Evidence map›Paper›PMID 14648121›Full record

ArticlePlanta2004

Functional expression in yeast of an N-deleted form of At-ACA8, a plasma membrane Ca(2+)-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant.

Maria Cristina Bonza, Laura Luoni, Maria Ida De Michelis

Abstract read
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In one paragraph

Article in Planta, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Evolutionarily conserved BON1 regulates the basal cytosolic CaProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  4. Tonoplast-localized CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Article
  6. The Journal of biological chemistry · 2017
    Article
  7. Article
  8. Article
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  15. Review
  16. A plant plasma membrane Ca2+ pump is required for normal pollen tube growth and fertilization.Proceedings of the National Academy of Sciences of the United States of America · 2004
    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 2 institutions in 2 countries.

Maria Cristina BonzaDipartimento di Biologia "L Gorini", Università di Milano, CNR Istituto di Biofisica-Sezione di Milano, via G Celoria 26, 20133, Milano, Italy.
Laura Luoni
Maria Ida De Michelis
University of Milan · ITInstituto Biofisika · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A constitutively active form of At-ACA8, a plasma membrane Ca(2+)-ATPase from Arabidopsis thaliana (L.) Heynh., from which the first 74 amino acids containing the calmodulin-binding domain (delta74- At-ACA8) had been deleted, was expressed in Saccharomyces cerevisiae strain K616, which lacks the main endogenous active Ca(2+) transport systems. Delta74- At-ACA8 complemented the K616 phenotype, making it able to grow in a calcium-depleted medium. Delta74- At-ACA8 protein, which co-migrated with the endoplasmic reticulum marker BiP in a sucrose-density gradient, catalyzed MgATP-dependent Ca(2+) uptake and Ca(2+)-dependent MgATP hydrolysis, and retained the biochemical characteristics of the native plant plasma membrane Ca(2+)-ATPase (low specificity for nucleoside triphosphate, high sensitivity to inhibition by the fluorescein derivatives erythrosin B and eosin Y), thus confirming that it is correctly folded and functional. Substitution of the (794)HE residues (numbers refer to full-length At-ACA8) following the highly conserved TGDG(TV)NDP(AS)L motif in the cytoplasmic headpiece with two lysine residues generated an hyperactive protein, with a catalytic activity 2-fold higher than that of delta74- At-ACA8. The (794)HE-->KK mutant was also about 6-fold more sensitive than delta74- At-ACA8 to inhibition by vanadate, indicating that the mutation determines an increase in the proportion of enzyme in the E(2) state during the catalytic cycle.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCalcium-Transporting ATPasesGene Expression Regulation, EnzymologicGene Expression Regulation, PlantMembrane ProteinsMolecular Sequence DataMutationSaccharomyces cerevisiaeSequence Homology, Amino AcidArabidopsis ProteinsCalcium-Transporting ATPasesMembrane Proteins

Identifiers

PMID14648121
OpenAlexW2076140221

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.