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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2005-8-16
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pubmed:abstractText |
The Krüppel-associated box (KRAB) domain is a potent transcription repression bipartite domain, shared by over 400 zinc finger proteins in humans, involved in the regulation of many functions. KRAB domains are both physically and functionally bipartite (A and B modules). The lone KRAB-A and composite KRAB-AB domains from the human ZNF2 protein were over-expressed as recombinant proteins in E. coli, isolated and purified to homogeneity to investigate their structure to function relationship.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0929-8665
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
527-32
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16101389-Amino Acid Sequence,
pubmed-meshheading:16101389-Chromatography, Gel,
pubmed-meshheading:16101389-Chromatography, High Pressure Liquid,
pubmed-meshheading:16101389-DNA-Binding Proteins,
pubmed-meshheading:16101389-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:16101389-Escherichia coli,
pubmed-meshheading:16101389-Gene Expression,
pubmed-meshheading:16101389-Humans,
pubmed-meshheading:16101389-Kruppel-Like Transcription Factors,
pubmed-meshheading:16101389-Molecular Sequence Data,
pubmed-meshheading:16101389-Molecular Weight,
pubmed-meshheading:16101389-Protein Structure, Tertiary,
pubmed-meshheading:16101389-Recombinant Proteins,
pubmed-meshheading:16101389-Sequence Alignment,
pubmed-meshheading:16101389-Sequence Analysis, DNA
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pubmed:year |
2005
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pubmed:articleTitle |
Expression, purification and partial characterization of the Krüppel-associated box (KRAB) from the human ZNF2 protein.
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pubmed:affiliation |
Istituto di Genetica e Biofisica A. Buzzati Traverso, Consiglio Nazionale delle Ricerche, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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