The Resolution Revolution

RELION: Implementation of a Bayesian approach to cryo-EM structure determination

Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446

The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution

Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327

Structure of the 30S ribosomal subunit

Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035

Electron counting and beam-induced motion correction enable near atomic resolution single particle cryoEM

Li, X.-M., Mooney, P., Zheng, S., Booth, C., Braunfeld, M. B., Gubbens, S., Agard, D., & Cheng, Y.-F. (2013) · Nature Methods · doi:10.1038/nmeth.2472 · Cited by 1,866

Structure of the TRPV1 ion channel determined by electron cryo-microscopy

Liao, M., Cao, E., Julius, D. J., & Cheng, Y. (2013) · Nature · doi:10.1038/nature12822 · Cited by 1,731

Structure of the Yeast Mitochondrial Large Ribosomal Subunit

Amunts, A., Brown, A., Bai, X., Llacer, J. L., Hussain, T., Emsley, P., Long, F., Murshudov, G. N., Scheres, S. H. W., & Ramakrishnan, V. (2014) · Science · doi:10.1126/science.1249410 · Cited by 580

Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria

Daum, B., Walter, A., Horst, A., Osiewacz, H. D., & Kühlbrandt, W. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305462110 · Cited by 229

Electronic detectors for electron microscopy

Faruqi, A. R., & Henderson, R. A. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.08.014 · Cited by 138

Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector

Allegretti, M., Mills, D. J., McMullan, G., Kühlbrandt, W., & Vonck, J. (2014) · eLife · doi:10.7554/elife.01963 · Cited by 138

Determination of protein structure at 8.5 Å resolution using cryo-electron tomography and sub-tomogram averaging

Schur, F. K. M., Hagen, W. J. H., de Marco, A., & Briggs, J. A. G. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.10.015 · Cited by 90

CryoSift : an accessible and automated CNN-driven tool for cryo-EM 2D class selection

Schäfer, J.-H., Calza, A., Hom, K., Damodar, P., Peng, R., Bogdanović, N., Lander, G. C., Stagg, S. M., & Cianfrocco, M. A. (2025) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x25008866 · Cited by 5

Advancing Electrocatalyst Design Principles via Liquid-Phase Transmission Electron Microscopy

Vigil, S. A., Lin, Z., & Moreno‐Hernandez, I. A. (2025) · ACS Catalysis · doi:10.1021/acscatal.5c06165 · Cited by 5

Deep Learning-Based Event Classification of Mass Photometry Data for Optimal Mass Measurement at the Single-Molecule Level

Iqbal, K., Thiele, J. C., Šaman, D., Peters, J. S., Thorpe, S., Tusk, S. E., Bardzil, J., Benesch, J. L. P., & Kukura, P. (2026) · ACS Nano · doi:10.1021/acsnano.5c13074 · Cited by 4

Direct evidence of acid-driven protein desolvation

Hamdi, F., Skalidis, I., Schwerin, I. K., Belapure, J., Semchonok, D. A., Kyrilis, F. L., Tüting, C., Müller, J., Künze, G., & Kastritis, P. L. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2525949123 · Cited by 5

Recent advances in the structural biology of photosystem II

Murray, J. W. (2026) · The Plant Journal · doi:10.1111/tpj.70925 · Cited by 5

A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat

Geerds, C., Bleymüller, W. M., Meyer, T., Widmann, C., & Niemann, H. H. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322000432 · Cited by 5

Three-dimensional atomic-scale characterization of titanium oxyhydroxide nanoparticles by data-driven lattice correlation analysis

Aso, K., Higashimine, K., Miyata, M., Kamio, H., & Oshima, Y. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01513-2 · Cited by 5

Databases and web-based tools for studying structures of protein-nucleic acid complexes

Dapkūnas, J., & Venclovas, Č. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103079 · Cited by 5

