引言：从差点倒闭的"小公司"到全球资本追捧的"小分子玩家" 如果把时间拨到今天，亚盛医药已经是一家"站在聚光灯下"的公司： 一边是在香港联交所主板挂牌，早在2019年就成为首批登陆港股的小分子创新药企之一； 一边是在2025年1月敲开纳斯达克的大门，拿下约1.26亿美元募资，成为 首家"先港后美"双重上市的中国生物医药企业 。 资本市场之外，2024年又与武田制药签下总金额高达13亿美元的全球合作，将核心产品耐立克的海外权益打包交给这家跨国巨头， 刷新国产小分子肿瘤 药的对外 BD 纪录 。 产品线的"现实画面"同样不逊色。 第三代BCR-ABL抑制剂耐立克已在中国获批两项适应症，2023年进入国家医保目录后加速放量，2025年上半年贡献了2.17亿元销售收入，同比大增 93%，一款单品就撑起了公司九成以上营收。 另一边，Bcl-2抑制剂利生妥也在2025年7月迎来首个上市许可，成为 中国首个国产原研Bcl-2抑制剂、全球第二个同类产品 ，被普遍视作具备Best-in- class潜力的新一代重磅品种。 但如果把时间轴向回拨20多年，故事的开头却完全不是这样。亚盛医药的前身，是2003年三位海归科学家在美国创 ...

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]