Evidence map›Paper›PMID 11809846›Full record

ArticleMolecular biology of the cell2002

Pairwise assembly determines the intrinsic potential for self-organization and mechanical properties of keratin filaments.

Soichiro Yamada, Denis Wirtz, Pierre A Coulombe

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Functional cell death, corneoptosis, requires temporally controlled intracellular acidification.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. A unique mode of keratinocyte death requires intracellular acidification.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Soichiro YamadaDepartment of Chemical Engineering, The Johns Hopkins University, Baltimore, MD 21218, USA.
Denis Wirtz
Pierre A Coulombe
Johns Hopkins University · US

Funding

TYPE II KERATIN GENES /PROTEINS IN COMPLEX EPITHELIAR01AR042047 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI COULOMBE, PIERRE · 1995 to 2018
$7.1M
Role of keratin intermediate filaments in skin epithelial architecture and homeostasisR56AR042047 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI COULOMBE, PIERRE · 2020 to 2020
$429k
KERATIN INTERMEDIATE FILAMENTS AND SKIN DISEASESR55AR042047 · NIAMS · JOHNS HOPKINS UNIVERSITY · PI COULOMBE, PIERRE · 1994 to 1994
–
NIAMS NIH HHS AR 42047NIAMS NIH HHS R01 AR042047NIAMS NIH HHS R56 AR042047
6 · The paper itself

Abstract

Most type I and II keratin genes are spatially and temporally regulated in a pairwise manner in epithelial tissues, where they represent the major structural proteins. Epithelia can be partitioned into simple (single-layered) and complex (multilayered) types. We compared the structural and mechanical properties of natural keratin polymers occurring in complex (K5-K14) and simple (K8-K18) epithelia. The intrinsic properties of these distantly related keratin filaments, whether dispersed or bundled in vitro, were surprisingly similar in all respects when at high polymer concentration. When type I and II assembly partners were switched to give rise to mismatched polymers (K5-K18; K8-K14), the interfilament interactions, which determine the structural and mechanical properties of keratin polymers, were significantly altered. We also show that a K5-K16 polymer exhibits lesser elasticity than K5- K14, which may help explain the inability of K16 to fully rescue the skin blistering characteristic of K14 null mice. The property of self-interaction exhibited by keratin filaments is likely to assist their function in vivo and may account for the relative paucity of cytoplasmic and keratin-specific cross-linkers. Our findings underscore the fundamental importance of pairwise polymerization and have implications for the functional significance of keratin sequence diversity.

Indexed as

BiopolymersElasticityEpithelial CellsEscherichia coliGelsHumansHydrogen-Ion ConcentrationIntermediate FilamentsKeratinsRecombinant Fusion ProteinsRheologyStress, MechanicalTransformation, GeneticViscosityBiopolymersGelsKeratinsRecombinant Fusion Proteins

Identifiers

PMID11809846
PMCPMC65095
OpenAlexW2049526346

What OpenQuestion holds

Textmetadata
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.