Source:http://linkedlifedata.com/resource/pubmed/id/10796990
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-4
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pubmed:dateCreated |
2000-5-25
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pubmed:abstractText |
The high affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. While it is extremely useful as the native protein, there are many applications where its function can be improved re-engineering the subunits. We review here our efforts to construct streptavidin tetramers that have 'smart' recognition capabilities, and which display functional peptide sequences. These smart and biofunctional streptavidin derivatives can 'talk' to cells, and 'listen' to external signals which control capture and release of biotinylated molecules.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1389-0344
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
93-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10796990-Affinity Labels,
pubmed-meshheading:10796990-Binding Sites,
pubmed-meshheading:10796990-Biotechnology,
pubmed-meshheading:10796990-Biotin,
pubmed-meshheading:10796990-Models, Molecular,
pubmed-meshheading:10796990-Protein Conformation,
pubmed-meshheading:10796990-Protein Engineering,
pubmed-meshheading:10796990-Protein Structure, Quaternary,
pubmed-meshheading:10796990-Recombinant Fusion Proteins,
pubmed-meshheading:10796990-Streptavidin
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pubmed:year |
1999
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pubmed:articleTitle |
Smart and biofunctional streptavidin.
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pubmed:affiliation |
Department of Bioengineering, University of Washington, Seattle 98195, USA. stayton@u.washington.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Review
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