Evidence map›Paper›PMID 17176761›Full record

ArticleFolia microbiologica2006

Exploration of yeast alkali metal cation/H+ antiporters: sequence and structure comparison.

L Pribylová, K Papousková, M Zavrel, J L Souciet, H Sychrová

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In one paragraph

Article in Folia microbiologica, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

9 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Alkali metal cation transport and homeostasis in yeasts.Microbiology and molecular biology reviews : MMBR · 2010
    Review
  8. Article
  9. 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

5 authors at 3 institutions in 2 countries.

L PribylováDepartment of Membrane Transport, Institute of Physiology, Academy of Sciences of the Czech Republic, 142 20 Prague, Czechia.
K Papousková
M Zavrel
J L Souciet
H Sychrová
Czech Academy of Sciences · CZCentre National de la Recherche Scientifique · FRCzech Academy of Sciences, Institute of Physiology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Saccharomyces cerevisiae genome contains three genes encoding alkali metal cation/H+ antiporters (Nha1p, Nhx1p, Kha1p) that differ in cell localization, substrate specificity and physiological function. Systematic genome sequencing of other yeast species revealed highly conserved homologous ORFs in all of them. We compared the yeast sequences both at DNA and protein levels. The subfamily of yeast endosomal/prevacuolar Nhx1 antiporters is closely related to mammalian plasma membrane NHE proteins and to both plasma membrane and vacuolar plant antiporters. The high sequence conservation within this subfamily of yeast antiporters suggests that Nhx1p is of great importance in cell physiology. Yeast Kha1 proteins probably belong to the same subfamily as bacterial antiporters, whereas Nhal proteins form a distinct subfamily.

Indexed as

Amino Acid SequenceCation Transport ProteinsDNA, FungalMembrane ProteinsMolecular Sequence DataPhylogenyPotassium-Hydrogen AntiportersSaccharomyces cerevisiae ProteinsSequence Analysis, DNASequence Homology, Amino AcidSodium-Hydrogen ExchangersCation Transport ProteinsDNA, FungalKHA1 protein, S cerevisiaeMembrane ProteinsNHA1 protein, S cerevisiaeNHX1 protein, S cerevisiaePotassium-Hydrogen AntiportersSaccharomyces cerevisiae ProteinsSodium-Hydrogen Exchangers

Identifiers

PMID17176761
OpenAlexW2060788725

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.