ArticleBioMed research international2018
Biochemical and Biophysical Characterization of the Enolase from
Article in BioMed research international, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 13 citations in OpenAlex.
- Parasites and allergies: a complex bidirectional relationship from evolutionary origins to modern therapeutics.Antonie van Leeuwenhoek · 2026Review
- Multifunctional roles of γ-enolase in the central nervous system: more than a neuronal marker.Cell & bioscience · 2024Review
- An alternative vaccine target for bovine Anaplasmosis based on enolase, a moonlighting protein.Frontiers in veterinary science · 2023Article
- The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding.Acta crystallographica. Section F, Structural biology communications · 2022Article
- ENO1 and Cancer.Molecular therapy oncolytics · 2022Review
- Cloning and Characterization of Immunological Properties ofJournal of immunology research · 2021Article
- Proteomics-based analysis indicating α-enolase as a potential biomarker in primary Sjögren's syndrome.Gland surgery · 2020Article
- Structural Insights into the Interactions of Candidal Enolase with Human Vitronectin, Fibronectin and Plasminogen.International journal of molecular sciences · 2020Article
- Discovery of a Vertebrate-Specific Factor that Processes Flagellar Glycolytic Enolase during Motile Ciliogenesis.iScience · 2020Article
- The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli.Scientific reports · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enolase, which catalyses the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate, is an important enzyme in the classic glycolysis pathway in cells. Enolase is highly conserved in organisms from bacteria to humans, indicating its importance in cells. Thus, enolase is a good target for developing new drugs. In the last decade, new functions of this enzyme have been found.
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.