The Mechanism for Activation of GTP Hydrolysis on the Ribosome

The GTPase superfamily: conserved structure and molecular mechanism

Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392

Structure of the 70S Ribosome Complexed with mRNA and tRNA

Selmer, M., Dunham, C., Murphy, F., Weixlbaumer, A., Petry, S., Kelley, A. C., Weir, J., & Ramakrishnan, V. (2006) · Science · doi:10.1126/science.1131127 · Cited by 1,352

Recognition of Cognate Transfer RNA by the 30 S Ribosomal Subunit

Ogle, J. M., Brodersen, D. E., Clemons, W. M., Tarry, M. J., Carter, A. P., & Ramakrishnan, V. (2001) · Science · doi:10.1126/science.1060612 · Cited by 1,162

Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin

Blow, D. M., Birktoft, J. J., & Hartley, B. S. (1969) · Nature · doi:10.1038/221337a0 · Cited by 1,069

Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog

Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L. S., Clark, B. F. C., & Nyborg, J. (1995) · Science · doi:10.1126/science.270.5241.1464 · Cited by 851

Structure of RGS4 Bound to AlF4−-Activated Giα1: Stabilization of the Transition State for GTP Hydrolysis

Tesmer, J. J. G., Berman, D. M., Gilman, A. G., & Sprang, S. R. (1997) · Cell · doi:10.1016/s0092-8674(00)80204-4 · Cited by 782

GTP-binding domain: three consensus sequence elements with distinct spacing.

Dever, T. E., Glynias, M. J., & Merrick, W. C. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.7.1814 · Cited by 603

The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA

Schmeing, T. M., Voorhees, R. M., Kelley, A. C., Gao, Y., Murphy, F. V., Weir, J. R., & Ramakrishnan, V. (2009) · Science · doi:10.1126/science.1179700 · Cited by 557

Crystal structure of active elongation factor Tu reveals major domain rearrangements

Berchtold, H., Reshetnikova, L. S., Reiser, C. O. A., Schirmer, N. K., Sprinzl, M., & Hilgenfeld, R. (1993) · Nature · doi:10.1038/365126a0 · Cited by 523

Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue

Rittinger, K., Walker, P. A., Eccleston, J. F., Smerdon, S. J., & Gamblin, S. J. (1997) · Nature · doi:10.1038/39651 · Cited by 490

Structural dynamics of translation elongation factor Tu during aa-tRNA delivery to the ribosome

Kavaliauskas, D., Chen, C., Liu, W., Cooperman, B. S., Goldman, Y. E., & Knudsen, C. R. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky651 · Cited by 19

Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations

Maruyama, K., Imai, H., Kawamura, M., Ishino, S., Ishino, Y., Ito, K. R., & Uchiumi, T. (2019) · Scientific Reports · doi:10.1038/s41598-019-51266-x · Cited by 19

Translation initiation and its relevance in colorectal cancer

Minnee, E., & Faller, W. J. (2020) · FEBS Journal · doi:10.1111/febs.15690 · Cited by 20

A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases

Wang, L., Fang, Y., Zhang, D., Chen, Z., Xu, R.-M., Nierhaus, K. H., Gong, W., & Qin, Y. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2254 · Cited by 19

Fast fitting to low resolution density maps: elucidating large-scale motions of the ribosome

Flores, S. C. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt906 · Cited by 18

Structural Insights into tRNA Dynamics on the Ribosome

Agirrezabala, X., & Valle, M. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16059866 · Cited by 21

Probing the Translation Dynamics of Ribosomes Using Zero-Mode Waveguides

Tsai, A., Puglisi, J. D., & Uemura, S. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.10.006 · Cited by 18

Bioinformatics and Molecular Dynamics Simulation Study of L1 Stalk Non-Canonical rRNA Elements: Kink-Turns, Loops, and Tetraloops

Krepl, M., Réblová, K., Koča, J., & Šponer, J. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp401482m · Cited by 18

The central role of transfer RNAs in mistranslation

Schuntermann, D. B., Jaskółowski, M., Reynolds, N. M., & Vargas‐Rodriguez, O. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107679 · Cited by 17

Recent Advances in Understanding Biological GTP Hydrolysis through Molecular Simulation

Calixto, A. R., Moreira, C., & Kamerlin, S. C. L. (2020) · ACS Omega · doi:10.1021/acsomega.0c00240 · Cited by 17

Genetic code degeneracy is established by the decoding center of the ribosome

Ye, S., & Lehmann, J. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac171 · Cited by 17

