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.
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany. schulman@biochem.mpg.de.ORCID http://orcid.org/0000-0002-3083-1126
Funding
Identification of small molecule inhibitors of the DDI2 proteaseR01CA279255 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Gary L. Kleiger, Senthil Kumar Radhakrishnan · 2023 to 2026
$2.9M
How ubiquitin-carrying enzymes contribute to ubiquitin ligase specificityR01GM141409 · NIGMS · UNIVERSITY OF NEVADA LAS VEGAS · PI KLEIGER, GARY L. · 2021 to 2024
$1.6M
Boehringer Ingelheim Fonds (Stiftung für medizinische Grundlagenforschung) PhD fellowshipBoehringer Ingelheim Fonds (Stiftung für medizinische Grundlagenforschung) PhD FellowshipEC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) ERC AdG UPSmeetMet 101098161Max-Planck-Gesellschaft (Max Planck Society) Matthias Mann DepartmentMax-Planck-Gesellschaft (Max Planck Society) Peter Murray Research GroupMax-Planck-Gesellschaft (Max Planck Society) Schulman departmentNCI NIH HHS R01 CA279255NIGMS NIH HHS R01 GM141409U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) NIH R01CA279255U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) NIH R01GM141409
6 · The paper itself
Abstract
Cellular responses to amino acid fluctuations often hinge on ubiquitin-mediated control of metabolic enzymes, yet the underlying E3 ligase pathways remain poorly defined. Using quantitative proteomics and active cullin-RING ligase (CRL) profiling, we identify LRRC58 as a cysteine-responsive substrate receptor whose stability increases sharply under cysteine starvation. Proteomics reveals an inverse relationship between LRRC58 and the metabolic enzyme cysteine dioxygenase 1 (CDO1), suggesting a cysteine-linked regulatory axis. Biochemical reconstitution and cryo-EM structures show that LRRC58 forms an active CUL2- or CUL5-based CRL that selectively positions CDO1 for ubiquitylation at Lys8. Disease mutant versions of CDO1 mapping to the LRRC58 interface and impaired for the endogenous ubiquitylation pathway were degraded through orthogonal targeting by a VHL-based degrader. Together, our proteomics-guided discovery pipeline, cellular stability studies, and structural analyses uncover a metabolically-tuned LRRC58-CDO1 pathway that links cysteine availability to selective proteasomal turnover, reveals principles of metabolite-regulated CRL activity, and showcases mechanisms distinguishing endogenous and targeted protein degradation.
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.
Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1. · full record | OpenQuestion