ReviewTrends in biochemical sciences2009
Sumoylation and human disease pathogenesis.
Review in Trends in biochemical sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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.
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.
Who cites it
73 citing papers in PubMed, 144 citations in OpenAlex.
- SENP1 mitigates intervertebral disc degeneration: mechanisms involving suppression of pyroptosis and apoptosis in nucleus pulposus cells.Journal of orthopaedic surgery and research · 2026Article
- UBC9-mediated p53 SUMOylation drives tubular senescence and exacerbates acute kidney injury in mice.Acta pharmacologica Sinica · 2026Article
- ROS-SUMO Crosstalk in Oxidative Stress: Disease Mechanisms and Reproductive Health.Antioxidants (Basel, Switzerland) · 2026Review
- SUMOylation is destined for regulatory T cell-related immune dysregulation.Cell death discovery · 2026Review
- Curcumin attenuates α-synuclein pathology in Parkinson's disease model mice through modulation of UBC9-associated SUMOylation signaling.Frontiers in neuroscience · 2026Article
- UBC9-Mediated SUMO Pathway Drives Prohibitin-1 Nuclear Accumulation and PITX1 Repression in Primary Osteoarthritis.International journal of molecular sciences · 2025Article
- Polyglutamine (PolyQ) Diseases: Navigating the Landscape of Neurodegeneration.ACS chemical neuroscience · 2024Review
- Protein modification in neurodegenerative diseases.MedComm · 2024Review
- Regulation of Enhancers by SUMOylation Through TFAP2C Binding and Recruitment of HDAC Complex to the Chromatin.Research square · 2024Article
- Post-Translational Modifications in Tau and Their Roles in Alzheimer's Pathology.Current Alzheimer research · 2024Review
- Critical Non-Covalent Binding Intermediate for an Allosteric Covalent Inhibitor of SUMO E1.The journal of physical chemistry letters · 2023Article
- SIRT1 pathway in Parkinson's disease: a faraway snapshot but so close.Inflammopharmacology · 2023Review
- Review
- Epac1 activation by cAMP regulates cellular SUMOylation and promotes the formation of biomolecular condensates.Science advances · 2022Article
- Viruses, SUMO, and immunity: the interplay between viruses and the host SUMOylation system.Journal of neurovirology · 2021Review
- Enzymatic Machinery of Ubiquitin and Ubiquitin-Like Modification Systems in Chondrocyte Homeostasis and Osteoarthritis.Current rheumatology reports · 2021Review
- Isoforsythiaside Attenuates Alzheimer's Disease via Regulating Mitochondrial Function Through the PI3K/AKT Pathway.International journal of molecular sciences · 2020Article
- Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation.Frontiers in neurology · 2020Review
- Chemical Tools and Biochemical Assays for SUMO Specific Proteases (SENPs).ACS chemical biology · 2019Review
- SAE1 promotes human glioma progression through activating AKT SUMOylation-mediated signaling pathways.Cell communication and signaling : CCS · 2019Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Covalent modification by SUMO polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are several proteins implicated in human diseases including cancer, Huntington's, Alzheimer's, and Parkinson's diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. Recent reports reveal two new examples of human disease-associated proteins that are SUMO modified: amyloid precursor protein and lamin A. These findings point to a function for sumoylation in modulating amyloid-beta peptide levels, indicating a potential role in Alzheimer's disease, and for decreased lamin A sumoylation as a causative factor in familial dilated cardiomyopathy.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.