Publication:
Therapeutic targeting of cancer metabolism with triosephosphate isomerase

dc.contributor.buuauthorPekel, Gonca
dc.contributor.buuauthorArı, Ferda
dc.contributor.departmentFen Edebiyat Fakültesi
dc.contributor.departmentBiyoloji Bölümü
dc.contributor.orcid0000-0002-6729-7908
dc.contributor.orcid0000-0003-2567-8056
dc.contributor.scopusid57216587784
dc.contributor.scopusid24376085300
dc.date.accessioned2023-01-23T05:56:23Z
dc.date.available2023-01-23T05:56:23Z
dc.date.issued2020-03-16
dc.description.abstractThe 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.
dc.identifier.citationPekel, G. ve Arı, F. (2020). "Therapeutic targeting of cancer metabolism with triosephosphate isomerase". Chemistry & Biodeversity, 17(5).
dc.identifier.issn1612-1872
dc.identifier.issn1612-1880
dc.identifier.issue5
dc.identifier.pubmed32180338
dc.identifier.scopus2-s2.0-85083970461
dc.identifier.urihttps://doi.org/10.1002/cbdv.202000012
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/10.1002/cbdv.202000012
dc.identifier.urihttp://hdl.handle.net/11452/30579
dc.identifier.volume17
dc.identifier.wos000528935400001
dc.indexed.scopusScopus
dc.indexed.wosSCIE
dc.language.isoen
dc.publisherWiley
dc.relation.journalChemistry & Biodiversity
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectBiochemistry & molecular biology
dc.subjectChemistry
dc.subjectCancer
dc.subjectTriosephosphate isomerase
dc.subjectMetabolism
dc.subjectWarburg effect
dc.subjectCrystal-structure
dc.subjectBreast-cancer
dc.subjectDifferential expression
dc.subjectProteomic analysis
dc.subjectEnzyme catalysis
dc.subjectCell carcinoma
dc.subjectIdentification
dc.subjectProteins
dc.subjectGenes
dc.subjectGlycolysis
dc.subject.emtreeFatty acid
dc.subject.emtreeGlycolytic enzyme
dc.subject.emtreeTriosephosphate isomerase
dc.subject.emtreeTumor marker
dc.subject.emtreeAntineoplastic agent
dc.subject.emtreeEnzyme inhibitor
dc.subject.emtreeTriosephosphate isomerase
dc.subject.emtreeAerobic glycolysis
dc.subject.emtreeCarcinogenesis
dc.subject.emtreeEnzyme inhibition
dc.subject.emtreeFatty acid synthesis
dc.subject.emtreeGluconeogenesis
dc.subject.emtreeHuman
dc.subject.emtreeMalignant neoplasm
dc.subject.emtreeMetabolism
dc.subject.emtreeMetastasis
dc.subject.emtreeNonhuman
dc.subject.emtreePentose phosphate cycle
dc.subject.emtreePhenotype
dc.subject.emtreeReview
dc.subject.emtreeAnimal
dc.subject.emtreeChemical structure
dc.subject.emtreeChemistry
dc.subject.emtreeMetabolism
dc.subject.emtreeMolecular model
dc.subject.emtreeNeoplasm
dc.subject.emtreePathology
dc.subject.meshAnimals
dc.subject.meshAntineoplastic agents
dc.subject.meshEnzyme inhibitors
dc.subject.meshHumans
dc.subject.meshModels, molecular
dc.subject.meshMolecular structure
dc.subject.meshNeoplasms
dc.subject.meshTriose-phosphate isomerase
dc.subject.scopusPyruvate Kinase Deficiency of Red Cells; Triose-Phosphate Isomerase; Hereditary Hemolytic Anemia
dc.subject.wosBiochemistry & molecular biology
dc.subject.wosChemistry, multidisciplinary
dc.titleTherapeutic targeting of cancer metabolism with triosephosphate isomerase
dc.typeReview
dc.wos.quartileQ3 (Chemistry, multidisciplinary)
dc.wos.quartileQ4
dc.wos.quartileQ3
dc.wos.quartileQ4
dspace.entity.typePublication
local.contributor.departmentFen Edebiyat Fakültesi/Biyoloji Bölümü
local.indexed.atPubMed
local.indexed.atWOS
local.indexed.atScopus

Files

License bundle

Now showing 1 - 1 of 1
Placeholder
Name:
license.txt
Size:
1.71 KB
Format:
Item-specific license agreed upon to submission
Description: