ReviewJournal of biomedicine & biotechnology2012
α-Enolase, a multifunctional protein: its role on pathophysiological situations.
Review in Journal of biomedicine & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 215 papers, 2 of them syntheses that pooled it.
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.
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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.
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Who cites it
215 citing papers in PubMed, 2 syntheses or guidelines pooled it, 370 citations in OpenAlex.
- Identification ofVirulence · 2021Pooled it
- Biomarkers of systemic lupus erythematosus identified using mass spectrometry-based proteomics: a systematic review.Journal of cellular and molecular medicine · 2017Pooled it
- Giardiavirus rewires host translation and glycolytic metabolism to support its replication inVirulence · 2026Article
- Enolase-1 and Inflammation.Biomolecules · 2026Review
- ENO1 as an Immunoregulatory Hub in Cancer: Mechanisms and Translational Implications.Biomolecules · 2026Review
- Profile of lysine acetylation in Eimeria tenella and its potential implications for anticoccidial research.Parasites & vectors · 2026Article
- Heterodera schachtii enolase does not elicit canonical immune responses in Arabidopsis thaliana.Scientific reports · 2026Article
- Extracellular Enolase-1 Promotes CAF-Associated Stromal Reprogramming via the Plasmin/TGF-β Axis in Multiple Myeloma.Cancers · 2026Article
- Protein NS4A of ZIKV Inhibits Glycolytic Flux by Targeting Enolase-1.Current issues in molecular biology · 2026Article
- RESCUE: recovery of unattributed expression patterns in spatial transcriptomics.Nature communications · 2026Article
- ENO1 inhibition synergizes with chidamide to induce ferroptosis in PTCL-NOS through metabolic remodeling.Blood science (Baltimore, Md.) · 2026Article
- Article
- Systematic genomic Mendelian randomization profiling of early molecular markers of optic atrophy.International journal of ophthalmology · 2026Article
- NELL-1: role and mechanisms in disease pathogenesis and development.Frontiers in cell and developmental biology · 2026Review
- ENO1-mediated deoxycytidine synthesis and gemcitabine resistance by stabilizing RRM2 in pancreatic cancer.Cell death & disease · 2025Article
- Chios Mastic Gum Extract Enhances Antioxidant Defense in Zebrafish.International journal of molecular sciences · 2025Article
- SENP1 drives glycolysis and cisplatin resistance in gastric cancer via desumoylating ENO1.Journal of experimental & clinical cancer research : CR · 2025Article
- Proteomics of arterial thrombi in acute limb ischemia.Journal of thrombosis and thrombolysis · 2025Article
- Elucidating the Role and Mechanism of Alpha-Enolase in Senescent Amelioration via Metabolic Reprogramming.Cell proliferation · 2025Article
- Article
155 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
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Enolase is a key glycolytic enzyme in the cytoplasm of prokaryotic and eukaryotic cells and is considered a multifunctional protein. α-enolase is expressed on the surface of several cell types, where it acts as a plasminogen receptor, concentrating proteolytic plasmin activity on the cell surface. In addition to glycolytic enzyme and plasminogen receptor functions, α-Enolase appears to have other cellular functions and subcellular localizations that are distinct from its well-established function in glycolysis. Furthermore, differential expression of α-enolase has been related to several pathologies, such as cancer, Alzheimer's disease, and rheumatoid arthritis, among others. We have identified α-enolase as a plasminogen receptor in several cell types. In particular, we have analyzed its role in myogenesis, as an example of extracellular remodelling process. We have shown that α-enolase is expressed on the cell surface of differentiating myocytes, and that inhibitors of α-enolase/plasminogen binding block myogenic fusion in vitro and skeletal muscle regeneration in mice. α-Enolase could be considered as a marker of pathological stress in a high number of diseases, performing several of its multiple functions, mainly as plasminogen receptor. This paper is focused on the multiple roles of the α-enolase/plasminogen axis, related to several pathologies.
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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.