Evidence map›Paper›PMID 7635312›Full record

ArticleGenetics1995

Genetic analysis of the fimbrin-actin binding interaction in Saccharomyces cerevisiae.

S M Brower, J E Honts, A E Adams

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Genetics, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  7. The yeast actin cytoskeleton: from cellular function to biochemical mechanism.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Amphiphysin I antisense oligonucleotides inhibit neurite outgrowth in cultured hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
  14. 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.

S M BrowerDepartment of Molecular and Cellular Biology, University of Arizona, Tucson 85721, USA.
J E Honts
A E Adams
University of Arizona · US

Funding

Integrative Cancer Scholars Training GrantT32CA009213 · NCI · UNIVERSITY OF ARIZONA · PI CAREW, JENNIFER S, CURIEL-LEWANDROWSKI, CLARA · 1985 to 2024
$8.6M
MOLECULAR ANALYSIS OF THE YEAST ACTIN CYTOSKELETONR01GM045288 · NIGMS · UNIVERSITY OF ARIZONA · PI ADAMS, ALISON E · 1991 to 1999
–
NCI NIH HHS CA-09213NIGMS NIH HHS GM-45288
6 · The paper itself

Abstract

Yeast fimbrin is encoded by the SAC6 gene, mutations of which suppress temperature-sensitive mutations in the actin gene (ACT1). To examine the mechanism of suppression, we have sequenced 17 sac6 suppressor alleles, and found that they change nine different residues, all of which cluster in three regions of one of the two actin-binding domains of Sac6p. Two of these clusters occur in highly conserved regions (ABS1 and ABS3) that have been strongly implicated in the binding of related proteins to actin. The third cluster changes residues not previously implicated in the interaction with actin. As changes in any of nine different residues can suppress several different act1 alleles, it is likely that the suppressors restore the overall affinity, rather than specific lost interactions, between Sac6p and actin. Using mutagenesis, we have identified two mutations of the second actin-binding domain that can also suppress the act1 mutations of interest. This result suggests the two actin-binding domains of Sac6p interact with the same region of the actin molecule. However, differences in strength of suppression of temperature-sensitivity and sporulation indicate that the two actin-binding domains are distinct, and explain why second-domain mutations were not identified previously.

Indexed as

Genes, FungalMicrofilament ProteinsSuppression, GeneticActinsAmino Acid SequenceBase SequenceDNA RepairFungal ProteinsMembrane GlycoproteinsMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingRecombinant Fusion ProteinsSaccharomyces cerevisiaeSequence AlignmentSequence Homology, Amino AcidActinsFungal ProteinsMembrane GlycoproteinsMicrofilament ProteinsplastinRecombinant Fusion Proteins

Identifiers

PMID7635312
PMCPMC1206575
OpenAlexW2112484783

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.