Evidence map›Paper›PMID 2839826›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1988

Villin sequence and peptide map identify six homologous domains.

W L Bazari, P Matsudaira, M Wallek, T Smeal, R Jakes, Y Ahmed

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

43 citing papers in PubMed, 136 citations in OpenAlex.

  1. The unusual internal motion of the villin headpiece subdomain.Protein science : a publication of the Protein Society · 2016
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. The 3D structure of villin as an unusual F-Actin crosslinker.Structure (London, England : 1993) · 2008
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain.Protein science : a publication of the Protein Society · 2002
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Refined structure of villin 14T and a detailed comparison with other actin-severing domains.Protein science : a publication of the Protein Society · 1997
    Article
  17. Comparative FISH-mapping of villin (VIL) gene in river buffalo, sheep and goat chromosomes.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 1997
    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

6 authors at 2 institutions in 1 country.

W L BazariWhitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142.
P Matsudaira
M Wallek
T Smeal
R Jakes
Y Ahmed
Whitehead Institute for Biomedical Research · USMassachusetts Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Site-specific proteases and antisera to the amino terminus of villin have been used to show that villin is organized into seven protease-resistant domains. Six are contained in the amino-terminal Mr 87,000 villin core, a Ca2+-regulated actin-severing fragment, whereas the carboxyl-terminal domain includes the villin "headpiece," a fragment involved in bundling of actin filaments. Ca2+ inhibits proteolytic cleavage between domains in the amino-terminal half of villin. The protein sequence of villin deduced from a single cDNA clone contains a conserved sequence that is repeated six times and is found in each domain of the villin core. The conserved repeats are found in other actin-severing proteins but not in the villin headpiece. Our results suggest that actin-severing proteins are organized around a common Mr 14,000-17,000 domain.

Indexed as

Carrier ProteinsMicrofilament ProteinsAmino Acid SequenceAnimalsBase SequenceCalciumCalcium-Binding ProteinsChickensChymotrypsinDNAElectrophoresis, Polyacrylamide GelGelsolinImmunoassayMolecular Sequence DataMolecular WeightPeptide FragmentsCalciumCalcium-Binding ProteinsCarrier ProteinsChymotrypsinDNAGelsolinglutamyl endopeptidaseMicrofilament ProteinsPeptide FragmentsSerine EndopeptidasesTrypsinvillin

Identifiers

PMID2839826
PMCPMC281672
OpenAlexW2092302879

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.