Pub Date : 2025-10-15DOI: 10.1038/s41594-025-01648-9
Hugo Sepulveda
Doing science in Latin America can be as exciting as it is challenging. Starting my laboratory for transcription and epigenetics in Chile after working in the USA has required deep conviction and constant effort. It is a long-term project aimed at creating new opportunities for the next generation of Chilean scientists, offering Latin American perspectives to contribute to science.
{"title":"Returning home: building a scientific future in Chile","authors":"Hugo Sepulveda","doi":"10.1038/s41594-025-01648-9","DOIUrl":"10.1038/s41594-025-01648-9","url":null,"abstract":"Doing science in Latin America can be as exciting as it is challenging. Starting my laboratory for transcription and epigenetics in Chile after working in the USA has required deep conviction and constant effort. It is a long-term project aimed at creating new opportunities for the next generation of Chilean scientists, offering Latin American perspectives to contribute to science.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 10","pages":"1846-1846"},"PeriodicalIF":10.1,"publicationDate":"2025-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145290299","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-10-15DOI: 10.1038/s41594-025-01694-3
We are delighted to introduce additional content types at Nature Structural & Molecular Biology, which allow us to offer more discussion of societal and scientific issues, better represent the unique perspectives of our readers, showcase their stories, and amplify their voices.
{"title":"Voices of NSMB","authors":"","doi":"10.1038/s41594-025-01694-3","DOIUrl":"10.1038/s41594-025-01694-3","url":null,"abstract":"We are delighted to introduce additional content types at Nature Structural & Molecular Biology, which allow us to offer more discussion of societal and scientific issues, better represent the unique perspectives of our readers, showcase their stories, and amplify their voices.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 10","pages":"1841-1841"},"PeriodicalIF":10.1,"publicationDate":"2025-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41594-025-01694-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145290285","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-10-14DOI: 10.1038/s41594-025-01677-4
Yan Li, David W. Adams, Hon Wing Liu, Steven J. Shaw, Emiko Uchikawa, Milena Jaskólska, Sandrine Stutzmann, Laurie Righi, Mark D. Szczelkun, Melanie Blokesch, Stephan Gruber
Lamassu is a diverse family of defense systems that protect bacteria, including seventh-pandemic strains of Vibrio cholerae, against both plasmids and phage infection. During phage infection, Lamassu targets essential cellular processes, thereby halting phage propagation by terminating the infected host. The mechanisms by which Lamassu effectors are activated when needed and otherwise suppressed are unknown. Here we present structures of a Lamassu defense system from Salmonella enterica. We show that an oligomerization domain of the nuclease effector subunit, LmuA, is sequestered by two tightly folded SMC-like LmuB protomers and LmuC. Upon activation, liberated LmuA assembles into homotetramers, in which two of four nuclease domains are brought into proximity to create an active site capable of cleaving DNA. We propose that tetramer formation is likely a one-way switch that establishes a threshold to limit potential spontaneous activation and cell death. Our findings reveal a mechanism of cellular defense, involving liberation and oligomerization of immune effectors, and shed light on how Lamassu systems balance potent immune responses with self-preservation. Li et al. show that a Lamassu defense system protects bacteria from phage infection by activating a lethal tetrameric DNA-cutting enzyme. In the absence of phages, a protein clamp holds the enzyme as an inactive monomer, preventing self-damage.
