Evidence map›Paper›PMID 31996377›Full record

ArticleThe Journal of biological chemistry2020

The yeast protein Ubx4p contributes to mitochondrial respiration and lithium-galactose-mediated activation of the unfolded protein response.

Evandro A De-Souza, Felipe S A Pimentel, Ana Luiza F V De-Queiroz, Henrique Camara, Mikaella L Felix-Formiga, Caio M Machado, Silas Pinto, Antonio Galina, Marcelo A Mori, Monica Montero-Lomeli and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 43% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. 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

11 authors at 2 institutions in 1 country.

Evandro A De-SouzaPrograma de Biologia Molecular e Biotecnologia, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.ORCID 0000-0002-9080-3864
Felipe S A PimentelPrograma de Biologia Molecular e Biotecnologia, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.ORCID 0000-0002-4753-8612
Ana Luiza F V De-QueirozPrograma de Biologia Molecular e Biotecnologia, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.
Henrique CamaraDepartment of Biochemistry and Tissue Biology, Instituto de Biologia, Universidade Estadual de Campinas, Campinas SP, 13083-970, Brazil.
Mikaella L Felix-FormigaPrograma de Biologia Molecular e Biotecnologia, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.
Caio M MachadoPrograma de Biologia Molecular e Biotecnologia, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.
Silas PintoDepartment of Biochemistry and Tissue Biology, Instituto de Biologia, Universidade Estadual de Campinas, Campinas SP, 13083-970, Brazil.
Antonio GalinaPrograma de Bioquímica e Biofísica Celular, Instituto de Bioquímica M[c33c]zpi;●dica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.
Marcelo A MoriDepartment of Biochemistry and Tissue Biology, Instituto de Biologia, Universidade Estadual de Campinas, Campinas SP, 13083-970, Brazil.
Monica Montero-LomeliPrograma de Biologia Molecular e Biotecnologia, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil.
Claudio A MasudaPrograma de Biologia Molecular e Biotecnologia, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazil cmasuda@bioqmed.ufrj.br.ORCID 0000-0002-0310-7108
Universidade Federal do Rio de Janeiro · BRUniversidade Estadual de Campinas (UNICAMP) · BR

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Ann E. Rougvie · 2012 to 2026
$7.5M
NIH HHS P40 OD010440
6 · The paper itself

Abstract

In the presence of galactose, lithium ions activate the unfolded protein response (UPR) by inhibiting phosphoglucomutase activity and causing the accumulation of galactose-related metabolites, including galactose-1-phosphate. These metabolites also accumulate in humans who have the disease classic galactosemia. Here, we demonstrate that

Indexed as

Basic-Leucine Zipper Transcription FactorsEndoplasmic ReticulumGalactoseGalactosephosphatesIntracellular Signaling Peptides and ProteinsLithiumMitochondriaOxygen ConsumptionProtein Serine-Threonine KinasesRepressor ProteinsRNA SplicingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUnfolded Protein ResponseBasic-Leucine Zipper Transcription FactorsGalactosegalactose-1-phosphateGalactosephosphatesHAC1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsLithiumProtein Serine-Threonine KinasesRepressor ProteinsSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesUBX4 protein, S cerevisiaeASPS-1ASPSCR1Caenorhabditis elegans (C. elegans)endoplasmic reticulum–associated protein degradation (ERAD)endoplasmic reticulum stress (ER stress)galactosegalactosemialithiummitochondriaSaccharomyces cerevisiae

Identifiers

PMID31996377
PMCPMC7086034
OpenAlexW3003874934

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.