Protein complexes in focus

Glaeser, R. M. (2016) · eLife · doi:10.7554/elife.16156 · Cited by 5

Thermal management function of graphene under cryogenic temperature

Kato, R., Naya, M., Kasahata, N., Senga, R., Sato, C., Koshino, M., Suenaga, K., & Hasegawa, M. (2021) · Carbon · doi:10.1016/j.carbon.2021.07.077 · Cited by 5

Combined Bayesian and Normal Mode Flexible Fitting with Hamiltonian Monte Carlo Sampling for Cryo Electron Microscopy

Vuillemot, R., & Jonić, S. (2021) · European Signal Processing Conference (EUSIPCO) · doi:10.23919/eusipco54536.2021.9616150 · Cited by 5

Electron microscopy overview of SARS-COV2 and its clinical impact

Mansy, S. S., & AbouSamra, M. M. (2022) · Ultrastructural Pathology · doi:10.1080/01913123.2022.2035475 · Cited by 5

Structural insights into promiscuous GPCR-G protein coupling

Carrión-Antolí, Á., Mallor-Franco, J., Arroyo‐Urea, S., & García‐Nafría, J. (2022) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2022.06.015 · Cited by 6

An Iridium (III) complex revealing cytoskeleton nanostructures under super-resolution nanoscopy and liquid-phase electron microscopy

Liu, T., Pace, C. D., Huang, R., Bruno, G., Shao, T., Tian, X., Chen, B., Chen, B., Luo, K., Gong, Q., et al. (2023) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2023.133839 · Cited by 5

Cryo-EM of a heterogeneous biochemical fraction elucidates multiple protein complexes from a multicellular thermophilic eukaryote

Semchonok, D. A., Kyrilis, F. L., Hamdi, F., & Kastritis, P. L. (2023) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2023.100094 · Cited by 6

AutoEMage : automatic data transfer, preprocessing, real-time display and monitoring in cryo-EM

Cheng, Y., Huang, X., Xu, B., & Ding, W. (2023) · Journal of Applied Crystallography · doi:10.1107/s1600576723008257 · Cited by 5

A web-based dashboard for RELION metadata visualization

González-Rodríguez, N., Areán-Ulloa, E., & Fernández-Leiro, R. (2024) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798323010902 · Cited by 5

Structural biology of microbial gas vesicles: historical milestones and current knowledge

Huber, S. T., & Jakobi, A. J. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230396 · Cited by 5

Ion-driven rotary membrane motors: From structure to function

Martin, F. J. O., Santiveri, M., Hu, H., & Taylor, N. M. I. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102884 · Cited by 5

Perspectives Toward an Integrative Structural Biology Pipeline With Atomic Force Microscopy Topographic Images

Pellequer, J. (2024) · Journal of Molecular Recognition · doi:10.1002/jmr.3102 · Cited by 6

A closer look at pathogenic amyloid-β in Alzheimer’s disease using cryo-electron microscopy: a narrative review

Gao, Y., Schedin‐Weiss, S., & Tjernberg, L. O. (2024) · Advanced technology in neuroscience . · doi:10.4103/atn.atn-d-24-00014 · Cited by 5

A Double Emulsion-Based, Plastic-Glass Hybrid Microfluidic Platform for Protein Crystallization

Zhu, D., Zhou, X., & Zheng, B. (2015) · Micromachines · doi:10.3390/mi6111446 · Cited by 5

Ribosome Structure and Dynamics by smFRET Microscopy

Shebl, B., Norman, Z., & Cornish, P. V. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801122-5.00016-7 · Cited by 4

After the revolution: how is Cryo-EM contributing to muscle research?