Distinct functional classes of ram mutations in 16S rRNA

McClory, S. P., Devaraj, A., & Fredrick, K. (2014) · RNA · doi:10.1261/rna.043331.113 · Cited by 17

Mutations in the G-domain of Ski7 cause specific dysfunction in non-stop decay

Horikawa, W., Endo, K., WADA, M., & Ito, K. (2016) · Scientific Reports · doi:10.1038/srep29295 · Cited by 17

The ribosomal stalk protein is crucial for the action of the conserved ATPase ABCE1

Imai, H., Abe, T., Miyoshi, T., Nishikawa, S., Ito, K. R., & Uchiumi, T. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky619 · Cited by 17

Integrative approaches in cryogenic electron microscopy: Recent advances in structural biology and future perspectives

Banerjee, A., Bhakta, S., & Sengupta, J. (2021) · iScience · doi:10.1016/j.isci.2021.102044 · Cited by 16

Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome

Kumar, V., Ero, R., Ahmed, T. U., Goh, K. J., Yin, Z., Bhushan, S., & Gao, Y. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.725945 · Cited by 16

Exploring allosteric communication in multiple states of the bacterial ribosome using residue network analysis

Kürkçüoğlu, Ö. (2018) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-1802-77 · Cited by 16

Ribosomal ambiguity ( ram ) mutations promote the open (off) to closed (on) transition and thereby increase miscoding

Hoffer, E. D., Maehigashi, T., Fredrick, K. L., & Dunham, C. M. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1178 · Cited by 16

Structures of the ribosome bound to EF-Tu–isoleucine tRNA elucidate the mechanism of AUG avoidance

Rybak, M. Y., & Gagnon, M. G. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01236-3 · Cited by 15

Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome

Jetzt, A. E., Li, X.-P., Tumer, N. E., & Cohick, W. S. (2016) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2016.09.004 · Cited by 15

A genetic approach for analyzing the co-operative function of the tRNA mimicry complex, eRF1/eRF3, in translation termination on the ribosome

WADA, M., & Ito, K. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku493 · Cited by 15

An ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaea

Atkinson, G. C., Hauryliuk, V., & Tenson, T. (2011) · BMC Evolutionary Biology · doi:10.1186/1471-2148-11-22 · Cited by 15

Biochemical aspects of bacterial strategies for handling the incomplete translation processes

Shimizu, Y. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00170 · Cited by 15

Substrate-Induced Formation of Ribosomal Decoding Center for Accurate and Rapid Genetic Code Translation

Pavlov, M. Y., & Ehrenberg, M. (2018) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-060414-034148 · Cited by 15

Decoding on the ribosome depends on the structure of the mRNA phosphodiester backbone

Keedy, H. E., Thomas, E. N., & Zaher, H. S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721431115 · Cited by 15

Structure of an archaeal ribosome reveals a divergent active site and hibernation factor

Nissley, A. J., Shulgina, Y., Kivimae, R. W., Downing, B. E., Penev, P. I., Banfield, J. F., Nayak, D. D., & Cate, J. H. D. (2025) · Nature Microbiology · doi:10.1038/s41564-025-02065-w · Cited by 14

Abasic RNA: its formation and potential role in cellular stress response

Prashar, T., Selle, F. D. L., & Hudak, K. A. (2023) · RNA Biology · doi:10.1080/15476286.2023.2223466 · Cited by 18

Histidine 66 in Escherichia coli Elongation Factor Tu Selectively Stabilizes Aminoacyl-tRNAs

Chapman, S. J., Schrader, J. M., & Uhlenbeck, O. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.294850 · Cited by 14

A mutation in the ribosomal protein uS12 reveals novel functions of its universally conserved PNSA loop

Datta, M., Pillai, M., Modak, M. J., Liiv, A., Khaja, F. T., Hussain, T., Rèmme, J., & Varshney, U. (2020) · Molecular Microbiology · doi:10.1111/mmi.14675 · Cited by 14

Gut colonization by Bacteroides requires translation by an EF‐G paralog lacking GTPase activity

Han, W., Peng, B., Wang, C., Townsend, G. E., Barry, N. A., Peske, F., Goodman, A. L., Liu, J., Rodnina, M. V., & Groisman, E. A. (2022) · The EMBO Journal · doi:10.15252/embj.2022112372 · Cited by 14

Conformational transitions in the γ subunit of the archaeal translation initiation factor 2

