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- W2600134345 endingPage "489" @default.
- W2600134345 startingPage "479" @default.
- W2600134345 abstract "Introduction: In modern vaccinology and immunotherapy, recombinant proteins more and more replace whole organisms to induce protective or curative immune responses. Structural stability of proteins is of crucial importance for efficient presentation of antigenic peptides on MHC, which plays a decisive role for triggering strong immune reactions.Areas covered: In this review, we discuss structural stability as a key factor for modulating the potency of recombinant vaccines and its importance for antigen proteolysis, presentation, and stimulation of B and T cells. Moreover, the impact of fold stability on downstream events determining the differentiation of T cells into effector cells is reviewed. We summarize studies investigating the impact of protein fold stability on the outcome of the immune response and provide an overview on computational methods to estimate the effects of point mutations on protein stability.Expert commentary: Based on this information, the rational design of up-to-date vaccines is discussed. A model for predicting immunogenicity of proteins based on their conformational stability at different pH values is proposed." @default.
- W2600134345 created "2017-04-07" @default.
- W2600134345 creator A5034136678 @default.
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- W2600134345 creator A5050114729 @default.
- W2600134345 creator A5083173373 @default.
- W2600134345 creator A5083635405 @default.
- W2600134345 date "2017-03-24" @default.
- W2600134345 modified "2023-10-16" @default.
- W2600134345 title "Influence of protein fold stability on immunogenicity and its implications for vaccine design" @default.
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- W2600134345 doi "https://doi.org/10.1080/14760584.2017.1306441" @default.
- W2600134345 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5490637" @default.
- W2600134345 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28290225" @default.
- W2600134345 hasPublicationYear "2017" @default.
- W2600134345 type Work @default.