Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing 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.
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
18 authors.
Paulo E Santo *Centre de Biologie Intégrative (CBI), University of Toulouse CNRS, Equipe labellisée Ligue Nationale Contre le Cancer, Toulouse, France.ORCID 0000-0003-4277-3573
Marie-Eve Chagot *Université de Lorraine, CNRS, IMoPA, Nancy, France.
Hugo Gizardin-Fredon *Laboratoire de Spectrométrie de Masse BioOrganique, IPHC UMR 7178, Université de Strasbourg, CNRS, Strasbourg, France.ORCID 0000-0002-3566-7206
Marie Ley *Laboratoire de Spectrométrie de Masse BioOrganique, IPHC UMR 7178, Université de Strasbourg, CNRS, Strasbourg, France.
Thomas ChenuelSorbonne Université, PSL, CNRS, UMR8226, Institut de Biologie Physico-Chimique, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Paris, France.ORCID 0000-0002-3113-0559
Evolène DeslignièreLaboratoire de Spectrométrie de Masse BioOrganique, IPHC UMR 7178, Université de Strasbourg, CNRS, Strasbourg, France.
Laura PlassartCentre de Biologie Intégrative (CBI), University of Toulouse CNRS, Equipe labellisée Ligue Nationale Contre le Cancer, Toulouse, France.
Ana C F PaivaiBET, Instituto de Biologia Experimental e Tecnológica, Apartado 12, Oeiras, Portugal.
Pedro M F SousaiBET, Instituto de Biologia Experimental e Tecnológica, Apartado 12, Oeiras, Portugal.ORCID 0000-0002-6672-3610
Edouard BertrandIGH, CNRS, Univ Montpellier, Montpellier, France. Equipe labellisée Ligue Nationale Contre le Cancer, Montpellier, France.ORCID 0000-0002-9642-7994
Céline VerheggenIGH, CNRS, Univ Montpellier, Montpellier, France. Equipe labellisée Ligue Nationale Contre le Cancer, Montpellier, France.ORCID 0000-0003-2459-9700
Marc QuinternetUniversité de Lorraine, CNRS, IMoPA, Nancy, France.
Philippe MeyerSorbonne Université, PSL, CNRS, UMR8226, Institut de Biologie Physico-Chimique, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Paris, France.
Tiago M BandeirasiBET, Instituto de Biologia Experimental e Tecnológica, Apartado 12, Oeiras, Portugal.
Sarah CianféraniLaboratoire de Spectrométrie de Masse BioOrganique, IPHC UMR 7178, Université de Strasbourg, CNRS, Strasbourg, France. sarah.cianferani@unistra.fr.ORCID 0000-0003-4013-4129
Célia Plisson-ChastangCentre de Biologie Intégrative (CBI), University of Toulouse CNRS, Equipe labellisée Ligue Nationale Contre le Cancer, Toulouse, France. celia.plisson-chastang@utoulouse.fr.ORCID 0000-0002-8439-8428
Xavier ManivalUniversité de Lorraine, CNRS, IMoPA, Nancy, France. xavier.manival@univ-lorraine.fr.ORCID 0000-0002-7717-7096
Funding
Agence Nationale de la Recherche (French National Research Agency) ANR-10-INBS-08-03Agence Nationale de la Recherche (French National Research Agency) ANR-23-CE12-0022 YMCRAgence Nationale de la Recherche (French National Research Agency) ANR-23-CE44-0035Agence Nationale de la Recherche (French National Research Agency) ANR-23-CE44-0035 NAProt-XLMS
6 · The paper itself
Abstract
R2SP belongs to the R2TP-like quaternary chaperone family and consists of RUVBL1/RUVBL2 AAA+ ATPases, which powers the machinery, and SPAG1 and PIH1D2 adapter proteins that engage specific clients to promote their quaternary assembly. However, little is known about the structure of R2SP and the precise mode of action of these R2TP-like complexes. Here, we combined biochemical (ATPase and fluorescence polarization assays) and structural approaches (NMR, structural mass spectrometry, cryo-EM) to investigate the 3D organization of the R2SP complex, its mode of assembly and ATPase activity. Together with our binding, mutational and kinetic studies, these results led us to propose a model in which SPAG1 and PIH1D2 bind and cooperatively engage RUVBL1/RUVBL2 to produce R2SP. This reveals a 3D structure close to the canonical R2TP complex but also highlights differences in RUVBL1/RUVBL2 ATPase activity, as well as the cooperative binding of SPAG1 and PIH1D2 to this catalytic core that may explain functional difference between the two systems.
Indexed as
ATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsDNA HelicasesMolecular ChaperonesAdenosine TriphosphatasesCryoelectron MicroscopyHumansModels, MolecularProtein BindingAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsDNA HelicasesMolecular ChaperonesRUVBL1 protein, humanRUVBL2 protein, human
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 Socratic graph.
An integrative structural biology approach reveals the dynamic organization of the R2SP quaternary chaperone complex. · full record | Socratic