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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1999-1-11
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pubmed:abstractText |
Selectively infective phage (SIP) can be used to identify protein-protein interactions. SIP was modified to facilitate the simultaneous selection of interacting protein pairs from large combinatorial libraries. An interference-resistant phage was constructed which non-covalently, but stably links the genetic information of an interacting pair, encoded separately on phage and phagemid vectors, by co-packaging into heteropolyphages. In a model system, the interaction between a SIP-selected peptide and the intracellular domain of the p75 neurotrophin receptor was detected in the presence of a 10(4)-fold excess of a non-interacting control pair (jun leucine zipper and p75 intracellular domain) via SIP hetero-polyphage transductants. To minimize the redundancy of transductants and to minimize possible ligand exchange generated in a solution-based SIP screening, a filter-based in situ infectivity screening was developed. The combination of the above techniques may provide a powerful system for rapid screening of very large sequence spaces.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PEP3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-jun,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Nerve Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nerve Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
440
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
135-40
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9862442-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:9862442-Bacteriophages,
pubmed-meshheading:9862442-Cell Cycle Proteins,
pubmed-meshheading:9862442-Cloning, Molecular,
pubmed-meshheading:9862442-Fungal Proteins,
pubmed-meshheading:9862442-Gene Library,
pubmed-meshheading:9862442-Genetic Vectors,
pubmed-meshheading:9862442-Leucine Zippers,
pubmed-meshheading:9862442-Membrane Proteins,
pubmed-meshheading:9862442-Peptide Library,
pubmed-meshheading:9862442-Protein Binding,
pubmed-meshheading:9862442-Proto-Oncogene Proteins c-jun,
pubmed-meshheading:9862442-Receptor, Nerve Growth Factor,
pubmed-meshheading:9862442-Receptors, Nerve Growth Factor,
pubmed-meshheading:9862442-Recombinant Fusion Proteins,
pubmed-meshheading:9862442-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9862442-Transduction, Genetic,
pubmed-meshheading:9862442-Viral Proteins,
pubmed-meshheading:9862442-Virus Assembly
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pubmed:year |
1998
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pubmed:articleTitle |
A phage-based system to select multiple protein-protein interactions simultaneously from combinatorial libraries.
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pubmed:affiliation |
MorphoSys AG, Martinsried/Munich, Germany. rudert@morphosys.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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