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The quiescin sulfhydryl oxidase (hQSOX1b) tunes the expression of resistin-like molecule alpha (RELM-α or mFIZZ1) in a wheat germ cell-free extract.

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  • معلومة اضافية
    • الموضوع:
      2013
    • Collection:
      DI-fusion : dépôt institutionnel de l'Université libre de Bruxelles (ULB)
    • نبذة مختصرة :
      Although disulfide bond formation in proteins is one of the most common types of post-translational modifications, the production of recombinant disulfide-rich proteins remains a challenge. The most popular host for recombinant protein production is Escherichia coli, but disulfide-rich proteins are here often misfolded, degraded, or found in inclusion bodies. ; Journal Article ; Research Support, N.I.H. Extramural ; Research Support, Non-U.S. Gov't ; SCOPUS: ar.j ; info:eu-repo/semantics/published
    • File Description:
      1 full-text file(s): application/pdf
    • Relation:
      uri/info:doi/10.1371/journal.pone.0055621; uri/info:pii/PONE-D-12-08975; uri/info:pmid/23383248; uri/info:scp/84873208973; uri/info:pmcid/PMC3561318; https://dipot.ulb.ac.be/dspace/bitstream/2013/159626/4/doi_144934.pdf; http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/159626
    • الدخول الالكتروني :
      http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/159626
      https://dipot.ulb.ac.be/dspace/bitstream/2013/159626/4/doi_144934.pdf
    • الرقم المعرف:
      edsbas.3AC5A260