# Publications Sort & Filters close ## Filters Publications expand\_more - Cryo-EM Center Publications (134) - MEMS Publications (24) Year of Publication expand\_more 2026 (1) 2025 (29) 2024 (25) 2023 (23) 2022 (21) 2021 (24) 2020 (16) 2019 (3) 2018 (3) 2017 (3) 2015 (1) Search Within Results Search Within Results search ## 149 results Show filters filter\_alt Sort by Year of PublicationAlphabetical A-Z sort ## 149 results Download 149 citations download- [BibTeX](/node/1922706/export?format=bibtex) - [EndNote X3 XML](/node/1922706/export?format=endnote8) - [EndNote 7 XML](/node/1922706/export?format=endnote7) - [Endnote tagged](/node/1922706/export?format=tagged) - [Marc](/node/1922706/export?format=marc) - [PubMedId](/node/1922706/export?format=pubmed_id) - [RIS](/node/1922706/export?format=ris) ### 2026 Benjamin D. Thomson, Melissa D. Marquez, Shaun Rawson, Thiago M. A. dos Santos, Stephen C. Harrison, and Daniel Kahne. 2026. “[Structures of Folding Intermediates on BAM Show Diverse Substrates Fold by a Conserved Mechanism](/publication/structures-folding-intermediates-bam-show-diverse-substrates-fold-conserved-mechanism)”. Proceedings of the National Academy of Sciences, 123, Pp. e2534936123. doi:10.1073/pnas.2534936123 Benjamin D. Thomson, Melissa D. Marquez, Shaun Rawson, Thiago M. A. dos Santos, Stephen C. Harrison, and Daniel Kahne. 2026. “[Structures of Folding Intermediates on BAM Show Diverse Substrates Fold by a Conserved Mechanism](/publication/structures-folding-intermediates-bam-show-diverse-substrates-fold-conserved-mechanism)”. Proceedings of the National Academy of Sciences, 123, Pp. e2534936123. doi:10.1073/pnas.2534936123 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://www.pnas.org/doi/abs/10.1073/pnas.2534936123) The outer membrane of Gram-negative bacteria contains a wide variety of integral β-barrel proteins. Here, we study the conserved β-barrel assembly machine which is responsible for folding and inserting these membrane β-barrels. By determining the... - [ descriptionPublisher's Version](https://www.pnas.org/doi/abs/10.1073/pnas.2534936123) ### 2025 2025. “[Translational Activators Align MRNAs at the Small Mitoribosomal Subunit for Translation Initiation](/publication/translational-activators-align-mrnas-small-mitoribosomal-subunit-translation-initiation)”. doi:10.1038/s41594-025-01726-y 2025. “[Translational Activators Align MRNAs at the Small Mitoribosomal Subunit for Translation Initiation](/publication/translational-activators-align-mrnas-small-mitoribosomal-subunit-translation-initiation)”. doi:10.1038/s41594-025-01726-y - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.1038/s41594-025-01726-y) Mitochondrial gene expression is essential for oxidative phosphorylation. Mitochondrial-encoded mRNAs are translated by dedicated mitochondrial ribosomes (mitoribosomes), whose regulation remains elusive. In Saccharomyces cerevisiae, nuclear-encoded... - [ descriptionPublisher's Version](https://doi.org/10.1038/s41594-025-01726-y) Morgan S. A. Gilman, Irina Shlosman, Daniel D. Samé Guerra, Masy Domecillo, Elayne M. Fivenson, Claire Bourett, Thomas G. Bernhardt, Nicholas F. Polizzi, Joseph J. Loparo, and Andrew C. Kruse. 2025. “[Conformational Regulation of Two Essential Activators of Bacterial Cell Elongation](/publication/conformational-regulation-two-essential-activators-bacterial-cell-elongation)”. Proceedings of the National Academy of Sciences, 122, Pp. e2514198122. doi:10.1073/pnas.2514198122 Morgan S. A. Gilman, Irina Shlosman, Daniel D. Samé Guerra, Masy Domecillo, Elayne M. Fivenson, Claire Bourett, Thomas G. Bernhardt, Nicholas F. Polizzi, Joseph J. Loparo, and Andrew C. Kruse. 