The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
The Resolution Revolution
Abstract
Advances in detector technology and image processing are yielding high-resolution electron cryo-microscopy structures of biomolecules. [Also see Report by Amunts et al. ]
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The computational cost to run all of this is ~5 days on an Nvidia A100 system and has since the development of the pipeline presented here, deemed FoldDock, been applied37.”
From Improved prediction of protein-protein interactions using AlphaFold2 (2021) · cites this paper as [37]
In the citing paper
“The computational cost to run all of this is ~5 days on an Nvidia A100 system and has since the development of the pipeline presented here, deemed FoldDock, been applied37.”
From Improved prediction of protein-protein interactions using AlphaFold2 (2021) · cites this paper as [37]
Citations
Cites
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
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
Self-citationElectronic 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
Allegretti, M., Mills, D. J., McMullan, G., Kühlbrandt, W., & Vonck, J. (2014) · eLife · doi:10.7554/elife.01963 · Cited by 138
Self-citationSchur, 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
Flagged first, then by citations
Cited by
Sorted by citations
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 11,626
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E. J., Armache, J., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,496
Liebschner, D., Afonine, P. V., Baker, M. L., Bunkóczi, G., Chen, V. B., Croll, T. I., Hintze, B., Hung, L.-W., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 7,953
New tools for automated high-resolution cryo-EM structure determination in RELION-3
Zivanov, J., Nakane, T., Forsberg, B., Kimanius, D., Hagen, W., Lindahl, E., & Scheres, S. (2018) · eLife · doi:10.7554/elife.42166 · Cited by 4,377
New tools for automated cryo-EM single-particle analysis in RELION-4.0
Kimanius, D., Dong, L., Sharov, G., Nakane, T., & Scheres, S. H. W. (2021) · Biochemical Journal · doi:10.1042/bcj20210708 · Cited by 1,029
Improved prediction of protein-protein interactions using AlphaFold2
Bryant, P., Pozzati, G., & Elofsson, A. (2021) · doi:10.1101/2021.09.15.460468 · Cited by 1,022
A new era for understanding amyloid structures and disease
Iadanza, M. G., Jackson, M. P., Hewitt, E. W., Ranson, N. A., & Radford, S. E. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0060-8 · Cited by 1,002
How cryo-EM is revolutionizing structural biology
Bai, X., McMullan, G., & Scheres, S. H. W. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.10.005 · Cited by 967
Single-particle cryo-EM at atomic resolution
Nakane, T., Kotecha, A., Sente, A., McMullan, G., Masiulis, S., Brown, P. M. G. E., Grigoras, I. T., Malinauskaitė, L., Malinauskas, T., Miehling, J., et al. (2020) · Nature · doi:10.1038/s41586-020-2829-0 · Cited by 881
Mechanistic diversity in ATP-binding cassette (ABC) transporters.
