Evidence map›Paper›PMID 15767464›Full record

ArticleThe Journal of cell biology2005

A small surface hydrophobic stripe in the coiled-coil domain of type I keratins mediates tetramer stability.

Kelsie M Bernot, Chang-Hun Lee, Pierre A Coulombe

Abstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Molecular Modeling of Pathogenic Mutations in the Keratin 1B Domain.International journal of molecular sciences · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  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.

Kelsie M BernotDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Chang-Hun Lee
Pierre A Coulombe

Funding

Non-Canonical Functions of Keratin Proteins in SkinR01AR044232 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI COULOMBE, PIERRE · 1996 to 2020
$8.6M
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 AR42047NIAMS NIH HHS AR44232NIAMS NIH HHS R01 AR042047NIAMS NIH HHS R01 AR044232NIAMS NIH HHS R56 AR042047
6 · The paper itself

Abstract

Intermediate filaments (IFs) are fibrous polymers encoded by a large family of differentially expressed genes that provide crucial structural support in the cytoplasm and nucleus in higher eukaryotes. The mechanisms involved in bringing together approximately 16 elongated coiled-coil dimers to form an IF are poorly defined. Available evidence suggests that tetramer subunits play a key role during IF assembly and regulation. Through molecular modeling and site-directed mutagenesis, we document a hitherto unnoticed hydrophobic stripe exposed at the surface of coiled-coil keratin heterodimers that contributes to the extraordinary stability of heterotetramers. The inability of K16 to form urea-stable tetramers in vitro correlates with an increase in its turnover rate in vivo. The data presented support a specific conformation for the assembly competent IF tetramer, provide a molecular basis for their differential stability in vitro, and point to the physiological relevance associated with this property in vivo.

Indexed as

Hydrophobic and Hydrophilic InteractionsAmino Acid SequenceAmino Acid SubstitutionAnimalsCells, CulturedChromatography, Ion ExchangeConsensus SequenceCross-Linking ReagentsDimerizationElectrophoresis, Agar GelElectrophoresis, Polyacrylamide GelEscherichia coliHumansKeratinocytesKeratinsMiceCross-Linking ReagentsKeratinsRecombinant Proteins

Identifiers

PMID15767464
PMCPMC2171788

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.