2025. “[Conformational Regulation of Two Essential Activators of Bacterial Cell Elongation](/publication/conformational-regulation-two-essential-activators-bacterial-cell-elongation)”. Proceedings of the National Academy of Sciences, 122, Pp. e2514198122. doi:10.1073/pnas.2514198122 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://www.pnas.org/doi/abs/10.1073/pnas.2514198122) Rod-shaped bacteria rely on the Rod complex to synthesize and maintain their peptidoglycan (PG) cell wall during growth. While the enzymatic machinery at its core is well studied, the role of accessory proteins within the complex remains unclear. In this... - [ descriptionPublisher's Version](https://www.pnas.org/doi/abs/10.1073/pnas.2514198122) Martin S. Taylor, Maggie Chen, Matthew Hancock, Maximilian Wranik, Bryant D. Miller, Timothy R. O’Meara, Brad A. Palanski, Scott B. Ficarro, Brian J. Groendyke, Yufei Xiang, Kazuma T. Kondo, Karen Y. Linde-Garelli, Michelle J. Lee, Dibyendu Mondal, Daniel Freund, Samantha Congreve, Kaay Matas, Maximiliaan Hennink, Kera Xibinaku, Max L. Valenstein, Trevor van Eeuwen, Jarrod A. Marto, Andrej Sali, Yi Shi, Nathanael S. Gray, David M. Sabatini, Nam Chu, Kacper B. Rogala, and Philip A. Cole. 2025. “[Structural Basis for the Recruitment and Selective Phosphorylation of Akt by MTORC2](/publication/structural-basis-recruitment-and-selective-phosphorylation-akt-mtorc2)”. Science, Pp. eadv7111. doi:10.1126/science.adv7111 Martin S. Taylor, Maggie Chen, Matthew Hancock, Maximilian Wranik, Bryant D. Miller, Timothy R. O’Meara, Brad A. Palanski, Scott B. Ficarro, Brian J. Groendyke, Yufei Xiang, Kazuma T. Kondo, Karen Y. Linde-Garelli, Michelle J. Lee, Dibyendu Mondal, Daniel Freund, Samantha Congreve, Kaay Matas, Maximiliaan Hennink, Kera Xibinaku, Max L. Valenstein, Trevor van Eeuwen, Jarrod A. Marto, Andrej Sali, Yi Shi, Nathanael S. Gray, David M. Sabatini, Nam Chu, Kacper B. Rogala, and Philip A. Cole. 2025. “[Structural Basis for the Recruitment and Selective Phosphorylation of Akt by MTORC2](/publication/structural-basis-recruitment-and-selective-phosphorylation-akt-mtorc2)”. Science, Pp. eadv7111. doi:10.1126/science.adv7111 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://www.science.org/doi/abs/10.1126/science.adv7111) The mTOR protein kinase forms two multiprotein complexes, mTORC1 and mTORC2, that function in distinct signaling pathways. mTORC1 is regulated by nutrients, and mTORC2 is a central node in phosphoinositide-3 kinase (PI3K) and small guanosine triphosphate... - [ descriptionPublisher's Version](https://www.science.org/doi/abs/10.1126/science.adv7111) Dong Man " Jang, Kayla Boxer, Byung Hak Ha, and . 2025. “[‘Cryo-EM Structures of CRAF MEK1 14-3-3 Complexes in Autoinhibited and Open-Monomer States Reveal Features of RAF Regulation’](/publication/cryo-em-structures-crafmek114-3-3-complexes-autoinhibited-and-open-monomer-states)”. "Nature Communications", 16, Pp. "8150" Dong Man " Jang, Kayla Boxer, Byung Hak Ha, and . 2025. “[‘Cryo-EM Structures of CRAF MEK1 14-3-3 Complexes in Autoinhibited and Open-Monomer States Reveal Features of RAF Regulation’](/publication/cryo-em-structures-crafmek114-3-3-complexes-autoinhibited-and-open-monomer-states)”. "Nature Communications", 16, Pp. "8150" - add\_circle do\_not\_disturb\_on Abstract "CRAF (RAF1) is one of three RAF-family kinases that initiate MAP kinase signaling in response to activated RAS and is essential for oncogenic signaling from mutant KRAS. Like BRAF, CRAF is regulated by 14-3-3 engagement and by intramolecular... Binita " Shah, Moritz Hunkeler, Ariana Bratt, and Hong Yue. 2025. “[‘Structural Basis of VCP-VCPIP1-P47 Ternary Complex in Golgi Maintenance’](/publication/structural-basis-vcp-vcpip1-p47-ternary-complex-golgi-maintenance)”. "Nature