Nature Structural & Molecular Biology
Nature Structural and Molecular Biology reflects the growing integration of structural and molecular studies. The journal places a strong emphasis on understanding the molecular mechanisms underlying biological processes. Specific areas include (but are not limited to) DNA replication, repair and recombination; chromatin structure and remodeling; transcription; translation; folding, processing, transport and degradation of proteins and RNA; signal transduction and membrane processes.
http://feeds.nature.com/nsmb/rss/current
Nature Publishing Group
en
© 2024 Macmillan Publishers Limited, part of Springer Nature. All rights reserved.
Nature Structural & Molecular Biology
© 2024 Macmillan Publishers Limited, part of Springer Nature. All rights reserved.
permissions@nature.com
Nature Structural & Molecular Biology
https://www.nature.com/uploads/product/nsmb/rss.gif
http://feeds.nature.com/nsmb/rss/current
-
https://www.nature.com/articles/s41594-024-01238-1
Nature Structural & Molecular Biology, Published online: 27 March 2024; doi:10.1038/s41594-024-01238-1Precise protein synthesis is achieved by tRNA modifications. Here the authors revealed that modified cytidines in tRNAIle use their long side chains to make additional interactions with mRNA for stable tRNA binding on the ribosome.]]>
Naho AkiyamaKensuke IshiguroTakeshi YokoyamaKenjyo MiyauchiAsuteka NagaoMikako ShirouzuTsutomu Suzuki
doi:10.1038/s41594-024-01238-1
Nature Structural & Molecular Biology, Published online: 2024-03-27; | doi:10.1038/s41594-024-01238-1
2024-03-27
Nature Structural & Molecular Biology
10.1038/s41594-024-01238-1
https://www.nature.com/articles/s41594-024-01238-1
-
https://www.nature.com/articles/s41594-024-01236-3
Nature Structural & Molecular Biology, Published online: 27 March 2024; doi:10.1038/s41594-024-01236-3Rybak and Gagnon elucidate the mechanism of AUG codon avoidance by the minor isoleucine tRNA in Escherichia coli. The lysidinylated C34 in the anticodon loop of tRNAIle weakens interactions with the mRNA and destabilizes the EF-Tu ternary complex.]]>
Mariia Yu. RybakMatthieu G. Gagnon
doi:10.1038/s41594-024-01236-3
Nature Structural & Molecular Biology, Published online: 2024-03-27; | doi:10.1038/s41594-024-01236-3
2024-03-27
Nature Structural & Molecular Biology
10.1038/s41594-024-01236-3
https://www.nature.com/articles/s41594-024-01236-3
-
https://www.nature.com/articles/s41594-024-01253-2
Nature Structural & Molecular Biology, Published online: 27 March 2024; doi:10.1038/s41594-024-01253-2Transcription of toxin–antitoxin modules is regulated by conditional cooperativity, where the toxin enables or disrupts antitoxin-driven repression. Here, the authors solve the structural basis for the conditional cooperativity of Salmonella TacAT3.]]>
Grzegorz J. GrabeRachel T. GiorgioMiłosz WieczórBridget GollanMolly SargenModesto OrozcoStephen A. HareSophie Helaine
doi:10.1038/s41594-024-01253-2
Nature Structural & Molecular Biology, Published online: 2024-03-27; | doi:10.1038/s41594-024-01253-2
2024-03-27
Nature Structural & Molecular Biology
10.1038/s41594-024-01253-2
https://www.nature.com/articles/s41594-024-01253-2
-
https://www.nature.com/articles/s41594-024-01258-x
Nature Structural & Molecular Biology, Published online: 25 March 2024; doi:10.1038/s41594-024-01258-xCryo-EM studies reveal that RYBP–PRC1 uses two distinct interfaces for binding unmodified and H2Aub1-modified nucleosomes. These binding modes enable the complex to generate H2Aub1 chromatin domains by a read–write mechanism.]]>
Maria CiapponiElena KarlukovaSven SchkölzigerChristian BendaJürg Müller
doi:10.1038/s41594-024-01258-x
Nature Structural & Molecular Biology, Published online: 2024-03-25; | doi:10.1038/s41594-024-01258-x
2024-03-25
Nature Structural & Molecular Biology
10.1038/s41594-024-01258-x
https://www.nature.com/articles/s41594-024-01258-x
-
https://www.nature.com/articles/s41594-024-01273-y
Nature Structural & Molecular Biology, Published online: 19 March 2024; doi:10.1038/s41594-024-01273-yAuthor Correction: Structure and interactions of the endogenous human Commander complex]]>
Saara LaulumaaEsa-Pekka KumpulaJuha T. HuiskonenMarkku Varjosalo
doi:10.1038/s41594-024-01273-y
Nature Structural & Molecular Biology, Published online: 2024-03-19; | doi:10.1038/s41594-024-01273-y
2024-03-19
Nature Structural & Molecular Biology
10.1038/s41594-024-01273-y
https://www.nature.com/articles/s41594-024-01273-y
-
https://www.nature.com/articles/s41594-024-01266-x
Nature Structural & Molecular Biology, Published online: 18 March 2024; doi:10.1038/s41594-024-01266-xIn addition to the usual dose of compelling science, our March issue features thoughtful reflections on the last 30 years from readers, as well as past and present editors. Perhaps influenced by these pieces or by our stunning cover — or maybe it is just the changing seasons — we are in an introspective mood this month.]]>
doi:10.1038/s41594-024-01266-x
Nature Structural & Molecular Biology, Published online: 2024-03-18; | doi:10.1038/s41594-024-01266-x
2024-03-18
Nature Structural & Molecular Biology
10.1038/s41594-024-01266-x
https://www.nature.com/articles/s41594-024-01266-x
-
Nature Structural & Molecular Biology]]>
https://www.nature.com/articles/s41594-024-01248-z
Nature Structural & Molecular Biology, Published online: 18 March 2024; doi:10.1038/s41594-024-01248-zOver the past 30 years, Nature Structural & Molecular Biology (NSMB) has covered an enormous breadth of subjects in the broad field of molecular and structural biology. Here, some of the journal’s past and present editors recount their editorial experience at NSMB and some of the more memorable papers they worked on.]]>
Nature Structural & Molecular Biology]]>
Guy RiddihoughChristopher SurridgeAndreas G. LadurnerRosemary K. ClyneMaria HodgesArianne HeinrichsKatarzyna MarcinkiewiczFlorian UllrichCarolina PerdigotoSara OsmanKatarzyna CiazynskaDimitris Typas
doi:10.1038/s41594-024-01248-z
Nature Structural & Molecular Biology, Published online: 2024-03-18; | doi:10.1038/s41594-024-01248-z
2024-03-18
Nature Structural & Molecular Biology
10.1038/s41594-024-01248-z
https://www.nature.com/articles/s41594-024-01248-z
-
https://www.nature.com/articles/s41594-024-01241-6
Nature Structural & Molecular Biology, Published online: 18 March 2024; doi:10.1038/s41594-024-01241-6In this Review, the authors present an overview of our current understanding of the relationship between DNA methylation and three-dimensional chromatin architecture, discussing the extent to which DNA methylation may regulate the folding of the genome.]]>
Ana Monteagudo-SánchezDaan NoordermeerMaxim V. C. Greenberg
doi:10.1038/s41594-024-01241-6
Nature Structural & Molecular Biology, Published online: 2024-03-18; | doi:10.1038/s41594-024-01241-6
2024-03-18
Nature Structural & Molecular Biology
10.1038/s41594-024-01241-6
https://www.nature.com/articles/s41594-024-01241-6