Locher, K. P. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3216 · Cited by 804
New tools for the analysis and validation of cryo-EM maps and atomic models
Afonine, P. V., Klaholz, B. P., Moriarty, N. W., Poon, B. K., Sobolev, O. V., Terwilliger, T. C., Adams, P. D., & Urzhumtsev, A. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318009324 · Cited by 742
Atomic-resolution protein structure determination by cryo-EM
Yip, K. M., Fischer, N., Paknia, E., Chari, A., & Stark, H. (2020) · Nature · doi:10.1038/s41586-020-2833-4 · Cited by 792
Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., et al. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000131 · Cited by 686
Structure and function of mitochondrial membrane protein complexes
Kühlbrandt, W. (2015) · BMC Biology · doi:10.1186/s12915-015-0201-x · Cited by 780
Self-citationComputational methods in drug discovery
Leelananda, S. P., & Lindert, S. (2016) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.12.267 · Cited by 675
Zhang, A., & Lieber, C. M. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00608 · Cited by 642
Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
Brown, A., Long, F., Nicholls, R. A., Toots, J., Emsley, P., & Murshudov, G. N. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004714021683 · Cited by 607
de la Rosa-Trevin, J. M., Quintana, A., del Caño, L., Zaldívar-Peraza, A., Foche, I., Gutiérrez, J., Gómez-Blanco, J., Burguet–Castell, J., Cuenca-Alba, J., Abrishami, V., et al. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.04.010 · Cited by 594
Single-Particle Cryo-EM at Crystallographic Resolution
Cheng, Y. (2015) · Cell · doi:10.1016/j.cell.2015.03.049 · Cited by 597
Shi, D., Beasock, D., Fessler, A., Szebeni, J., Ljubimova, J. Y., Afonin, K. A., & Dobrovolskaia, M. A. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2021.114079 · Cited by 535
Bernardi, P., Gerle, C., Halestrap, A. P., Jonas, E. A., Karch, J. M., Mnatsakanyan, N., Pavlov, E. V., Sheu, S., & Soukas, A. A. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01187-0 · Cited by 504
Cryo-EM in drug discovery: achievements, limitations and prospects
Renaud, J., Chari, A., Ciferri, C., Liu, W.-T., Rémigy, H., Stark, H., & Wiesmann, C. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.77 · Cited by 473
Structure and Mechanisms of F-Type ATP Synthases
Kühlbrandt, W. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-110903 · Cited by 445
Self-citationUnravelling biological macromolecules with cryo-electron microscopy
Fernández-Leiro, R., & Scheres, S. H. W. (2016) · Nature · doi:10.1038/nature19948 · Cited by 420
Kidmose, R. T., Juhl, J., Nissen, P., Boesen, T. P., Karlsen, J. L., & Pedersen, B. P. (2019) · IUCrJ · doi:10.1107/s2052252519007619 · Cited by 359
Cryo-EM: A Unique Tool for the Visualization of Macromolecular Complexity
Nogales, E., & Scheres, S. H. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.019 · Cited by 398
RCSB Protein Data Bank: Enabling biomedical research and drug discovery
Goodsell, D. S., Zardecki, C., Costanzo, L. D., Duarte, J. M., Hudson, B. P., Persikova, I., Segura, J., Shao, C., Voigt, M., Westbrook, J., et al. (2019) · Protein Science · doi:10.1002/pro.3730 · Cited by 366
Recent developments in the CCP-EM software suite
Burnley, B. T., Palmer, C. M., & Winn, M. (2017) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798317007859 · Cited by 340
Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine
Wong, W., Bai, X., Brown, A., Fernández, I. S., Hanssen, E. G., Condron, M. M., Tan, Y. H., Baum, J., & Scheres, S. H. W. (2014) · eLife · doi:10.7554/elife.03080 · Cited by 351
Cryo-electron microscopy for structural analysis of dynamic biological macromolecules