Bradshaw, M., & Paul, D. M. (2019) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-019-09537-7 · Cited by 5

A Personal History of Using Crystals and Crystallography to Understand Biology and Advanced Drug Discovery

Blundell, T. L. (2020) · Crystals · doi:10.3390/cryst10080676 · Cited by 5

The revolution evolution

Amunts, A. (2021) · Nature Plants · doi:10.1038/s41477-021-01050-5 · Cited by 5

An electron counting algorithm improves imaging of proteins with low-acceleration-voltage cryo-electron microscope

Zhu, D., Shi, H., Wu, C., & Zhang, X. (2022) · Communications Biology · doi:10.1038/s42003-022-03284-1 · Cited by 5

Synthetic Biology-Based Solution NMR Studies on Membrane Proteins in Lipid Environments

Henrich, E., Löhr, F., Mezhyrova, J., Laguerre, A., Bernhard, F., & Dötsch, V. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.08.019 · Cited by 5

Fluorescent platinum nanoclusters as correlative light electron microscopy probes

Tanner, H., Hodgson, L. R., Mantell, J., & Verkade, P. (2021) · Methods in cell biology · doi:10.1016/bs.mcb.2020.12.002 · Cited by 5

Electron cryo-microscopy structure of the canonical TRPC4 ion channel

Vinayagam, D., Mager, T., Apelbaum, A., Bothe, A., Merino, F., Hofnagel, O., Gatsogiannis, C., & Raunser, S. (2018) · Worldwide Protein Data Bank · doi:10.2210/pdb6g1k/pdb · Cited by 5

Crystallography and the development of therapeutic medicines

Baker, E. N. (2018) · IUCrJ · doi:10.1107/s2052252518002555 · Cited by 5

Structure of the II2-III2-IV2 mitochondrial supercomplex from the parasite Perkinsus marinusPreprint

Wú, F., Mühleip, A., Gruhl, T., Sheiner, L., Maréchal, A., & Amunts, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.25.595893 · Cited by 6

Cryo-EM image processing of amyloid filaments in RELION-5.1Preprint

Lövestam, S., Shi, J., Li, D., Jamali, K., & Scheres, S. H. W. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.17.712386 · Cited by 5

CryoTRANS: predicting high-resolution maps of rare conformations from self-supervised trajectories in cryo-EM

Fan, X., Zhang, Q., Zhang, H., Zhu, J., Ju, L., Shi, Z., Hu, M., & Bao, C. (2024) · Communications Biology · doi:10.1038/s42003-024-06739-9 · Cited by 4

Recent Advances in Amyloids Structural Studies and Thin Film Applications

Pechkova, E., Fiordoro, S., Izzotti, A., & Riekel, C. (2025) · Molecules · doi:10.3390/molecules30142908 · Cited by 5

Macromolecular crystallography

Afonine, P. V., Albert, A., Diederichs, K., Hermoso, J. A., Krissinel, E., Márquez, J. A., Panjikar, S., Solà, M., Thorn, A., & Usón, I. (2025) · Nature Reviews Methods Primers · doi:10.1038/s43586-025-00433-8 · Cited by 6

The rise of AlphaFold in drug design

Stecuła, A., Paul, R., Litchfield, K., Dalton, S. E., Low, C. M. R., Reis, C. R., & Congreve, M. (2025) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2025.09.002 · Cited by 4

CryoWriter: a robotic solution for improved Cryo-EM grid preparation

V., C., Ekundayo, B., Fabrizio, M. D., Mohammed, I., Radecke, J., Stahlberg, H., & Kube, M. (2026) · Nature Communications · doi:10.1038/s41467-026-73752-3 · Cited by 4

Cryogenic light microscopy of vitrified samples with angstrom precision

Mazal, H., Wieser, F.-F., Bollschweiler, D., & Sandoghdar, V. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2513583122 · Cited by 4

Strategic advances for cryo-EM structural studies of small (<100 kDa) GPCRs

Singh, S. K., Agrawal, M., Pattanayak, A., Baidya, M., & Kumari, P. (2026) · Communications Biology · doi:10.1038/s42003-026-09516-y · Cited by 6

Membrane Protein Glycosylation Revisited: Functional Dynamics and Emerging Clinical Insights

Kim, K. D., & Yoo, B. C. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27083575 · Cited by 4

In Situ Cryo-Electron Tomography and Advanced Micromanipulator Techniques

Klumpe, S., & Erdmann, P. S. (2024) · Focus on structural biology · doi:10.1007/978-3-031-51171-4_5 · Cited by 4

