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rdf:type |
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lifeskim:mentions |
umls-concept:C0002518,
umls-concept:C0009015,
umls-concept:C0017337,
umls-concept:C0033684,
umls-concept:C0205214,
umls-concept:C0439659,
umls-concept:C0542341,
umls-concept:C0936012,
umls-concept:C0994894,
umls-concept:C1706366,
umls-concept:C2347858
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pubmed:issue |
18
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pubmed:dateCreated |
1988-11-21
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pubmed:abstractText |
Small patches of identical amino acid sequences commonly occur in proteins that have the same function but are derived from evolutionarily distant organisms. Reverse translation of such patches into degenerate pools of oligonucleotides provide useful hybridization probes for cloning the gene for the corresponding protein from other organisms. Since the conserved patches of identical amino acid sequence are probably important for the protein's biological function, they are preferred targets for reverse genetic studies aimed at defining structure-function relationships.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-1134550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-193030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-2840550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-2896195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-2948189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-3025593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-3076279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-3282306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-3335481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-3430622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2845364-6261696
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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 |
Sep
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9017-26
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:2845364-Amino Acid Sequence,
pubmed-meshheading:2845364-Biological Evolution,
pubmed-meshheading:2845364-Cloning, Molecular,
pubmed-meshheading:2845364-Geobacillus stearothermophilus,
pubmed-meshheading:2845364-Glyceraldehyde-3-Phosphate Dehydrogenases,
pubmed-meshheading:2845364-Humans,
pubmed-meshheading:2845364-Molecular Sequence Data,
pubmed-meshheading:2845364-Phosphotransferases,
pubmed-meshheading:2845364-Proteins,
pubmed-meshheading:2845364-Saccharomyces cerevisiae,
pubmed-meshheading:2845364-Structure-Activity Relationship,
pubmed-meshheading:2845364-Transferases (Other Substituted Phosphate Groups),
pubmed-meshheading:2845364-Triose-Phosphate Isomerase
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pubmed:year |
1988
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pubmed:articleTitle |
Conservation of short patches of amino acid sequence amongst proteins with a common function but evolutionarily distinct origins: implications for cloning genes and for structure-function analysis.
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pubmed:affiliation |
Department of Biochemistry, Stanford University School of Medicine, CA 94305.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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