Murata, K., & Wolf, M. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.07.020 · Cited by 364
Structure and function of mitochondrial complex I
Wirth, C., Brandt, U., Hunte, C., & Zickermann, V. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.02.013 · Cited by 346
Bian, K., Gerber, C., Heinrich, A. J., Müller, D. J., Scheuring, S., & Jiang, Y. X. (2021) · Nature Reviews Methods Primers · doi:10.1038/s43586-021-00033-2 · Cited by 336
Protein denaturation at the air-water interface and how to prevent it
D’Imprima, E., Floris, D., Joppe, M., Sánchez, R. M., Grininger, M., & Kühlbrandt, W. (2019) · eLife · doi:10.7554/elife.42747 · Cited by 299
Self-citationStructure and mechanism of the RNA polymerase II transcription machineryPreprint
Schier, A. C., & Taatjes, D. J. (2020) · Genes & Development · doi:10.1101/gad.335679.119 · Cited by 327
Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids
Scheres, S. H. W., Falcon, B., & Goedert, M. (2023) · Nature · doi:10.1038/s41586-023-06437-2 · Cited by 308
EMDataBank unified data resource for 3DEM
Lawson, C. L., Patwardhan, A., Baker, M. L., Hryc, C. F., Sanz‐García, E., Hudson, B. P., Lagerstedt, I. C., Ludtke, S. J., Pintilie, G. D., Sala, R., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1126 · Cited by 288
Cryo-EM structures of tau filaments
Scheres, S. H. W., Zhang, W., Falcon, B., & Goedert, M. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.05.011 · Cited by 276
An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology
Thompson, R. F., Walker, M. L., Siebert, C. A., Muench, S. P., & Ranson, N. A. (2016) · Methods · doi:10.1016/j.ymeth.2016.02.017 · Cited by 277
Automated map sharpening by maximization of detail and connectivity
Terwilliger, T. C., Sobolev, O. V., Afonine, P. V., & Adams, P. D. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318004655 · Cited by 271
Tubiana, J., Schneidman-Duhovny, D., & Wolfson, H. J. (2022) · Nature Methods · doi:10.1038/s41592-022-01490-7 · Cited by 274
Schaffer, M., Mahamid, J., Engel, B. D., Laugks, T., Baumeister, W. P., & Plitzko, J. M. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.07.010 · Cited by 259
Structural Biology and Regulation of Protein Import into the Nucleus
Christie, M., Chang, C.-W. M., Róna, G., Smith, K. M. L., Stewart, A. G., Takeda, A. A. S., Fontes, M. R. M., Stewart, M., Vértessy, B. G., Forwood, J. K., et al. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.10.023 · Cited by 259
Kühlbrandt, W. (2014) · eLife · doi:10.7554/elife.03678 · Cited by 248
Self-citationStructure and Aggregation Mechanisms in Amyloids
Almeida, Z. L., & Brito, R. M. M. (2020) · Molecules · doi:10.3390/molecules25051195 · Cited by 258
Structure of the Type VI Secretion System Contractile Sheath
Kudryashev, M., Wang, R. Y., Brackmann, M., Scherer, S., Maier, T., Baker, D. A., DiMaio, F., Stahlberg, H., Egelman, E. H., & Basler, M. (2015) · Cell · doi:10.1016/j.cell.2015.01.037 · Cited by 245
The molecular principles governing the activity and functional diversity of AAA+ proteins
Puchades, C., Sandate, C. R., & Lander, G. C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0183-6 · Cited by 239
Calcium-release channels: structure and function of IP3 receptors and ryanodine receptors
Woll, K. A., & Petegem, F. V. (2021) · Physiological Reviews · doi:10.1152/physrev.00033.2020 · Cited by 235
Model-based local density sharpening of cryo-EM maps
Jakobi, A. J., Wilmanns, M., & Sachse, C. (2017) · eLife · doi:10.7554/elife.27131 · Cited by 223
Cryo-Electron Microscopy Methodology: Current Aspects and Future Directions
Danev, R., Yanagisawa, H., & Kikkawa, M. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.04.008 · Cited by 231