Nikonov, O. S., Stolboushkina, E. A., Arkhipova, V., Kravchenko, O. V., Nikonov, S. V., & Garber, M. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004713032240 · Cited by 14

The Interface between Escherichia coli Elongation Factor Tu and Aminoacyl-tRNA

Yikilmaz, E., Chapman, S. J., Schrader, J. M., & Uhlenbeck, O. C. (2014) · Biochemistry · doi:10.1021/bi500533x · Cited by 14

Free energy calculations of RNA interactions

Lind, C., Esguerra, M., Jespers, W., Satpati, P., Gutiérrez‐de‐Terán, H., & Åqvist, J. (2019) · Methods · doi:10.1016/j.ymeth.2019.02.014 · Cited by 14

Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding

Girodat, D. J., Wieden, H., Blanchard, S. C., & Sanbonmatsu, K. Y. (2023) · Nature Communications · doi:10.1038/s41467-023-40404-9 · Cited by 15

Functional role of the C ‐terminal tail of the archaeal ribosomal stalk in recruitment of two elongation factors to the sarcin/ricin loop of 23S r RNA

Imai, H., Miyoshi, T., Murakami, R., Ito, K. R., Ishino, Y., & Uchiumi, T. (2015) · Genes to Cells · doi:10.1111/gtc.12256 · Cited by 13

Functional Replacement of Two Highly Conserved Tetraloops in the Bacterial Ribosome

Sahu, B., Khade, P. K., & Joseph, S. (2012) · Biochemistry · doi:10.1021/bi300930r · Cited by 12

Centers of motion associated with EF-Tu binding to the ribosome

Paci, M., & Fox, G. E. (2016) · RNA Biology · doi:10.1080/15476286.2015.1114204 · Cited by 12

The mechanism of translation

Frank, J. (2017) · F1000Research · doi:10.12688/f1000research.9760.1 · Cited by 12

Functional divergence between the two P1–P2 stalk dimers on the ribosome in their interaction with ricin A chain

Grela, P., Li, X., Tchórzewski, M., & Tumer, N. E. (2014) · Biochemical Journal · doi:10.1042/bj20140014 · Cited by 12

The influence of ricin-mediated rRNA depurination on the translational machinery in vivo - New insight into ricin toxicity

Szajwaj, M., Wawiórka, L., Molestak, E., Michalec‐Wawiórka, B., Mołoń, M., Wojda, I., & Tchórzewski, M. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118554 · Cited by 12

Thermus thermophilus 70S containing 16S G299A point mutation and near-cognate ASL Leucine in A site.

Hoffer, E. D., Maehigashi, T., Fagan, C. E., & Dunham, C. M. (2017) · Worldwide Protein Data Bank · doi:10.2210/pdb6bz7/pdb · Cited by 12

Conservation of mRNA quality control factor Ski7 and its diversification through changes in alternative splicing and gene duplication

Marshall, A. N., Han, J., Kim, M., & van Hoof, A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1801997115 · Cited by 11

Novel small molecule retrograde transport blocker confers post-exposure protection against ricin intoxication

Zhao, X., Li, H., Li, J., Liu, K., Wang, B., Wang, Y., Li, X., & Zhong, W. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.08.005 · Cited by 10

Looking for a sequence based allostery definition: A statistical journey at different resolution scales

Namboodiri, S., Giuliani, A., Nair, A. S., & Dhar, P. K. (2012) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2012.03.005 · Cited by 10

The Acidic Ribosomal Stalk Proteins Are Not Required for the Highly Specific Inactivation Exerted by α-Sarcin of the Eukaryotic Ribosome

Olombrada, M., Rodríguez-Mateos, M., Prieto, D., Plá, J., Remacha, M., Martínez‐del‐Pozo, Á., Gavilanes, J. G., Ballesta, J. P. G., & Garciá‐Ortega, L. (2014) · Biochemistry · doi:10.1021/bi401470u · Cited by 10

The role of dysregulated mRNA translation machinery in cancer pathogenesis and therapeutic value of ribosome-inactivating proteins

Jia, W., Yuan, J., Li, S., & Cheng, B. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.189018 · Cited by 9

Structure and Switch Cycle of SRβ as Ancestral Eukaryotic GTPase Associated with Secretory Membranes

Jadhav, B., Wild, K., Pool, M., & Sinning, I. (2015) · Structure · doi:10.1016/j.str.2015.07.010 · Cited by 9

