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cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.

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Fisher, D Z, Chaudhary, N, Blobel, G·1986·Proceedings of the National Academy of Sciences

Abstract

The amino acid sequences deduced from cDNA clones of human lamin A and lamin C show identity between these two lamins except for an extra 9.0-kDa carboxyl-terminal tail that is present only in lamin A. Both lamins A and C contain an alpha-helical domain of approximately 360 residues that shows striking homology to a corresponding alpha-helical rod domain that is the structural hallmark of all intermediate filament proteins. However, the lamin alpha-helical domain is 14% larger than that of the intermediate filament proteins. In addition to the extensive homology to intermediate filament proteins as reported [McKeon, F., Kirschner, M. & Caput, D. (1986) Nature (London) 319, 463-468], a different 82-amino acid residue stretch at the carboxyl terminus of lamin A has been deduced and verified by amino acid sequencing. This region contains sequence homology to amino- and carboxylterminal domains of type I and type II epidermal keratins. Implications of the presence of these and other domains in lamins A and C for the assembly of the nuclear lamina are discussed.

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Metadata

Authors
Fisher, D. Z., Chaudhary, N., & Blobel, G.
Venue
Proceedings of the National Academy of Sciences
Published
1986-09
Volume
83
Issue
17
Pages
6450-6454
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1978705807
Cited by
711
References
0
FWCI
14.51
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. https://app.cochat.ai/papers/10.1073/pnas.83.17.6450
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Fisher, D. Z., Chaudhary, N., & Blobel, G. (1986). cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.83.17.6450

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