A competitive genetic algorithm for resource-constrained project scheduling
In: Naval research logistics: an international journal, Volume 45, Issue 7, p. 733-750
ISSN: 1520-6750
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In: Neue Zeitschrift für Verwaltungsrecht: NVwZ ; vereinigt mit Verwaltungsrechtsprechung, Volume 31, Issue 11, p. 665-670
ISSN: 0721-880X
In: Synthese: an international journal for epistemology, methodology and philosophy of science, Volume 179, Issue 2, p. 321-338
ISSN: 1573-0964
In: Österreichische Wasser- und Abfallwirtschaft, Volume 57, Issue 11-12, p. 185-190
ISSN: 1613-7566
In: Internet interventions: the application of information technology in mental and behavioural health ; official journal of the European Society for Research on Internet Interventions (ESRII) and the International Society for Research on Internet Interventions (ISRII), Volume 35, p. 100716
ISSN: 2214-7829
In: Internet interventions: the application of information technology in mental and behavioural health ; official journal of the European Society for Research on Internet Interventions (ESRII) and the International Society for Research on Internet Interventions (ISRII), Volume 30, p. 100584
ISSN: 2214-7829
Glycosylation is a topic of intense current interest in the development of biopharmaceuticals since it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.
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