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  • 1
    Electronic Resource
    Electronic Resource
    Magnetic-field-induced orientation of crystallites in powders of layered intercalation compounds detected by NMR (1988)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 92 (1988), S. 7167-7168 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100337a003
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    FS11.2
Contact allergy to herbal teas from Asteraceae plants (2004)
    Oxford, UK; Malden, USA : Blackwell Science Ltd/Inc.
    Contact dermatitis 50 (2004), S. 0 
    Details
    ISSN: 1600-0536
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Objective:  A possible contact allergy to herbal teas, in particular those derived from the Asteraceae plant family, was investigated in patients allergic to sesquiterpene lactones (SL).Method:  Twenty patients with a contact allergy to SL were recalled and patch-tested with aqueous, ethanol and acetone extracts of 8 different herbal teas based on Asteraceae plants as well as with parthenolide and other SL.Results:  In 18/20 patients with SL allergy there were positive test reactions to the Asteraceae teas, mainly to those based on German chamomile, dandelion and milfoil. Among the SL, parthenolide was the most frequent co-reactor.Conclusion:  Most patients with a contact allergy to SL are allergic to commercial teas derived from the Asteraceae plant family as well.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0105-1873.2004.0309cv.x
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  • 3
    Electronic Resource
    Electronic Resource
    FS02.8
Patch testing with gold trichloride can give false test results (2004)
    Oxford, UK; Malden, USA : Blackwell Science Ltd/Inc.
    Contact dermatitis 50 (2004), S. 0 
    Details
    ISSN: 1600-0536
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background:  Hydrochloric acid is formed in water solutions of gold trichloride. Hydrochloric acid in contact with aluminium generates hydrogen gas which can reduce and transform trivalent gold to elemental gold.Objective:  To investigate whether patch testing with aqueous gold trichloride can cause false positive (irritant) reactions in patients without contact allergy to gold and false negative reactions in patients with gold allergy.Methods:  13 patients with and 13 patients without positive patch test reactions to gold sodium thiosulfate were tested with gold trichloride in 2 different vehicles, water and alkaline buffer, using 2 different test techniques, the Finn Chamber technique with aluminium chambers and van der Bend technique with polypropene chambers.Results:  Irritant patch test reactions were obtained with aqueous gold trichloride tested in van der Bend chambers in 10 patients without gold allergy. In gold-allergic patients no positive test reactions were obtained from aqueous gold trichloride in Finn chambers while 2 positive test reactions were obtained from gold trichloride in alkaline buffer tested in van der Bend chambers.Conclusion:  If gold trichloride is patch tested in wrong vehicle and with wrong test technique irritant test reactions may occur which can be misinterpreted as positive allergic reactions in patients without gold allergy as well as negative reactions in patients with gold allergy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0105-1873.2004.0309z.x
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    Paper (German National Licenses)
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  • 4
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    Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins (2013)
    Oxford University Press
    Details
    Publication Date: 2013-09-06
    Description: In metazoans, replication-dependent histone mRNAs end in a stem-loop structure instead of the poly(A) tail characteristic of all other mature mRNAs. This specialized 3' end is bound by stem-loop binding protein (SLBP), a protein that participates in the nuclear export and translation of histone mRNAs. The translational activity of SLBP is mediated by interaction with SLIP1, a m iddle domain of i nitiation f actor 4G (MIF4G)-like protein that connects to translation initiation. We determined the 2.5 Å resolution crystal structure of zebrafish SLIP1 bound to the translation–activation domain of SLBP and identified the determinants of the recognition. We discovered a SLIP1-binding motif (SBM) in two additional proteins: the translation initiation factor eIF3g and the mRNA-export factor DBP5. We confirmed the binding of SLIP1 to DBP5 and eIF3g by pull-down assays and determined the 3.25 Å resolution structure of SLIP1 bound to the DBP5 SBM. The SBM-binding and homodimerization residues of SLIP1 are conserved in the MIF4G domain of CBP80/20-dependent translation initiation factor (CTIF). The results suggest how the SLIP1 homodimer or a SLIP1–CTIF heterodimer can function as platforms to bridge SLBP with SBM-containing proteins involved in different steps of mRNA metabolism.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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  • 5
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    Entrapment of DNA in an intersubunit tunnel system of a single-stranded DNA-binding protein (2014)
    Oxford University Press
    Details
    Publication Date: 2014-06-03
    Description: Instead of a classical s ingle- s tranded deoxyribonuleic acid (DNA)- b inding protein (SSB), some hyperthermophilic crenarchaea harbor a non-canonical SSB termed ThermoDBP. Two related but poorly characterized groups of proteins, which share the ThermoDBP N-terminal DNA-binding domain, have a broader phylogenetic distribution and co-exist with ThermoDBPs and/or other SSBs. We have investigated the nucleic acid binding properties and crystal structures of representatives of these groups of ThermoDBP- r elated p roteins (ThermoDBP-RPs) 1 and 2. ThermoDBP-RP 1 and 2 oligomerize by different mechanisms and only ThermoDBP-RP2 exhibits strong single-stranded DNA affinity in vitro . A crystal structure of ThermoDBP-RP2 in complex with DNA reveals how the NTD common to ThermoDBPs and ThermoDBP-RPs can contact the nucleic acid in a manner that allows a symmetric homotetrameric protein complex to bind single-stranded DNA molecules asymmetrically. While single-stranded DNA wraps around the surface or binds along channels of previously investigated SSBs, it traverses an internal, intersubunit tunnel system of a ThermoDBP-RP2 tetramer. Our results indicate that some archaea have acquired special SSBs for genome maintenance in particularly challenging environments.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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