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Ribosomal proteins: Structure, function, and evolution
Abstract
The question concerning reasons for the variety of ribosomal proteins that arose for more than 40 years ago is still open. Ribosomes of modern organisms contain 50-80 individual proteins. Some are characteristic for all domains of life (universal ribosomal proteins), whereas others are specific for bacteria, archaea, or eucaryotes. Extensive information about ribosomal proteins has been obtained since that time. However, the role of the majority of ribosomal proteins in the formation and functioning of the ribosome is still not so clear. Based on recent data of experiments and bioinformatics, this review presents a comprehensive evaluation of structural conservatism of ribosomal proteins from evolutionarily distant organisms. Considering the current knowledge about features of the structural organization of the universal proteins and their intermolecular contacts, a possible role of individual proteins and their structural elements in the formation and functioning of ribosomes is discussed. The structural and functional conservatism of the majority of proteins of this group suggests that they should be present in the ribosome already in the early stages of its evolution.
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“Four of the overlapping putative targets with the highest betweenness centrality play a role in protein translation [82, 83] (RPL3, EIF4A2), MAPK signaling (MAPK3) and p53 signaling [84] (DAZAP2) (Fig. 5E) (Supplementary Table 7).”
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Cites
Construction of Escherichia coli K‐12 in‐frame, single‐gene knockout mutants: the Keio collection
Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., Datsenko, K. A., Tomita, M., Wanner, B. L., & Mori, H. (2006) · Molecular Systems Biology · doi:10.1038/msb4100050 · Cited by 7,858
ExPASy: the proteomics server for in-depth protein knowledge and analysis
Gasteiger, E. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg563 · Cited by 5,595
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
The Structural Basis of Ribosome Activity in Peptide Bond Synthesis
Nissen, P., Hansen, J., Ban, N., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.920 · Cited by 2,269
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
Crystal structure of the ribosome at 5.5 Å resolution
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944
Structures of the Bacterial Ribosome at 3.5 Å Resolution
Schuwirth, B. S., Borovinskaya, M. A., Hau, C. W., Zhang, W., Vila-Sanjurjo, A., Holton, J. M., & Cate, J. H. D. (2005) · Science · doi:10.1126/science.1117230 · Cited by 1,418
Structure of the 70 S Ribosome Complexed with mRNA and tRNA
Selmer, M., Dunham, C. M., Murphy, F. V., Weixlbaumer, A., Petry, S., Kelley, A. C., Weir, J. R., & Ramakrishnan, V. (2006) · Science · doi:10.1126/science.1131127 · Cited by 1,283
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
The Structure of the Eukaryotic Ribosome at 3.0 Å Resolution
Ben-Shem, A., Garreau de Loubresse, N., Melnikov, S., Jenner, L., Yusupova, G., & Yusupov, M. (2011) · Science · doi:10.1126/science.1212642 · Cited by 1,134
A minimal gene set for cellular life derived by comparison of complete bacterial genomes
Mushegian, A. R., & Koonin, E. V. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.19.10268 · Cited by 916
High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium
Harms, J., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Franceschi, F., & Yonath, A. (2001) · Cell · doi:10.1016/s0092-8674(01)00546-3 · Cited by 901
Structure, Function, and Genetics of Ribosomes
(1986) · Springer Series in Molecular Biology · doi:10.1007/978-1-4612-4884-2 · Cited by 849
A ratchet-like inter-subunit reorganization of the ribosome during translocation
Frank, J., & Agrawal, R. K. (2000) · Nature · doi:10.1038/35018597 · Cited by 799