Reducing effects of particle adsorption to the air-water interface in cryoEM
Noble, A., Wei, H., Dandey, V., Zhang, Z.-N., Tan, Y.-Z., Potter, C., & Carragher, B. (2018) · Nature Methods · doi:10.1038/s41592-018-0139-3 · Cited by 194
A guide to studying protein aggregation
Housmans, J. A. J., Wu, G., Schymkowitz, J. W. H., & Rousseau, F. (2021) · FEBS Journal · doi:10.1111/febs.16312 · Cited by 228
Data-driven regularization lowers the size barrier of cryo-EM structure determination
Kimanius, D., Jamali, K., Wilkinson, M. E., Lövestam, S., Velazhahan, V., Nakane, T., & Scheres, S. H. W. (2024) · Nature Methods · doi:10.1038/s41592-024-02304-8 · Cited by 210
Franken, L. E., Boekema, E. J., & Stuart, M. C. A. (2017) · Advanced Science · doi:10.1002/advs.201600476 · Cited by 208
Burley, S. K., Bhikadiya, C., Bi, C., Bittrich, S., Chen, L., Crichlow, G. V., Duarte, J. M., Dutta, S., Fayazi, M., Feng, Z., et al. (2021) · Protein Science · doi:10.1002/pro.4213 · Cited by 210
EMPIAR: the Electron Microscopy Public Image Archive
Iudin, A., Korir, P. K., Somasundharam, S., Weyand, S. N., Cattavitello, C., Fonseca, N., Salih, O., Kleywegt, G. J., & Patwardhan, A. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1062 · Cited by 202
Bridging structural and cell biology with cryo-electron microscopy
Nogales, E., & Mahamid, J. (2024) · Nature · doi:10.1038/s41586-024-07198-2 · Cited by 220
Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold
Fontana, P., Dong, Y., Pi, X., Tong, A. B., Hecksel, C. W., Wang, L., Fu, T.-M., Bustamante, C., & Wu, H. (2022) · Science · doi:10.1126/science.abm9326 · Cited by 195
In Situ Cryo-Electron Tomography: A Post-Reductionist Approach to Structural Biology
Asano, S. M., Engel, B. D., & Baumeister, W. P. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.09.030 · Cited by 198
Focus: The interface between data collection and data processing in cryo-EM.
Biyani, N., Righetto, R., McLeod, R., Caujolle-Bert, D., Castaño-Díez, D., Goldie, K., & Stahlberg, H. (2017) · Journal of Structural Biology · doi:10.1016/j.jsb.2017.03.007 · Cited by 203
Understanding the invisible hands of sample preparation for cryo-EM
Weissenberger, G., Henderikx, R., & Peters, P. J. (2021) · Nature Methods · doi:10.1038/s41592-021-01130-6 · Cited by 183
A fully automatic method yielding initial models from high-resolution cryo-electron microscopy maps
Terwilliger, T. C., Adams, P. D., Afonine, P. V., & Sobolev, O. V. (2018) · Nature Methods · doi:10.1038/s41592-018-0173-1 · Cited by 170
How cryo‐electron microscopy and X‐ray crystallography complement each other
Wang, H., & Wang, J. (2016) · Protein Science · doi:10.1002/pro.3022 · Cited by 167
Campbell, M. G., Veesler, D., Cheng, A., Potter, C. S., & Carragher, B. O. (2015) · eLife · doi:10.7554/elife.06380 · Cited by 163
Damage-free vibrational spectroscopy of biological materials in the electron microscope
Rez, P., Aoki, T., March, K., Gur, D., Krivanek, O. L., Dellby, N., Lovejoy, T. C., Wolf, S. G., & Cohen, H. (2016) · Nature Communications · doi:10.1038/ncomms10945 · Cited by 162
Discovery and significance of protein-protein interactions in health and disease
Greenblatt, J. F., Alberts, B., & Krogan, N. J. (2024) · Cell · doi:10.1016/j.cell.2024.10.038 · Cited by 181
Pick, H. M., Alves, A. C., & Vogel, H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00777 · Cited by 160
CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin
van Pee, K., Neuhaus, A., D’Imprima, E., Mills, D. J., Kühlbrandt, W., & Yıldız, Ö. (2017) · eLife · doi:10.7554/elife.23644 · Cited by 155
Self-citationTop-down characterization of endogenous protein complexes with native proteomics
