Evidence map›Paper›PMID 8741835›Full record

ArticleMolecular biology of the cell1996

Mutational analysis of capping protein function in Saccharomyces cerevisiae.

G I Sizonenko, T S Karpova, D J Gattermeir, J A Cooper

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Capping protein regulators fine-tune actin assembly dynamics.Nature reviews. Molecular cell biology · 2014
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. New insights into mechanism and regulation of actin capping protein.International review of cell and molecular biology · 2008
    Review
  15. Article
  16. Article
  17. Article
  18. 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

4 authors at 1 institution in 1 country.

G I SizonenkoDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
T S Karpova
D J Gattermeir
J A Cooper
Washington University in St. Louis · US

Funding

The Function of Dynein in Budding YeastR01GM047337 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1993 to 2009
$2.6M
NIGMS NIH HHS GM-47337
6 · The paper itself

Abstract

To investigate physiologic functions and structural correlates for actin capping protein (CP), we analyzed site-directed mutations in CAP1 and CAP2, which encode the alpha and beta subunits of CP in Saccharomyces cerevisiae. Mutations in four different regions caused a loss of CP function in vivo despite the presence of mutant protein in the cells. Mutations in three regions caused a complete loss of all aspects of function, including the actin distribution, viability with sac6, and localization of CP to actin cortical patches. Mutation of the fourth region led to partial loss of only one function-formation of actin cables. Some mutations retained function and exhibited the complete wild-type phenotype, and some mutations led to a complete loss of protein and therefore loss of function. The simplest hypothesis that can explain these results is that a single biochemical property is necessary for all in vivo functions. This biochemical property is most likely binding to actin filaments, because the nonfunctional mutant CPs no longer co-localize with actin filaments in vivo and because direct binding of CP to actin filaments has been well established by studies with purified proteins in vitro. More complex hypotheses, involving the existence of additional biochemical properties important for function, cannot be excluded by this analysis.

Indexed as

Actin Capping ProteinsActin Depolymerizing FactorsAmino Acid SequenceBase SequenceDestrinDNA Mutational AnalysisMicrofilament ProteinsMicroscopy, FluorescenceMolecular Sequence DataMutagenesis, Site-DirectedPeptide Chain Termination, TranslationalProtein BindingProtein ConformationSaccharomyces cerevisiaeStructure-Activity RelationshipActin Capping ProteinsActin Depolymerizing FactorsDestrinMicrofilament Proteins

Identifiers

PMID8741835
PMCPMC278608
OpenAlexW2063234966

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.