ArticleBiomacromolecules2012
Designed ankyrin repeat proteins as scaffolds for multivalent recognition.
Article in Biomacromolecules, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Nuclear Import and Export of YAP and TAZ.Cancers · 2023Review
- Emerging functions for ANKHD1 in cancer-related signaling pathways and cellular processes.BMB reports · 2020Review
- ANKHD1 silencing suppresses the proliferation, migration and invasion of CRC cells by inhibiting YAP1-induced activation of EMT.American journal of cancer research · 2018Article
- Article
- Recent advances in engineering polyvalent biological interactions.Biomacromolecules · 2015Review
- A protein-based pentavalent inhibitor of the cholera toxin B-subunit.Angewandte Chemie (International ed. in English) · 2014Article
- Glycopolymer probes of signal transduction.Chemical Society reviews · 2013Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Ankyrin repeat (AR) proteins are composed of tandem repeats of a basic structural motif of ca. 33 amino acid residues that form a β-turn followed by two antiparallel α-helices. Multiple repeats stack together in a modular fashion to form a scaffold that is ideally suited for the presentation of multiple functional groups and/or recognition elements. Here we describe a biosynthetic strategy that takes advantage of the modular nature of these proteins to generate multivalent ligands that are both chemically homogeneous and structurally well-defined. Glycosylated AR proteins cluster the tetrameric lectin concanavalin A (Con A) at a rate that is comparable to the rate of Con A aggregation mediated by globular protein conjugates and variable density linear polymers. Thus, AR proteins define a new class of multivalent ligand scaffolds that have significant potential application in the study and control of a variety of multivalent interactions.
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Registered trials
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