NDT‐C11 as a Viable Novel Detergent for Single Particle Cryo‐EM

Jiko, C., Li, J., Moon, Y., Tanaka, Y. Y., Gopalasingam, C. C., Shigematsu, H., Chae, P. S., Kurisu, G., & Gerle, C. (2024) · ChemPlusChem · doi:10.1002/cplu.202400242 · Cited by 4

Rigid enlargement of sybodies with antibody fragments for cryo-EM analyses of small membrane proteins

Ackle, F., Thavarasah, S., Earp, J. C., & Seeger, M. A. (2025) · Scientific Reports · doi:10.1038/s41598-025-92950-5 · Cited by 4

Foam film vitrification for cryo-EM

Zhang, Y., Nandy, B., Sader, K., Russo, C. J., & Löwe, J. (2025) · Nature Communications · doi:10.1038/s41467-025-61270-7 · Cited by 5

Spatially Aware Diffraction Mapping Enables Fully Autonomous MicroED

Eremin, D. B., Jha, K. K., Delgadillo, D. A., Zhang, H., Foxman, S. H., Johnson, S. N., Vlahakis, N. W., Cascio, D., Lavallo, V., Rodríguez, J. A., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c10751 · Cited by 4

PhaseT3M: 3D imaging at 1.6 Å resolution via electron cryo-tomography with nonlinear phase retrieval

Lee, J., Song, S. M.-H., Cho, M. G., Varnavides, G., Ribet, S. M., Ophus, C., Scott, M. C., & Whittaker, M. (2025) · Nature Communications · doi:10.1038/s41467-025-67303-5 · Cited by 4

Computational Protocol for Assessing the Optimal Pixel Size to Improve the Accuracy of Single-particle Cryo-electron Microscopy Maps

Tiwari, S. P., Chhabra, S., Tama, F., & Miyashita, O. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b01107 · Cited by 4

Cryo-EM to visualize the structural organization of viruses

de Oliveira, G. A. P., & Silva, J. L. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.04.011 · Cited by 6

Insights into neurodegeneration from electron microscopy studies

Crowther, R. A. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210719 · Cited by 5

MEPSi: A tool for simulating tomograms of membrane-embedded proteins

de Francisco, B. R., Bezault, A., Xu, X., Hanein, D., & Volkmann, N. (2022) · Journal of Structural Biology · doi:10.1016/j.jsb.2022.107921 · Cited by 4

Lysate-to-grid: Rapid Isolation of Native Complexes from Budding Yeast for Cryo-EM Imaging

Cooney, I., Mack, D., Ferrell, A. J., Stewart, M., Wang, S., Donelick, H., Tamayo-Jaramillo, D., Greer, D. L., Zhu, D., Li, W., et al. (2023) · BIO-PROTOCOL · doi:10.21769/bioprotoc.4596 · Cited by 4

Crystal search – feasibility study of a real-time deep learning process for crystallization well images

Thielmann, Y., Luft, T., Zint, N., & Koepke, J. (2023) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s2053273323001948 · Cited by 4

Proceedings of the 22nd Python in Science Conference

(2023) · Proceedings of the Python in Science Conferences · doi:10.25080/gerudo-f2bc6f59-039 · Cited by 4

Holliday junction branch migration driven by AAA+ ATPase motors

Wald, J., & Marlovits, T. C. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102650 · Cited by 4

Structural determination and modeling of ciliary microtubules

Walton, T., Doran, M. H., & Brown, A. (2024) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798324001815 · Cited by 4

Cryo-EM sample preparation for high-resolution structure studies

Wang, L., & Zimanyi, C. M. (2024) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x24002553 · Cited by 4

The C-terminal disordered loop domain of Apc8 unlocks APC/C mitotic activation

Darling, S., Fujimitsu, K., Chia, K. H., Zou, J., Rappsilber, J., & Yamano, H. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114262 · Cited by 4

Bridging the microscopic divide: a comprehensive overview of micro-crystallization and in vivo crystallography

