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Targeting Moonlighting Enzymes in Cancer.
Lin, Chunxu; Yu, Mingyang; Wu, Ximei; Wang, Hui; Wei, Min; Zhang, Luyong.
Afiliación
  • Lin C; Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, China.
  • Yu M; Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, China.
  • Wu X; Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, China.
  • Wang H; Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, China.
  • Wei M; Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, China.
  • Zhang L; Center for Drug Research and Development, Guangdong Pharmaceutical University, Guangzhou 510006, China.
Molecules ; 29(7)2024 Apr 01.
Article en En | MEDLINE | ID: mdl-38611852
ABSTRACT
Moonlighting enzymes are multifunctional proteins that perform multiple functions beyond their primary role as catalytic enzymes. Extensive research and clinical practice have demonstrated their pivotal roles in the development and progression of cancer, making them promising targets for drug development. This article delves into multiple notable moonlighting enzymes, including GSK-3, GAPDH, and ENO1, and with a particular emphasis on an enigmatic phosphatase, PTP4A3. We scrutinize their distinct roles in cancer and the mechanisms that dictate their ability to switch roles. Lastly, we discuss the potential of an innovative approach to develop drugs targeting these moonlighting enzymes target protein degradation. This strategy holds promise for effectively tackling moonlighting enzymes in the context of cancer therapy.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glucógeno Sintasa Quinasa 3 / Neoplasias Límite: Humans Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Suiza
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glucógeno Sintasa Quinasa 3 / Neoplasias Límite: Humans Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: China Pais de publicación: Suiza