{"title":"Structure and activation mechanism of a Lamassu phage and plasmid defense system","authors":"Yan Li, David W. Adams, Hon Wing Liu, Steven J. Shaw, Emiko Uchikawa, Milena Jaskólska, Sandrine Stutzmann, Laurie Righi, Mark D. Szczelkun, Melanie Blokesch, Stephan Gruber","doi":"10.1038/s41594-025-01677-4","DOIUrl":"10.1038/s41594-025-01677-4","url":null,"abstract":"Lamassu is a diverse family of defense systems that protect bacteria, including seventh-pandemic strains of Vibrio cholerae, against both plasmids and phage infection. During phage infection, Lamassu targets essential cellular processes, thereby halting phage propagation by terminating the infected host. The mechanisms by which Lamassu effectors are activated when needed and otherwise suppressed are unknown. Here we present structures of a Lamassu defense system from Salmonella enterica. We show that an oligomerization domain of the nuclease effector subunit, LmuA, is sequestered by two tightly folded SMC-like LmuB protomers and LmuC. Upon activation, liberated LmuA assembles into homotetramers, in which two of four nuclease domains are brought into proximity to create an active site capable of cleaving DNA. We propose that tetramer formation is likely a one-way switch that establishes a threshold to limit potential spontaneous activation and cell death. Our findings reveal a mechanism of cellular defense, involving liberation and oligomerization of immune effectors, and shed light on how Lamassu systems balance potent immune responses with self-preservation. Li et al. show that a Lamassu defense system protects bacteria from phage infection by activating a lethal tetrameric DNA-cutting enzyme. In the absence of phages, a protein clamp holds the enzyme as an inactive monomer, preventing self-damage.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 12","pages":"2503-2516"},"PeriodicalIF":10.1,"publicationDate":"2025-10-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145292993","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-10-10DOI: 10.1038/s41594-025-01649-8
David Moi, Charles Bernard, Martin Steinegger, Yannis Nevers, Mauricio Langleib, Christophe Dessimoz
Recent advances in artificial-intelligence-based protein structure modeling have yielded remarkable progress in predicting protein structures. Because structures are constrained by their biological function, their geometry tends to evolve more slowly than the underlying amino acids sequences. This feature of structures could in principle be used to reconstruct phylogenetic trees over longer evolutionary timescales than sequence-based approaches; however, until now, a reliable structure-based tree-building method has been elusive. Here, we introduce a rigorous framework for empirical tree accuracy evaluation and tested multiple approaches using sequence and structure information. The best results were obtained by inferring trees from sequences aligned using a local structural alphabet—an approach robust to conformational changes that confound traditional structural distance measures. We illustrate the power of structure-informed phylogenetics by deciphering the evolutionary diversification of a particularly challenging family: the fast-evolving RRNPPA quorum-sensing receptors. We were able to propose a more parsimonious evolutionary history for this critical protein family that enables gram-positive bacteria, plasmids and bacteriophages to communicate and coordinate key behaviors. The advent of high-accuracy structural phylogenetics enables a myriad of applications across biology, such as uncovering deeper evolutionary relationships, elucidating unknown protein functions or refining the design of bioengineered molecules. Using a new method called FoldTree, the authors compare proteins on the basis of their shape to construct more accurate family trees over long evolutionary timescales and capture distant relationships where sequence information becomes less reliable.
{"title":"Structural phylogenetics unravels the evolutionary diversification of communication systems in gram-positive bacteria and their viruses","authors":"David Moi, Charles Bernard, Martin Steinegger, Yannis Nevers, Mauricio Langleib, Christophe Dessimoz","doi":"10.1038/s41594-025-01649-8","DOIUrl":"10.1038/s41594-025-01649-8","url":null,"abstract":"Recent advances in artificial-intelligence-based protein structure modeling have yielded remarkable progress in predicting protein structures. Because structures are constrained by their biological function, their geometry tends to evolve more slowly than the underlying amino acids sequences. This feature of structures could in principle be used to reconstruct phylogenetic trees over longer evolutionary timescales than sequence-based approaches; however, until now, a reliable structure-based tree-building method has been elusive. Here, we introduce a rigorous framework for empirical tree accuracy evaluation and tested multiple approaches using sequence and structure information. The best results were obtained by inferring trees