Posts

Showing posts with the label EGCG,cancer cells,molecular mechanisms ,p53,tumor suppressor,MDM2, ubiquitination, anti-tumor activity, polyphenolic compounds,tumor suppressor,anti-aging effects,DNA damage

Daily Consumption of These Two Beverages Might Really Lower Cancer Risk: Research Data Reveals the Answer

Image
  In the hustle and bustle of daily life, a cup of tea or coffee has become an indispensable ritual for many. Some drink tea for its refreshing qualities, while others rely on coffee for a mental boost. But have you ever considered that these seemingly ordinary beverages might also have a connection to “cancer prevention”? The latest research presents a surprising finding: consistently drinking a moderate amount of sugar-free tea or coffee daily might not only boost your health but also reduce the risk of cancer. New Research Unveils: 2 Cups of Sugar-Free Tea or Coffee Significantly Reduce Risks In March 2024, a large epidemiological study by Harbin Medical University was published in “The Journal of Nutrition,” involving over 180,000 participants and spanning 8.8 years. The study focused on the relationship between daily beverage choices and cancer incidence and mortality rates. The results were clear: Drinking 2 cups of sugar-free coffee daily reduced overall cancer incidence by ...

New study finds that EGCG in green tea can inhibit cancer cell growth by interacting with the N-terminal domain of p53.

Image
  The major polyphenolic compound in  green tea , epigallocatechin-3-gallate (EGCG), has been shown to induce apoptosis in cancer cells, but its  molecular mechanism  is not fully understood. Recently, a team led by  Chunyu Wang  at Rensselaer Polytechnic Institute (with  China Agricultural University  as the first affiliation and Jing Zhao as the first author of the paper) published a research paper in  Nature Communications  titled "EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction". Using SPR and  NMR techniques , the study found that EGCG directly interacts with the  tumor suppressor p53 , with the intrinsically disordered N-terminal domain (NTD) identified as the main binding site. Large-scale atomic simulations, SAXS and AUC results showed that the EGCG-NTD interaction is dynamic, and EGCG leads to the appearance of a subset of compact bound conformations. The EGCG-p53 interact...