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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
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pubmed:dateCreated |
1992-10-19
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D10345,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D10346,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D10347,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D10348,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D10872,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M94538,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M94539,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M94540,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M94541,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M96803
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pubmed:abstractText |
The complete primary structure of the general form of human beta-spectrin (beta G) has been deduced from cDNAs isolated from human brain. beta G-Spectrin is encoded by a gene located on human chromosome 2. beta G-Spectrin and erythrocyte beta-spectrin (beta R) share identical domain organization, with sequence identity of 60% and sequence similarity of 77%. beta-Spectrins have closely related N-terminal domains implicated in binding to actin, and 17 copies of a 106-residue repeat motif with consensus residues that are highly conserved between beta-spectrins as well as alpha-spectrins. C-terminal domains of beta G and the 270-kDa beta R-spectrins are candidate regions to associate with alpha-spectrin, and exhibit 75% similarity. beta G- and beta R-spectrins exhibit different patterns of expression in tissues and follow different developmental programs in those tissues where they are co-expressed. beta G-Spectrin is present in all tissues examined except for erythrocytes, while beta R-spectrin could be detected only in erythrocytes, brain, and heart. beta G- and beta R-Spectrins are both expressed in brain, but beta R appeared later in post-natal development and was highly enriched in cerebellum in contrast to the broad regional distribution of beta G-spectrin. beta-Spectrins are likely to perform related but distinct functions, with beta G in a general, constitutive role and beta R-spectrin involved in more specialized activities of differentiated cells.
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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:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
|
pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18715-22
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:1527002-Amino Acid Sequence,
pubmed-meshheading:1527002-Blotting, Northern,
pubmed-meshheading:1527002-Blotting, Southern,
pubmed-meshheading:1527002-Blotting, Western,
pubmed-meshheading:1527002-Brain,
pubmed-meshheading:1527002-Chromosome Mapping,
pubmed-meshheading:1527002-Chromosomes, Human, Pair 2,
pubmed-meshheading:1527002-DNA,
pubmed-meshheading:1527002-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1527002-Humans,
pubmed-meshheading:1527002-Molecular Sequence Data,
pubmed-meshheading:1527002-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:1527002-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1527002-Spectrin
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pubmed:year |
1992
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pubmed:articleTitle |
Characterization of human brain cDNA encoding the general isoform of beta-spectrin.
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pubmed:affiliation |
Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710.
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pubmed:publicationType |
Journal Article
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