from sequences aligned using a local structural alphabet—an approach robust to conformational changes that confound traditional structural distance measures. We illustrate the power of structure-informed phylogenetics by deciphering the evolutionary diversification of a particularly challenging family: the fast-evolving RRNPPA quorum-sensing receptors. We were able to propose a more parsimonious evolutionary history for this critical protein family that enables gram-positive bacteria, plasmids and bacteriophages to communicate and coordinate key behaviors. The advent of high-accuracy structural phylogenetics enables a myriad of applications across biology, such as uncovering deeper evolutionary relationships, elucidating unknown protein functions or refining the design of bioengineered molecules. Using a new method called FoldTree, the authors compare proteins on the basis of their shape to construct more accurate family trees over long evolutionary timescales and capture distant relationships where sequence information becomes less reliable.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 12","pages":"2492-2502"},"PeriodicalIF":10.1,"publicationDate":"2025-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41594-025-01649-8.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145275379","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Nuclear transport receptors (NTRs) carry cargo across the permeability barrier of nuclear pore complexes (NPCs)—an FG phase condensed from disordered but cohesive FG-repeat domains. This phase repels inert macromolecules but allows NTR passage. When the human immunodeficiency virus (HIV) infects nondividing cells, its capsid is transported into nuclei not like a cargo but crosses NPCs like an NTR. Here we uncovered the molecular determinants of the capsid’s NTR behavior. The FG-binding pocket is insufficient. Hexameric and pentameric capsomers contribute. The highly exposed outer capsid surface is key. It lacks FG-repulsive charged residues (K, D and E) that are very abundant on other protein surfaces. FG-attractive residues dominate the capsid surface instead. Introducing FG-repulsive amino acids impedes FG phase partitioning, NPC targeting and NPC passage of assembled capsids. Capsids are, thus, made soluble in the FG phase by a myriad of transient FG-attractive interactions originating from individual surface side chains. We propose that CPSF6 releases the capsid from NPCs by masking its FG-attractive surface and switching the capsid to an FG-repulsive species. Fu et al. uncover the features that allow the HIV capsid to cross the permeability barrier of nuclear pores in an importin-independent manner, explaining how the viral genome can reach the nuclear compartment when infecting nondividing cells.
{"title":"Nuclear pore passage of the HIV capsid is driven by its unusual surface amino acid composition","authors":"Liran Fu, Shiya Cheng, Dietmar Riedel, Leonie Kopecny, Melina Schuh, Dirk Görlich","doi":"10.1038/s41594-025-01684-5","DOIUrl":"10.1038/s41594-025-01684-5","url":null,"abstract":"Nuclear transport receptors (NTRs) carry cargo across the permeability barrier of nuclear pore complexes (NPCs)—an FG phase condensed from disordered but cohesive FG-repeat domains. This phase repels inert macromolecules but allows NTR passage. When the human immunodeficiency virus (HIV) infects nondividing cells, its capsid is transported into nuclei not like a cargo but crosses NPCs like an NTR. Here we uncovered the molecular determinants of the capsid’s NTR behavior. The FG-binding pocket is insufficient. Hexameric and pentameric capsomers contribute. The highly exposed outer capsid surface is key. It lacks FG-repulsive charged residues (K, D and E) that are very abundant on other protein surfaces. FG-attractive residues dominate the capsid surface instead. Introducing FG-repulsive amino acids impedes FG phase partitioning, NPC targeting and NPC passage of assembled capsids. Capsids are, thus, made soluble in the FG phase by a myriad of transient FG-attractive interactions originating from individual surface side chains. We propose that CPSF6 releases the capsid from NPCs by masking its FG-attractive surface and switching the capsid to an FG-repulsive species. Fu et al. uncover the features that allow the HIV capsid to cross the permeability barrier of nuclear pores in an importin-independent manner, explaining how the viral genome can reach the nuclear compartment when infecting nondividing cells.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 12","pages":"2476-2491"},"PeriodicalIF":10.1,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41594-025-01684-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145254766","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-10-06DOI: 10.1038/s41594-025-01645-y
Mayra Furlan-Magaril
Exile, discovery, and resilience have shaped my journey as a group leader in Mexico. From exploring chromatin architecture to building a lab and community, this is how science became my vocation and my home.
