Search Results - "Goetze, Andrew M."

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  1. 1

    Identification and quantification of host cell protein impurities in biotherapeutics using mass spectrometry by Schenauer, Matthew R., Flynn, Gregory C., Goetze, Andrew M.

    Published in Analytical biochemistry (15-09-2012)
    “…Residual host cell proteins (HCPs) in biotherapeutics can present potential safety risks to patients or compromise product stability. As such, their levels are…”
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    Journal Article
  2. 2

    Comprehensive tracking of host cell proteins during monoclonal antibody purifications using mass spectrometry by Zhang, Qingchun, Goetze, Andrew M, Cui, Huanchun, Wylie, Jenna, Trimble, Steve, Hewig, Art, Flynn, Gregory C

    Published in mAbs (01-05-2014)
    “…An advanced two-dimensional liquid chromatography/mass spectrometry platform was used to quantify individual host cell proteins (HCPs) present at various…”
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  3. 3

    Assessing monoclonal antibody product quality attribute criticality through clinical studies by Goetze, Andrew M., Schenauer, Matthew R., Flynn, Gregory C.

    Published in mAbs (01-09-2010)
    “…Recombinant therapeutic proteins, including antibodies, contain a variety of chemical and physical modifications. Great effort is expended during process and…”
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  4. 4

    High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans by Goetze, Andrew M, Liu, Y Diana, Zhang, Zhongqi, Shah, Bhavana, Lee, Edward, Bondarenko, Pavel V, Flynn, Gregory C

    Published in Glycobiology (Oxford) (01-07-2011)
    “…Glycan structures attached to the CH2 domain of the Fc region of immunoglobulin G (IgG) are essential for specific effector functions but their role in…”
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  5. 5

    N-terminal Glutamate to Pyroglutamate Conversion in Vivo for Human IgG2 Antibodies by Liu, Y. Diana, Goetze, Andrew M., Bass, Randal B., Flynn, Gregory C.

    Published in The Journal of biological chemistry (01-04-2011)
    “…Therapeutic proteins contain a large number of post-translational modifications, some of which could potentially impact their safety or efficacy. In one of…”
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  6. 6

    Characterization of the co-elution of host cell proteins with monoclonal antibodies during protein A purification by Zhang, Qingchun, Goetze, Andrew M., Cui, Huanchun, Wylie, Jenna, Tillotson, Ben, Hewig, Art, Hall, Michael P., Flynn, Gregory C.

    Published in Biotechnology progress (01-05-2016)
    “…Protein A chromatography is commonly used as the initial step for purifying monoclonal antibody biotherapeutics expressed in mammalian tissue culture cells…”
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  7. 7

    Rates and impact of human antibody glycation in vivo by Goetze, Andrew M, Liu, Y Diana, Arroll, Thomas, Chu, Lily, Flynn, Gregory C

    Published in Glycobiology (Oxford) (01-02-2012)
    “…Glycation of immunoglobulin G (IgG) can result from incubation with a reducing sugar in vitro or during circulation in vivo. Upon injection of a recombinantly…”
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  8. 8

    Profiling the effects of process changes on residual host cell proteins in biotherapeutics by mass spectrometry by Schenauer, Matthew R., Flynn, Gregory C., Goetze, Andrew M.

    Published in Biotechnology progress (01-07-2013)
    “…An advanced liquid chromatography/mass spectrometry (MS) platform was used to identify and quantify residual Escherichia coli host cell proteins (HCPs) in the…”
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  9. 9

    Assessment of naturally occurring covalent and total dimer levels in human IgG1 and IgG2 by Yang, Jane, Goetze, Andrew M., Flynn, Gregory C.

    Published in Molecular immunology (01-03-2014)
    “…•Low levels (<1%) of dimer can be measured on endogenous human IgG1 and IgG2.•About 0.4% of IgG2, but little IgG1, is in a covalent dimer form.•Covalent IgG2…”
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  10. 10

    Rapid LC–MS screening for IgG Fc modifications and allelic variants in blood by Goetze, Andrew M., Zhang, Zhongqi, Liu, Ling, Jacobsen, Frederick W., Flynn, Gregory C.

    Published in Molecular immunology (01-10-2011)
    “…► We demonstrate a rapid LC–MS method for profiling IgG Fc modifications and allelic variants in blood. ► Information is obtained at the haplotype level. ►…”
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  11. 11

    IgG2 disulfide isoform conversion kinetics by Liu, Yaoqing Diana, Wang, Tian, Chou, Robert, Chen, Louise, Kannan, Gunasekaran, Stevenson, Riki, Goetze, Andrew M., Jiang, Xinzhao Grace, Huang, Gang, Dillon, Thomas M., Flynn, Gregory C.

    Published in Molecular immunology (01-06-2013)
    “…► We describe a flow-through dialysis system to mimic blood redox chemistry. ► In vivo IgG2 disulfide isoform conversions can be accurately replicated in…”
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  12. 12

    In vivo characterization of hydroxamic acid inhibitors of 5-lipoxygenase by Summers, James B, Gunn, Bruce P, Mazdiyasni, Hormoz, Goetze, Andrew M, Young, Patrick R, Bouska, Jennifer B, Dyer, Richard D, Brooks, Dee W, Carter, George W

    Published in Journal of medicinal chemistry (01-11-1987)
    “…The hydroxamic acid functionally can be incorporated into simple molecules to produce potent inhibitors of 5-lipoxygenase. The ability of many of these…”
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  13. 13

    Structure-activity analysis of a class of orally active hydroxamic acid inhibitors of leukotriene biosynthesis by Summers, James B, Gunn, Bruce P, Martin, Jonathan G, Martin, Michael B, Mazdiyasni, Hormoz, Stewart, Andrew O, Young, Patrick R, Bouska, Jennifer B, Goetze, Andrew M

    Published in Journal of medicinal chemistry (01-10-1988)
    “…The nature of the carbonyl and nitrogen substituents of hydroxamic acids has a major influence on the biological profile of these compounds. Hydroxamates with…”
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    Purification of a mammalian 5-lipoxygenase from rat basophilic leukemia cells by Goetze, A M, Fayer, L, Bouska, J, Bornemeier, D, Carter, G W

    Published in Prostaglandins (01-05-1985)
    “…5-Lipoxygenase (5-lipox) has been purified to homogeneity from the 20,000 xg supernatant of sonicated rat basophilic leukemia (RBL-1) cells using a 4-step…”
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    Structure-Function Relations in Phosphorylcholine-Binding Mouse Myeloma Proteins by Goetze, Andrew M., Richards, John H.

    “…The binding site interactions between the phosphorylcholine (phosphocholine)-binding mouse myeloma proteins TEPC 15, W3207, McPC 603, MOPC 167, and MOPC 511…”
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