Nature Chemical Biology Nature Chemical Biology is an interdisciplinary journal that publishes the most innovative and important research advances at the interface of chemistry and biology. The journal publishes research from chemists who are applying the principles, language and tools of chemistry to biological systems and from biologists who are interested in understanding biological processes at the molecular level. The scope of the journal covers all areas of contemporary research at the interface of chemistry and biology. http://feeds.nature.com/nchembio/rss/current Nature Publishing Group en © 2025 Macmillan Publishers Limited, part of Springer Nature. All rights reserved. Nature Chemical Biology © 2025 Macmillan Publishers Limited, part of Springer Nature. All rights reserved. [email protected]
  • Nature Chemical Biology https://www.nature.com/uploads/product/nchembio/rss.png http://feeds.nature.com/nchembio/rss/current https://www.nature.com/articles/s41589-025-01981-6 Nature Chemical Biology, Published online: 01 August 2025; doi:10.1038/s41589-025-01981-6Cryo-electron microscopy and biochemical reconstitution analysis reveals that Nde1 enhances Lis1 binding to autoinhibited dynein, promoting formation of a Phi-like–Lis1 intermediate during dynein activation.]]> Jun YangYuanchang ZhaoPengxin ChaiAhmet YildizKai Zhang doi:10.1038/s41589-025-01981-6 Nature Chemical Biology, Published online: 2025-08-01; | doi:10.1038/s41589-025-01981-6 2025-08-01 Nature Chemical Biology 10.1038/s41589-025-01981-6 https://www.nature.com/articles/s41589-025-01981-6 https://www.nature.com/articles/s41589-025-01973-6 Nature Chemical Biology, Published online: 01 August 2025; doi:10.1038/s41589-025-01973-6LaccID, an engineered laccase, enables hydrogen-peroxide-free proximity labeling and electron microscopy (EM) in mammalian cells. Notably, LaccID is selectively active at the cell surface, enabling the mapping of the dynamic T cell–tumor surfaceome and its use as a genetically encodable EM tag, expanding the toolkit for cell-based imaging and proteomics.]]> Song-Yi LeeHeegwang RohDavid Gonzalez-PerezMason R. MackeyDaniel HocesColleen N. McLaughlinChang LinStephen R. AdamsKhanh NguyenKeun-Young KimDavid J. LuginbuhlLiqun LuoNamrata D. UdeshiSteven A. CarrRogelio A. Hernández-LópezMark H. EllismanMiguel AlcaldeAlice Y. Ting doi:10.1038/s41589-025-01973-6 Nature Chemical Biology, Published online: 2025-08-01; | doi:10.1038/s41589-025-01973-6 2025-08-01 Nature Chemical Biology 10.1038/s41589-025-01973-6 https://www.nature.com/articles/s41589-025-01973-6 https://www.nature.com/articles/s41589-025-01971-8 Nature Chemical Biology, Published online: 31 July 2025; doi:10.1038/s41589-025-01971-8Structural studies of certain Tn and STn antigen-targeting antibodies reveal that their VH and VL domains recognize the glycan antigen and the adjacent peptide region, respectively, enabling a VH domain-focused and VL domain-varying phage display library to generate antibodies targeting diverse glycopeptide epitopes.]]> Ramon Hurtado-GuerreroSpyridon GatosIrene Ginés-AlcoberJavier Macías-LeónAndrés Manuel González-RamírezIlknur KasapogluBilly VelozIsmael CompañónMattia GhirardelloPedro MerinoFrancisco CorzanaOla Blixt doi:10.1038/s41589-025-01971-8 Nature Chemical Biology, Published online: 2025-07-31; | doi:10.1038/s41589-025-01971-8 2025-07-31 Nature Chemical Biology 10.1038/s41589-025-01971-8 https://www.nature.com/articles/s41589-025-01971-8 https://www.nature.com/articles/s41589-025-01961-w Nature Chemical Biology, Published online: 31 July 2025; doi:10.1038/s41589-025-01961-wA noncanonical pathway of DELLA regulation by a conserved inositol pyrophosphate synthase was identified in the liverwort, Marchantia polymorpha, that lacks the canonical gibberellin-induced DELLA degradation module found in angiosperms.]]> Priyanshi RanaAnjana Edathil KadangodanPaulami KoleyRiya GhoshNaga Jyothi PullagurlaHemant Chandru NaikPadmabati MondalSrimonta GayenDebabrata Laha doi:10.1038/s41589-025-01961-w Nature Chemical Biology, Published online: 2025-07-31; | doi:10.1038/s41589-025-01961-w 2025-07-31 Nature Chemical Biology 10.1038/s41589-025-01961-w https://www.nature.com/articles/s41589-025-01961-w https://www.nature.com/articles/s41589-025-01979-0 Nature Chemical Biology, Published online: 25 July 2025; doi:10.1038/s41589-025-01979-0The discovery of lipoamide offers a unique approach to modulate stress granule dynamics. It will advance studies of stress granule biology and inform the therapeutic modification of these biomolecular condensates as a potential treatment option for amyotrophic lateral sclerosis.]]> Alicia DubinskiChristine Vande Velde doi:10.1038/s41589-025-01979-0 Nature Chemical Biology, Published online: 2025-07-25; | doi:10.1038/s41589-025-01979-0 2025-07-25 Nature Chemical Biology 10.1038/s41589-025-01979-0 https://www.nature.com/articles/s41589-025-01979-0 https://www.nature.com/articles/s41589-025-01966-5 Nature Chemical Biology, Published online: 23 July 2025; doi:10.1038/s41589-025-01966-5The primary entry route of vanilloid ligands to the vanilloid-binding site in transient receptor potential vanilloid 1 (TRPV1) is found to be a distinct and targetable hydrophobic pathway at the TRPV1–cell membrane interface rather than through direct membrane penetration.]]> Meng-Yang SunYu-Jing BianXiao-Ying ChenXue ZhangMing LiBo-Ying ZhouYang YangYi-Zhe HuangRui YangYu-Hao GaoWen-Wen CuiYa-Qi WangSi-Jia ZhuPeng CaoChang-Zhu LiMichael X. ZhuYun-Tao LeiFan YangYe Yu doi:10.1038/s41589-025-01966-5 Nature Chemical Biology, Published online: 2025-07-23; | doi:10.1038/s41589-025-01966-5 2025-07-23 Nature Chemical Biology 10.1038/s41589-025-01966-5 https://www.nature.com/articles/s41589-025-01966-5 https://www.nature.com/articles/s41589-025-02001-3 Nature Chemical Biology, Published online: 21 July 2025; doi:10.1038/s41589-025-02001-3Publisher Correction: Nonheme Fe 1,3-nitrogen migratases for asymmetric noncanonical amino acid synthesis]]> Liu-Peng ZhaoHuichong LiuBinh Khanh MaiYu ZhangLida ChengPeng LiuYang Yang doi:10.1038/s41589-025-02001-3 Nature Chemical Biology, Published online: 2025-07-21; | doi:10.1038/s41589-025-02001-3 2025-07-21 Nature Chemical Biology 10.1038/s41589-025-02001-3 https://www.nature.com/articles/s41589-025-02001-3 https://www.nature.com/articles/s41589-025-01988-z Nature Chemical Biology, Published online: 17 July 2025; doi:10.1038/s41589-025-01988-zAuxin branches out]]> Grant Miura doi:10.1038/s41589-025-01988-z Nature Chemical Biology, Published online: 2025-07-17; | doi:10.1038/s41589-025-01988-z 2025-07-17 Nature Chemical Biology 10.1038/s41589-025-01988-z https://www.nature.com/articles/s41589-025-01988-z