Evidence map›Paper›PMID 41719407›Full record

ArticleScience advances2026

Structures of the 26

Moisés Maestro-López, Tat Cheung Cheng, Jimena Muntaner, Margarita Menéndez, Melissa Alonso, Andreas Schweitzer, Masato Ishizaka, Robert J Tomko, Jorge Cuéllar, José María Valpuesta and 1 more

Abstract read
In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Tryptophan-EnrichedBiomaterials research · 2026
    Article
  3. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    Review
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.

Moisés Maestro-LópezCentro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.ORCID 0000-0002-7955-9135
Tat Cheung ChengInstitute for Neuropathology, University Medical Center Göttingen, 37073 Göttingen, Germany.ORCID 0000-0003-2801-3084
Jimena MuntanerCentro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.
Margarita MenéndezInstituto de Química-Física Blas Cabrera (IQF-CSIC), 28006 Madrid, Spain.ORCID 0000-0002-3267-4443
Melissa AlonsoCentro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.
Andreas SchweitzerMultiscale Bioimaging: From Molecular Machines to Networks of Excitable Cells (MBExC), University of Göttingen, 37073 Göttingen, Germany.
Masato IshizakaInstitute for Neuropathology, University Medical Center Göttingen, 37073 Göttingen, Germany.ORCID 0000-0003-0906-5209
Robert J TomkoDepartment of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL 32306, USA.ORCID 0000-0003-2515-1078
Jorge CuéllarCentro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.ORCID 0000-0002-7789-807X
José María ValpuestaCentro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.ORCID 0000-0001-7468-8053
Eri SakataMultiscale Bioimaging: From Molecular Machines to Networks of Excitable Cells (MBExC), University of Göttingen, 37073 Göttingen, Germany.ORCID 0000-0002-8580-3683

Funding

Engagement and Communication Between Proteasonal SubcomplexesR01GM118600 · NIGMS · FLORIDA STATE UNIVERSITY · PI ROBERT JOSEPH TOMKO · 2017 to 2026
$2.7M
NIGMS NIH HHS R01 GM118600
6 · The paper itself

Abstract

Coupling between the chaperone and degradation systems, particularly under stress, is essential for eliminating unfolded proteins. The co-chaperone Bag1 links Hsp70 to the 26

Indexed as

DNA-Binding ProteinsHSP70 Heat-Shock ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsTranscription FactorsAdenosine TriphosphatasesCryoelectron MicroscopyModels, MolecularMolecular ChaperonesProtein BindingProtein ConformationProteolysisSubstrate SpecificityAdenosine TriphosphatasesATP dependent 26S proteaseBCL2-associated athanogene 1 proteinDNA-Binding ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID41719407
PMCPMC12922752

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.