Skinner, O. S., Haverland, N. A., Fornelli, L., Melani, R. D., Do Vale, L. H. F., Seckler, H. S., Doubleday, P. F., Schachner, L. F., Srzentić, K., Kelleher, N. L., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2515 · Cited by 155
Membrane protein structural biology in the era of single particle cryo-EM
Cheng, Y. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.08.008 · Cited by 162
EMDB—the Electron Microscopy Data Bank
Turner, J., Abbott, S., Fonseca, N., Pye, R., de Oliveira, L. C., Duraisamy, A. K., Salih, O., Wang, Z., Kleywegt, G. J., Morris, K. L., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1019 · Cited by 154
Bendory, T., Bartesaghi, A., & Singer, A. (2020) · IEEE Signal Processing Magazine · doi:10.1109/msp.2019.2957822 · Cited by 153
Advances in the field of single-particle cryo-electron microscopy over the last decade
Frank, J. (2017) · Nature Protocols · doi:10.1038/nprot.2017.004 · Cited by 149
Uchański, T., Masiulis, S., Fischer, B., Kalichuk, V., López-Sánchez, U., Zarkadas, E., Weckener, M., Sente, A., Ward, P. N., Wohlkönig, A., et al. (2021) · Nature Methods · doi:10.1038/s41592-020-01001-6 · Cited by 155
Cryo-EM advances in RNA structure determination
Ma, H., Jia, X., Zhang, K., & Su, Z. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00916-0 · Cited by 151
Serial Lift-Out: sampling the molecular anatomy of whole organisms
Schiøtz, O. H., Kaiser, C. J. O., Klumpe, S., Morado, D. R., Poege, M., Schneider, J., Beck, F., Klebl, D. P., Thompson, C., & Plitzko, J. M. (2023) · Nature Methods · doi:10.1038/s41592-023-02113-5 · Cited by 146
Prokaryotic cytoskeletons: protein filaments organizing small cells
Wagstaff, J. M., & Löwe, J. (2018) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.153 · Cited by 141
Engineering strategies for rational polyketide synthase design
Klaus, M., & Grininger, M. (2018) · Natural Product Reports · doi:10.1039/c8np00030a · Cited by 142
Franken, L. E., Grünewald, K., Boekema, E. J., & Stuart, M. C. A. (2020) · Small · doi:10.1002/smll.201906198 · Cited by 144
Cryo-EM structures from sub-nl volumes using pin-printing and jet vitrification
Ravelli, R. B. G., Nijpels, F. J. T., Henderikx, R., Weissenberger, G., Thewessem, S., Gijsbers, A., Beulen, B. W. A. M. M., López‐Iglesias, C., & Peters, P. J. (2020) · Nature Communications · doi:10.1038/s41467-020-16392-5 · Cited by 139
Burley, S. K., Berman, H. M., Duarte, J. M., Feng, Z., Flatt, J. W., Hudson, B. P., Lowe, R., Peisach, E., Piehl, D. W., Rose, Y., et al. (2022) · Biomolecules · doi:10.3390/biom12101425 · Cited by 152
High-yield monolayer graphene grids for near-atomic resolution cryoelectron microscopy
Han, Y., Fan, X., Wang, H., Zhao, F., Tully, C. G., Kong, J., Yao, N., & Yan, N. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1919114117 · Cited by 138
A new method for vitrifying samples for cryoEM
Razinkov, I., Dandey, V. P., Wei, H. A., Zhang, Z., Melnekoff, D. T., Rice, W. J., Wigge, C., Potter, C. S., & Carragher, B. O. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.06.001 · Cited by 136
Structure determination of GPCRs: cryo-EM compared with X-ray crystallography
García‐Nafría, J., & Tate, C. G. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210431 · Cited by 149
Bringing Structure to Cell Biology with Cryo-Electron Tomography
Young, L. N., & Villa, E. (2023) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-111622-091327 · Cited by 131
Cianfrocco, M. A., Wong-Barnum, M., Youn, C., Wagner, R., & Leschziner, A. E. (2017) · Practice and Experience in Advanced Research Computing · doi:10.1145/3093338.3093390 · Cited by 129
Thompson, R. F., Iadanza, M. G., Hesketh, E. L., Rawson, S. D., & Ranson, N. A. (2018) · Nature Protocols · doi:10.1038/s41596-018-0084-8 · Cited by 128