A Central Interdomain Protein Joint in Elongation Factor G Regulates Antibiotic Sensitivity, GTP Hydrolysis, and Ribosome Translocation

Ticu, C., Murataliev, M. B., Nechifor, R., & Wilson, K. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.214056 · Cited by 9

Crippling the Essential GTPase Der Causes Dependence on Ribosomal Protein L9

Naganathan, A., & Moore, S. D. (2013) · Journal of Bacteriology · doi:10.1128/jb.00464-13 · Cited by 9

Labeled EF-Tus for Rapid Kinetic Studies of Pretranslocation Complex Formation

Liu, W., Kavaliauskas, D., Schrader, J. M., Poruri, K., Birkedal, V., Goldman, E., Jakubowski, H., Mandecki, W., Uhlenbeck, O. C., Knudsen, C. R., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb500409y · Cited by 9

Heterologous Inferential Analysis (HIA) as a Method to Understand the Role of Mitochondrial rRNA Mutations in Pathogenesis

Elson, J. L., Smith, P., & Vila‐Sanjurjo, A. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2257-4_32 · Cited by 9

Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP

Carbone, C. E., Loveland, A. B., Gamper, H., Hou, Y., Demo, G., & Korostelev, A. A. (2021) · The Medicine Forum · Cited by 9

Mechanisms of decoding and peptide bond formation

Rodnina, M. V. (2011) · Springer eBooks · doi:10.1007/978-3-7091-0215-2_16 · Cited by 8

The Ribotoxin Restrictocin Recognizes Its RNA Substrate by Selective Engagement of Active Site Residues

Plantinga, M. J., Korennykh, A. V., Piccirilli, J. A., & Correll, C. C. (2011) · Biochemistry · doi:10.1021/bi1018336 · Cited by 8

Phenotypic Suppression of Streptomycin Resistance by Mutations in Multiple Components of the Translation Apparatus

Carr, J. F., Lee, H. J., Jaspers, J. B., Dahĺberg, A. E., Jogl, G., & Gregory, S. T. (2015) · Journal of Bacteriology · doi:10.1128/jb.00219-15 · Cited by 7

Recent structural studies on Dom34/aPelota and Hbs1/aEF1α: important factors for solving general problems of ribosomal stall in translation

Kobayashi, K., Ishitani, R., & Nureki, O. (2013) · BIOPHYSICS · doi:10.2142/biophysics.9.131 · Cited by 7

Ricin in Castor Bean (Ricinus communis L.) Seeds: A Review on its Anticancer Activity and The Role of Cytotoxicity Enhancers

Herawati, I. E., Levita, J., Lesmana, R., & Subarnas, A. (2022) · Research Journal of Pharmacy and Technology · doi:10.52711/0974-360x.2022.00067 · Cited by 7

Deciphering the Genetic Code: Mechanisms, Evolution, and Implications for Biotechnology

Abdulsalam, M., Ubah, F. Z. Y., Ahmed, H. U., Tafida, U. A., & Nasir, A. W. (2024) · World Journal of Advanced Research and Reviews · doi:10.30574/wjarr.2024.21.1.2195 · Cited by 7

Electrostatic free energies in translational GTPases: Classic allostery and the rest

Simonson, T., Aleksandrov, A. V., & Satpati, P. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.07.006 · Cited by 7

Ribosomal ambiguity made less ambiguous

Moore, P. B. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1307288110 · Cited by 7

Nucleotide recognition by the initiation factor aIF5B: Free energy simulations of a neoclassical GTPase

Simonson, T., & Satpati, P. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24158 · Cited by 7

Flipping through the Genetic Code: New Developments in Discrimination between Cognate and Near-Cognate tRNAs and the Effect of Antibiotics

Sanbonmatsu, K. Y. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.07.005 · Cited by 6

Viewing the Mechanisms of Translation through the Computational Microscope

Gumbart, J. C., Schreiner, E., Trabuco, L. G., Chan, K. Y., & Schulten, K. (2011) · Cambridge University Press eBooks · doi:10.1017/cbo9781139003704.010 · Cited by 6

Water clusters in the nucleotide-binding pocket of the protein aIF2γ from the archaeon Sulfolobus solfataricus: Proton transmission

Nikonov, O. S., Kravchenko, O. V., Arkhipova, V., Stolboushkina, E. A., Nikonov, S. V., & Garber, M. (2015) · Biochimie · doi:10.1016/j.biochi.2015.11.029 · Cited by 6