Communications", 16, Pp. "8025" Binita " Shah, Moritz Hunkeler, Ariana Bratt, and Hong Yue. 2025. “[‘Structural Basis of VCP-VCPIP1-P47 Ternary Complex in Golgi Maintenance’](/publication/structural-basis-vcp-vcpip1-p47-ternary-complex-golgi-maintenance)”. "Nature Communications", 16, Pp. "8025" - add\_circle do\_not\_disturb\_on Abstract "VCP/p97 regulates a wide range of cellular processes, including post-mitotic Golgi reassembly. In this context, VCP is assisted by p47, an adapter protein, and VCPIP1, a deubiquitylase (DUB). However, how they organize into a functional ternary complex... 2025. “[Molecular Organization of the New World Arenavirus Spike Glycoprotein Complex](/publication/molecular-organization-new-world-arenavirus-spike-glycoprotein-complex)”. doi:10.1038/s41564-025-02085-6 2025. “[Molecular Organization of the New World Arenavirus Spike Glycoprotein Complex](/publication/molecular-organization-new-world-arenavirus-spike-glycoprotein-complex)”. doi:10.1038/s41564-025-02085-6 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.1038/s41564-025-02085-6) Of the multiple arenaviruses that cause haemorrhagic fevers in the Americas, all lack reliable therapeutic options, and only one has a vaccine. The arenavirus glycoprotein complex (GPC) binds cellular receptors and mediates pH-dependent fusion of viral... - [ descriptionPublisher's Version](https://doi.org/10.1038/s41564-025-02085-6) Mikołaj Słabicki, Jiho Park, Radosław P. Nowak, Shourya S. Roy Burman, Jesse Pellman, Charles Zou, Hlib Razumkov, Jeannie Carreiro, Simran Rastogi, Anna Goldstein, Marek M. Nagiec, Katherine A. Donovan, Jianwei Che, Moritz Hunkeler, Qixiang Geng, Chi-Lin Hsu, Megha Lakshminarayan, Chelsea Shu, Rebecca L. Zon, Zuzanna Kozicka, Paul M.C. Park, Jonathan M. Tsai, Hojong Yoon, Lyn H. Jones, Adam S. Sperling, Nathanael S. Gray, Eric S. Fischer, and Benjamin L. Ebert. 2025. “[Expanding the Druggable Zinc-Finger Proteome Defines Properties of Drug-Induced Degradation](/publication/expanding-druggable-zinc-finger-proteome-defines-properties-drug-induced-degradation)”. Molecular Cell, 85, Pp. 3184-3201. doi:https://doi.org/10.1016/j.molcel.2025.07.019 Mikołaj Słabicki, Jiho Park, Radosław P. Nowak, Shourya S. Roy Burman, Jesse Pellman, Charles Zou, Hlib Razumkov, Jeannie Carreiro, Simran Rastogi, Anna Goldstein, Marek M. Nagiec, Katherine A. Donovan, Jianwei Che, Moritz Hunkeler, Qixiang Geng, Chi-Lin Hsu, Megha Lakshminarayan, Chelsea Shu, Rebecca L. Zon, Zuzanna Kozicka, Paul M.C. Park, Jonathan M. Tsai, Hojong Yoon, Lyn H. Jones, Adam S. Sperling, Nathanael S. Gray, Eric S. Fischer, and Benjamin L. Ebert. 2025. “[Expanding the Druggable Zinc-Finger Proteome Defines Properties of Drug-Induced Degradation](/publication/expanding-druggable-zinc-finger-proteome-defines-properties-drug-induced-degradation)”. Molecular Cell, 85, Pp. 3184-3201. doi:https://doi.org/10.1016/j.molcel.2025.07.019 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://www.sciencedirect.com/science/article/pii/S1097276525006203) Summary Glutarimide analogs, such as thalidomide, redirect the E3 ubiquitin ligase CRL4CRBN to induce degradation of certain zinc finger (ZF) proteins. Although the core structural motif recognized by CRBN has been characterized, it does not fully explain... - [ descriptionPublisher's Version](https://www.sciencedirect.com/science/article/pii/S1097276525006203) 2025. “[Structural and Functional Basis of Mechanosensitive TMEM63 Channelopathies](/publication/structural-and-functional-basis-mechanosensitive-tmem63-channelopathies)”. Neuron. doi:10.1016/j.neuron.2025.05.009 2025. “[Structural and Functional Basis of Mechanosensitive TMEM63 Channelopathies](/publication/structural-and-functional-basis-mechanosensitive-tmem63-channelopathies)”. Neuron. doi:10.1016/j.neuron.2025.05.009 - [ descriptionPublisher's Version](https://doi.org/10.1016/j.neuron.2025.05.009) - [ descriptionPublisher's Version](https://doi.org/10.1016/j.neuron.2025.05.009) Allison M. James and Lucas Farnung. 