Chavas, L. M. G., Coulibaly, F., & Garriga, D. (2024) · IUCrJ · doi:10.1107/s205225252400513x · Cited by 4

A systematic approach of vitrification by high pressure freezing

Kodera, C., Bret, Y., Eyraud, F., Heiligenstein, J., Belle, M., & Heiligenstein, X. (2024) · Methods in microscopy · doi:10.1515/mim-2024-0002 · Cited by 4

Cryo‐electron tomography elucidates annular intraluminal configurations in Caenorhabditis elegans microtubules

Zhu, H., Li, M., Li, M., Li, X., & Ou, G. (2024) · Biology of the Cell · doi:10.1111/boc.202400064 · Cited by 4

How Cryo-EM Revolutionized the Field of Bioenergetics

Sottatipreedawong, M., Kazmi, A. A., & Vercellino, I. (2024) · Microscopy and Microanalysis · doi:10.1093/mam/ozae089 · Cited by 4

Electron Cryo-Tomography

Ferreira, J. L., Matthews-Palmer, T. R. S., & Beeby, M. (2017) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-319-68997-5_3 · Cited by 4

TopoStats - a program for automated tracing of biomolecules from AFM images

Beton, J. G., Moorehead, R., Helfmann, L., Gray, R., Hoogenboom, B. W., Joseph, A. P., Topf, M., & Pyne, A. L. B. (2021) · BIROn (Birkbeck, University of London) · Cited by 4

A Visual Environment for Data Driven Protein Modeling and Validation

Falk, M., Tobiasson, V., Böck, A., Hansen, C. D., & Ynnerman, A. (2023) · IEEE Transactions on Visualization and Computer Graphics · doi:10.1109/tvcg.2023.3286582 · Cited by 4

Effect of self and extrinsic encapsulation on electron resilience of porous 2D polymer nanosheets

Mücke, D., Linck, M., Guzzinati, G., Müller, H., Levin, B. D. A., Bammes, B. E., Brouwer, R. G., Jelezko, F., Qi, H., & Kaiser, U. A. (2023) · Micron · doi:10.1016/j.micron.2023.103525 · Cited by 4

Cryo-EM reconstruction of helical polymers: Beyond the simple cases

Kreutzberger, M. A. B., Sonani, R. R., & Egelman, E. H. (2024) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583524000155 · Cited by 4

Analyzing 3D cell data of optical diffraction tomography through volume rendering

Kim, T., & Park, J. (2018) · International Workshop on Advanced Imaging Technology (IWAIT) · doi:10.1109/iwait.2018.8369805 · Cited by 4

Preparation of RNA Polymerase Complexes for Their Analysis by Single-Particle Cryo-Electron Microscopy

Pilsl, M., Heiss, F. B., Pöll, G., Höcherl, M., Milkereit, P., & Engel, C. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2501-9_6 · Cited by 4

Protein Structure Databases

Armstrong, D. R., Berrisford, J. M., Conroy, M. J., Clark, A. R., Gupta, D. S., & Mukhopadhyay, A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809633-8.20280-x · Cited by 4

The Evolving Role of Structural Biology in Drug Discovery

Renaud, J. (2020) · Wiley eBooks · doi:10.1002/9781118681121.ch1 · Cited by 5

The impact of AlphaFold on experimental structure solutionPreprint

Edich, M., Briggs, D. C., Kippes, O., Gao, Y., & Thorn, A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.07.487522 · Cited by 4

A Research Journey: Over a Decade of Denaturing and Native-MS Analyses of Hydrophobic and Membrane Proteins in Amgen Therapeutic Discovery

Campuzano, I. D. G. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00175 · Cited by 4

A goldilocks computational protocol for inhibitor discovery targeting DNA damage responses including replication-repair functions

Moiani, D., & Tainer, J. A. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1442267 · Cited by 3

Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL

Wang, M. (2025) · Journal of Synchrotron Radiation · doi:10.1107/s1600577525005016 · Cited by 5

