Structural determinants of co-translational protein complex assembly
Open accessPublished version of a preprint
Abstract
Protein assembly into functional complexes is critical to life's processes. While complex assembly is classically described as occurring between fully synthesized proteins, recent work showed that co-translational assembly is prevalent in human cells. However, the biological basis for the existence of this process and the identity of protein pairs that assemble co-translationally remain unknown. We show that co-translational assembly is governed by structural characteristics of complexes and involves mutually stabilized subunits. Accordingly, co-translationally assembling subunits are unstable in isolation and exhibit synchronized proteostasis with their partner. By leveraging structural signatures and AlphaFold2-based predictions, we accurately predicted co-translational assembly, including pair identities, at proteome scale and across species. We validated our predictions by ribosome profiling, stoichiometry perturbations, and single-molecule RNA-fluorescence in situ hybridization (smFISH) experiments that revealed co-localized mRNAs. This work establishes a fundamental connection between protein structure and the translation process, highlighting the overarching impact of three-dimensional structure on gene expression, mRNA localization, and proteostasis.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669 · see citing works
Scikit-learn: Machine Learning in Python
Pedregosa, F., Varoquaux, G., Gramfort, A., Michel, V., Thirion, B., Grisel, O., Blondel, M., Müller, A., Nothman, J., Louppe, G., et al. (2012) · arXiv · doi:10.48550/arxiv.1201.0490 · Cited by 71,016 · see citing works
Fiji: an open-source platform for biological-image analysis
Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2019 · Cited by 66,890 · see citing works
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
UniProt: the Universal Protein Knowledgebase in 2023
The UniProt Consortium, Bateman, A., Martin, M.-J., Orchard, S., Magrane, M., Ahmad, S., Alpi, E., Bowler-Barnett, E. H., Britto, R., Bye-A-Jee, H., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkac1052 · Cited by 7,210 · see citing works
Statsmodels: Econometric and Statistical Modeling with Python
Seabold, S., & Perktold, J. (2010) · Proceedings of the Python in Science Conferences · doi:10.25080/majora-92bf1922-011 · Cited by 6,686 · see citing works
UniProt: the universal protein knowledgebase in 2021
The UniProt Consortium, Bateman, A., Martin, M.-J., Orchard, S., Magrane, M., Agivetova, R., Ahmad, S., Alpi, E., Bowler-Barnett, E. H., Britto, R., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1100 · Cited by 6,372 · see citing works
Biopython: freely available python tools for computational molecular biology and bioinformatics
Cock, P. J. A., Antao, T., Chang, J. T., Chapman, B. A., Cox, C. J., Dalke, A., Friedberg, I., Hamelryck, T., Kauff, F., Wilczynski, B., et al. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp163 · Cited by 6,080 · see citing works
Biomolecular condensates: organizers of cellular biochemistry
Banani, S. F., Lee, H. O., Hyman, A., & Rosen, M. (2017) · Nature reviews. Molecular cell biology · doi:10.1038/nrm.2017.7 · Cited by 5,574 · see citing works
The quickhull algorithm for convex hulls
Barber, C. B., Dobkin, D., & Huhdanpaa, H. T. (1996) · ACM Transactions on Mathematical Software · doi:10.1145/235815.235821 · Cited by 5,364 · see citing works
UCSF ChimeraX : Tools for structure building and analysis
Meng, E. C., Goddard, T. D., Pettersen, E. F., Couch, G. S., Pearson, Z., Morris, J. H., & Ferrin, T. E. (2023) · Protein Science · doi:10.1002/pro.4792 · Cited by 4,575 · see citing works
Brachmann, C. B., Davies, A., Cost, G. J., Caputo, E. M., Li, J., Hieter, P., & Boeke, J. D. (1998) · Yeast · doi:10.1002/(sici)1097-0061(19980130)14:2 · Cited by 3,411 · see citing works
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684 · see citing works
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648 · see citing works
Adapting Proteostasis for Disease Intervention
Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495 · see citing works
From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293 · see citing works
Imaging individual mRNA molecules using multiple singly labeled probes
Raj, A., van den Bogaard, P., Rifkin, S. A., van Oudenaarden, A., & Tyagi, S. (2008) · Nature Methods · doi:10.1038/nmeth.1253 · Cited by 2,028 · see citing works
Mumberg, D., Müller, R., & Funk, M. (1995) · Gene · doi:10.1016/0378-1119(95)00037-7 · Cited by 1,972 · see citing works
Saccharomyces Genome Database: the genomics resource of budding yeast
Cherry, J., Hong, E., Amundsen, C., Balakrishnan, R., Binkley, G., Chan, E. T., Christie, K., Costanzo, M., Dwight, S., Engel, S., et al. (2011) · Nucleic Acids Res. · doi:10.1093/nar/gkr1029 · Cited by 1,886 · see citing works
