ReviewThe FEBS journal2013
Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii.
Review in The FEBS journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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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
36 citing papers in PubMed, 73 citations in OpenAlex.
- Fractionated proteomics identifies a protein network mitigating resistance exercise-induced damage in human skeletal muscle.Nature communications · 2026Article
- Differential downstream signaling in microglia lacking Alzheimer's-related TREM2 or its adaptor TYROBP/DAP12.Molecular neurodegeneration advances · 2026Article
- Advances in gene therapy for Lafora disease: Intravenous recombinant adeno-associated virus-mediated delivery of EPM2A and EPM2B genes.Clinical and translational medicine · 2025Article
- Discovery and Evaluation of Active Site-Directed, Potent, and Selective Sulfophenyl Acetic Amide-Based Inhibitors for the Laforin Phosphatase.Journal of medicinal chemistry · 2025Article
- Gene therapy for Lafora disease in the Epm2aMolecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- Induction of Translational Readthrough on Protein Tyrosine Phosphatases Targeted by Premature Termination Codon Mutations in Human Disease.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Spatial metabolomics reveals glycogen as an actionable target for pulmonary fibrosis.Nature communications · 2023Article
- Laforin targets malin to glycogen in Lafora progressive myoclonus epilepsy.Disease models & mechanisms · 2023Article
- EPM2A acts as a protective factor in prostate cancer, evidence from a real-world patient cohort.Frontiers in pharmacology · 2022Article
- Article
- Generation and characterization of a laforin nanobody inhibitor.Clinical biochemistry · 2021Article
- A novel gene therapy for neurodegenerative Lafora disease viaNanomedicine (London, England) · 2021Article
- Beneficial Effects of Metformin on the Central Nervous System, with a Focus on Epilepsy and Lafora Disease.International journal of molecular sciences · 2021Review
- Genome-wide association study of pancreatic fat: The Multiethnic Cohort Adiposity Phenotype Study.PloS one · 2021Article
- Central Nervous System Delivery and Biodistribution Analysis of an Antibody-Enzyme Fusion for the Treatment of Lafora Disease.Molecular pharmaceutics · 2019Article
- [Lafora disease: a review of the literature].Revista de neurologia · 2019Review
- Brain Glycogen Structure and Its Associated Proteins: Past, Present and Future.Advances in neurobiology · 2019Review
- Regulation of CD4Frontiers in immunology · 2019Review
- Lafora disease - from pathogenesis to treatment strategies.Nature reviews. Neurology · 2018Review
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Lafora disease (LD) is a rare, fatal neurodegenerative disorder characterized by the accumulation of glycogen-like inclusions in the cytoplasm of cells from most tissues of affected patients. One hundred years after the first description of these inclusions, the molecular bases underlying the processes involved in LD physiopathology are finally being elucidated. The main cause of the disease is related to the activity of two proteins, the dual-specificity phosphatase laforin and the E3-ubiquitin ligase malin, which form a functional complex. Laforin is unique in humans, as it is composed of a carbohydrate-binding module attached to a cysteine-based catalytic dual-specificity phosphatase domain. Laforin directly dephosphorylates glycogen, but other proteinaceous substrates, if they exist, have remained elusive. Recently, an emerging set of laforin-binding partners apart from malin have been described, suggestive of laforin roles unrelated to its catalytic activity. Further investigations based on different transgenic mouse models have shown that the laforin-malin complex is also involved in other cellular processes, such as response to endoplasmic reticulum stress and misfolded protein clearance by the lysosomal pathway. However, controversial data and some missing links still make it difficult to assess the concrete relationship between glycogen deregulation and neuronal damage leading to the fatal symptoms observed in LD patients, such as myoclonic seizures and epilepsy. Consequently, clinical treatments are far from being achieved. In the present review, we focus on the knowledge of laforin biology, not only as a glucan phosphatase, but also as an adaptor protein involved in several physiological pathways.
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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.