Source:http://linkedlifedata.com/resource/pubmed/id/19107412
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2008-12-24
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pubmed:abstractText |
Ni-NTA affinity chromatography under denaturing conditions has proven to be a powerful method for the isolation of SUMO conjugates from total cell extracts, as it minimizes deconjugation and excludes noncovalent interactions. This chapter describes the use of both His-tagged SUMO and a His-tagged target protein for the characterization of the sumoylation process in the budding yeast Saccharomyces cerevisiae. Two well-studied model substrates, the septin Cdc3 and the replication clamp protein PCNA, are used as examples, but the protocol can easily be adapted to other targets and organisms.
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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:issn |
1064-3745
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
497
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
81-103
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:19107412-Clinical Laboratory Techniques,
pubmed-meshheading:19107412-Cloning, Molecular,
pubmed-meshheading:19107412-Models, Biological,
pubmed-meshheading:19107412-Organisms, Genetically Modified,
pubmed-meshheading:19107412-Protein Processing, Post-Translational,
pubmed-meshheading:19107412-Saccharomyces cerevisiae,
pubmed-meshheading:19107412-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:19107412-Small Ubiquitin-Related Modifier Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
In vivo detection and characterization of sumoylation targets in Saccharomyces cerevisiae.
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pubmed:affiliation |
Cancer Research UK London Research Institute, Clare Hall Laboratories, South Mimms, UK.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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