Benson, D. A., Karsch-Mizrachi, I., Lipman, D. J., Ostell, J., & Wheeler, D. L. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm929 · Cited by 774
Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form
Ogle, J. M., Murphy, F. V., Tarry, M. J., & Ramakrishnan, V. (2002) · Cell · doi:10.1016/s0092-8674(02)01086-3 · Cited by 663
The Path of Messenger RNA through the Ribosome
Yusupova, G. Z., Yusupov, M. M., Cate, J. H. D., & Noller, H. F. (2001) · Cell · doi:10.1016/s0092-8674(01)00435-4 · Cited by 600
Locking and Unlocking of Ribosomal Motions
Valle, M., Zavialov, A., Sengupta, J., Rawat, U., Ehrenberg, M., & Frank, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00476-8 · Cited by 577
The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA
Schmeing, T. M., Voorhees, R. M., Kelley, A. C., Gao, Y.-G., Murphy, F. V., Weir, J. R., & Ramakrishnan, V. (2009) · Science · doi:10.1126/science.1179700 · Cited by 546
The Ribosome : structure, function, and evolution
Hill, W. E. (1990) · Medical Entomology and Zoology · Cited by 521
The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State
Gao, Y.-G., Selmer, M., Dunham, C. M., Weixlbaumer, A., Kelley, A. C., & Ramakrishnan, V. (2009) · Science · doi:10.1126/science.1179709 · Cited by 513
Spahn, C. M. T., Beckmann, R., Eswar, N., Penczek, P. A., Sali, A., Blobel, G., & Frank, J. (2001) · Cell · doi:10.1016/s0092-8674(01)00539-6 · Cited by 502
Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA
Moazed, D., Robertson, J. M., & Noller, H. F. (1988) · Nature · doi:10.1038/334362a0 · Cited by 483
Assembly Mapping of 30 S Ribosomal Proteins from Escherichia coli
Held, W. A., Ballou, B., Mizushima, S., & Nomura, M. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42644-6 · Cited by 424
Klein, D. J., Moore, P. B., & Steitz, T. A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.03.076 · Cited by 422
Traub, P., & Nomura, M. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.59.3.777 · Cited by 409
Ribosome Biogenesis and the Translation Process in Escherichia coli
Kaczanowska, M., & Rydén-Aulin, M. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00013-07 · Cited by 400
Voorhees, R. M., Weixlbaumer, A., Loakes, D., Kelley, A. C., & Ramakrishnan, V (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1577 · Cited by 371
Brodersen, D. E., Clemons, W. M., Carter, A. P., Wimberly, B. T., & Ramakrishnan, V. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5359 · Cited by 364
AEvarsson, A., Brazhnikov, E., Garber, M., Zheltonosova, J., Chirgadze, Y., al‐Karadaghi, S., Svensson, L. A., & Liljas, A. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06676.x · Cited by 363
Self-citationHamel, E., Koka, M., & Nakamoto, T. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45679-2 · Cited by 362
Lecompte, O. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf693 · Cited by 359
Crystal Structure of the Eukaryotic 60 S Ribosomal Subunit in Complex with Initiation Factor 6
Klinge, S., Voigts-Hoffmann, F., Leibundgut, M., Arpagaus, S., & Ban, N. (2011) · Science · doi:10.1126/science.1211204 · Cited by 359
A Detailed View of a Ribosomal Active Site
Wimberly, B. T., Guymon, R., McCutcheon, J. P., White, S. W., & Ramakrishnan, V (1999) · Cell · doi:10.1016/s0092-8674(00)80759-x · Cited by 332
Agrawal, R. K., Penczek, P., Grassucci, R. A., & Frank, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6134 · Cited by 325
Structure and evolution of mammalian ribosomal proteins
Wool, I. G., Chan, Y.-L., & Glück, A. (1995) · Biochemistry and Cell Biology · doi:10.1139/o95-101 · Cited by 315
Kaltschmidt, E., & Wittmann, H. G. (1970) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.67.3.1276 · Cited by 303
RIBOSOMAL GENES IN ESCHERICHIA COLI
Lindahl, L., & Zengel, J. M. (1986) · Annual Review of Genetics · doi:10.1146/annurev.ge.20.120186.001501 · Cited by 301
A minimal gene set for cellular life derived by comparison of complete bacterial genomes
Mushegian (1996) · Medical Entomology and Zoology · Cited by 294