{"title":"Returning home: a story of chromatin and community","authors":"Mayra Furlan-Magaril","doi":"10.1038/s41594-025-01645-y","DOIUrl":"10.1038/s41594-025-01645-y","url":null,"abstract":"Exile, discovery, and resilience have shaped my journey as a group leader in Mexico. From exploring chromatin architecture to building a lab and community, this is how science became my vocation and my home.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 10","pages":"1847-1847"},"PeriodicalIF":10.1,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145235642","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-10-06DOI: 10.1038/s41594-025-01686-3
Till Schwämmle, Gemma Noviello, Eleni Kanata, Jonathan J. Froehlich, Melissa Bothe, Alexandra Martitz, Aybuge Altay, Jade Scouarnec, Vivi-Yun Feng, Heleen Mallie, Martin Vingron, Edda G. Schulz
Developmental genes are controlled by an ensemble of cis-acting regulatory elements (REs), which in turn respond to multiple trans-acting transcription factors (TFs). Understanding how a cis-regulatory landscape integrates information from many dynamically expressed TFs has remained a challenge. Here we develop a combined CRISPR screening approach using endogenous RNA and RE reporters as readouts. Applied to the murine Xist locus, which is crucial for X-chromosome inactivation in females, this method allows us to comprehensively identify Xist-controlling TFs and map their TF–RE wiring. We find a group of transiently upregulated TFs, including ZIC3, that regulate proximal REs, driving the binary activation of Xist expression. These basal activators are more highly expressed in cells with two X chromosomes, potentially governing female-specific Xist upregulation. A second set of developmental TFs that include OTX2 is upregulated later during differentiation and targets distal REs. This regulatory axis is crucial to achieve high levels of Xist RNA, which is necessary for X-chromosome inactivation. OCT4 emerges as the strongest activator overall, regulating both proximal and distal elements. Our findings support a model for developmental gene regulation, in which factors targeting proximal REs drive binary on–off decisions, whereas factors interacting with distal REs control the transcription output. Here Schwämmle et al. develop CRISPR reporter screens to map transcription-factor-regulatory element interactions at the Xist locus, revealing a two-step mechanism integrating developmental and X-dosage signals to initiate X-chromosome inactivation.
{"title":"Reporter CRISPR screens decipher cis-regulatory and trans-regulatory principles at the Xist locus","authors":"Till Schwämmle, Gemma Noviello, Eleni Kanata, Jonathan J. Froehlich, Melissa Bothe, Alexandra Martitz, Aybuge Altay, Jade Scouarnec, Vivi-Yun Feng, Heleen Mallie, Martin Vingron, Edda G. Schulz","doi":"10.1038/s41594-025-01686-3","DOIUrl":"10.1038/s41594-025-01686-3","url":null,"abstract":"Developmental genes are controlled by an ensemble of cis-acting regulatory elements (REs), which in turn respond to multiple trans-acting transcription factors (TFs). Understanding how a cis-regulatory landscape integrates information from many dynamically expressed TFs has remained a challenge. Here we develop a combined CRISPR screening approach using endogenous RNA and RE reporters as readouts. Applied to the murine Xist locus, which is crucial for X-chromosome inactivation in females, this method allows us to comprehensively identify Xist-controlling TFs and map their TF–RE wiring. We find a group of transiently upregulated TFs, including ZIC3, that regulate proximal REs, driving the binary activation of Xist expression. These basal activators are more highly expressed in cells with two X chromosomes, potentially governing female-specific Xist upregulation. A second set of developmental TFs that include OTX2 is upregulated later during differentiation and targets distal REs. This regulatory axis is crucial to achieve high levels of Xist RNA, which is necessary for X-chromosome inactivation. OCT4 emerges as the strongest activator overall, regulating both proximal and distal elements. Our findings support a model for developmental gene regulation, in which factors targeting proximal REs drive binary on–off decisions, whereas factors interacting with distal REs control the transcription output. Here Schwämmle et al. develop CRISPR reporter screens to map transcription-factor-regulatory element interactions at the Xist locus, revealing a two-step mechanism integrating developmental and X-dosage signals to initiate X-chromosome inactivation.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 12","pages":"2465-2475"},"PeriodicalIF":10.1,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41594-025-01686-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145235665","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-29DOI: 10.1038/s41594-025-01680-9
