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  • The American Society for Biochemistry and Molecular Biology (ASBMB)  (3)
  • Alfred Wegener Institute for Polar and Marine Research & German Society of Polar Research  (2)
  • BMJ Publishing Group  (2)
  • 2015-2019  (6)
  • 2000-2004
  • 1985-1989  (1)
Document type
Publisher
Years
  • 2015-2019  (6)
  • 2000-2004
  • 1985-1989  (1)
  • 2010-2014  (1)
Year
  • 1
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    Shift work practices and opportunities for intervention (2016)
    BMJ Publishing Group
    Details
    Publication Date: 2016-12-15
    Description: There is increasing evidence that shift work, an occupational exposure affecting about one-fourth of the working population, increases the risk of major chronic disease outcomes, such as cardiovascular disease and cancer. 1–4 Currently, there is an open discussion on whether shift work should be included in national lists of occupational hazards for compensation purposes. Denmark was the first (and to date only) country to consider breast cancer an occupational disease in shift workers, and to compensate women with over 20 years of night work who developed breast cancer. Chronic disease risk reduction and prevention in shift workers is an emerging field, which points to the need for more intervention studies. Whether and how companies or governments translate existing evidence into real-world policy or preventive actions currently remains largely unknown. The study by Hall et al 5 is a unique effort and first...
    Print ISSN: 1351-0711
    Electronic ISSN: 1470-7926
    Topics: Medicine
    Published by BMJ Publishing Group
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  • 2
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    Analysis of the Catalytic Site of the GTPase Ran [Protein Structure and Folding] (2015)
    The American Society for Biochemistry and Molecular Biology (ASBMB)
    Details
    Publication Date: 2015-10-03
    Description: Small GTPases regulate key processes in cells. Malfunction of their GTPase reaction by mutations is involved in severe diseases. Here, we compare the GTPase reaction of the slower hydrolyzing GTPase Ran with Ras. By combination of time-resolved FTIR difference spectroscopy and QM/MM simulations we elucidate that the Mg2+ coordination by the phosphate groups, which varies largely among the x-ray structures, is the same for Ran and Ras. A new x-ray structure of a Ran·RanBD1 complex with improved resolution confirmed this finding and revealed a general problem with the refinement of Mg2+ in GTPases. The Mg2+ coordination is not responsible for the much slower GTPase reaction of Ran. Instead, the location of the Tyr-39 side chain of Ran between the γ-phosphate and Gln-69 prevents the optimal positioning of the attacking water molecule by the Gln-69 relative to the γ-phosphate. This is confirmed in the RanY39A·RanBD1 crystal structure. The QM/MM simulations provide IR spectra of the catalytic center, which agree very nicely with the experimental ones. The combination of both methods can correlate spectra with structure at atomic detail. For example the FTIR difference spectra of RasA18T and RanT25A mutants show that spectral differences are mainly due to the hydrogen bond of Thr-25 to the α-phosphate in Ran. By integration of x-ray structure analysis, experimental, and theoretical IR spectroscopy the catalytic center of the x-ray structural models are further refined to sub-Å resolution, allowing an improved understanding of catalysis.
    Print ISSN: 0021-9258
    Electronic ISSN: 1083-351X
    Topics: Biology , Chemistry and Pharmacology
    Published by The American Society for Biochemistry and Molecular Biology (ASBMB)
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  • 3
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    Early, but not late chronotypes, are up during their biological night when working the night shift (2015)
    BMJ Publishing Group
    Details
    Publication Date: 2015-02-14
    Description: Bhatti et al 1 recently examined the impact of chronotype on melatonin levels in shift-workers and concluded that ‘(...) morning type shift-workers were better able to maintain normal patterns of melatonin secretion (...), suggesting that morning types may be protected against the negative effects of shift-work related melatonin disruption’. However, their data show that, compared to daytime workers sleeping at night, early chronotypes have lower melatonin levels than late chronotypes during daytime sleep after a nightshift. They also show a larger difference in melatonin secretion during their first regular night-time sleep after night shifts (table 3, dichotomous categorisation: =–34.6% and late types: =–4.2%), suggesting that early chronotypes are more affected by working night shifts than late chronotypes. This makes sense when considering the biological definition of chronotype, 2 where early chronotypes, with an earlier subjective, internal night, exhibit an earlier peak in melatonin secretion than late chronotypes.