Nucleobases Undergo Dynamic Rearrangements during RNA Tertiary Folding

Welty, R. S., & Hall, K. B. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.09.015 · Cited by 6

Tetracycline does not directly inhibit the function of bacterial elongation factor Tu

Gzyl, K. E., & Wieden, H. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178523 · Cited by 6

Hydroxylation of Protein Constituents of the Human Translation System: Structural Aspects and Functional Assignments

Graifer, D. M., Malygin, A. A., & Karpova, G. G. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2018-0317 · Cited by 6

Structural basis of elongation factor 2 switching

Fenwick, M. K., & Ealick, S. E. (2020) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2020.02.001 · Cited by 6

Translocation at work

Achenbach, J., & Nierhaus, K. H. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2661 · Cited by 6

Structural studies on decoding, termination and translocation in the bacterial ribosome

Ramakrishnan, V. (2011) · Springer eBooks · doi:10.1007/978-3-7091-0215-2_2 · Cited by 6

Heterologous Inferential Analysis (HIA) and Other Emerging Concepts: In Understanding Mitochondrial Variation In Pathogenesis: There is no More Low-Hanging Fruit

Vila‐Sanjurjo, A., Smith, P., & Elson, J. L. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1270-5_14 · Cited by 6

Human protein synthesis requires aminoacyl-tRNA pivoting during proofreading

Sapkota, D., Sanbonmatsu, K. Y., & Girodat, D. J. (2025) · Nature Communications · doi:10.1038/s41467-025-63617-6 · Cited by 5

How KRAS Mutations Impair Intrinsic GTP Hydrolysis: Experimental and Computational Investigations

Song, L. F., Rabara, D., Bali, S. K., Pei, J., Lau, E. Y., Kirshner, D. A., Lightstone, F. C., McCormick, F., Stephen, A. G., & Yang, Y. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c02061 · Cited by 7

In vitro anticancer effects of recombinant anisoplin through activation of SAPK/JNK and downregulation of NFκB

Patra, A., Kandasamy, T., Ghosh, S. S., & Saini, G. K. (2023) · Toxicology in Vitro · doi:10.1016/j.tiv.2023.105737 · Cited by 5

The ribonucleolytic activity of the ribotoxin α-sarcin is not essential for in vitro protein biosynthesis inhibition

Álvarez-García, E., Diago‐Navarro, E., Herrero‐Galán, E., Garciá‐Ortega, L., López-Villarejo, J., Olmo, N., Díaz‐Orejas, R., Gavilanes, J. G., & Martínez‐del‐Pozo, Á. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.06.017 · Cited by 5

The third structural switch in the archaeal translation initiation factor 2 (aIF2) molecule and its possible role in the initiation of GTP hydrolysis and the removal of aIF2 from the ribosome

Nikonov, O. S., Kravchenko, O. V., Nevskaya, N. A., Stolboushkina, E. A., Garber, M., & Nikonov, S. V. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319002304 · Cited by 5

Translation machinery captured in motion

Zafar, H., Hassan, A. H., & Demo, G. (2023) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1792 · Cited by 5

Highly Conserved Base A55 of 16S Ribosomal RNA Is Important for the Elongation Cycle of Protein Synthesis

Sahu, B., Khade, P. K., & Joseph, S. (2013) · Biochemistry · doi:10.1021/bi4008879 · Cited by 5

Network theory of the bacterial ribosome

Calvet, L. E., Matviienko, S., & Ducluzaux, P. (2020) · PLoS ONE · doi:10.1371/journal.pone.0239700 · Cited by 5

Linking interpersonal differences in gut microbiota composition and drug biotransformation activityPreprint

Mastrorilli, E., Herd, P., Rey, F. E., Goodman, A. L., & Zimmermann, M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.21.700809 · Cited by 5

Sports Participation Promotes Beneficial Adaptations in the Erythrocyte Guanylate Nucleotide Pool in Male Athletes Aged 20–90 Years

Pospieszna, B., Kusy, K., Slominska, E. M., Ciekot-Sołtysiak, M., & Zieliński, J. (2023) · Clinical Interventions in Aging · doi:10.2147/cia.s406555 · Cited by 4

The ribosome termination complex remodels release factor RF3 and ejects GDP

Li, L., Rybak, M. Y., Lin, J., & Gagnon, M. G. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01360-0 · Cited by 4

Nucleotides and nucleic acids; oligo- and polynucleotides

Loakes, D. (2012) · Royal Society of Chemistry eBooks · doi:10.1039/9781849734875-00169 · Cited by 4

