A novel glutamic acid to aspartic acid mutation near the end of the 2B rod domain in the keratin 1 chain in epidermolytic hyperkeratosis.

@article{Yang1999ANG,
  title={A novel glutamic acid to aspartic acid mutation near the end of the 2B rod domain in the keratin 1 chain in epidermolytic hyperkeratosis.},
  author={Jum-Mo Yang and K. Nam and Hyong-Cheol Kim and Jeung-Hoon Lee and Jang-Ku Park and K. Wu and Eil-Soo Lee and P. Steinert},
  journal={The Journal of investigative dermatology},
  year={1999},
  volume={112 3},
  pages={
          376-9
        }
}
We report a mutation in a mild case of epidermolytic hyperkeratosis that results in a glutamic acid to aspartic acid substitution in a novel location, codon 477 or position 106 of the 2B rod domain of the keratin 1 chain. This residue has been conserved in all intermediate filament chains and lies near the beginning of the highly conserved helix termination sequence and just prior to the predicted molecular overlap region. Keratin filaments assembled in vitro from chains bearing this… Expand
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References

SHOWING 1-10 OF 14 REFERENCES
Mutations in the H1 and 1A domains in the keratin 1 gene in epidermolytic hyperkeratosis.
  • 74
  • PDF
Preferential sites in keratin 10 that are mutated in epidermolytic hyperkeratosis.
  • 60
Intermediate filament structure
  • 203
Intermediate filaments in disease.
  • 236
...
1
2
...