Methods in yeast genetics : a Cold Spring Harbor Laboratory course manual
Amberg, D. C., Burke, D. J., & Strathern, J. N. (2005) · Cited by 1,853 · see citing works
Burley, S. K., Bhikadiya, C., Bi, C., Bittrich, S., Chen, L., Crichlow, G. V., Christie, C. H., Dalenberg, K., Di Costanzo, L., Duarte, J. M., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1038 · Cited by 1,581 · see citing works
Plaxco, K. W., Simons, K. T., & Baker, D. A. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1645 · Cited by 1,520 · see citing works
THE KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF THE REDUCED POLYPEPTIDE CHAIN
Anfinsen, C. B., Haber, E., Sela, M., & White, F. H. (1961) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.47.9.1309 · Cited by 1,182 · see citing works
mScarlet: a bright monomeric red fluorescent protein for cellular imaging
Bindels, D. S., Haarbosch, L., van Weeren, L., Postma, M., Wiese, K. E., Mastop, M., Aumonier, S., Gotthard, G., Royant, A., Hink, M. A., et al. (2016) · Nature Methods · doi:10.1038/nmeth.4074 · Cited by 1,100 · see citing works
Improved prediction of protein-protein interactions using AlphaFold2
Bryant, P., Pozzati, G., & Elofsson, A. (2021) · doi:10.1101/2021.09.15.460468 · Cited by 1,025 · see citing works
Šali, A., Shakhnovich, E. I., & Karplus, M. (1994) · Nature · doi:10.1038/369248a0 · Cited by 944 · see citing works
Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
Schuler, B., Lipman, E. A., & Eaton, W. A. (2002) · Nature · doi:10.1038/nature01060 · Cited by 921 · see citing works
Burley, S. K., Bhikadiya, C., Bi, C., Bittrich, S., Chao, H., Chen, L., Craig, P., Crichlow, G. V., Dalenberg, K., Duarte, J. M., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1077 · Cited by 903 · see citing works
Rose, P. W., Prlić, A., Altunkaya, A., Bi, C., Bradley, A. R., Christie, C. H., Costanzo, L. D., Duarte, J. M., Dutta, S., Feng, Z., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1000 · Cited by 800 · see citing works
Intrinsically disordered proteins: regulation and disease
Babu, M. M., van der Lee, R., de Groot, N. S., & Gsponer, J. A. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.03.011 · Cited by 597 · see citing works
FreeSASA: An open source C library for solvent accessible surface area calculations
Mitternacht, S. (2016) · F1000Research · doi:10.12688/f1000research.7931.1 · Cited by 560 · see citing works
Wang, M., Herrmann, C. J., Simonovic, M., Szklarczyk, D., & von Mering, C. (2015) · Proteomics · doi:10.1002/pmic.201400441 · Cited by 543 · see citing works
Computed structures of core eukaryotic protein complexes
Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S. R., et al. (2021) · Science · doi:10.1126/science.abm4805 · Cited by 542 · see citing works
Domain swapping: entangling alliances between proteins.
Bennett, M. J., Choe, S., & Eisenberg, D. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3127 · Cited by 535 · see citing works
The molecular sociology of the cell
Robinson, C. V., Šali, A., & Baumeister, W. P. (2007) · Nature · doi:10.1038/nature06523 · Cited by 533 · see citing works
Mapping the dynamic organization of the nuclear pore complex inside single living cells
Rabut, G. E. E., Doye, V., & Ellenberg, J. (2004) · Nature Cell Biology · doi:10.1038/ncb1184 · Cited by 476 · see citing works
Grantcharova, V., Alm, E. J., Baker, D. A., & Horwich, A. L. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00176-7 · Cited by 474 · see citing works
Alternative 3′ UTRs act as scaffolds to regulate membrane protein localization
Berkovits, B. D., & Mayr, C. (2015) · Nature · doi:10.1038/nature14321 · Cited by 474 · see citing works
Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation
Gsponer, J., Futschik, M. E., Teichmann, S. A., & Babu, M. M. (2008) · Science · doi:10.1126/science.1163581 · Cited by 466 · see citing works
Structure, Dynamics, Assembly, and Evolution of Protein Complexes
Marsh, J. A., & Teichmann, S. A. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034142 · Cited by 455 · see citing works
Complete RNA Polymerase II Elongation Complex Structure and Its Interactions with NTP and TFIIS
Kettenberger, H., Armache, K., & Cramer, P. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.040 · Cited by 437 · see citing works
Assembly reflects evolution of protein complexes
Levy, E. D., Erba, E. B., Robinson, C. V., & Teichmann, S. A. (2008) · Nature · doi:10.1038/nature06942 · Cited by 420 · see citing works
Self-citationContact order revisited: Influence of protein size on the folding rate
Ivankov, D. N., Garbuzynskiy, S. O., Alm, E. J., Plaxco, K. W., Baker, D. A., & Finkelstein, A. V. (2003) · Protein Science · doi:10.1110/ps.0302503 · Cited by 374 · see citing works
AI-based structure prediction empowers integrative structural analysis of human nuclear pores
Mosalaganti, S., Obarska-Kosinska, A., Siggel, M., Taniguchi, R., Turoňová, B., Zimmerli, C. E., Buczak, K., Schmidt, F. H., Margiotta, E., Mackmull, M.-T., et al. (2022) · Science · doi:10.1126/science.abm9506 · Cited by 355 · see citing works
