ALDOA
Gene Ontology Biological Process
- ATP biosynthetic process [IMP]
- actin filament organization [TAS]
- blood coagulation [TAS]
- carbohydrate metabolic process [TAS]
- fructose 1,6-bisphosphate metabolic process [IDA]
- fructose metabolic process [IMP]
- gluconeogenesis [TAS]
- glucose metabolic process [TAS]
- glycolytic process [IMP, TAS]
- muscle cell cellular homeostasis [IMP]
- platelet activation [TAS]
- platelet degranulation [TAS]
- protein homotetramerization [ISS]
- regulation of cell shape [IDA]
- small molecule metabolic process [TAS]
- striated muscle contraction [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ALDOA
Gene Ontology Biological Process
- ATP biosynthetic process [IMP]
- actin filament organization [TAS]
- blood coagulation [TAS]
- carbohydrate metabolic process [TAS]
- fructose 1,6-bisphosphate metabolic process [IDA]
- fructose metabolic process [IMP]
- gluconeogenesis [TAS]
- glucose metabolic process [TAS]
- glycolytic process [IMP, TAS]
- muscle cell cellular homeostasis [IMP]
- platelet activation [TAS]
- platelet degranulation [TAS]
- protein homotetramerization [ISS]
- regulation of cell shape [IDA]
- small molecule metabolic process [TAS]
- striated muscle contraction [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Cross-Linking-MS (XL-MS)
An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).
Publication
MaXLinker: Proteome-wide Cross-link Identifications with High Specificity and Sensitivity.
Protein-protein interactions play a vital role in nearly all cellular functions. Hence, understanding their interaction patterns and three-dimensional structural conformations can provide crucial insights about various biological processes and underlying molecular mechanisms for many disease phenotypes. Cross-linking mass spectrometry (XL-MS) has the unique capability to detect protein-protein interactions at a large scale along with spatial constraints between interaction partners. The ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ALDOA ALDOA | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3756153 | |
| ALDOA ALDOA | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | 2731213 | |
| ALDOA ALDOA | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | - | |
| ALDOA ALDOA | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | - |
Curated By
- BioGRID