-
Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins.
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.
PMID: 3453101 [PubMed - indexed for MEDLINE]
-
Cited by over 100 PubMed Central articles
-
Suppression of proliferative defects associated with processing-defective lamin A mutants by hTERT or inactivation of p53.
Kudlow BA, Stanfel MN, Burtner CR, Johnston ED, Kennedy BK.
Mol Biol Cell. 2008 Dec; 19(12):5238-48. Epub 2008 Oct 8.
[Mol Biol Cell. 2008]
-
Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production.
Lee CP, Huang YH, Lin SF, Chang Y, Chang YH, Takada K, Chen MR.
J Virol. 2008 Dec; 82(23):11913-26. Epub 2008 Sep 24.
[J Virol. 2008]
-
Glial fibrillary acidic protein filaments can tolerate the incorporation of assembly-compromised GFAP-delta, but with consequences for filament organization and alphaB-crystallin association.
Perng MD, Wen SF, Gibbon T, Middeldorp J, Sluijs J, Hol EM, Quinlan RA.
Mol Biol Cell. 2008 Oct; 19(10):4521-33. Epub 2008 Aug 6.
[Mol Biol Cell. 2008]
- » See all...