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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 211 (2002), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: To better understand the protein secretion mechanisms involved in the growth and pathogenesis of Mycobacterium tuberculosis, we examined the secA gene from M. tuberculosis (tbsecA; cosmid sequence accession No. z95121.gb_ba). We generated plasmids containing the full-length tbsecA gene or a fusion containing the 5′ sequence from the M. tuberculosis secA gene and the remainder from the Escherichia coli secA gene and evaluated the ability of each construct to complement the defective SecA protein in E. coli MM52ts when grown at the non-permissive temperature. The full-length tbsecA gene was unable to compensate for the temperature-sensitive defect, whereas E. coli MM52ts that has been transformed with plasmid pMF8TB226 containing a chimeric secA gene was able to grow at 42°C. This work confirms that the topography of SecA and its ATP binding sites are highly conserved, whereas its membrane insertion domains are species specific.
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 215 (2002), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In this report we describe the development of a highly stringent and dually regulated promoter system for Shigella flexneri. Dual regulation was provided by utilizing a promoter susceptible to control by the bacteriophage P1 temperature-sensitive C1 repressor that in turn was under the transcriptional control of LacI. The level of induction/repression ratios observed was up to 3700-fold in S. flexneri. The general utility of this promoter system was evaluated by demonstrating that the bacteriophage P1 post-segregational killer protein Doc mediates a bactericidal effect in S. flexneri. This represents the first report of Doc (death on curing)-mediated killing in this Gram-negative species.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 252 (1972), S. 255-282 
    ISSN: 1434-601X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract We discuss the degeneracy structure of Regge trajectories and residues in mesonbaryon scattering amplitudes which results from non-exoticism in a dualSU(3) picture. Plots of universal baryon residue functions are presented, which show to what extent this structure is realized by the experimental baryon resonances. TheEXD structure of the Regge trajectories in the mesonict-channel is tested in the highenergy forward scattering region. We present fits to the experimental data, including weak absorption corrections. A value ofF/D∼1/3 for theA-Amplitude, and a suppressedA′, are found to be consistent with both the resonance and scattering data. A common description of the high-energy and low-energy data is sought in terms of a five parameter Veneziano amplitude.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 21 (1984), S. 383-385 
    ISSN: 1434-6052
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract We demonstrate that the sliding singlet mechanism for keeping the doublet Higgs components light is influenced by the radiative effects of spontaneous breaking of global supersymmetry induced by a still unobserved field. An upper limit on the mass of this field arises.
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  • 5
    ISSN: 1423-0127
    Keywords: HIV-1 Rev ; Nuclear export ; Cis acting repressor sequences ; HIV-1 protease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Rev has been shown to promote the export of HIV-1 RNAs fromXenopus oocyte nuclei, but a system to examine the direct effect of Rev on HIV-1 RNA export in mammalian somatic cells does not exist. In this report, the development of a cell-free RNA export system using COS cells is described. This system is capable of examining the movement of RNA from nuclei of COS cells transfected with an HIV-1 proviral construct into reconstituted cytosol from nontransfected cells. A reproducible preparation of nuclei free of residual cytoplasmic RNA is demonstrated. Export of RNA from these nuclei into reconstituted cell-free extracts was saturable and dependent on temperature and energy. Further validation of the system was obtained by confirming that the nuclear export of HIV-1-unspliced and partially spliced RNAs was dependent upon the expression of HIV-1 Rev and that the presence of Rev appeared to decrease the export of an HIV-1-spliced RNA. The system was also able to demonstrate that Rev did not appear to significantly enhance the export of an HIV-1 protease-containing RNA that has been shown to be dependent upon Rev for maximal expression. Consequently, the system appears useful for the examination of parameters of nuclear export of HIV-1 and cellular RNAs.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of biomedical science 5 (1998), S. 305-308 
    ISSN: 1423-0127
    Keywords: HIV-1 protease ; Regulation ; Capsid ; Major homology region
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The maturation of human immunodeficiency type-1 virions is accomplished through the proteolytic processing of Gag and GagPol precursor proteins by the viral protease (PR). Since virions must be assembled at the cell surface from uncleaved precursor molecules, intracellular activation of PR must be inhibited. We have previously developed a system where the intracellular activity of PR, associated with GagPol, was inhibited by the expression of Gagin trans. The disproportionate synthesis of Gag inhibits the activation of PR in the cytoplasm. Sequences capable of mediating this inhibition were localized to capsid. In this communication, the region of HIV-1 capsid capable of mediating inhibition was further defined and shown to require the major homology region of capsid within Gag.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 64 (1994), S. 111-116 
    ISSN: 1434-6052
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The higher derivative expansion of the one-loop effective action for an external scalar potential is calculated to order {ie111-1}, using the string-inspired Bern-Kosower method in the first quantized path integral formulation. Comparisons are made with standard heat kernel calculations and with the corresponding Feynman diagrammatic calculation in order to show the efficiency of the present method.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 23 (1984), S. 157-163 
    ISSN: 1434-6052
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract We investigate the potentials of supergravity models with canonical kinetic energy and derive several properties. If the model isR-invariant with non-negativeR-charges, we prove that the potential is strictly positive and vanishes without finetuning if and only if supersymmetry is unbroken. Allowing for negativeR-charges we present a model where supersymmetry is broken in the absolute minimum which is finetuned toV min=0.
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  • 9
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The SecA protein occupies a pivotal position in the public protein export pathway inEscherichia coli. The multifunctional SecA protein recognizes cytoplasmic factors associated with export including the presecretory protein and targets the complex to the inner membrane, where it acts in the early stages of protein translocation. The ability of SecA to bind ATP was the basis for the development of a novel, rapid purification scheme involving a single chromatographic step. Affinity chromatography was carried out on Red Sepharose CL-6B. The SecA present in crude extracts ofE. coli binds strongly to this dye-ligand matrix, and active protein was purified to greater than 90% homogeneity. The protein isolated by this procedure retained the previously described ATPase and RNA-binding activities of SecA. This approach should permit the rapid purification of SecA homologs from a variety microorganisms.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Current microbiology 38 (1999), S. 113-121 
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Expression from the secA gene, encoding a key component of the general secretory pathway of Escherichia coli, is influenced by the secretion status of the cell, autogenous translational repression, and translational coupling to the upstream gene, X. SecA binds to its mRNA in a region overlapping its ribosome binding site, thus competing with ribosomes that would initiate secA translation. Mapping of the geneX-secA mRNA secondary structure has demonstrated that the RNA can adopt two distinct conformations in solution. The first conformation arises from the base-pairing of the secA Shine-Dalgarno (SD) sequence with the geneX terminus. The second conformation, in which the secA SD sequence is no longer paired with the geneX terminus, contains a GC-rich stem upstream of the secA SD sequence. The presence of this GC-rich stem is supported by structure mapping of a mutant RNA containing a deletion in the geneX terminus. The former structure appears to be involved in translational coupling by directly linking the geneX and secA sequences, where geneX translation activates secA translational initiation through the unpairing and unmasking of the secA SD sequence. As indicated by SecA-RNA binding assays, the latter structure is probably involved in SecA binding and translational repression of the secA gene. The stabilizing effect of magnesium ions toward occlusion of the secA SD sequence supports the presence of RNA tertiary structure in this regulatory domain.
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