabolic engineering ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A simple and reliable method for the efficient inactivation of metabolism and for quantitative metabolite extraction from yeast cells is presented. It is based on the use of a boiling solution made of 75% ethanol (volume/final volume) buffered with 70 mm-Hepes (final concentration), pH 7·5, to guarantee the stability throughout the whole procedure of a large variety of metabolites, including all glycolytic intermediates, nucleotides, pyridine nucleotides and organic acids compounds. The extraction is fast, requiring only 3 min incubation of yeast cells in the ethanol-buffered mixture maintained at 80°C. It can be carried out either directly by spraying the cells into the boiling mixture, or after quenching the whole culture in 60% methanol kept at -40°C. Extracts are subsequently concentrated by evaporation under partial vacuum and the residue is resuspended in a small volume of water. This concentration step and the use of a highly sensitive analytical method allow us to quantify metabolites in less than 10 mg dry weight cells. This method, which can be applied to other fungi, could be very helpful for the determination of true metabolites in mutants generated through the EUROFAN programme and for metabolic flux analysis. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 3 Ill.
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