Evidence map›Paper›PMID 23974285›Full record

ReviewCurrent genetics2013

Endocytic regulation of alkali metal transport proteins in mammals, yeast and plants.

José Miguel Mulet, Vicent Llopis-Torregrosa, Cecilia Primo, Ma Carmen Marqués, Lynne Yenush

Open access · greenAbstract readComparative StudyReview
PubMed Publisher
In one paragraph

Review in Current genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.3field-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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. The Biostimulant, Potassium Humate Ameliorates Abiotic Stress inInternational journal of molecular sciences · 2023
    Article
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  8. Ubiquitination in plant nutrient utilization.Frontiers in plant science · 2013
    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 1 country.

José Miguel MuletInstituto de Biología Molecular y Celular de Plantas (IBMCP), Universitat Politècnica de València-Consejo Superior de Investigaciones Científicas, Avd. de los Naranjos s/n, 46022, Valencia, Spain.
Vicent Llopis-Torregrosa
Cecilia Primo
Ma Carmen Marqués
Lynne Yenush
Consejo Superior de Investigaciones Científicas · ESInstituto de Biología Molecular y Celular de Plantas · ESUniversitat Politècnica de València · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The relative concentrations of ions and solutes inside cells are actively maintained by several classes of transport proteins, in many cases against their concentration gradient. These transport processes, which consume a large portion of cellular energy, must be constantly regulated. Many structurally distinct families of channels, carriers, and pumps have been characterized in considerable detail during the past decades and defects in the function of some of these proteins have been linked to a growing list of human diseases. The dynamic regulation of the transport proteins present at the cell surface is vital for both normal cellular function and for the successful adaptation to changing environments. The composition of proteins present at the cell surface is controlled on both the transcriptional and post-translational level. Post-translational regulation involves highly conserved mechanisms of phosphorylation- and ubiquitylation-dependent signal transduction routes used to modify the cohort of receptors and transport proteins present under any given circumstances. In this review, we will summarize what is currently known about one facet of this regulatory process: the endocytic regulation of alkali metal transport proteins. The physiological relevance, major contributors, parallels and missing pieces of the puzzle in mammals, yeast and plants will be discussed.

Indexed as

AnimalsCation Transport ProteinsEndocytosisMammalsMetals, AlkaliModels, BiologicalPhosphorylationPlantsProtein Processing, Post-TranslationalSaccharomyces cerevisiae ProteinsSignal TransductionSodium-Hydrogen ExchangersSpecies SpecificityUbiquitinationYeastsCation Transport ProteinsMetals, AlkaliNHX1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSodium-Hydrogen Exchangers

Identifiers

PMID23974285
OpenAlexW1971370697

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.