Enolase is a crucial glycolytic enzyme involved within the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Mammalian enolase exists as three subunits: enolase-1 (α-enolase), enolase-2 (γ-enolase) and enolase-3 (β-enolase) which will form both homo- and heterodimers. Expression of the enolase isoforms differs during a tissue specific manner (1). Enolase-1 plays a key role in anaerobic metabolism under hypoxic conditions and should act as a cell surface plasminogen receptor during tissue invasion (2,3). Abnormal expression of enolase-1 is related to tumor progression in some cases of breast and carcinoma (4-7). Alternatively, an enolase-1 splice variant (MBP-1) binds the c-myc promoter p2 and should function as a tumor suppressor. For this reason enolase-1 is taken into account as a possible therapeutic target within the treatment of some sorts of cancer.
Review Article: Cancer Science & Therapy
Review Article: Cancer Science & Therapy
Editorial: Cancer Science & Therapy
Editorial: Cancer Science & Therapy
Case Report: Cancer Science & Therapy
Case Report: Cancer Science & Therapy
Research Article: Cancer Science & Therapy
Research Article: Cancer Science & Therapy
Research Article: Cancer Science & Therapy
Research Article: Cancer Science & Therapy
Posters & Accepted Abstracts: Pulmonary & Respiratory Medicine
Posters & Accepted Abstracts: Pulmonary & Respiratory Medicine
Scientific Tracks Abstracts: Cancer Science & Therapy
Scientific Tracks Abstracts: Cancer Science & Therapy
Posters & Accepted Abstracts: Journal of Physiotherapy & Physical Rehabilitation
Posters & Accepted Abstracts: Journal of Physiotherapy & Physical Rehabilitation
Posters & Accepted Abstracts: Journal of Surgery
Posters & Accepted Abstracts: Journal of Surgery
Cancer Science & Therapy received 3968 citations as per Google Scholar report
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