Fusion Protein Linkers: Property, Design and Functionality
By Xiaoying Chen, J. Zaro, W. Shen. Advanced Drug Delivery Reviews, 2012
1,858 citations recorded by the source corpus.
As an indispensable component of recombinant fusion proteins, linkers have shown increasing importance in the construction of stable, bioactive fusion proteins. This review covers the current knowledge of fusion protein linkers and summarizes examples for their design and application. The general properties of linkers derived from naturally-occurring multi-domain proteins can be considered as the foundation in linker design. Empirical linkers designed by researchers are generally classified into 3 categories according to their structures: flexible linkers, rigid linkers, and in vivo cleavable linkers. Besides the basic role in linking the functional domains together (as in flexible and rigid linkers) or releasing free functional domain in vivo (as in in vivo cleavable linkers), linkers may offer many other advantages for the production of fusion proteins, such as improving biological activity, increasing expression yield, and achieving desirable pharmacokinetic profiles.
Subfields: Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/8788c12c3e058ad0ffabd61e5f7823f8d6d911f7
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In Molecular Biology
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In Radiology, Nuclear Medicine and Imaging
Citations in the corpus
- Directed evolution of the fusion enzyme for improving astaxanthin biosynthesis in Saccharomyces cerevisiae (2022, background): “close to each other in the spatial structure and can increase the domain interaction between the two enzymes [34].”
- DFLpred: High-throughput prediction of disordered flexible linker regions in protein sequences (2016, positive): “A subclass of linkers are flexible linkers, defined as flexible inter-domain regions that allow two domains to move relatively to each other (Chen et al., 2013).”