DOI: 10.1042/bj2380305. Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins

Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins

10.1042/bj2380305

Crossref journal-article

Portland Press Ltd.

Biochemical Journal (288)

Abstract

Analysis of the amino acid sequences of lamins A and C has revealed that each chain has an almost continuous heptad-containing coiled-coil domain containing structural regularities in the linear disposition of the acidic and the basic residues. The data suggest that the lamin molecules are two-stranded ropes, that the two chains are parallel to one another and in axial register, and that the molecules aggregate in vivo through periodic ionic interactions. These results indicate that significant changes in stability of the nuclear envelope may be achieved between interphase and mitosis through changes in the degree of phosphorylation of the lamin proteins.

Authors 3

D A D Parry (first)
J F Conway (additional)
P M Steinert (additional)

References 0 Referenced 55

None

Dates

Type	When
Created	10 years ago (Aug. 10, 2015, 4:55 p.m.)
Deposited	3 years, 8 months ago (Nov. 25, 2021, 1:22 p.m.)
Indexed	11 months, 3 weeks ago (Aug. 29, 2024, 7:07 a.m.)
Issued	39 years ago (Aug. 15, 1986)
Published	39 years ago (Aug. 15, 1986)
Published Print	39 years ago (Aug. 15, 1986)

Funders 0

None

BibTeX

@article{Parry_1986, title={Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins}, volume={238}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj2380305}, DOI={10.1042/bj2380305}, number={1}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Parry, D A D and Conway, J F and Steinert, P M}, year={1986}, month=aug, pages={305–308} }

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