3D Complex: A Structural Classification of Protein Complexes
Levy, E. D., Pereira‐Leal, J. B., Chothia, C., & Teichmann, S. A. (2006) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0020155 · Cited by 337 · see citing works
Self-citationCotranslational assembly of protein complexes in eukaryotes revealed by ribosome profiling
Shiber, A., Döring, K., Friedrich, U. A., Klann, K., Merker, D., Zedan, M., Tippmann, F., Krämer, G., & Bukau, B. (2018) · Nature · doi:10.1038/s41586-018-0462-y · Cited by 328 · see citing works
Self-citationProtein topology determines binding mechanism
Levy, Y., Wolynes, P. G., & Onuchic, J. N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2534828100 · Cited by 324 · see citing works
Fersht, A. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1525 · Cited by 323 · see citing works
Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region
Venkatakrishnan, A., Deupí, X., Lebon, G., Heydenreich, F. M., Flock, T., Miljuš, T., Santhanam, B., Bouvier, M., Veprintsev, D. B., Tate, C. G., et al. (2016) · Nature · doi:10.1038/nature19107 · Cited by 304 · see citing works
The Ribosome Modulates Nascent Protein Folding
Kaiser, C., Goldman, D. H., Chodera, J. D., Tinoco, I., & Bustamante, C. (2011) · Science · doi:10.1126/science.1209740 · Cited by 302 · see citing works
Wu, C. C., Zinshteyn, B., Wehner, K. A., & Green, R. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.009 · Cited by 298 · see citing works
Following translation by single ribosomes one codon at a time
Wen, J.-D., Lancaster, L., Hodges, C., Zeri, A., Yoshimura, S., Noller, H., Bustamante, C., & Tinoco, I. (2008) · Nature · doi:10.1038/nature06716 · Cited by 292 · see citing works
Meltome atlas—thermal proteome stability across the tree of life
Jarząb, A., Kurzawa, N., Hopf, T. A., Moerch, M., Zecha, J., Leijten, N. M., Bian, Y., Musiol, E., Maschberger, M., Stoehr, G., et al. (2020) · Nature Methods · doi:10.1038/s41592-020-0801-4 · Cited by 275 · see citing works
Towards a structurally resolved human protein interaction network
Burke, D. F., Bryant, P., Barrio-Hernandez, I., Memon, D., Pozzati, G., Shenoy, A., Zhu, W., Dunham, A. S., Albanese, P., Keller, A., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00910-8 · Cited by 269 · see citing works
Principles of assembly reveal a periodic table of protein complexes
Ahnert, S. E., Marsh, J. A., Hernández, H., Robinson, C. V., & Teichmann, S. A. (2015) · Science · doi:10.1126/science.aaa2245 · Cited by 253 · see citing works
Protein Complexes Are under Evolutionary Selection to Assemble via Ordered Pathways
Marsh, J. A., Hernández, H., Hall, Z., Ahnert, S. E., Perica, T., Robinson, C. V., & Teichmann, S. A. (2013) · Cell · doi:10.1016/j.cell.2013.02.044 · Cited by 245 · see citing works
Mohammad, F., Green, R., & Buskirk, A. R. (2019) · eLife · doi:10.7554/elife.42591 · Cited by 242 · see citing works
Structural mechanism of glutamate receptor activation and desensitization
Meyerson, J. R., Kumar, J., Chittori, S., Rao, P., Pierson, J., Bartesaghi, A., Mayer, M. L., & Subramaniam, S. (2014) · Nature · doi:10.1038/nature13603 · Cited by 227 · see citing works
Thermal proximity coaggregation for system-wide profiling of protein complex dynamics in cells
Tan, C. S. H., Go, K. D., Bisteau, X., Dai, L., Yong, C. H., Prabhu, N., Ozturk, M. B., Lim, Y. T., Sreekumar, L., Lengqvist, J., et al. (2018) · Science · doi:10.1126/science.aan0346 · Cited by 224 · see citing works
Expression Atlas update: gene and protein expression in multiple species
Moreno, P. A., Fexova, S. K., George, N., Manning, J. R., Miao, Z., Mohammed, S., Fuentes, A. M.-P., Füllgrabe, A., Bi, Y., Bush, N. G., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1030 · Cited by 223 · see citing works
Protein synthesis rate is the predominant regulator of protein expression during differentiation
Kristensen, A. R., Gsponer, J., & Foster, L. J. (2013) · Molecular Systems Biology · doi:10.1038/msb.2013.47 · Cited by 217 · see citing works
The Unfolding Story of Three-Dimensional Domain Swapping
Rousseau, F., Schymkowitz, J. W. H., & Itzhaki, L. S. (2003) · Structure · doi:10.1016/s0969-2126(03)00029-7 · Cited by 213 · see citing works
The Yeast Ski Complex: Crystal Structure and RNA Channeling to the Exosome Complex
Halbach, F., Reichelt, P., Rode, M., & Conti, E. (2013) · Cell · doi:10.1016/j.cell.2013.07.017 · Cited by 210 · see citing works
The Bgee suite: integrated curated expression atlas and comparative transcriptomics in animals
Bastian, F., Roux, J., Niknejad, A., Comte, A., Costa, S. S. F., de Farias, T. M., Moretti, S., Parmentier, G., de Laval, V. R., Rosikiewicz, M., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa793 · Cited by 192 · see citing works
Central dogma rates and the trade-off between precision and economy in gene expression