2025. “[Structural Basis of Human CHD1 Nucleosome Recruitment and Pausing](/publication/structural-basis-human-chd1-nucleosome-recruitment-and-pausing)”. Molecular Cell. doi:https://doi.org/10.1016/j.molcel.2025.04.020 Allison M. James and Lucas Farnung. 2025. “[Structural Basis of Human CHD1 Nucleosome Recruitment and Pausing](/publication/structural-basis-human-chd1-nucleosome-recruitment-and-pausing)”. Molecular Cell. doi:https://doi.org/10.1016/j.molcel.2025.04.020 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://www.sciencedirect.com/science/article/pii/S1097276525003624) Summary Chromatin remodelers regulate gene expression and genome maintenance by controlling nucleosome positioning, but the structural basis for their regulated and directional activity remains poorly understood. Here, we present three cryoelectron... - [ descriptionPublisher's Version](https://www.sciencedirect.com/science/article/pii/S1097276525003624) Katrina Warner, Moritz Hunkeler, Kheewoong Baek, Anna Schmoker, Shourya S. Roy Burman, Daan Overwijn, Cyrus Jin, Katherine A. Donovan, and Eric S. Fischer. 2025. “[Structural Ubiquitin Contributes to K48 Linkage Specificity of the HECT Ligase Tom1](/publication/structural-ubiquitin-contributes-k48-linkage-specificity-hect-ligase-tom1)”. Cell Reports, 44, Pp. 115688. doi:https://doi.org/10.1016/j.celrep.2025.115688 Katrina Warner, Moritz Hunkeler, Kheewoong Baek, Anna Schmoker, Shourya S. Roy Burman, Daan Overwijn, Cyrus Jin, Katherine A. Donovan, and Eric S. Fischer. 2025. “[Structural Ubiquitin Contributes to K48 Linkage Specificity of the HECT Ligase Tom1](/publication/structural-ubiquitin-contributes-k48-linkage-specificity-hect-ligase-tom1)”. Cell Reports, 44, Pp. 115688. doi:https://doi.org/10.1016/j.celrep.2025.115688 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://www.sciencedirect.com/science/article/pii/S2211124725004590) Summary Homologous to E6AP C terminus (HECT) ubiquitin ligases play key roles in essential pathways such as DNA repair, cell cycle control, or protein quality control. Tom1 is one of five HECT ubiquitin E3 ligases in budding yeast S. cerevisiae and is... - [ descriptionPublisher's Version](https://www.sciencedirect.com/science/article/pii/S2211124725004590) 2025. “[Cryo-EM of Human P-Glycoprotein Reveals an Intermediate Occluded Conformation During Active Drug Transport](/publication/cryo-em-human-p-glycoprotein-reveals-intermediate-occluded-conformation-during-active)”, 16, 1, Pp. 3619+. doi:10.1038/s41467-025-58561-4 2025. “[Cryo-EM of Human P-Glycoprotein Reveals an Intermediate Occluded Conformation During Active Drug Transport](/publication/cryo-em-human-p-glycoprotein-reveals-intermediate-occluded-conformation-during-active)”, 16, 1, Pp. 3619+. doi:10.1038/s41467-025-58561-4 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.1038/s41467-025-58561-4) P-glycoprotein (Pgp) is an important human multidrug transporter that contributes to pharmacokinetics and multidrug resistance. Despite decades of study, the conformation transition cycle of Pgp undergoing active drug transport is not defined, thus the... - [ descriptionPublisher's Version](https://doi.org/10.1038/s41467-025-58561-4) - Previous page chevron\_left - [1](?page=0 "Current page") - [2](?page=1 "Go to page 2") - [3](?page=2 "Go to page 3") - [ Last page 13 ](?page=12 "Go to last page") - [ Next page chevron\_right ](?page=1 "Go to next page")