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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1998-1-14
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pubmed:abstractText |
Zinc-finger proteins of the Cys2His2 type constitute an important family of DNA-binding proteins. Each zinc-finger domain has three residues that are thought to be important in determining DNA binding site specificity. Proteins have been designed previously by combining zinc-finger domains with a fixed sequence framework with different DNA-contacting residues.
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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 |
Feb
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pubmed:issn |
1074-5521
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
83-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9383408-Amino Acid Sequence,
pubmed-meshheading:9383408-Base Sequence,
pubmed-meshheading:9383408-Binding Sites,
pubmed-meshheading:9383408-Chelating Agents,
pubmed-meshheading:9383408-Cloning, Molecular,
pubmed-meshheading:9383408-DNA,
pubmed-meshheading:9383408-DNA Footprinting,
pubmed-meshheading:9383408-DNA Methylation,
pubmed-meshheading:9383408-DNA-Binding Proteins,
pubmed-meshheading:9383408-Edetic Acid,
pubmed-meshheading:9383408-Escherichia coli,
pubmed-meshheading:9383408-Humans,
pubmed-meshheading:9383408-Molecular Sequence Data,
pubmed-meshheading:9383408-Plasmids,
pubmed-meshheading:9383408-Thermodynamics,
pubmed-meshheading:9383408-Zinc Fingers
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pubmed:year |
1995
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pubmed:articleTitle |
A direct comparison of the properties of natural and designed zinc-finger proteins.
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pubmed:affiliation |
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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