Karim Housseini B. Issa, Muyang Ren, Bradley Burnet, Hao Lu, Charlotte Melia, Kate Heesom, Anthony J. Roberts, Sudipto Roy, Girish R. Mali
Multiciliogenesis requires large-scale biosynthesis of motility-powering axonemal inner and outer dynein arm motors (IDAs and ODAs) before their intraflagellar transport (IFT) into cilia. ODAs are inhibited by the packaging chaperone Shulin during ciliogenesis in Tetrahymena thermophila. How Shulin is released for ODAs to become active inside cilia remains unclear. Here we uncover a molecular mechanism for ODA activation. We establish interactions between DNAAF9 (human Shulin) and mammalian ODA subunits, IFT proteins and the ciliary small guanosine triphosphatase (GTPase) ARL3 using proteomics and in vitro reconstitutions. Mutagenesis combined with biochemical and structural studies reveal that DNAAF9 and Shulin preferentially bind active Arl3–GTP highlighting a cross-species conservation of this interaction. GTP-loaded Arl3 can access, bind and displace Shulin from the packaged ODA–Shulin complex. We propose that, once the inhibited ODA complex enters growing cilia, Arl3–GTP displaces Shulin (DNAAF9) and sequesters it away from ODAs, promoting activation of their motility specifically inside cilia. Issa et al. show that the ciliary small guanosine triphosphatase Arl3 displaces the inhibitory regulator Shulin/DNAAF9 from the outer dynein arm, leading to motor activation.
{"title":"Molecular basis for the activation of outer dynein arms in cilia","authors":"Karim Housseini B. Issa, Muyang Ren, Bradley Burnet, Hao Lu, Charlotte Melia, Kate Heesom, Anthony J. Roberts, Sudipto Roy, Girish R. Mali","doi":"10.1038/s41594-025-01680-9","DOIUrl":"10.1038/s41594-025-01680-9","url":null,"abstract":"Multiciliogenesis requires large-scale biosynthesis of motility-powering axonemal inner and outer dynein arm motors (IDAs and ODAs) before their intraflagellar transport (IFT) into cilia. ODAs are inhibited by the packaging chaperone Shulin during ciliogenesis in Tetrahymena thermophila. How Shulin is released for ODAs to become active inside cilia remains unclear. Here we uncover a molecular mechanism for ODA activation. We establish interactions between DNAAF9 (human Shulin) and mammalian ODA subunits, IFT proteins and the ciliary small guanosine triphosphatase (GTPase) ARL3 using proteomics and in vitro reconstitutions. Mutagenesis combined with biochemical and structural studies reveal that DNAAF9 and Shulin preferentially bind active Arl3–GTP highlighting a cross-species conservation of this interaction. GTP-loaded Arl3 can access, bind and displace Shulin from the packaged ODA–Shulin complex. We propose that, once the inhibited ODA complex enters growing cilia, Arl3–GTP displaces Shulin (DNAAF9) and sequesters it away from ODAs, promoting activation of their motility specifically inside cilia. Issa et al. show that the ciliary small guanosine triphosphatase Arl3 displaces the inhibitory regulator Shulin/DNAAF9 from the outer dynein arm, leading to motor activation.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 12","pages":"2454-2464"},"PeriodicalIF":10.1,"publicationDate":"2025-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s41594-025-01680-9.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145189271","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-26DOI: 10.1038/s41594-025-01682-7
Derek A. Pratt, Scott J. Dixon
Inhibitors of ferroptosis are key tools for studies of cell death and may ultimately prove useful for the treatment of various diseases. In this Comment, we discuss major types of ferroptosis inhibitors and considerations for their use in mechanistic and preclinical studies.
{"title":"A guide to using small-molecule ferroptosis inhibitors","authors":"Derek A. Pratt, Scott J. Dixon","doi":"10.1038/s41594-025-01682-7","DOIUrl":"10.1038/s41594-025-01682-7","url":null,"abstract":"Inhibitors of ferroptosis are key tools for studies of cell death and may ultimately prove useful for the treatment of various diseases. In this Comment, we discuss major types of ferroptosis inhibitors and considerations for their use in mechanistic and preclinical studies.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 10","pages":"1848-1851"},"PeriodicalIF":10.1,"publicationDate":"2025-09-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145153441","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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