Study of the Structural Dynamics of the E. coli 70S Ribosome Using Real-Space Refinement
Gao, H., Sengupta, J., Valle, M., Korostelev, A., Eswar, N., Stagg, S. M., Van Roey, P., Agrawal, R. K., Harvey, S. C., Sali, A., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00427-6 · Cited by 288
RNA-Protein Interactions in 30 S Ribosomal Subunits: Folding and Function of 16 S rRNA
Stern, S., Powers, T., Changchien, L.-M., & Noller, H. F. (1989) · Science · doi:10.1126/science.2658053 · Cited by 285
Catalysis of peptide bond formation by 50 s ribosomal subunits from Escherichia coli
Monro, R. E. (1967) · Journal of Molecular Biology · doi:10.1016/0022-2836(67)90271-9 · Cited by 276
Structural basis for messenger RNA movement on the ribosome
Yusupova, G., Jenner, L., Rees, B., Moras, D., & Yusupov, M. (2006) · Nature · doi:10.1038/nature05281 · Cited by 264
The Plastid Ribosomal Proteins
Yamaguchi, K., von Knoblauch, K., & Subramanian, A. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004350200 · Cited by 261
Total Reconstitution of Functionally Active 50S Ribosomal Subunits from Escherichia coli
Nierhaus, K. H., & Dohme, F. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.12.4713 · Cited by 258
An assembly landscape for the 30S ribosomal subunit
Talkington, M. W. T., Siuzdak, G. E., & Williamson, J. R. (2005) · Nature · doi:10.1038/nature04261 · Cited by 256
Structure-based analysis of protein-RNA interactions using the program ENTANGLE
Allers, J., & Shamoo, Y. E. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4857 · Cited by 244
The Plastid Ribosomal Proteins
Yamaguchi, K., & Subramanian, A. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005012200 · Cited by 241
The assembly of prokaryotic ribosomes
Nierhaus, K. H. (1991) · Biochimie · doi:10.1016/0300-9084(91)90054-5 · Cited by 235
The Weird and Wonderful World of Bacterial Ribosome Regulation
Wilson, D. N., & Nierhaus, K. H. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701360843 · Cited by 221
Hydroxyl radical footprinting of ribosomal proteins on 16S rRNA.
Powers, T., & Noller, H. F. (1995) · PubMed · Cited by 219
Components of Bacterial Ribosomes
Wittmann, H. G. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.001103 · Cited by 215
Hyper‐accurate ribosomes inhibit growth.
Ruusala, T., Andersson, D. I., Ehrenberg, M., & Kurland, C. G. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02176.x · Cited by 213
Visualizing Ribosome Biogenesis: Parallel Assembly Pathways for the 30 S Subunit
Mulder, A. M., Yoshioka, C., Beck, A. H., Bunner, A. E., Milligan, R. A., Potter, C. S., Carragher, B. O., & Williamson, J. R. (2010) · Science · doi:10.1126/science.1193220 · Cited by 196
STUDIES ON THE COMPOSITION OF THE PROTEIN FROM ESCHERICHIA COLI RIBOSOMES
Waller, J. P., & Harris, J. I. (1961) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.47.1.18 · Cited by 194
The ribosome: Structure, function and evolution
Cox, R. A. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80412-v · Cited by 194
Assembly map of the large subunit (50S) of Escherichia coli ribosomes.
Röhl, R., & Nierhaus, K. H. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.3.729 · Cited by 193
Reconstructing the evolution of the mitochondrial ribosomal proteome
Smits, P., Smeitink, J. A. M., van den Heuvel, L. P., Huynen, M. A., & Ettema, T. J. G. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm441 · Cited by 187
Modeling a Minimal Ribosome Based on Comparative Sequence Analysis
Mears, J. A., Cannone, J. J., Stagg, S. M., Gutell, R. R., Agrawal, R. K., & Harvey, S. C. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00568-5 · Cited by 158
Identification of a site on 23S ribosomal RNA located at the peptidyl transferase center.
Barta, A., Steiner, G. E., Brosius, J., Noller, H. F., & Kuechler, E. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.12.3607 · Cited by 144
The binding site for ribosomal protein L11 within 23 S ribosomal RNA of Escherichia coli.
