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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6053
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pubmed:dateCreated |
1986-3-21
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pubmed:databankReference |
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pubmed:abstractText |
The A, B and C lamins are the major proteins of the nuclear envelope. The complete nucleotide sequence of the coding region of the A and C lamins shows that these proteins are identical except for their carboxy termini. The most prominent structural feature of both lamins is an alpha-helical region of repeating heptads of amino acids that shows striking homology with the entire family of cytoplasmic intermediate filament proteins. These features suggest that the nuclear envelope is made up of a network of coiled-coil polymers.
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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:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
319
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
463-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3453101-Amino Acid Sequence,
pubmed-meshheading:3453101-Base Sequence,
pubmed-meshheading:3453101-Cloning, Molecular,
pubmed-meshheading:3453101-DNA,
pubmed-meshheading:3453101-Humans,
pubmed-meshheading:3453101-Intermediate Filament Proteins,
pubmed-meshheading:3453101-Lamins,
pubmed-meshheading:3453101-Nucleoproteins,
pubmed-meshheading:3453101-Peptide Fragments,
pubmed-meshheading:3453101-Protein Conformation,
pubmed-meshheading:3453101-Sequence Homology, Nucleic Acid,
pubmed-meshheading:3453101-Structure-Activity Relationship
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pubmed:articleTitle |
Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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