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  • 1
    Electronic Resource
    Electronic Resource
    Ultrastructural Damage by Cadmium in a Marine Dinoflagellate, Prorocentrum micans (1981)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 28 (1981), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Prorocentrum micans Ehrenberg, a free-living marine dinoflagellate, was used to test the intracellular toxic action of cadmium. The cells were cultivated in Erdschreiber medium, with Cd concentrations of 10–100 ppb. Thin sections of treated cells, examined ultramicroscopically, exhibited vacuolations, increased numbers of lysosomes, and severe mitochondrial damage. The first two alterations are a general response to toxicity; the third is Cd specific. Although some chloroplasts were affected by Cd, they were not very sensitive to its action. The nuclear apparatus was not morphologically affected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1981.tb02856.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Changes in ATP Concentration, Mitochondrial Structures, and Rhodamine 123 Binding in Two Marine Dinoflagellates Cultured in the Presence of Parathion (1994)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 41 (1994), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Parathion, an organophosphorus insecticide, is highly toxic to the two free-living marine dinoflagellates Prorocentrum micans Ehrenberg (autotrophic) and Crypthecodinium cohnii Biechler (heterotrophic). To study its non-antiacetylcholinesterase action we assessed its effect on the mitochondrial system, as shown by changes in intracellular ATP concentration and in rhodamine 123 fluorescence evaluated by image analysis. The technique of image analysis permits direct assessment of changes in the overall activity of mitochondria in living cells. Mitochondrial structures were also examined in the electron microscope. The three methods of investigation yielded complementary results. In P. micans, parathion noticeably altered mitochondria but did not significantly alter ATP concentrations. In C. cohnii, however, mitochondrial disturbance was slight, whereas ATP increased greatly. We think, therefore, that parathion has different effects on mitochondria in the two organisms, and in particular that it increases mitochondrial activity in C. cohnii.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1994.tb05935.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Structure–activity relationship study of the plasma membrane translocating potential of a short peptide from HIV-1 Tat protein (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 429-436 
    Details
    ISSN: 1573-3904
    Keywords: Membrane ; Tat ; Vectorization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Tat, a 86-amino acid protein involved in thereplication of Human Immunodeficiency Virus type 1(HIV-1), is able to translocate efficiently throughthe plasma membrane and to reach the nucleus totransactivate the viral genome. The region 37–72 ofthe Tat protein, centered on a cluster of basicamino acids, has been assigned to this translocationactivity. Recent data in our group have attributedthis membrane translocating activity to a peptideextending from residues 48 to 60, which contains acluster of eight basic amino acids within a linearsequence of nine residues. Internalization of thispeptide into cells occurred within minutes atconcentrations as low as 100 nM. In order to definemore precisely the involvement of these basic aminoacids in peptide translocation, several analoguescarrying deletions or substitutions of one, orseveral, of the basic residues were synthesized andtested for their cellular uptake and nucleartranslocation. A direct correlation between theoverall charge of the peptide and its cellinternalization was found. In addition, the covalentlinkage of this short basic peptide allows theefficient translocation of a non-membrane permeant peptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008850300184
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Structure-activity relationship study of the plasma membrane translocating potential of a short peptide from HIV-1 Tat protein (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 429-436 
    Details
    ISSN: 1573-3904
    Keywords: Membrane ; Tat ; Vectorization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Tat, a 86-amino acid protein involved in the replication of Human Immunodeficiency Virus type 1 (HIV-1), is able to translocate efficiently through the plasma membrane and to reach the nucleus to transactivate the viral genome. The region 37–72 of the Tat protein, centered on a cluster of basic amino acids, has been assigned to this translocation activity. Recent data in our group have attributed this membrane translocating activity to a peptide extending from residues 48 to 60, which contains a cluster of eight basic amino acids within a linear sequence of nine residues. Internalization of this peptide into cells occurred within minutes at concentrations as low as 100 nM. In order to define more precisely the involvement of these basic amino acids in peptide translocation, several analogues carrying deletions or substitutions of one, or several, of the basic residues were synthesized and tested for their cellular uptake and nuclear translocation. A direct correlation between the overall charge of the peptide and its cell internalization was found. In addition, the covalent linkage of this short basic peptide allows the efficient translocation of a non-membrane permeant peptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02442912
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    Paper (German National Licenses)
    Fulltext
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