Schmidt, F. J., Thompson, J. E., Lee, K., Dijk, J., & Cundliffe, E. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43270-x · Cited by 138
Tracing the evolution of RNA structure in ribosomes
Caetano‐Anollés, G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.11.2575 · Cited by 121
Structure and function of bacterial ribosomes
Nashimoto, H., Held, W. A., Kaltschmidt, E., & Nomura, M. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90135-5 · Cited by 115
Bubunenko, M. G., Baker, T., & Court, D. L. (2007) · Journal of Bacteriology · doi:10.1128/jb.01713-06 · Cited by 114
Spillmann, S., Dohme, F., & Nierhaus, K. H. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90168-1 · Cited by 113
Maguire, B. A., Beniaminov, A. D., Ramu, H., Mankin, A. S., & Zimmermann, R. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.009 · Cited by 112
Niebhaus, K. H., Bordasch, K., & Homann, H. E. (1973) · Journal of Molecular Biology · doi:10.1016/0022-2836(73)90049-1 · Cited by 111
Dontsova, O. А., Kopylov, A. M., & Brimacombe, R. L. C. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07803.x · Cited by 107
Belova, L., Tenson, T., Xiong, L., McNicholas, P. M., & Mankin, A. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071527498 · Cited by 99
Held, W. A., & Nomura, M. (1973) · Biochemistry · doi:10.1021/bi00741a020 · Cited by 99
Walsh, T. P., Webber, C., Searle, S. M. J., Sturrock, S. S., & Barton, G. J. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn320 · Cited by 92
E.co1iリボソームの構造と機能 V RNAとたんぱく質から活性30Sリポソーム粒子の再構成
Traub, P., & Nomura, M. (1968) · Cited by 92
Rinke-Appel, J., Jünke, N., Stade, K., & Brimacombe, R. L. C. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07755.x · Cited by 89
Creating ribosomes with an all-RNA 30S subunit P site
Hoang, L., Fredrick, K., & Noller, H. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405227101 · Cited by 86
RNA-protein interactions in the Escherichia coli ribosome
Brimacombe, R. L. C. (1991) · Biochimie · doi:10.1016/0300-9084(91)90134-m · Cited by 82
Collatz, E., Wool, I. G., Lin, A., & Stöffler, G. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33254-4 · Cited by 79
Functional Studies on Ribosomes Lacking Protein L1 from Mutant Escherichia coli
Subramanian, A. R., & Dabbs, E. R. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb07222.x · Cited by 77
Wower, I. K., Wower, J., & Zimmermann, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19847 · Cited by 77
Franceschi, F. J., & Nierhaus, K. H. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46274-0 · Cited by 76
Cukras, A. R., & Green, R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.03.075 · Cited by 72
Mapping structural differences between 30S ribosomal subunit assembly intermediates
Holmes, K., & Culver, G. M. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb719 · Cited by 71
The E-site story: the importance of maintaining two tRNAs on the ribosome during protein synthesis
Wilson, D. N., & Nierhaus, K. H. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6125-4 · Cited by 71
Proteome Evolution and the Metabolic Origins of Translation and Cellular Life
Caetano-Anollés, D., Kim, K. M., Mittenthal, J. E., & Caetano‐Anollés, G. (2010) · Journal of Molecular Evolution · doi:10.1007/s00239-010-9400-9 · Cited by 65
A role for the 30S subunit E site in maintenance of the translational reading frame
Devaraj, A., Shoji, S., Holbrook, E. D., & Fredrick, K. (2008) · RNA · doi:10.1261/rna.1320109 · Cited by 65
Stöffler, G., Deusser, E., Wittmann, H. G., & Apirion, D. (1971) · Molecular and General Genetics MGG · doi:10.1007/bf00569785 · Cited by 65
Tsurugi, K., Collatz, E., Todokoro, K., & Wool, I. G. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40344-9 · Cited by 63
Mutants lacking individual ribosomal proteins as a tool to investigate ribosomal properties
Dabbs, E. R. (1991) · Biochimie · doi:10.1016/0300-9084(91)90043-z · Cited by 59
The Evolutionary History of the Structure of 5S Ribosomal RNA
Sun, F.-J., & Caetano‐Anollés, G. (2009) · Journal of Molecular Evolution · doi:10.1007/s00239-009-9264-z · Cited by 57
30S ribosomal subunits can be assembled in vivo without primary binding ribosomal protein S15
Bubunenko, M. G., Korepanov, A. P., Court, D. L., Jagannathan, I., Dickinson, D. J., Roy‐Chaudhuri, B., Garber, M., & Culver, G. M. (2006) · RNA · doi:10.1261/rna.2262106 · Cited by 54