Epistasis analysis of 16S rRNA ram mutations helps define the conformational dynamics of the ribosome that influence decoding

Ying, L., & Fredrick, K. L. (2016) · RNA · doi:10.1261/rna.054486.115 · Cited by 4

Fatal Attraction: Ricinus communis Provides an Attractive but Risky Mating Site for Holotrichia parallela Beetles

Zhang, H., Li, W., Luo, Q., Yang, L., Gong, D.-F., Teng, X., Guo, X., & GuoHui, Y. (2018) · Journal of Chemical Ecology · doi:10.1007/s10886-018-0994-5 · Cited by 4

Mechanism of Translation in Eukaryotes

Villa, N., & Fraser, C. S. (2014) · Springer eBooks · doi:10.1007/978-94-017-9078-9_2 · Cited by 4

Nonhydrolysable Analogues of (p)ppGpp and (p)ppApp Alarmone Nucleotides as Novel Molecular Tools

Mojr, V., Roghanian, M., Tamman, H., Pham, D. D. D., Petrová, M., Pohl, R., Takada, H., Nerom, K. V., Ainelo, H., Caballero-Montes, J., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00398 · Cited by 4

Ribosomal RNAs and Protein Synthesis

Joseph, S. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10054-9 · Cited by 4

Translocation in Action

Rodnina, M. V. (2013) · Science · doi:10.1126/science.1240090 · Cited by 4

Another Look at Mutations in Ribosomal Protein S4 Lends Strong Support to the Domain Closure Model

Fredrick, K. L. (2014) · Journal of Bacteriology · doi:10.1128/jb.02579-14 · Cited by 4

The Ribosome and Protein Synthesis

Huter, P., Graf, M., & Wilson, D. N. (2021) · Wiley eBooks · doi:10.1002/9783527814527.ch8 · Cited by 4

The promiscuous ribosomal P-stalk: a new functional portrait

Tchórzewski, M., & Michalec‐Wawiórka, B. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.09.003 · Cited by 3

Precise Steric Features Control Aminoacyl-tRNA Accommodation on the Ribosome

Wang, Y., Wang, A., Mohanty, U., & Whitford, P. C. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c05513 · Cited by 3

D-stem mutation in an essential tRNA increases translation speed at the cost of fidelity

Schrock, M. N., Parsawar, K., Hughes, K. T., & Chevance, F. F. V. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011569 · Cited by 3

Computational physical organic chemistry using the empirical valence bond approach

Kulkarni, Y., & Kamerlin, S. C. L. (2019) · Advances in physical organic chemistry · doi:10.1016/bs.apoc.2019.07.001 · Cited by 3

Analysis of the Sequence Preference of Saporin by Deep Sequencing

Hauf, S., Rotrattanadumrong, R., & Yokobayashi, Y. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00531 · Cited by 3

A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle

McQuown, A. J., Nelliat, A. R., Reif, D., Sabbarini, I. M., Membreno, B. S., Wu, C. C., & Denic, V. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.07.028 · Cited by 3

Lensless coherent imaging of proteins and supramolecular assemblies: Efficient phase retrieval by the charge flipping algorithm

Dumas, C., van der Lee, A., & Palatinus, L. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.01.008 · Cited by 3

Solution NMR structure of the ribosomal protein RP‐L35Ae from Pyrococcus furiosus

Snyder, D. A., Aramini, J. M., Yu, B., Huang, Y. J., Xiao, R., Cort, J., Shastry, R., Ma, L., Liu, J., Rost, B., et al. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24071 · Cited by 3

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Carbone, C. E., Loveland, A. B., Gamper, H., Hou, Y., Demo, G., & Korostelev, A. A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.31.446434 · Cited by 4

A Likely Conformation

(2010) · Science · doi:10.1126/science.330.6005.729-g

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Åqvist, J., & Kamerlin, S. C. L. (2014) · Biochemistry · doi:10.1021/bi501373g · Cited by 34

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

Villa, E., Sengupta, J., Trabuco, L. G., LeBarron, J., Baxter, W. T., Shaikh, T. R., Grassucci, R. A., Nissen, P., Ehrenberg, M., Schulten, K. J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811370106 · Cited by 232

Comment on “The Mechanism for Activation of GTP Hydrolysis on the Ribosome”

Liljas, A., Ehrenberg, M., & Åqvist, J. (2011) · Science · doi:10.1126/science.1202472 · Cited by 42

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