Hausser, J., Mayo, A., Keren, L., & Alon, U. (2019) · Nature Communications · doi:10.1038/s41467-018-07391-8 · Cited by 188 · see citing works
Profiling Ssb-Nascent Chain Interactions Reveals Principles of Hsp70-Assisted Folding
Döring, K., Ahmed, N., Riemer, T., Suresh, H. G., Vainshtein, Y., Habich, M., Riemer, J., Mayer, M. P., O’Brien, E. P., Krämer, G., et al. (2017) · Cell · doi:10.1016/j.cell.2017.06.038 · Cited by 185 · see citing works
Clare, D. K., Vasishtan, D., Stagg, S. M., Quispe, J. D., Farr, G. W., Topf, M., Horwich, A. L., & Saibil, H. R. (2012) · Cell · doi:10.1016/j.cell.2012.02.047 · Cited by 183 · see citing works
Molecular structures of unbound and transcribing RNA polymerase III
Hoffmann, N. A., Jakobi, A. J., Moreno‐Morcillo, M., Glatt, S., Kosiński, J., Hagen, W. J. H., Sachse, C., & Müller, C. W. (2015) · Nature · doi:10.1038/nature16143 · Cited by 177 · see citing works
Domain swapping is a consequence of minimal frustration
Yang, S., Cho, S. S., Levy, Y., Cheung, M. S., Levine, H., Wolynes, P. G., & Onuchic, J. N. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403724101 · Cited by 171 · see citing works
Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly
Bertolini, M., Fenzl, K., Kats, I., Wruck, F., Tippmann, F., Schmitt, J. L., Auburger, J. J., Tans, S. J., Bukau, B., & Krämer, G. (2020) · Science · doi:10.1126/science.abc7151 · Cited by 153 · see citing works
PDBe: improved accessibility of macromolecular structure data from PDB and EMDB
Velankar, S. S., van Ginkel, G., Alhroub, Y., Battle, G. M., Berrisford, J. M., Conroy, M. J., Dana, J. M., Gore, S. P., Gutmanas, A., Haslam, P., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1047 · Cited by 145 · see citing works
An atlas of protein homo-oligomerization across domains of life
Schweke, H., Pacesa, M., Levin, T., Goverde, C. A., Kumar, P., Duhoo, Y., Dornfeld, L. J., Dubreuil, B., Georgeon, S., Ovchinnikov, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.01.022 · Cited by 144 · see citing works
Self-citationDrew, K., Wallingford, J. B., & Marcotte, E. M. (2021) · Molecular Systems Biology · doi:10.15252/msb.202010016 · Cited by 137 · see citing works
Complex Portal 2018: extended content and enhanced visualization tools for macromolecular complexes
Meldal, B., Bye‐A‐Jee, H., Gajdos, L., Hammerová, Z., Horáčková, A., Melicher, F., Perfetto, L., Pokorný, D., Rodríguez-López, M., Tuerkova, A., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1001 · Cited by 134 · see citing works
Widespread Cotranslational Formation of Protein Complexes
Duncan, C. D. S., & Mata, J. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002398 · Cited by 131 · see citing works
Co-translational assembly of proteasome subunits in NOT1-containing assemblysomes
Panasenko, O. O., Somasekharan, S. P., Villányi, Z., Zagatti, M., Bezrukov, F., Rashpa, R., Cornut, J., Iqbal, J., Longis, M., Carl, S. H., et al. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0179-5 · Cited by 128 · see citing works
Braselmann, E., Chaney, J. L., & Clark, P. L. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.05.001 · Cited by 125 · see citing works
Co-translational assembly of mammalian nuclear multisubunit complexes
Kamenova, I., Mukherjee, P., Conic, S., Mueller, F., El-Saafin, F., Bardot, P., Garnier, J., Dembélé, D., Capponi, S., Timmers, H. T. M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09749-y · Cited by 120 · see citing works
Ribosome–NatA architecture reveals that rRNA expansion segments coordinate N-terminal acetylation
Knorr, A. G., Schmidt, C. M., Těšina, P., Berninghausen, O., Becker, T. A., Beatrix, B., & Beckmann, R. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0165-y · Cited by 113 · see citing works
Designer protein assemblies with tunable phase diagrams in living cells
Heidenreich, M., Georgeson, J. M., Locatelli, E., Rovigatti, L., Nandi, S. K., Steinberg, A., Nadav, Y., Shimoni, E., Safran, S. A., Doye, J. P. K., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0576-z · Cited by 99 · see citing works
Self-citationEvolution of increased complexity and specificity at the dawn of form I Rubiscos
Schulz, L., Guo, Z., Zarzycki, J., Steinchen, W., Schuller, J. M., Heimerl, T., Prinz, S., Mueller‐Cajar, O., Erb, T. J., & Hochberg, G. K. A. (2022) · Science · doi:10.1126/science.abq1416 · Cited by 99 · see citing works
Distributing many points on spheres: Minimal energy and designs
Brauchart, J. S., & Grabner, P. J. (2015) · Journal of Complexity · doi:10.1016/j.jco.2015.02.003 · Cited by 97 · see citing works
Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer
Jia, W., & Tong, L. (2015) · Nature · doi:10.1038/nature15375 · Cited by 95 · see citing works
Structures of Tetrahymena ’s respiratory chain reveal the diversity of eukaryotic core metabolism
Zhou, L., Maldonado, M., Padavannil, A., Guo, F., & Letts, J. A. (2022) · Science · doi:10.1126/science.abn7747 · Cited by 94 · see citing works
