Engineering novel binding proteins from nonimmunoglobulin domains
By H. Binz, P. Amstutz, A. Plückthun. Nature Biotechnology, 2005
665 citations recorded by the source corpus.
Subfields: Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/4eaf3a654dc2d39d79997af320d456ce25696bc0
How researchers see this paper
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In Molecular Biology
- David Baker
- Gaetano T. Montelione
- R. Fernández-Lafuente
- Gaohua Liu
- John Karanicolas
- I. Samish
- J. Corn
- C. Ortiz
In Radiology, Nuclear Medicine and Imaging
- C. Ortiz
- R. Fernández-Lafuente
- A. Teplyakov
- Gary Gilliland
- John Karanicolas
- David Baker
- I. Samish
- Frances H. Arnold
Citations in the corpus
- Efficient selection of DARPins with sub-nanomolar affinities using SRP phage display. (2008, background): “Antibodies are currently by far the most frequently used binding molecules, but proteins based on non-immunoglobin scaffolds have become an appealing alternative.(1) From both anti-”
- Protein Engineering by Combined Computational and In Vitro Evolution Approaches. (2016, background): “Several NBDs have been evolved using combinatorial approaches [38–40], although not all attempts to isolate novel binders have been successful.”
- Strategies for the one-step immobilization-purification of enzymes as industrial biocatalysts. (2015, methodology): “First, a rapid view of different affinity immobilization strategies using supports bearing specific receptors to domains included in the target protein structure will be presented (Binz et al., 2005; Linder and Teeri, 1997; Ong et al., 1989; Saleemuddin, 1999).”
- A de novo protein binding pair by computational design and directed evolution (2011, methodology): “Directed evolution techniques have been used to successfully create protein interfaces never before seen in nature (Binz et al., 2005); however, these methods currently allow the redesign of only one partner at a time and are thus unable to generate an interface that is simultaneously co-optimized o”
- Design of novel FN3 domains with high stability by a consensus sequence approach. (2012, background): “From a biotechnology perspective, these properties may also make alternative scaffolds more amenable to novel routes of drug delivery and formulations that require high stability (Skerra, 2000; Binz et al., 2005).”
- Affibody molecules: Engineered proteins for therapeutic, diagnostic and biotechnological applications (2010, background): “Several of these scaffolds have made substantial scientific progress recently [1,2], and some are al-”