ReviewCellular and molecular life sciences : CMLS2014
Lysosomal multienzyme complex: pros and cons of working together.
Review in Cellular and molecular life sciences : CMLS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled 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.
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
67 citing papers in PubMed, 1 synthesis or guideline pooled it, 116 citations in OpenAlex.
- Mammalian Neuraminidases in Immune-Mediated Diseases: Mucins and Beyond.Frontiers in immunology · 2022Pooled it
- Article
- Review
- Associations of genetic proxies for non-steroidal anti-inflammatory drugs with increased kidney stone risk: a Mendelian randomization study.Inflammopharmacology · 2025Article
- Type I Sialidosis in a Chinese family: a case report and literature review.Acta epileptologica · 2025Article
- Evaluation of the Landscape of Pharmacodynamic Biomarkers in GM1 and GM2 Gangliosidosis.Clinical and translational science · 2025Review
- Genetic Insights and Clinical Implications ofGenes · 2025Review
- Neuraminidase-1 (NEU1): Biological Roles and Therapeutic Relevance in Human Disease.Current issues in molecular biology · 2024Review
- AAV-mediated gene therapy for sialidosis.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- Gene therapy corrects the neurological deficits of mice with sialidosis.Gene therapy · 2024Article
- The role of sialidase Neu1 in respiratory diseases.Respiratory research · 2024Review
- Non-steroidal anti-inflammatory drug target gene associations with major depressive disorders: a Mendelian randomisation study integrating GWAS, eQTL and mQTL Data.The pharmacogenomics journal · 2023Article
- Restoring Epigenetic Reprogramming with Diet and Exercise to Improve Health-Related Metabolic Diseases.Biomolecules · 2023Review
- Review
- Activated microglia release β-galactosidase that promotes inflammatory neurodegeneration.Frontiers in aging neuroscience · 2023Article
- Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 2022Review
- In Silico Structural Analysis of Serine CarboxypeptidaseInternational journal of molecular sciences · 2022Article
- Article
- Altered sialidase expression in human myeloid cells undergoing apoptosis and differentiation.Scientific reports · 2022Article
- NEU1-A Unique Therapeutic Target for Alzheimer's Disease.Frontiers in pharmacology · 2022Review
7 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
3 authors at 1 institution in 1 country.
Funding
Abstract
The ubiquitous distribution of lysosomes and their heterogeneous protein composition reflects the versatility of these organelles in maintaining cell homeostasis and their importance in tissue differentiation and remodeling. In lysosomes, the degradation of complex, macromolecular substrates requires the synergistic action of multiple hydrolases that usually work in a stepwise fashion. This catalytic machinery explains the existence of lysosomal enzyme complexes that can be dynamically assembled and disassembled to efficiently and quickly adapt to the pool of substrates to be processed or degraded, adding extra tiers to the regulation of the individual protein components. An example of such a complex is the one composed of three hydrolases that are ubiquitously but differentially expressed: the serine carboxypeptidase, protective protein/cathepsin A (PPCA), the sialidase, neuraminidase-1 (NEU1), and the glycosidase β-galactosidase (β-GAL). Next to this 'core' complex, the existence of sub-complexes, which may contain additional components, and function at the cell surface or extracellularly, suggests as yet unexplored functions of these enzymes. Here we review how studies of basic biological processes in the mouse models of three lysosomal storage disorders, galactosialidosis, sialidosis, and GM1-gangliosidosis, revealed new and unexpected roles for the three respective affected enzymes, Ppca, Neu1, and β-Gal, that go beyond their canonical degradative activities. These findings have broadened our perspective on their functions and may pave the way for the development of new therapies for these lysosomal storage disorders.
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.