DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee H.W. | ko |
dc.contributor.author | Ko J. | ko |
dc.contributor.author | Kim, Eunjoon | ko |
dc.date.accessioned | 2013-03-07T15:47:39Z | - |
dc.date.available | 2013-03-07T15:47:39Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2006-04 | - |
dc.identifier.citation | METHODS IN MOLECULAR BIOLOGY (CLIFTON, N.J.), v.332, pp.233 - 244 | - |
dc.identifier.issn | 1064-3745 | - |
dc.identifier.uri | http://hdl.handle.net/10203/90584 | - |
dc.description.abstract | The PDZ domain is a protein-protein interaction module that interacts with a C-terminal short peptide motif in its binding partners. A variety of methods have been used to study PDZ domain interactions. This chapter details the two methods most commonly used in the analysis of PDZ interactions: yeast two-hybrid and coimmunoprecipitation assays. In addition, we discuss the features that must be considered for an efficient analysis of PDZ interactions. | - |
dc.language | English | - |
dc.publisher | HUMANA PRESS, INC. | - |
dc.title | Analysis of PDZ domain interactions using yeast two-hybrid and coimmunoprecipitation assays | - |
dc.type | Article | - |
dc.identifier.scopusid | 2-s2.0-33747401616 | - |
dc.type.rims | ART | - |
dc.citation.volume | 332 | - |
dc.citation.beginningpage | 233 | - |
dc.citation.endingpage | 244 | - |
dc.citation.publicationname | METHODS IN MOLECULAR BIOLOGY (CLIFTON, N.J.) | - |
dc.contributor.localauthor | Kim, Eunjoon | - |
dc.contributor.nonIdAuthor | Lee H.W. | - |
dc.contributor.nonIdAuthor | Ko J. | - |
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