Core Insights - A key gene mutation in the human immune protein Fas ligand (FasL) may increase cancer susceptibility in humans compared to close relatives like chimpanzees, providing important clues for developing new cancer therapies [1][2] Group 1: Research Findings - The study published in Nature Communications highlights that elevated levels of plasmin, a protease, in the tumor microenvironment act like "molecular scissors" that cut mutated FasL, leading to a loss of its anti-cancer function [1] - This unique vulnerability in humans explains why immunotherapies like CAR-T are effective against blood cancers but struggle with solid tumors such as triple-negative breast cancer, as blood cancer cells do not rely on plasmin for dissemination [1] Group 2: Implications for Treatment - The mutation in FasL may have contributed to increased brain capacity in humans but also poses a risk for higher cancer susceptibility, suggesting a potential "key" to unlocking immunotherapy [2] - Blocking plasmin or protecting FasL could reactivate the immune system's anti-cancer capabilities, offering new strategies for treating challenging cancers like triple-negative breast cancer through the combined use of plasmin inhibitors and existing therapies [2]

Core Viewpoint - The research conducted by the team led by Academician Shi Yigong reveals the structural basis of BAX pore formation, which is crucial for understanding mitochondrial outer membrane permeability during apoptosis [2][3]. Group 1: Research Findings - The study elucidates the assembly principles of various BAX oligomers, providing a structural foundation for BAX-mediated mitochondrial outer membrane permeability [3]. - The research team purified recombinant human BAX protein and confirmed its membrane permeability activity through cytochrome c release experiments based on liposomes [5]. - The activated BAX oligomers were extracted and purified from overexpressed BAX protein in human embryonic kidney 293F cells for cryo-electron microscopy analysis [6]. Group 2: Structural Insights - The study identified that the dimer of BAX is the basic repeating structural unit of its various oligomeric forms (arc, line, and ring) [7]. - The structure of the BAX repeating unit revealed interactions within and between dimers, with the α9 helix facilitating end-to-end stacking to form linear, arc, polygonal, and ring shapes [7]. - Structural characterization was performed on quadrilateral, pentagonal, hexagonal, and heptagonal forms composed of 16, 20, 24, and 28 BAX monomers, respectively [7]. Group 3: Implications of Findings - The results clarify how activated BAX oligomers permeabilize (or rupture) the mitochondrial outer membrane and explain how different shapes (arc, line, and ring) are assembled from the same repeating unit [9].

Core Insights - Scientists from Walter and Eliza Hall Institute in Australia have discovered a small molecule that can selectively inhibit apoptosis, which opens new avenues for treating neurodegenerative diseases such as Parkinson's and Alzheimer's [1] Group 1 - The research findings were published in the latest issue of the journal "Science Advances" [1]