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December 1, 1997Journal of Biological ChemistryOpen Access

A Proline Residue in the α-Helical Rod Domain of Type I Keratin 16 Destabilizes Keratin Heterotetramers

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Authors

MWMatthew WawersikWilliam & MaryRPRudolph D. PaladiniSystem Biosciences (United States)ENErick N. NoensieJohns Hopkins University

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Wawersik et al. (1997) studied this question.

synapsesocial.com/papers/69ff8cc3b124fe5819857de0https://doi.org/10.1074/jbc.272.51.32557
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1INTERMEDIATE FILAMENTS: Structure, Dynamics, Function and Disease1994 · 1,422 citations
  2. 2A nontetrameric species is the major soluble form of keratin in Xenopus oocytes and rabbit reticulocyte lysates.1996 · 22 citations
  3. 3Do the ends justify the mean? Proline mutations at the ends of the keratin coiled-coil rod segment are more disruptive than internal mutations.1992 · 152 citations
  4. 4Elucidating the early stages of keratin filament assembly.1990 · 249 citations