Cotranslational assembly of the yeast SET1C histone methyltransferase complex
Halbach, A., Zhang, H., Wengi, A., Jabłońska, Z., Gruber, I. M. L., Halbeisen, R. E., Dehé, P.-M., Kemmeren, P., Holstege, F. C. P., Géli, V., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.240 · Cited by 91 · see citing works
Genome-wide C-SWAT library for high-throughput yeast genome tagging
Meurer, M., Duan, Y., Sass, E., Kats, I., Herbst, K., Buchmuller, B. C., Dederer, V., Huber, F., Kirrmaier, D., Štefl, M., et al. (2018) · Nature Methods · doi:10.1038/s41592-018-0045-8 · Cited by 91 · see citing works
Self-citationMolecular Structures of Transcribing RNA Polymerase I
Tafur, L., Sadian, Y., Hoffmann, N. A., Jakobi, A. J., Wetzel, R., Hagen, W. J. H., Sachse, C., & Müller, C. W. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.11.013 · Cited by 89 · see citing works
The proteomic landscape of genome-wide genetic perturbations
Messner, C. B., Demichev, V., Muenzner, J., Aulakh, S. K., Barthel, N., Röhl, A., Herrera-Domínguez, L., Egger, A.-S., Kamrad, S., Hou, J., et al. (2023) · Cell · doi:10.1016/j.cell.2023.03.026 · Cited by 84 · see citing works
Nonrefoldability is Pervasive Across the E. coli Proteome
To, P., Whitehead, B., Tarbox, H. E., & Fried, S. D. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c03270 · Cited by 80 · see citing works
PDB-wide identification of biological assemblies from conserved quaternary structure geometry
Dey, S., Ritchie, D. W., & Levy, E. D. (2017) · Nature Methods · doi:10.1038/nmeth.4510 · Cited by 76 · see citing works
Self-citationStructures of +1 nucleosome–bound PIC-Mediator complex
Chen, X., Wang, X., Liu, W., Ren, Y., Qu, X., Li, J., Yin, X., & Xu, Y. (2022) · Science · doi:10.1126/science.abn8131 · Cited by 76 · see citing works
Subcytoplasmic Location of Translation Controls Protein Output
Horste, E. L., Fansler, M. M., Cai, T., Chen, X., Mitschka, S., Zhen, G., Lee, F. C. Y., Ule, J., & Mayr, C. (2022) · Molecular Cell · doi:10.1016/j.molcel.2023.11.025 · Cited by 73 · see citing works
Lautier, O., Penzo, A., Rouvière, J. O., Chevreux, G., Collet, L., Loïodice, I., Taddei, A., Devaux, F., Collart, M. A., & Palancade, B. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.030 · Cited by 73 · see citing works
The Benefits of Cotranslational Assembly: A Structural Perspective
Schwarz, A., & Beck, M. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.07.006 · Cited by 72 · see citing works
Tsai, M., Koo, J. T., Yip, P., Colman, R. F., Segall, M. L., & Howell, P. L. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.052 · Cited by 66 · see citing works
Evolution of oligomeric state through allosteric pathways that mimic ligand binding
Perica, T., Kondo, Y., Tiwari, S. P., McLaughlin, S. H., Kemplen, K. R., Zhang, X., Steward, A., Reuter, N., Clarke, J., & Teichmann, S. A. (2014) · Science · doi:10.1126/science.1254346 · Cited by 63 · see citing works
A structural inventory of native ribosomal ABCE1‐43S pre‐initiation complexes
Kratzat, H., Mackens‐Kiani, T., Ameismeier, M., Potočnjak, M., Cheng, J., Dacheux, E., Namane, A., Berninghausen, O., Herzog, F., Fromont‐Racine, M., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020105179 · Cited by 61 · see citing works
Cotranslational Mechanisms of Protein Biogenesis and Complex Assembly in Eukaryotes
Morales-Polanco, F., Lee, J. H., Barbosa, N. M., & Frydman, J. (2022) · Annual Review of Biomedical Data Science · doi:10.1146/annurev-biodatasci-121721-095858 · Cited by 58 · see citing works
Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps
Bitran, A., Jacobs, W. M., Zhai, X., & Shakhnovich, E. I. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1913207117 · Cited by 57 · see citing works
Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins
Natan, E., Endoh, T., Haim-Vilmovsky, L., Flock, T., Chalancon, G., Hopper, J. T. S., Kintses, B., Horvath, P., Daruka, L., Fekete, G., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0029-5 · Cited by 56 · see citing works
Stellaris™ fluorescence in situ hybridization (FISH) probes: a powerful tool for mRNA detection
Orjalo, A. V., Johansson, H. E., & Ruth, J. L. (2011) · Nature Methods · doi:10.1038/nmeth.f.349 · Cited by 55 · see citing works
Co-translational assembly orchestrates competing biogenesis pathways
Seidel, M., Becker, A., Pereira, F. M., Landry, J. J. M., de Azevedo, N. T. D., Fusco, C. M., Kaindl, E., Romanov, N., Baumbach, J., Langer, J. D., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28878-5 · Cited by 52 · see citing works
Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex
Deng, S., Magin, R. S., Wei, X., Pan, B., Petersson, E. J., & Marmorstein, R. (2019) · Structure · doi:10.1016/j.str.2019.04.014 · Cited by 51 · see citing works
Massively parallel identification of mRNA localization elements in primary cortical neurons
Mendonsa, S., von Kügelgen, N., Dantsuji, S., Ron, M., Breimann, L., Baranovskii, A., Loedige, I., Kirchner, M., Fischer, M., Zerna, N., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-022-01243-x · Cited by 51 · see citing works
