Evidence map›Paper›PMID 7891662›Full record

ArticleMolecular & general genetics : MGG1995

Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin.

P Sivadon, F Bauer, M Aigle, M Crouzet

Abstract read
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In one paragraph

Article in Molecular & general genetics : MGG, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing 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

65 citing papers in PubMed.

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5 more citing papers are in PubMed but not listed here.

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.

P SivadonLaboratoire de Génétique, CNRS UPR 9026, Université de Bordeaux II, Talence, France.
F Bauer
M Aigle
M Crouzet

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The actin cytoskeleton cells is altered in rvs161 mutant yeast, with the defect becoming more pronounced under unfavorable growth conditions, as described for the rvs167 mutant. The cytoskeletal alteration has no apparent effect on invertase secretion and polarized growth. Mutations in RVS161, just as in RVS167, lead to a random budding pattern in a/alpha diploid cells. This behavior is not observed in a/a diploid cells homozygous for the rvs161-1 or rvs167-1 mutations. In addition, sequence comparisons revealed that amphiphysin, a protein first found in synaptic vesicles of chicken and shown to be the autoantigen of Stiff Man syndrome, presents similarity with both Rvs proteins. Furthermore, limited similarities with myosin heavy chain and tropomyosin alpha chain from higher eukaryotic cells allow for the definition of a possible consensus sequence. The finding of related sequences suggests the existence of a function for these proteins that is conserved among eukaryotic organisms.

Indexed as

Cytoskeletal ProteinsSaccharomyces cerevisiae ProteinsActinsAmino Acid Sequencebeta-FructofuranosidaseCytoskeletonFungal ProteinsGlycoside HydrolasesMolecular Sequence DataMutationNerve Tissue ProteinsPhenotypeSaccharomyces cerevisiaeSequence Homology, Amino AcidActinsamphiphysinbeta-FructofuranosidaseCytoskeletal ProteinsFungal ProteinsGlycoside HydrolasesNerve Tissue ProteinsRVS161 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID7891662

What OpenQuestion holds

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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.