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- Publisher Website: 10.1021/cb800069c
- Scopus: eid_2-s2.0-53149108997
- PMID: 18590330
- WOS: WOS:000258503800005
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Article: mRNA display selection of a high-affinity, modification-specific phospho-iκbα-binding fibronectin
Title | mRNA display selection of a high-affinity, modification-specific phospho-iκbα-binding fibronectin |
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Authors | |
Issue Date | 2008 |
Citation | ACS Chemical Biology, 2008, v. 3, n. 8, p. 480-485 How to Cite? |
Abstract | The complexity of the human proteome is greatly expanded by post-translational modifications. New tools capable of recognizing these modifications in a sequence-specific fashion provide a route to purify these modified proteins, to alter protein trafficking, and to visualize signal transduction in real time. Here, we have evolved novel, modification-specific ligands that target phosphorylated IκBα. To do this, we employed mRNA display-based in vitro selection using a 30-trillion-member protein library based on the fibronectin type III domain. The selection yielded one fibronectin molecule, 10C17C25, that binds a phospho-IκBα peptide with K d = 18 nM and is over 1000-fold specific compared to the nonphosphorylated peptide. 10C17C25 specifically recognizes endogenous phosphorylated IκBα from mammalian cell extract and stabilizes phospho-IκBα in vivo. We also incorporated 10C17C25 into a FRET indicator that detects IκB kinase (IKK) activity in vitro, demonstrating the utility of selecting designed adaptors for kinase activity sensors. © 2008 American Chemical Society. |
Persistent Identifier | http://hdl.handle.net/10722/285637 |
ISSN | 2023 Impact Factor: 3.5 2023 SCImago Journal Rankings: 1.344 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Olson, C. Anders | - |
dc.contributor.author | Liao, Hsiang I. | - |
dc.contributor.author | Sun, Ren | - |
dc.contributor.author | Roberts, Richard W. | - |
dc.date.accessioned | 2020-08-18T04:56:15Z | - |
dc.date.available | 2020-08-18T04:56:15Z | - |
dc.date.issued | 2008 | - |
dc.identifier.citation | ACS Chemical Biology, 2008, v. 3, n. 8, p. 480-485 | - |
dc.identifier.issn | 1554-8929 | - |
dc.identifier.uri | http://hdl.handle.net/10722/285637 | - |
dc.description.abstract | The complexity of the human proteome is greatly expanded by post-translational modifications. New tools capable of recognizing these modifications in a sequence-specific fashion provide a route to purify these modified proteins, to alter protein trafficking, and to visualize signal transduction in real time. Here, we have evolved novel, modification-specific ligands that target phosphorylated IκBα. To do this, we employed mRNA display-based in vitro selection using a 30-trillion-member protein library based on the fibronectin type III domain. The selection yielded one fibronectin molecule, 10C17C25, that binds a phospho-IκBα peptide with K d = 18 nM and is over 1000-fold specific compared to the nonphosphorylated peptide. 10C17C25 specifically recognizes endogenous phosphorylated IκBα from mammalian cell extract and stabilizes phospho-IκBα in vivo. We also incorporated 10C17C25 into a FRET indicator that detects IκB kinase (IKK) activity in vitro, demonstrating the utility of selecting designed adaptors for kinase activity sensors. © 2008 American Chemical Society. | - |
dc.language | eng | - |
dc.relation.ispartof | ACS Chemical Biology | - |
dc.title | mRNA display selection of a high-affinity, modification-specific phospho-iκbα-binding fibronectin | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1021/cb800069c | - |
dc.identifier.pmid | 18590330 | - |
dc.identifier.pmcid | PMC2962918 | - |
dc.identifier.scopus | eid_2-s2.0-53149108997 | - |
dc.identifier.volume | 3 | - |
dc.identifier.issue | 8 | - |
dc.identifier.spage | 480 | - |
dc.identifier.epage | 485 | - |
dc.identifier.isi | WOS:000258503800005 | - |
dc.identifier.issnl | 1554-8929 | - |