Electron spin resonance spectroscopy in a transmission electron microscope

Jaroš, A., Toyfl, J., Pupić, A., Czasch, B., Boero, G., Bicket, I. C., & Haslinger, P. (2025) · Ultramicroscopy · doi:10.1016/j.ultramic.2025.114224 · Cited by 3

Nanoscale Imaging of Biological Tissues: Techniques, Challenges and Emerging Frontiers

Kajla, R., Leija-Cardenas, R., Shivalingaiah, M. M., Shabbir, M. W., & Ou, Z. (2025) · Nanomaterials · doi:10.3390/nano15231752 · Cited by 4

Explicit correction of severely non-uniform distributions of cryo-EM views

Barchet, C., von Loeffelholz, O., Bahena-Ceron, R., Klaholz, B. P., & Urzhumtsev, A. (2026) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798326000306 · Cited by 3

CHARMM-GUI Quick Bilayer: Simple and Intuitive One-Stop Membrane Bilayer Builder

Park, S., & Im, W. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.169672 · Cited by 4

Cryo-EM of kinesin-binding protein: challenges and opportunities from protein-surface interactions

Atherton, J., & Moores, C. A. (2021) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321001935 · Cited by 3

Methods to Analyze Post-transcriptional Modifications Applied to Stable RNAs in Staphylococcus aureus

Bahena-Ceron, R., Ponce, J. R. J., Kanazawa, H., Antoine, L., Wolff, P., Marchand, V., Klaholz, B. P., Motorin, Y., Romby, P., & Marzi, S. (2023) · RNA technologies · doi:10.1007/978-3-031-36390-0_11 · Cited by 3

Rational Design of Drugs Targeting G-Protein-Coupled Receptors: A Structural Biology Perspective

Khorn, P. A., Luginina, A. P., Pospelov, V. A., Dashevskii, D. E., Khnykin, A. N., Moiseeva, O. V., Safronova, N. A., Belousov, A., Mishin, A., & Borshchevskiy, V. I. (2024) · Biochemistry (Moscow) · doi:10.1134/s0006297924040138 · Cited by 3

Structure and Dynamics of Type 4a Pili and Type 2 Secretion System Endopili

Izadi‐Pruneyre, N., Karami, Y., & Nilges, M. (2024) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-58843-3_21 · Cited by 3

Structure of Aquifex aeolicus lumazine synthase by cryo-electron microscopy to 1.42 Å resolution

Savva, C. G., Sobhy, M. A., Biasio, A. D., & Hamdan, S. M. (2024) · IUCrJ · doi:10.1107/s2052252524005530 · Cited by 3

Roodmus : a toolkit for benchmarking heterogeneous electron cryo-microscopy reconstructions

Joosten, M., Greer, J., Parkhurst, J. M., Burnley, B. T., & Jakobi, A. J. (2024) · IUCrJ · doi:10.1107/s2052252524009321 · Cited by 3

Comparative Analysis of Symmetry Parameters in the E2 Inner Core of the Pyruvate Dehydrogenase Complex

Kim, H., Jeong, M. S., An, M. Y., Park, Y. H., Park, S. H., Chung, S. J., Yi, Y.-S., Jun, S., Kim, Y. K., & Jung, H. S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252413731 · Cited by 3

Integrative Approaches to Study Virus Structures

Stuart, D. I., Oksanen, H. M., & Abrescia, N. G. A. (2024) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-65187-8_7 · Cited by 3

An Overview of Epitopes and Methods for Antibody Epitope Mapping

Nilvebrant, J., Thalén, N., Rockberg, J., & Malm, M. (2025) · Methods in molecular biology · doi:10.1007/978-1-0716-4591-8_1 · Cited by 3

TextFold: A Geometric Hypergraph Framework for Protein Structure Prediction with Scientific Literature Integration

Harit, A., Sun, Z., & Moubayed, N. A. (2025) · Procedia Computer Science · doi:10.1016/j.procs.2025.07.142 · Cited by 2

Cryo-EM sample preparation with soft-landing and laser flash melting

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NoiseFlow: Learning Optical Flow from Low SNR Cryo-EM Movie

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