Self-citationBunner, A. E., Beck, A. H., & Williamson, J. R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912007107 · Cited by 51
The archaeal origins of the eukaryotic translational system
Hartman, H., Favaretto, P., & Smith, T. F. (2005) · Archaea · doi:10.1155/2006/431618 · Cited by 50
Acidic ribosomal proteins from the extreme halophile,Halobacterium cutirubrum
Strøm, A. R., & Visentin, L. P. (1973) · FEBS Letters · doi:10.1016/0014-5793(73)80477-6 · Cited by 49
Osswald, M., Döring, T. F., & Brimacombe, R. L. C. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.22.4635 · Cited by 49
The subunit interface of the Escherichia coli ribosome
Lambert, J. M., & Traut, R. R. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90481-2 · Cited by 48
A Functional Interaction between Ribosomal Proteins S7 and S11 within the Bacterial Ribosome
Robert, F., & Brakier‐Gingras, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306534200 · Cited by 44
Ribosome origins: The relative age of 23S rRNA Domains
Hury, J., Nagaswamy, U., Larios‐Sanz, M., & Fox, G. E. (2006) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-006-9011-z · Cited by 43
Quantitative Proteomic Analysis of Ribosome Assembly and Turnover In Vivo
Sykes, M. T., Shajani, Z., Sperling, E., Beck, A. H., & Williamson, J. R. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.08.005 · Cited by 42
Fedorov, R., Meshcheryakov, V., Gongadze, G. M., Fomenkova, N. P., Nevskaya, N. A., Selmer, M., Laurberg, M., Kristensen, O., Al‐Karadaghi, S., Liljas, A., et al. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444901006291 · Cited by 42
Self-citationSchrier, P. I., & Möller, W. J. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80059-7 · Cited by 41
Korepanov, A. P., Gongadze, G. M., Garber, M., Court, D. L., & Bubunenko, M. G. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.097 · Cited by 41
Self-citationSköld, S. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06859.x · Cited by 41
Mitchell, P., Stade, K., Oβwald, M., & Brimacombe, R. L. C. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.4.887 · Cited by 41
Elongation factor‐dependent reactions on ribosomes deprived of proteins L7 and L12
Koteliansky, V., Domogatsky, S. P., Gudkov, A. T., & Spirin, A. S. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80003-3 · Cited by 40
Similarity in the Size and Number of Ribosomal Proteins from Different Prokaryotes
Sun, T., Bickle, T. A., & Traut, R. R. (1972) · Journal of Bacteriology · doi:10.1128/jb.111.2.474-480.1972 · Cited by 38
How does the mRNA pass through the ribosome ?
Shatsky, I. N., Bakin, A. V., Bogdanov, A. A., & Vasiliev, V. D. (1991) · Biochimie · doi:10.1016/0300-9084(91)90135-n · Cited by 38
Assembly of proteins and 5 S rRNA to transcripts of the major structural domains of 23 S rRNA
Østergaard, P., Phan, H., Johansen, L. B., et al. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2185 · Cited by 38
Arndt, E., Scholzen, T. E., Krömer, W., Hatakeyama, T., & Kimura, M. (1991) · Biochimie · doi:10.1016/0300-9084(91)90045-3 · Cited by 35
MAASSEN, J. A., & Möller, W. J. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb05235.x · Cited by 35
Changes in the primary structure of a mutationally altered ribosomal protein S 4 of Escherichia coli
Donner, D., & Kurland, C. G. (1972) · Molecular and General Genetics MGG · doi:10.1007/bf00272217 · Cited by 32
Herold, M., Nowotny, V., Dabbs, E. R., & Nierhaus, K. H. (1986) · Molecular and General Genetics MGG · doi:10.1007/bf00333967 · Cited by 28
The proteins of the messenger RNA binding site of Escherichia coli ribosomes
Гимаутдинова, О. И., Karpova, G. G., Knorre, D. G., & Kobetz, N. D. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.14.3465 · Cited by 27
Olson, H. M., Nicholson, A. W., Cooperman, B. S., & Glitz, D. G. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39251-7 · Cited by 25
A spontaneous mutant of Escherichia coli with protein L24 lacking from the ribosome
Dabbs, E. R. (1982) · Molecular and General Genetics MGG · doi:10.1007/bf00332627 · Cited by 25
Tumminia, S. J., Hellmann, W., Wall, J. S., & Boublík, M. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1077 · Cited by 25