ATP Synthase Diseases of Mitochondrial Genetic Origin
Dautant, A., Meier, T., Hahn, A., Tribouillard-Tanvier, D., di Rago, J.-P., & Kucharczyk, R. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00329 · Cited by 127
Laser cooling in solids: advances and prospects
Seletskiy, D. V., Epstein, R. I., & Sheik‐Bahae, M. (2016) · Reports on Progress in Physics · doi:10.1088/0034-4885/79/9/096401 · Cited by 126
High-throughput stability screening for detergent-solubilized membrane proteins
Kotov, V., Bartels, K., Veith, K., Josts, I., Subhramanyam, U. K. T., Günther, C., Labahn, J., Marlovits, T. C., Moraes, I., Tidow, H., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-46686-8 · Cited by 126
Respiratory complex I — structure, mechanism and evolution
Parey, K., Wirth, C., Vonck, J., & Zickermann, V. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.01.004 · Cited by 127
PDB ‐101: Educational resources supporting molecular explorations through biology and medicine
Zardecki, C., Dutta, S., Goodsell, D. S., Lowe, R., Voigt, M., & Burley, S. K. (2021) · Protein Science · doi:10.1002/pro.4200 · Cited by 127
Rules of Engagement: GPCRs and G Proteins
Glukhova, A., Draper-Joyce, C. J., Sunahara, R. K., Christopoulos, A., Wootten, D. L., & Sexton, P. M. (2018) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.8b00026 · Cited by 122
Structural mechanisms of transient receptor potential ion channels
Cao, E. (2020) · The Journal of General Physiology · doi:10.1085/jgp.201811998 · Cited by 119
Electron Microscopy Methods for Virus Diagnosis and High Resolution Analysis of Viruses
Richert‐Pöggeler, K. R., Franzke, K., Hipp, K., & Kleespies, R. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.03255 · Cited by 120
Time-resolved transmission electron microscopy for nanoscale chemical dynamics
Alcorn, F. M., Jain, P. K., & van der Veen, R. M. (2023) · Nature Reviews Chemistry · doi:10.1038/s41570-023-00469-y · Cited by 122
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) · eLife · doi:10.7554/elife.36615 · Cited by 121
Tailoring cryo-electron microscopy grids by photo-micropatterning for in-cell structural studies
Toro‐Nahuelpan, M., Zagoriy, I., Senger, F., Blanchoin, L., Théry, M., & Mahamid, J. (2019) · Nature Methods · doi:10.1038/s41592-019-0630-5 · Cited by 113
Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., Sivertsen, A. C., Schmidt, E. Y., Kerfah, R., Mas, G., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10490-9 · Cited by 119
García‐Nafría, J., & Tate, C. G. (2019) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010919-023545 · Cited by 126
Structural biology and molecular pharmacology of voltage-gated ion channels
Huang, J., Pan, X., & Yan, N. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00763-7 · Cited by 147
Metadata
- Authors
- Kühlbrandt, W.
- Affiliations
- Max Planck Institute of Biophysics (DE)
- Corresponding author
- Kühlbrandt, Werner
- ORCID
- Kühlbrandt, Werner
- Venue
- Science
- Published
- 2014-03-28
- Volume
- 343
- Issue
- 6178
- Pages
- 1443-1444
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2051925784
- Cited by
- 1,325
- References
- 10
- Citations by year
- 2026: 120 · 2025: 117 · 2024: 130 · 2023: 110 · 2022: 135 · 2021: 142 · 2020: 121 · 2019: 142 · 2018: 109 · 2017: 73 · 2016: 60 · 2015: 51 · 2014: 15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- cryo-electron microscopy, high-resolution structure determination, biomolecular structure, detector technology, image processing
- MeSH terms
- Mitochondria, Saccharomyces cerevisiae, Ribosome Subunits, Large, Eukaryotic
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review