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malfunction
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enolase 1 and calreticulin siRNA reduce the [Ca2+]i levels, amounts of total TNF-alpha, and the release of TNF-alpha and leukotrienes, all of which are increased in the bone marrow-derived mast cells activated with antigen/antibody reaction
malfunction
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the down-regulation of enolase selectively increases the susceptibility to phosphomycin
malfunction
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the down-regulation of enolase selectively increases the susceptibility to phosphomycin
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metabolism
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alpha-enolase is involved in glucose metabolism in Alzheimer's disease brain
metabolism
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enolase 1 is a glycolytic enzyme expressed in most tissues
metabolism
enolase is a key enzyme in the glycolytic pathway
metabolism
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enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
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enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
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enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
Streptomyces mutans
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enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
Streptomyces pneumoniae
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enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
-
enolase is the enzyme responsible for the reversible conversion of D-2-phosphoglycerate and phosphoenolpyruvate in glycolysis and gluconeogenesis, two metabolic pathways that are often vital for cellular function
metabolism
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in the glycolysis-related energy pathway, enolase might be involved in higher metabolic activity during the day than at night, at least in part, overview
metabolism
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in tumor cells, ENOA is upregulated and supports anaerobic proliferation, cf. Warburg effect, it is expressed at the cell surface, where it promotes cancer invasion, and is subjected to a specific array of post-translational modifications, namely acetylation, methylation and phosphorylation
metabolism
anaerobic fermentative metabolism of glycerol. Proteome analysis as well as enzyme assays performed in cell-free extracts demonstrate that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen
physiological function
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alfa-enolase is a fibronectin-binding protein
physiological function
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alpha-enolase is a glycolytic enzyme that also acts as a surface plasminogen receptor, alpha-enolase elicits a pancreatic ductal adenocarcinoma cell-specific, integrated humoral and cellular response
physiological function
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ENO-1 binds plasminogen at the cell surface, enhancing local plasmin production, overexpression of ENO-1 in U937 cells increases their migratory and matrix-penetrating capacity
physiological function
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enolase from Botrytis is cold responsive, influenced by cAMP and acts putatively as a transcriptional regulator of the zinc-C6 protein family and calpain like proteases
physiological function
enolase functions as a protective antigen displayed on the bacterial cell surface
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
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enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
physiological function
-
enolase is a multifunctional protein that participates in glycolysis and gluconeogenesis and can act as a plasminogen receptor on the cell surface
physiological function
-
enolase is involved in bacterial adhesion to host epithelial cells
physiological function
-
enolase plays a role in encystation
physiological function
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glycolytic/gluconeogenesis enzyme, eye lens tau-crystallin protein, plasminogen binding protein, c-Myc binding protein and transcription factor in tumor formationk
physiological function
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cell surface ENOA is one of the many plasminogen-binding molecules, interaction of the plasminogen lysinebinding sites with ENOA is dependent upon recognition of ENOA C-terminal lysines K420, K422 and K434, and also K256. Binding with ENOA lysyl residues leads to activation of plasminogen to plasmin by the proteolytic action of either tissue-type or urokinase-type plasminogen activators, overview. ENOA takes part, together with urokinase plasminogen activator receptor, integrins and some cytoskeletal proteins, in a multiprotein complex, called metastasome, responsible for adhesion, migration and proliferation in ovarian cancer cells
physiological function
-
enolase 1 and calreticulin are important proteins in regulating the differentiation and functions of bone marrow-derived mast cells
physiological function
enolase acts as a fibronectin binding protein in Paracoccidioides brasiliensis. Association between recombinant PbEno and plasminogen is lysine-dependent and is dependent on cell surface localization of PbENo, since purified rPbEno, in its soluble form, inhibits plasminogen binding to fixed cells, interaction analysis, overview. Exposure of epithelial cells and phagocytes to enolase is associated with an increased expression of surface sites of adhesion. In fact, the association of Paracoccidioides brasiliensis with epithelial cells and phagocytes is increased in the presence of rPbEno
physiological function
-
enolase can act as a plasminogen-binding protein
physiological function
-
enolase can act as a plasminogen-binding protein
physiological function
-
enolase can act as a plasminogen-binding protein
physiological function
-
enolase can act as a plasminogen-binding protein, an internal motif, FYDAEKKEY, is responsible for the plasminogen recognition
physiological function
Streptomyces pneumoniae
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enolase can act as a plasminogen-binding protein, an internal motif, FYDKERKVYD, is responsible for the plasminogen recognition
physiological function
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enolase is a multifunctional enzyme that is involved in the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate in glycolytic and gluconeogenesis pathways. Csenolase might play key roles in the growth of the parasites. Csenolase is an important glycolytic enzyme required for the development of Clonorchis sinensis
physiological function
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enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
physiological function
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enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
physiological function
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enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
physiological function
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enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids
physiological function
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enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids. Enolase can act as a plasminogen-binding protein, an internal motif, AYDAERKMY, is responsible for the plasminogen recognition
physiological function
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enolase plays an important role in glycolysis. It also binds RNA, overview
physiological function
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main physiological role of enolase is the reversible conversion of 2-phospho-D-glycerate and to phosphoenolpyruvate within the glycolytic pathway. Enolases play an important role in Cyclamen embryogenesis, overview