Perederina, A. A., Nevskaya, N. A., Nikonov, O. S., Никулин, А. Д., Dumas, P., Yao, M., Tanaka, I., Garber, M., Gongadze, G. M., & Nikonov, S. V. (2002) · RNA · doi:10.1017/s1355838202029953 · Cited by 25
Self-citationMandiyan, V., Tumminia, S. J., Wall, J. S., Hainfeld, J. F., & Boublík, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.18.8174 · Cited by 24
Binding of Aminoacyl‐tRNA to Reconstituted Subparticles of Escherichia coli Large Ribosomal Subunits
Kazemie, M. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb10701.x · Cited by 22
Many nonuniversal archaeal ribosomal proteins are found in conserved gene clusters
Wang, J., Dasgupta, I., & Fox, G. E. (2009) · Archaea · doi:10.1155/2009/971494 · Cited by 22
Studies on the significance of sequence homologies among proteins from Escherichia coli ribosomes
Wittmann-Liebold, B., & Dzionara, M. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80129-9 · Cited by 21
Dontsova, O. А., Rosen, K. V., Bogdanova, S. L., Skripkin, Е., Kopylov, A. M., & Bogdanov, A. A. (1992) · Biochimie · doi:10.1016/0300-9084(92)90114-t · Cited by 19
A decade of progress in understanding the structural basis of protein synthesis
Al‐Karadaghi, S., Kristensen, O., & Liljas, A. (2000) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(00)00005-5 · Cited by 19
Specific interaction of the elongation factor EF‐G with the ribosomal 23 S RNA from Escherichia coli
Girshovich, A. S., Bochkareva, E. S., & Gudkov, A. T. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)81312-4 · Cited by 18
Self-Organization of Ribosomal RNA
Vasiliev, V. D., Serdyuk, I. N., Gudkov, A. T., & Spirin, A. S. (1986) · Springer series in molecular biology · doi:10.1007/978-1-4612-4884-2_8 · Cited by 17
Woestenenk, E. A., Gongadze, G. M., Shcherbakov, D. V., Rak, A., Garber, M., Härd, T., & Berglund, H. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630553 · Cited by 17
Self-citationDirect tRNA-protein interactions in ribosomal complexes
Abdurashidova, G., Tsvetkova, E. A., & BUDOWSKY, E. I. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.8.1909 · Cited by 14
Protein structure: experimental and theoretical aspects
Harms, J. M., Schluenzen, F., Zarivach, R., Bashan, A., Bartels, H., Agmon, I., & Yonath, A. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02960-5 · Cited by 11
Malygin, A. A., & Karpova, G. G. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1170 · Cited by 11
The proteins of donor tRNA‐binding site of Escherichia coli ribosomes
Vladimirov, S. N., Graifer, D. M., & Karpova, G. G. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80966-0 · Cited by 9
Parker, K. K., & Wickstrom, E. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.2.515 · Cited by 3
Research works printed but not linked: 1
- Powers, T., and Noller, H. F. (1995) RNA, 1, 194–209.
Cited by
Altered Machinery of Protein Synthesis in Alzheimer's: From the Nucleolus to the Ribosome
Hernández‐Ortega, K., Garcia‐Esparcia, P., Gil, L., Lucas, J. J., & Ferrer, I. (2016) · Brain Pathology · doi:10.1111/bpa.12335 · Cited by 245
The Peptidyl Transferase Center: a Window to the Past
Tirumalai, M. R., Rivas, M., Tran, Q., & Fox, G. E. (2021) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00104-21 · Cited by 53
On the possible origin of protein homochirality, structure, and biochemical function
Skolnick, J., Zhou, H., & Gao, M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1908241116 · Cited by 45
Li, Q., Chang, R., Sun, Y., & Li, B. (2016) · PLOS ONE · doi:10.1371/journal.pone.0166876 · Cited by 19
Penning, A., Snoeck, S., Ormaechea, O. R., Ayyildiz, D., Polzer, O., Buitrago-Arango, M., Capobianco, R., de Winter, F., Balusu, S., Verhaagen, J., et al. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02228-8 · Cited by 6
Metadata
- Authors
- Korobeinikova, A. V., Garber, M. B., & Gongadze, G. M.
- Venue
- Biochemistry (Moscow)
- Publisher
- Pleiades Publishing Ltd
- Published
- 2012-06
- Volume
- 77
- Issue
- 6
- Pages
- 562-574
- ISSN
- 0006-2979
- 1608-3040
- Cited by
- 63
- References
- 129
- Language
- en
- Licence
- www.springernature.com/gp/researchers/text-and-data-mining (tdm)
- www.springernature.com/gp/researchers/text-and-data-mining (vor)
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 ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.