Structural and evolutionary versatility in protein complexes with uneven stoichiometry
Marsh, J. A., Rees, H. A., Ahnert, S. E., & Teichmann, S. A. (2015) · Nature Communications · doi:10.1038/ncomms7394 · Cited by 50 · see citing works
Plessa, E., Chu, L. P., Chan, S. H. S., Thomas, O. L., Cassaignau, A. M. E., Waudby, C. A., Christodoulou, J. C., & Cabrita, L. D. (2021) · Nature Communications · doi:10.1038/s41467-021-26531-1 · Cited by 49 · see citing works
Kassem, S., Villányi, Z., & Collart, M. A. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1059 · Cited by 49 · see citing works
Lian, X., Guo, J., Gu, W., Cui, Y., Zhong, J., Jin, J., He, Q., Wang, T., & Zhang, G. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1005901 · Cited by 48 · see citing works
Matalon, O., Horovitz, A., & Levy, E. D. (2014) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.06.001 · Cited by 45 · see citing works
Self-citationBusso, D., Peleg, Y., Heidebrecht, T., Romier, C., Jacobovitch, Y., Dantes, A., Salim, L., Troesch, E., Schuetz, A., Heinemann, U., et al. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.03.004 · Cited by 43 · see citing works
Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID
Bernardini, A., Mukherjee, P., Scheer, E., Kamenova, I., Antonova, S., Sanchez, P. K. M., Yayli, G., Morlet, B., Timmers, H. T. M., & Tora, L. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01026-3 · Cited by 42 · see citing works
Programming multi-protein assembly by gene-brush patterns and two-dimensional compartment geometry
Vonshak, O., Divon, Y., Förste, S., Garenne, D., Noireaux, V., Lipowsky, R., Rudorf, S., Daube, S. S., & Bar‐Ziv, R. (2020) · Nature Nanotechnology · doi:10.1038/s41565-020-0720-7 · Cited by 30 · see citing works
Large protein complex interfaces have evolved to promote cotranslational assembly
Badonyi, M., & Marsh, J. A. (2022) · eLife · doi:10.7554/elife.79602 · Cited by 29 · see citing works
Ray, S. P., Deaton, M. K., Capodagli, G. C., Calkins, L. A. F., Sawle, L., Ghosh, K., Patterson, D., & Pegan, S. D. (2012) · Biochemistry · doi:10.1021/bi300796y · Cited by 29 · see citing works
Nair, R. R., Zabezhinsky, D., Gelin-Licht, R., Haas, B. J., Dyhr, M. C. A., Sperber, H. S., Nusbaum, C., & Gerst, J. E. (2021) · eLife · doi:10.7554/elife.66050 · Cited by 27 · see citing works
Rabuck-Gibbons, J. N., Lyumkis, D., & Williamson, J. R. (2022) · Structure · doi:10.1016/j.str.2021.12.005 · Cited by 25 · see citing works
Pairwise biosynthesis of ion channels stabilizes excitability and mitigates arrhythmias
Jameson, M. B., Pérez, E. B. R., Liu, F., Eichel, C. A., & Robertson, G. A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2305295120 · Cited by 20 · see citing works
Not1 and Not4 inversely determine mRNA solubility that sets the dynamics of co-translational events
Allen, G., Weiss, B., Panasenko, O., Huch, S., Villányi, Z., Albert, B., Dilg, D., Zagatti, M., Schaughency, P. M., Liao, S. E., et al. (2022) · bioRxiv · doi:10.1186/s13059-023-02871-7 · Cited by 16 · see citing works
Venezian, J., Bar-Yosef, H., Zilberman, H., Cohen, N., Kleifeld, O., Fernández‐Recio, J., Glaser, F., & Shiber, A. (2024) · Nature Communications · doi:10.1038/s41467-024-46881-w · Cited by 12 · see citing works
Self-citationGilat, A., Alexandrov, A. I., Dubreuil, B., & Levy, E. D. (2026) · Nature Communications · doi:10.1038/s41467-026-73800-y · Cited by 10 · see citing works
Self-citationReprogramming protein abundance fluctuations in single cells by degradationPreprint
Matalon, O., Steinberg, A., Sass, E., Hausser, J., & Levy, E. D. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/260695 · Cited by 7 · see citing works
Self-citationGlobal Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
Venezian, J., Zilberman, H., & Shiber, A. (2021) · Journal of Visualized Experiments · doi:10.3791/62878 · Cited by 2 · see citing works
Self-citationGlobal Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
Venezian, J., Zilberman, H., & Shiber, A. (2021) · Journal of Visualized Experiments · doi:10.3791/62878-v · Cited by 1 · see citing works
Self-citation
Flagged first, then by citations
2 of the 125 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Evolutionary causes and consequences of gene duplication
Cisneros, A. F., Dibyachintan, S., Bédard, F., Aubé, S., Lemieux, P., & Landry, C. R. (2026) · Nature Reviews Genetics · doi:10.1038/s41576-026-00935-5 · Cited by 16 · see citing works
Dynamic BTB-domain filaments promote clustering of ZBTB proteins
Mance, L., Bigot, N., Sánchez, E. Z., Coste, F., Martín-González, N., Zentout, S., Biliškov, M., Pukało, Z., Mishra, A., Chapuis, C., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.05.029 · Cited by 19 · see citing works
Xia, M., Liu, Q., Zhang, W., Ge, J., & Mei, Z. (2025) · MedComm · doi:10.1002/mco2.70328 · Cited by 14 · see citing works