physiological function
recombinant SjENO binds to human plasminogen as its receptor
physiological function
the recombinant enolase exhibits fibronectin-binding ability in immunoblotting assay, suggesting that enolase may play a role in Brucella abortus colonization, persistence, and invasion of host tissue
physiological function
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the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
the enzyme probably functions in sugar fermentation pathway
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
enolase is a moonlighting cytoplasmic protein which also associates with the bacterial outer surface and facilitates binding to host plasminogen
physiological function
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enolase is essential for Staphylococcus aureus and involved in the process of bacterial autolysis
physiological function
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the enzyme plays a role in pathogen interaction with host molecules like plasminogen, which may contribute to the pathogenesis of leptospirosis
physiological function
the enzyme promotes infection by Xenorhabdus poinarii and Metarhizium anisopliae
physiological function
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the plasminogen-enolase association may play a critical role in the virulence of Salmonella Typhi by causing direct damage to the host cell extracellular matrix
physiological function
enzyme can bind to gen, binding is competitively inhibited by epsilon-aminocaproic acid. Plasminogen bound to Eno can be converted into active plasmin using host-derived activators
physiological function
enzyme can bind to human plasminogen and generate plasmin, activated by a tissue-type plasminogen activator. 6-Aminocaproic acid inhibits the binding of plasminogen to Eno
physiological function
enzyme interacts with human plasminogen and participates in Streptococcus iniae adhesion to and invasion of BHK-21 cells
physiological function
enzyme is involved in type I collagen binding. A strain carrying a null mutation in the EnoA1 gene, binds to immobilized collagen less efficiently than wild-type. EnoA1 binds collagen both under denaturing and native conditions. The region spanning from 73rd to the 140th amino acid residues is involved in collagen binding
physiological function
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enzyme selectively binds to calcium oxalate monohydrate crystals and interacts directly with Ca2+ and Mg2+. Calcium oxalate monohydrate and Mg2+ competitively bind to alpha-enolase
physiological function
recombinant ENO1 specifically binds to a TTTTCT DNA motif present in the cyst matrix antigen 1 gene promoter
physiological function
recombinant ENO2 specifically binds to a TTTTCT DNA motif present in the cyst matrix antigen 1 gene promoter
physiological function
recombinant enolase EnoA shows a strong plasminogen binding and activating activity in vitro
physiological function
recombinant enolase retains its enzymatic activity and binds to human plasminogen. Binding can be significantly reduced in the presence of epsilon-aminocaproic acid. Eno promotes plasminogen to plasmin conversion in the presence of plasminogen activator
physiological function
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the enzyme plays a role in pathogen interaction with host molecules like plasminogen, which may contribute to the pathogenesis of leptospirosis
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physiological function
-
enzyme is involved in type I collagen binding. A strain carrying a null mutation in the EnoA1 gene, binds to immobilized collagen less efficiently than wild-type. EnoA1 binds collagen both under denaturing and native conditions. The region spanning from 73rd to the 140th amino acid residues is involved in collagen binding
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physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
-
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
-
physiological function
-
enolase acts as a fibronectin binding protein in Paracoccidioides brasiliensis. Association between recombinant PbEno and plasminogen is lysine-dependent and is dependent on cell surface localization of PbENo, since purified rPbEno, in its soluble form, inhibits plasminogen binding to fixed cells, interaction analysis, overview. Exposure of epithelial cells and phagocytes to enolase is associated with an increased expression of surface sites of adhesion. In fact, the association of Paracoccidioides brasiliensis with epithelial cells and phagocytes is increased in the presence of rPbEno
-
physiological function
-
enolase is a conserved putative human plasminogen receptor in Bifidobacterium
-
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
physiological function
-
the enzyme promotes infection by Xenorhabdus poinarii and Metarhizium anisopliae
-
physiological function
-
enolase plays a role in encystation
-
physiological function
-
alfa-enolase is a fibronectin-binding protein
-
physiological function
-
the recombinant enolase exhibits fibronectin-binding ability in immunoblotting assay, suggesting that enolase may play a role in Brucella abortus colonization, persistence, and invasion of host tissue
-
physiological function
-
recombinant enolase retains its enzymatic activity and binds to human plasminogen. Binding can be significantly reduced in the presence of epsilon-aminocaproic acid. Eno promotes plasminogen to plasmin conversion in the presence of plasminogen activator
-
physiological function
-
enolase is a moonlighting cytoplasmic protein which also associates with the bacterial outer surface and facilitates binding to host plasminogen
-
physiological function
-
enolase is essential for Staphylococcus aureus and involved in the process of bacterial autolysis
-
physiological function
-
enolase functions as a protective antigen displayed on the bacterial cell surface
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additional information
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circadian rhythm of enolase in suprachiasmatic nucleus depends on mitochondrial function. Enolase activity, coupled with lactate dehydrogenase, is higher during the light period than that in the dark. However, enolase mRNA, analyzed by RT-PCR, shows higher levels during the dark period than in the light
additional information
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overexpression of ENOA is associated with tumor development through a process known as aerobic glycolysis or the Warburg effect. ENOA induces autoantibody production and induces a specific immune response in tumors, overview
additional information
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proteomic analysis and peptide mapping, 2D isoelectric focusing and mass spectrometry, overview
additional information
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proteomic analysis, peptide mapping, 2D isoelectric focusing, overview
additional information
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the human muscle-specific enolase is less susceptible to inactivation by reactive aldehydes than the pig enzyme
additional information
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the human muscle-specific enolase is less susceptible to inactivation by reactive aldehydes than the pig enzyme
additional information
the recombinant enolase is recognized by rabbit sera directed against an antigen preparation from adult worms. 24.28% reduction in the liver egg count and a reduction of 21.45% in the fecal egg count occur in BALB/c mice vaccinated with recombinant SjENO compared with control mice
additional information
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the recombinant enolase is recognized by rabbit sera directed against an antigen preparation from adult worms. 24.28% reduction in the liver egg count and a reduction of 21.45% in the fecal egg count occur in BALB/c mice vaccinated with recombinant SjENO compared with control mice