    Print ISSN: 1351-0711
    Electronic ISSN: 1470-7926
    Topics: Medicine
    Published by BMJ Publishing Group
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  • 4
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    A {mu}O-Conotoxin with Improved Potency for NaV1.8 [Neurobiology] (2016)
    The American Society for Biochemistry and Molecular Biology (ASBMB)
    Details
    Publication Date: 2016-05-28
    Description: The μO-conotoxins MrVIA, MrVIB, and MfVIA inhibit the voltage-gated sodium channel NaV1.8, a well described target for the treatment of pain; however, little is known about the residues or structural elements that define this activity. In this study, we determined the three-dimensional structure of MfVIA, examined its membrane binding properties, performed alanine-scanning mutagenesis, and identified residues important for its activity at human NaV1.8. A second round of mutations resulted in (E5K,E8K)MfVIA, a double mutant with greater positive surface charge and greater affinity for lipid membranes compared with MfVIA. This analogue had increased potency at NaV1.8 and was analgesic in the mouse formalin assay.
    Print ISSN: 0021-9258
    Electronic ISSN: 1083-351X
    Topics: Biology , Chemistry and Pharmacology
    Published by The American Society for Biochemistry and Molecular Biology (ASBMB)
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  • 5
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    Inhibitory Activity of hNaV1.7 by ProTx-II, the Membrane Link [Lipids] (2016)
    The American Society for Biochemistry and Molecular Biology (ASBMB)
    Details
    Publication Date: 2016-08-13
    Description: ProTx-II is a disulfide-rich peptide toxin from tarantula venom able to inhibit the human voltage-gated sodium channel 1.7 (hNaV1.7), a channel reported to be involved in nociception, and thus it might have potential as a pain therapeutic. ProTx-II acts by binding to the membrane-embedded voltage sensor domain of hNaV1.7, but the precise peptide channel-binding site and the importance of membrane binding on the inhibitory activity of ProTx-II remain unknown. In this study, we examined the structure and membrane-binding properties of ProTx-II and several analogues using NMR spectroscopy, surface plasmon resonance, fluorescence spectroscopy, and molecular dynamics simulations. Our results show a direct correlation between ProTx-II membrane binding affinity and its potency as an hNaV1.7 channel inhibitor. The data support a model whereby a hydrophobic patch on the ProTx-II surface anchors the molecule at the cell surface in a position that optimizes interaction of the peptide with the binding site on the voltage sensor domain. This is the first study to demonstrate that binding of ProTx-II to the lipid membrane is directly linked to its potency as an hNaV1.7 channel inhibitor.
    Print ISSN: 0021-9258
    Electronic ISSN: 1083-351X
    Topics: Biology , Chemistry and Pharmacology
    Published by The American Society for Biochemistry and Molecular Biology (ASBMB)
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  • 6
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    In memoriam Dr. h.c. Oskar Reinwarth (2018)
    Alfred Wegener Institute for Polar and Marine Research & German Society of Polar Research
    In:  EPIC3Polarforschung, Bremerhaven, Alfred Wegener Institute for Polar and Marine Research & German Society of Polar Research, 88(1), pp. 53-54, ISSN: 00322490
    Details
    Publication Date: 2019-07-17
    Repository Name: EPIC Alfred Wegener Institut
    Type: "Polarforschung" , peerRev
    Format: application/pdf
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  • 7
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    Paleozoic Accretion at the Paleopacitic Margin of Antarctica (1987)
    Alfred Wegener Institute for Polar and Marine Research & German Society of Polar Research
    In:  EPIC3Polarforschung, Bremerhaven, Alfred Wegener Institute for Polar and Marine Research & German Society of Polar Research, 57(1/2), pp. 1-8, ISSN: 0032-2490
    Details
    Publication Date: 2019-07-17
    Repository Name: EPIC Alfred Wegener Institut
    Type: "Polarforschung" , peerRev
    Format: application/pdf
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