Article in Nucleic acids research, 2025. 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
–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
19 authors.
Andrea Alegre-MartíDepartment of Biochemistry and Molecular Biomedicine, Faculty of Biology, University of Barcelona (UB), Barcelona 08028, Spain.ORCID 0000-0001-6646-8798
Alba Jiménez-PanizoDepartment of Biochemistry and Molecular Biomedicine, Faculty of Biology, University of Barcelona (UB), Barcelona 08028, Spain.ORCID 0000-0001-7046-6162
Agustina L LafuenteIFIBYNE, UBA-CONICET, Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Buenos Aires C1428EGA, Argentina.ORCID 0009-0004-8862-6880
Thomas A JohnsonNational Cancer Institute, National Institutes of Health, Bethesda, MD 20892-5055, United States.ORCID 0000-0002-9135-3252
Inés Montoya-NovoaDepartment of Biochemistry and Molecular Biomedicine, Faculty of Biology, University of Barcelona (UB), Barcelona 08028, Spain.
M Nuria Peralta-MorenoDepartment of Materials Science and Physical Chemistry, Faculty of Chemistry and Institut de Recerca en Química Teòrica i Computacional of the University of Barcelona (IQTCUB), Barcelona 08028, Spain.
Pilar Montanyà-VallugueraDepartment of Biochemistry and Molecular Biomedicine, Faculty of Biology, University of Barcelona (UB), Barcelona 08028, Spain.
Josep Ponsetí-PonsDepartment of Biochemistry and Molecular Biomedicine, Faculty of Biology, University of Barcelona (UB), Barcelona 08028, Spain.
Montserrat AbellaDepartment of Biochemistry and Molecular Biomedicine, Faculty of Biology, University of Barcelona (UB), Barcelona 08028, Spain.
Sohyoung KimNational Cancer Institute, National Institutes of Health, Bethesda, MD 20892-5055, United States.
Mireia DíazMass Spectrometry Core Facility, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Barcelona 08028, Spain.
Marta VilasecaMass Spectrometry Core Facility, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Barcelona 08028, Spain.
Paloma PérezInstituto de Biomedicina de Valencia (IBV-CSIC), Department of Pathology and Molecular and Cell Therapy, Valencia46010, Spain.ORCID 0000-0002-7166-2824
Juan Fernández-RecioInstituto de Ciencias de la Vid y del Vino (ICVV-CSIC), Universidad de La Rioja, Gobierno de La Rioja, Logroño 26007, Spain.ORCID 0000-0002-3986-7686
Jaime Rubio-MartínezDepartment of Materials Science and Physical Chemistry, Faculty of Chemistry and Institut de Recerca en Química Teòrica i Computacional of the University of Barcelona (IQTCUB), Barcelona 08028, Spain.ORCID 0000-0002-5529-2325
Diego M PresmanIFIBYNE, UBA-CONICET, Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Buenos Aires C1428EGA, Argentina.ORCID 0000-0003-4515-8058
Gordon L HagerNational Cancer Institute, National Institutes of Health, Bethesda, MD 20892-5055, United States.ORCID 0000-0002-9300-5331
Pablo Fuentes-PriorDepartment of Biochemistry and Molecular Biomedicine, Faculty of Biology, University of Barcelona (UB), Barcelona 08028, Spain.ORCID 0000-0002-6618-3204
Eva Estébanez-PerpiñáDepartment of Biochemistry and Molecular Biomedicine, Faculty of Biology, University of Barcelona (UB), Barcelona 08028, Spain.ORCID 0000-0003-2687-5801
Funding
Chromatin Structure and Gene ExpressionZIABC005450 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HAGER, GORDON L · 2009 to 2025
$35.2M
Agència de Gestió d'Ajuts Universitaris i de Recerca 2021SGR00350Agència de Gestió d'Ajuts Universitaris i de Recerca 2021SGR01433Agencia Estatal de Investigación BFU2017-86906-RAgencia Estatal de Investigación CPP2022-009586Agencia Estatal de Investigación JDC2022-048702-IAgencia Estatal de Investigación JDC2023-051138-IAgencia Estatal de Investigación PDC2021-121688-100Agencia Estatal de Investigación PID2022-141399-OB-100Agencia Estatal de Investigación PID2022-143215OB-I00Agencia Estatal de Investigación PID2023-1479660B-I00Agencia Nacional de Promoción de la Investigación, el Desarrollo Tecnológico y la Innovación PICT 2019-0397Consejo Nacional de Investigaciones Científicas y TécnicasG.E. Carretero FundMinisterio de Ciencia, Innovación y UniversidadesNCI NIH HHSNIH HHS ZIA BC 005450UB-CRAIUnidad de Excelencia María de Maeztu CEX2021-001202-MUniversitat de Barcelona
6 · The paper itself
Abstract
The glucocorticoid receptor (GR) is a leading drug target due to its antiinflammatory and immunosuppressive roles. The functional oligomeric conformation of full-length GR (FL-GR), which is key for its biological activity, remains disputed. Here we present a new crystal structure of agonist-bound GR ligand-binding domain (GR-LBD) comprising eight copies of a noncanonical dimer. We verified the biological relevance of this dimer for receptor multimerization in wild-type and selected FL-GR mutants using molecular dynamics and crosslinking-mass spectrometry together with fluorescence microscopy and transcriptomic analysis in living cells. Self-association of this GR-LBD basic dimer in two mutually exclusive assemblies reveals clues for FL-GR multimerization and activity in cells. We propose a model for the structure of multidomain GR based on our new data and suggest a detailed oligomerization pathway. This model reconciles all currently available structural and functional information and provides a more comprehensive understanding of the rare disorder, generalized glucocorticoid resistance.
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.
The multimerization pathway of the glucocorticoid receptor. · full record | OpenQuestion