Emergence and evolution of protein-coding de novo genes
Bornberg‐Bauer, E., & Eicholt, L. A. (2026) · Nature Reviews Genetics · doi:10.1038/s41576-025-00929-9 · Cited by 15 · see citing works
Co-translational determination of quaternary structures in chaperone factories
Philippe, M., Salloum, S., Slimani, F., Normanno, D., Barbosa, I., Chassé, H., Robert, M.-C., Urbach, S., Imbert, J., Sevéno, M., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-68687-8 · Cited by 7 · see citing works
The ribosome synchronizes folding and assembly to promote oligomeric protein biogenesis
Roeselová, A., Shivakumaraswamy, S., Jurkeviciute, G., He, J. Z., Auburger, J. J., Schmitt, J. L., Kramer, G., Bukau, B., Enchev, R. I., & Balchin, D. (2026) · Molecular Cell · doi:10.1016/j.molcel.2025.12.022 · Cited by 6 · see citing works
mRNA 3′ UTRs chaperone intrinsically disordered regions to control protein activity
Luo, Y., Zhong, Y., Basu, S., Wu, M.-C., & Mayr, C. (2026) · Cell · doi:10.1016/j.cell.2026.05.017 · Cited by 6 · see citing works
Polysome sorting controls mRNA localization and protein fate
Safieddine, A., Bizarro, J., Salloum, S., Hir, H. L., & Bertrand, É. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.08.005 · Cited by 5 · see citing works
Divergent proteome tolerance against gain and loss of chromosome arms
Di, Y., Li, W., Castellano, J. J., Jin, W., Modi, J. N., Šalovská, B., Khosroabadi, D., Hu, W., Taylor, A. M., & Liu, Y. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.10.023 · Cited by 5 · see citing works
Co-translational assembly promotes functional diversification of paralogous proteinsPreprint
Mallik, S., Cisneros, A. F., Landry, C. R., & Levy, E. D. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.22.634331 · Cited by 5 · see citing works
Self-citationGenome-wide mapping of mesoscale neuronal RNA organization and condensationPreprint
Becker, L. A., Quinodoz, S. A., Comi, T. J., Kimchi, O., Knowles, D. A., & Brangwynne, C. P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.19.649570 · Cited by 5 · see citing works
Condition-dependent amorphous protein agglomerates control cytoplasmic rheology
Losa, J., Simon, F., Linnik, D., Kaya, S., Stuart, M. C. A., Stetsenko, A., de Boer, R., Ho, F. Y., Incarnato, D., Stevens, J. A., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.03.018 · Cited by 3 · see citing works
Gomari, M. M., Alidadi, M., Rostami, N., & Bencherif, S. A. (2025) · Advanced NanoBiomed Research · doi:10.1002/anbr.202500017 · Cited by 4 · see citing works
Sequence features and dynamics of subcellular translation revealed by APEX-Ribo-SeqPreprint
Tomuro, K., Makino, S., Akaiwa, T., Harada, A., Kobayashi, K., Shiina, N., Fukaya, T., Kawaguchi, K., Shichino, Y., & Iwasaki, S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.26.656194 · Cited by 3 · see citing works
Shade, Q., Estrada, M. E., Hanna, R., Makhzumy, M., Bar-Yosef, H., Kramer, G., Bukau, B., & Shiber, A. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169546 · Cited by 2 · see citing works
Self-citationCotranslational assembly directs the biogenesis of the m 6 A methyltransferase complex
Wu, X., Zhang, H., Huang, L., Zhang, S., He, J., Wang, S., Zhu, W., Li, Y., Zhou, J. L., & Liu, X. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2517258123 · Cited by 2 · see citing works
Proteins that assemble co-translationally lean on their partner for stability
Baumann, K. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00824-x · Cited by 2 · see citing works
Sequence, Structure and Functional space of Drosophila de novo proteinsPreprint
Middendorf, L., Iyengar, B. R., & Eicholt, L. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.30.577933 · Cited by 2 · see citing works
Cooperative Architecture of Mitochondrial Proteome HomeostasisPreprint
Forny, P., Forny, M., Smith, A. J., Sung, A. Y., Liu, K., & Pagliarini, D. J. (2026) · medRxiv · doi:10.64898/2026.02.06.26345691 · Cited by 2 · see citing works
Unraveling the mechanisms of slack channel mutations in epileptic disorders
Wei, Y., Zahra, A., Wang, Q., & Wu, J. (2026) · Acta Epileptologica · doi:10.1186/s42494-026-00246-6 · Cited by 1 · see citing works
Xiong, W., Ser, Z., Sobota, R. M., & Lin, Z. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.02.007 · Cited by 1 · see citing works
The twisted tale of cotranslational protein complex assembly
Mallik, S., & Shiber, A. (2026) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2026.103281 · Cited by 1 · see citing works
Self-citationMembrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy
Kim, S. A., Kim, S., Nam, J., Kim, E., Yoon, T., & Min, D. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c01097 · Cited by 1 · see citing works
Peng, Y., Zhang, Y., Liu, L., Song, X., Li, M., & Wang, B. (2026) · Results in Chemistry · doi:10.1016/j.rechem.2026.103733 · Cited by 1 · see citing works
Collart, M. A., & Panasenko, O. O. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.01.007 · Cited by 1 · see citing works
