Matches in SemOpenAlex for { <https://semopenalex.org/work/W2508555854> ?p ?o ?g. }
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- W2508555854 startingPage "19" @default.
- W2508555854 abstract "Monoclonal antibodies (mAbs) are the fastest-growing biological therapeutics with important applications ranging from cancers, autoimmunity diseases and metabolic disorders to emerging infectious diseases. Aggregation of mAbs continues to be a major problem in their developability. Antibody aggregation could be triggered by partial unfolding of its domains, leading to monomer-monomer association followed by nucleation and growth. Although the aggregation propensities of antibodies and antibody-based proteins can be affected by the external experimental conditions, they are strongly dependent on the intrinsic antibody properties as determined by their sequences and structures. In this review, we describe how the unfolding and aggregation susceptibilities of IgG could be related to their cognate sequences and structures. The impact of antibody domain structures on thermostability and aggregation propensities, and effective strategies to reduce aggregation are discussed. Finally, the aggregation of antibody-drug conjugates (ADCs) as related to their sequence/structure, linker payload, conjugation chemistry and drug-antibody ratio (DAR) is reviewed." @default.
- W2508555854 created "2016-09-16" @default.
- W2508555854 creator A5000432967 @default.
- W2508555854 creator A5019558229 @default.
- W2508555854 creator A5050128204 @default.
- W2508555854 creator A5067025401 @default.
- W2508555854 creator A5069265733 @default.
- W2508555854 creator A5089862290 @default.
- W2508555854 date "2016-09-05" @default.
- W2508555854 modified "2023-10-17" @default.
- W2508555854 title "Antibody Aggregation: Insights from Sequence and Structure" @default.
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