Therapeutic targeting of cancer metabolism with triosephosphate isomerase
dc.contributor.buuauthor | Pekel, Gonca | |
dc.contributor.buuauthor | Arı, Ferda | |
dc.contributor.department | Bursa Uludağ Üniversitesi/Fen-Edebiyat Fakültesi/Biyoloji Bölümü. | tr_TR |
dc.contributor.orcid | 0000-0002-6729-7908 | tr_TR |
dc.contributor.orcid | 0000-0003-2567-8056 | tr_TR |
dc.contributor.scopusid | 57216587784 | tr_TR |
dc.contributor.scopusid | 24376085300 | tr_TR |
dc.date.accessioned | 2023-01-23T05:56:23Z | |
dc.date.available | 2023-01-23T05:56:23Z | |
dc.date.issued | 2020-03-16 | |
dc.description.abstract | The increase in glycolytic flux in cancer, known as aerobic glycolysis, is one of the most important hallmarks of cancer. Therefore, glycolytic enzymes have importance in understanding the molecular mechanism of cancer progression. Triosephosphate isomerase (TPI) is one of the key glycolytic enzymes. Furthermore, it takes a part in gluconeogenesis, pentose phosphate pathway and fatty acid biosynthesis. To date, it has been shown altered levels of TPI in various cancer types, especially in metastatic phenotype. According to other studies, TPI might be considered as a potential therapeutic target and a cancer-related biomarker in different types of cancer. However, its function in tumor formation and development has not been fully understood. Here, we reviewed the relationship between TPI and cancer for the first time. | en_US |
dc.identifier.citation | Pekel, G. ve Arı, F. (2020). "Therapeutic targeting of cancer metabolism with triosephosphate isomerase". Chemistry & Biodeversity, 17(5). | en_US |
dc.identifier.issn | 1612-1872 | |
dc.identifier.issn | 1612-1880 | |
dc.identifier.issue | 5 | tr_TR |
dc.identifier.pubmed | 32180338 | tr_TR |
dc.identifier.scopus | 2-s2.0-85083970461 | tr_TR |
dc.identifier.uri | https://doi.org/10.1002/cbdv.202000012 | |
dc.identifier.uri | https://onlinelibrary.wiley.com/doi/10.1002/cbdv.202000012 | |
dc.identifier.uri | http://hdl.handle.net/11452/30579 | |
dc.identifier.volume | 17 | tr_TR |
dc.identifier.wos | 000528935400001 | |
dc.indexed.pubmed | PubMed | en_US |
dc.indexed.scopus | Scopus | en_US |
dc.indexed.wos | SCIE | en_US |
dc.language.iso | en | en_US |
dc.publisher | Wiley | tr_TR |
dc.relation.journal | Chemistry & Biodiversity | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi | tr_TR |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Biochemistry & molecular biology | en_US |
dc.subject | Chemistry | en_US |
dc.subject | Cancer | en_US |
dc.subject | Triosephosphate isomerase | en_US |
dc.subject | Metabolism | en_US |
dc.subject | Warburg effect | en_US |
dc.subject | Crystal-structure | en_US |
dc.subject | Breast-cancer | en_US |
dc.subject | Differential expression | en_US |
dc.subject | Proteomic analysis | en_US |
dc.subject | Enzyme catalysis | en_US |
dc.subject | Cell carcinoma | en_US |
dc.subject | Identification | en_US |
dc.subject | Proteins | en_US |
dc.subject | Genes | en_US |
dc.subject | Glycolysis | en_US |
dc.subject.emtree | Fatty acid | en_US |
dc.subject.emtree | Glycolytic enzyme | en_US |
dc.subject.emtree | Triosephosphate isomerase | en_US |
dc.subject.emtree | Tumor marker | en_US |
dc.subject.emtree | Antineoplastic agent | en_US |
dc.subject.emtree | Enzyme inhibitor | en_US |
dc.subject.emtree | Triosephosphate isomerase | en_US |
dc.subject.emtree | Aerobic glycolysis | en_US |
dc.subject.emtree | Carcinogenesis | en_US |
dc.subject.emtree | Enzyme inhibition | en_US |
dc.subject.emtree | Fatty acid synthesis | en_US |
dc.subject.emtree | Gluconeogenesis | en_US |
dc.subject.emtree | Human | en_US |
dc.subject.emtree | Malignant neoplasm | en_US |
dc.subject.emtree | Metabolism | en_US |
dc.subject.emtree | Metastasis | en_US |
dc.subject.emtree | Nonhuman | en_US |
dc.subject.emtree | Pentose phosphate cycle | en_US |
dc.subject.emtree | Phenotype | en_US |
dc.subject.emtree | Review | en_US |
dc.subject.emtree | Animal | en_US |
dc.subject.emtree | Chemical structure | en_US |
dc.subject.emtree | Chemistry | en_US |
dc.subject.emtree | Metabolism | en_US |
dc.subject.emtree | Molecular model | en_US |
dc.subject.emtree | Neoplasm | en_US |
dc.subject.emtree | Pathology | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Antineoplastic agents | en_US |
dc.subject.mesh | Enzyme inhibitors | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Models, molecular | en_US |
dc.subject.mesh | Molecular structure | en_US |
dc.subject.mesh | Neoplasms | en_US |
dc.subject.mesh | Triose-phosphate isomerase | en_US |
dc.subject.scopus | Pyruvate Kinase Deficiency of Red Cells; Triose-Phosphate Isomerase; Hereditary Hemolytic Anemia | en_US |
dc.subject.wos | Biochemistry & molecular biology | en_US |
dc.subject.wos | Chemistry, multidisciplinary | en_US |
dc.title | Therapeutic targeting of cancer metabolism with triosephosphate isomerase | en_US |
dc.type | Review | |
dc.wos.quartile | Q3 (Chemistry, multidisciplinary) | en_US |
dc.wos.quartile | Q4 | en_US |
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