Structural basis for co-translational assembly of homo-oligomeric proteins in cis and in transPreprint
Koubek, J., Filbeck, S., Fixen, G., Kopetschke, S., Schmitt, J. L., Pfeffer, S., Kramer, G., & Bukau, B. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.12.687954 · Cited by 1 · see citing works
Proximal Co-Translation Facilitates Detection of Weak Protein-Protein Interactions
Kordonsky, A., Gabay, M., Rosinoff, A., Avishid, R., Florentin, A., Deouell, N., Alkhaleq, T. A., Efron, N., Milshtein, S., Shifman, J. M., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252011099
Reply to: Docking domains from modular polyketide synthases and their use in engineering
Liu, Y., & Wang, H. (2025) · Nature Communications · doi:10.1038/s41467-025-61436-3
Co-translational complex assembly
Venezian, J., & Shiber, A. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-99507-8.00023-8
Self-citationTranslating the green code: Ribo-Seq for photosynthetic eukaryotes in focus
Kawamoto, N., & Iwasaki, S. H. (2026) · The Journal of Biochemistry · doi:10.1093/jb/mvag004
Cotranslational Assembly of Oligomeric Proteins
Santos, J., Tans, S. J., Ban, N., Kramer, G., & Bukau, B. (2026) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051024-124747 · Cited by 2 · see citing works
Structural basis of NMI-IFP35 domains and swapping phenomenon in IFP35-NID
Sun, T., Shen, J., Wang, X., Wu, Y., Wu, Y., Weng, Z., Liang, H., & Liu, Y. (2026) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2026.100146
Cai, T., Cruz, N. M., Basu, S., White, R. M., & Mayr, C. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.05.723075
Programming the translational landscape for predictable gene expression
Yan, W., Hu, G., Liu, K., Liang, G., Gao, C., Li, X., & Wu, J. (2026) · Biotechnology Advances · doi:10.1016/j.biotechadv.2026.108950
Kvasov, N. A., & Bykov, Y. S. (2026) · Protein Science · doi:10.1002/pro.70682
mRNA-Scaffolded Cytoplasmic Compartments
Mayr, C. (2026) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111524-021431
A detailed molecular picture of protein folding during active translationPreprint
Bitran, A., Bustamante, C., & Marqusee, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.03.736445
Functional splice site variants in AVPR1A protect against idiopathic hyperaldosteronism
Hu, J., Wu, Z., Luo, W., Shen, H., Williams, T. A., Zeng, Q., Ma, L., Chen, X., Peng, C., Chen, Z., et al. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102377
Baddi, S., Gao, F., Zhao, C., Qiu, X., & Feng, C. (2026) · Advanced Materials · doi:10.1002/adma.74767
Bifunctional Enzymes for Deoxynivalenol Degradation in Prokaryotic and Eukaryotic Chassis
Liu, M., Guo, M., Tian, Y., Lin, H., Yan, Z., Jia, B., Sun, X., Saeger, S. D., Lootens, O., Rycke, E. D., et al. (2026) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6c10441
Born to Condense: Polysomes Drive Cotranslational Condensation of Biomolecular Condensate Proteins
He, Z., Chow, C. F. W., Tóth-Petróczy, Á., Sommer, J., & Harmon, T. S. (2026) · PRX Life · doi:10.1103/gjtk-ddjr
Joint protein, mRNA and DNA sequence design and optimization with nucleotide-level Potts modelsPreprint
Banaszewski, B., Dornfeld, L., Chen, D., Borgwardt, K. M., & Milles, L. F. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.05.756407
Molecular drivers of cotranslational protein assembly in bacteria
Schmitt, J. L., Auburger, J. J., Wruck, F., Koubek, J., Tans, S. J., Bukau, B., & Krämer, G. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2608997123
- Authors
- Mallik, S., Venezian, J., Lobov, A., Heidenreich, M., Garcia-Seisdedos, H., Yeates, T. O., Shiber, A., & Levy, E. D.
- Affiliations
- Weizmann Institute of Science (IL)
- Technion – Israel Institute of Technology (IL)
- Institut de Biologia Molecular de Barcelona (ES)
- University of California, Los Angeles (US)
- University of Geneva (CH)
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2025-02
- Volume
- 188
- Issue
- 3
- Pages
- 764-777.e22
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W4405632896
- Cited by
- 42
- References
- 125
- Citations by year
- 2026: 26 · 2025: 13 · 2024: 3
- FWCI
- 5.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (acceptedVersion)
- Funders
- Israel Ministry of Aliyah and Immigrant Absorption
- Abisch-Frenkel-Stiftung (2031817)
- European Research Council (819318)
- Israel Science Foundation (1452/18, 2106/20)
- Horizon 2020
- Weizmann Institute of Science
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- protein complex structure, protein stability, proteostasis, mRNA localization, ribosome profiling, single-molecule RNA FISH, AlphaFold2, protein-protein interaction, gene expression regulation
- MeSH terms
- Proteostasis, Animals, Humans, Ribosomes, RNA, Messenger, Protein Biosynthesis, In Situ Hybridization, Fluorescence, Proteome, Multiprotein Complexes, HEK293 Cells
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
