Evidence map›Paper›PMID 8320262›Full record

ArticleThe Journal of cell biology1993

The roles of the rod end and the tail in vimentin IF assembly and IF network formation.

M B McCormick, P Kouklis, A Syder, E Fuchs

Abstract read
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
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  12. A dysfunctional desmin mutation in a patient with severe generalized myopathy.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  13. Article
  14. Intermediate filaments as dynamic structures.Cancer metastasis reviews · 1996
    Review
  15. Article
  16. Article
  17. Article
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  20. Review
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.

M B McCormickHoward Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637.
P Kouklis
A Syder
E Fuchs

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Using mutagenesis, we investigated the importance of two vimentin domains: (a) a highly conserved segment near the carboxy end of the alpha-helical rod, and (b) the tail, with which the rod end is known to interact. As judged by in vitro filament assembly and expression in transiently transfected cells lacking an endogenous vimentin network, the rod-tail interaction is not essential for 10 nm filament structure in vitro or for formation of fibrous arrays in culture. However, when mutated, amino acid residues within the rod and the tail segments can cause perturbations in IF assembly and in IF network formation. Finally, our studies show that the vimentin tail seems to play a role both in thermodynamically stabilizing IF structure in vitro and in establishing proper IF networks in vivo.

Indexed as

Amino Acid SequenceAnimalsCell LineIntermediate Filament ProteinsIntermediate FilamentsMicrotubulesMolecular Sequence DataMutationPoint MutationProtein Structure, SecondaryTransfectionVimentinIntermediate Filament ProteinsVimentin

Identifiers

PMID8320262
PMCPMC2119649

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Registered trials

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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.