ReviewCellular and molecular life sciences : CMLS2016
Unique carbohydrate binding platforms employed by the glucan phosphatases.
Review in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 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
12 citing papers in PubMed, 29 citations in OpenAlex.
- Self-Feeding Living Materials Enabled by Cell Responsive Glycogen Nanoparticles as Metabolic Batteries.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Covalently linked phosphate monoesters on alpha-polyglucans reduce substrate affinity of branching enzymes.Carbohydrate polymers · 2025Article
- Polyglucosan body structure in Lafora disease.Carbohydrate polymers · 2020Article
- Targeting Pathogenic Lafora Bodies in Lafora Disease Using an Antibody-Enzyme Fusion.Cell metabolism · 2019Article
- Skeletal Muscle Glycogen Chain Length Correlates with Insolubility in Mouse Models of Polyglucosan-Associated Neurodegenerative Diseases.Cell reports · 2019Article
- Brain Glycogen Structure and Its Associated Proteins: Past, Present and Future.Advances in neurobiology · 2019Review
- A novel EPM2A mutation yields a slow progression form of Lafora disease.Epilepsy research · 2018Article
- The unique evolution of the carbohydrate-binding module CBM20 in laforin.FEBS letters · 2018Article
- Identification and analysis of OsttaDSP, a phosphoglucan phosphatase from Ostreococcus tauri.PloS one · 2018Article
- Fungal Hybrid B heme peroxidases - unique fusions of a heme peroxidase domain with a carbohydrate-binding domain.Scientific reports · 2017Article
- Pathogenesis of Lafora Disease: Transition of Soluble Glycogen to Insoluble Polyglucosan.International journal of molecular sciences · 2017Review
- Abnormal glycogen chain length pattern, not hyperphosphorylation, is critical in Lafora disease.EMBO molecular medicine · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Glucan phosphatases are a family of enzymes that are functionally conserved at the enzymatic level in animals and plants. These enzymes bind and dephosphorylate glycogen in animals and starch in plants. While the enzymatic function is conserved, the glucan phosphatases employ distinct mechanisms to bind and dephosphorylate glycogen or starch. The founding member of the family is a bimodular human protein called laforin that is comprised of a carbohydrate binding module 20 (CBM20) followed by a dual specificity phosphatase domain. Plants contain two glucan phosphatases: Starch EXcess4 (SEX4) and Like Sex Four2 (LSF2). SEX4 contains a chloroplast targeting peptide, dual specificity phosphatase (DSP) domain, a CBM45, and a carboxy-terminal motif. LSF2 is comprised of simply a chloroplast targeting peptide, DSP domain, and carboxy-terminal motif. SEX4 employs an integrated DSP-CBM glucan-binding platform to engage and dephosphorylate starch. LSF2 lacks a CBM and instead utilizes two surface binding sites to bind and dephosphorylate starch. Laforin is a dimeric protein in solution and it utilizes a tetramodular architecture and cooperativity to bind and dephosphorylate glycogen. This chapter describes the biological role of glucan phosphatases in glycogen and starch metabolism and compares and contrasts their ability to bind and dephosphorylate glucans.
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.