SwePub
Sök i SwePub databas

  Extended search

Träfflista för sökning "WFRF:(Thunnissen Marjolein M.G.M.) "

Search: WFRF:(Thunnissen Marjolein M.G.M.)

  • Result 1-2 of 2
Sort/group result
   
EnumerationReferenceCoverFind
1.
  • Awad, Wael, et al. (author)
  • Improvements in the order, isotropy and electron density of glypican-1 crystals by controlled dehydration.
  • 2013
  • In: Acta Crystallographica. Section D: Biological Crystallography. - 1399-0047. ; 69:Pt 12, s. 2524-2533
  • Journal article (peer-reviewed)abstract
    • The use of controlled dehydration for improvement of protein crystal diffraction quality is increasing in popularity, although there are still relatively few documented examples of success. A study has been carried out to establish whether controlled dehydration could be used to improve the anisotropy of crystals of the core protein of the human proteoglycan glypican-1. Crystals were subjected to controlled dehydration using the HC1 device. The optimal protocol for dehydration was developed by careful investigation of the following parameters: dehydration rate, final relative humidity and total incubation time Tinc. Of these, the most important was shown to be Tinc. After dehydration using the optimal protocol the crystals showed significantly reduced anisotropy and improved electron density, allowing the building of previously disordered parts of the structure.
  •  
2.
  • Uysal, Hüseyin, et al. (author)
  • The crystal structure of the pathogenic collagen type II-specific mouse monoclonal antibody CIIC1 Fab : Structure to function analysis
  • 2008
  • In: Molecular Immunology. - Oxford : Elsevier. - 0161-5890 .- 1872-9142. ; 45:8, s. 2196-2204
  • Journal article (peer-reviewed)abstract
    • Monoclonal anti-collagen type II antibody CIIC1 is an arthritogenic autoantibody, which induces arthritis in mice. We crystallized and solved the structure of CIIC1 Fab molecule. Analysis of structure revealed an interaction between the CDR regions of one Fab to the CH1 domain of another Fab, which resembles an antibody-antigen interaction. ELISA experiments confirmed the cross-reactivity of both the full CIIC1 antibody and a single chain Fv fragment to other anti-collagen antibodies which are of different isotypes and epitope specificity. The rheumatoid factor like reactivity of CIIC1 antibody together with its collagen type II specificity may explain the pathogenicity of this antibody. © 2007 Elsevier Ltd. All rights reserved.
  •  
Skapa referenser, mejla, bekava och länka
  • Result 1-2 of 2

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view