Evidence map›Paper›PMID 26181054›Full record

ArticlePloS one2015

Complete Structure of an Epithelial Keratin Dimer: Implications for Intermediate Filament Assembly.

David J Bray, Tiffany R Walsh, Massimo G Noro, Rebecca Notman

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Review
  3. Adsorption of Diclofenac and PFBS on a Hair Keratin Dimer.The journal of physical chemistry. B · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Deimination, Intermediate Filaments and Associated Proteins.International journal of molecular sciences · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

David J BrayDepartment of Chemistry University of Warwick, Coventry, United Kingdom; Centre for Scientific Computing, University of Warwick, Coventry, United Kingdom.
Tiffany R WalshInstitute for Frontier Materials, Deakin University, Geelong, VIC, Australia.
Massimo G NoroUnilever R&D Port Sunlight, Wirral, United Kingdom.
Rebecca NotmanDepartment of Chemistry University of Warwick, Coventry, United Kingdom; Centre for Scientific Computing, University of Warwick, Coventry, United Kingdom.
University of Warwick · GBDeakin University · AUUnilever (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Keratins are cytoskeletal proteins that hierarchically arrange into filaments, starting with the dimer sub-unit. They are integral to the structural support of cells, in skin, hair and nails. In skin, keratin is thought to play a critical role in conferring the barrier properties and elasticity of skin. In general, the keratin dimer is broadly described by a tri-domain structure: a head, a central rod and a tail. As yet, no atomistic-scale picture of the entire dimer structure exists; this information is pivotal for establishing molecular-level connections between structure and function in intermediate filament proteins. The roles of the head and tail domains in facilitating keratin filament assembly and function remain as open questions. To address these, we report results of molecular dynamics simulations of the entire epithelial human K1/K10 keratin dimer. Our findings comprise: (1) the first three-dimensional structural models of the complete dimer unit, comprising of the head, rod and tail domains; (2) new insights into the chirality of the rod-domain twist gained from analysis of the full domain structure; (3) evidence for tri-subdomain partitioning in the head and tail domains; and, (4) identification of the residue characteristics that mediate non-covalent contact between the chains in the dimer. Our findings are immediately applicable to other epithelial keratins, such as K8/K18 and K5/K14, and to intermediate filament proteins in general.

Indexed as

Protein MultimerizationAmino Acid SequenceDisulfidesHumansHydrogen BondingIntermediate FilamentsKeratin-1Keratin-10Molecular Dynamics SimulationMolecular Sequence DataProtein FoldingProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentDisulfidesKeratin-1Keratin-10KRT10 protein, humanKRT1 protein, human

Identifiers

PMID26181054
PMCPMC4504709
OpenAlexW1907678862

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.