Search Results - "Chumsae, Christopher"

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  1. 1

    Cell culture media supplementation of bioflavonoids for the targeted reduction of acidic species charge variants on recombinant therapeutic proteins by Hossler, Patrick, Wang, Min, McDermott, Sean, Racicot, Christopher, Chemfe, Kofi, Zhang, Yun, Chumsae, Christopher, Manuilov, Anton

    Published in Biotechnology progress (01-07-2015)
    “…Charge variants in recombinant proteins are an important series of protein modifications, whose potential role on protein stability, activity, immunogenicity,…”
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    Journal Article
  2. 2

    Arabinosylation of recombinant human immunoglobulin-based protein therapeutics by Hossler, Patrick, Chumsae, Christopher, Racicot, Christopher, Ouellette, David, Ibraghimov, Alexander, Serna, Daniel, Mora, Alessandro, McDermott, Sean, Labkovsky, Boris, Scesney, Susanne, Grinnell, Christine, Preston, Gregory, Bose, Sahana, Carrillo, Ralf

    Published in mAbs (19-05-2017)
    “…Protein glycosylation is arguably the paramount post-translational modification on recombinant glycoproteins, and highly cited in the literature for affecting…”
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    Journal Article
  3. 3

    Cell culture media supplementation of infrequently used sugars for the targeted shifting of protein glycosylation profiles by Hossler, Patrick, Racicot, Christopher, Chumsae, Christopher, McDermott, Sean, Cochran, Keith

    Published in Biotechnology progress (01-03-2017)
    “…Mammalian cells in culture rely on sources of carbohydrates to supply the energy requirements for proliferation. In addition, carbohydrates provide a large…”
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    Journal Article
  4. 4
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    Arabinosylation of recombinant human immunoglobulin-based protein therapeutics by Hossler, Patrick, Chumsae, Christopher, Racicot, Christopher, Ouellette, David, Ibraghimov, Alexander, Serna, Daniel, Mora, Alessandro, McDermott, Sean, Labkovsky, Boris, Scesney, Susanne, Grinnell, Christine, Preston, Gregory, Bose, Sahana, Carrillo, Ralf

    Published in mAbs (19-05-2017)
    “…Protein glycosylation is arguably the paramount post-translational modification on recombinant glycoproteins, and highly cited in the literature for affecting…”
    Get full text
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