The DOI matches its Crossref record; 106 of the 106 references it cites were found in a registry or an index.
Conformational buffering underlies functional selection in intrinsically disordered protein regions
Open accessPublished version of a preprint
Abstract
Many disordered proteins conserve essential functions in the face of extensive sequence variation, making it challenging to identify the mechanisms responsible for functional selection. Here we identify the molecular mechanism of functional selection for the disordered adenovirus early gene 1A (E1A) protein. E1A competes with host factors to bind the retinoblastoma (Rb) protein, subverting cell cycle regulation. We show that two binding motifs tethered by a hypervariable disordered linker drive picomolar affinity Rb binding and host factor displacement. Compensatory changes in amino acid sequence composition and sequence length lead to conservation of optimal tethering across a large family of E1A linkers. We refer to this compensatory mechanism as conformational buffering. We also detect coevolution of the motifs and linker, which can preserve or eliminate the tethering mechanism. Conformational buffering and motif-linker coevolution explain robust functional encoding within hypervariable disordered linkers and could underlie functional selection of many disordered protein regions.
Overview
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
Verification
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.
Citations
Cites
Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
Benjamini, Y., & Hochberg, Y. (1995) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1995.tb02031.x · Cited by 109,482
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,047
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
Jalview Version 2—a multiple sequence alignment editor and analysis workbench
Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M. E., & Barton, G. J. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp033 · Cited by 10,349
ColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391
Svergun, D. I., Barberato, C., & Koch, M. (1995) · Journal of Applied Crystallography · doi:10.1107/s0021889895007047 · Cited by 3,388
Ashkenazy, H., Abadi, S., Martz, E., Chay, O., Mayrose, I., Pupko, T., & Ben-Tal, N. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw408 · Cited by 3,163
NMR View: A computer program for the visualization and analysis of NMR data
Johnson, B. A., & Blevins, R. A. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00404272 · Cited by 3,093
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968
The FoldX web server: an online force field
Schymkowitz, J., Borg, J., Stricher, F., Nys, R., Rousseau, F., & Serrano, L. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki387 · Cited by 2,759
Research works printed but not linked: 2
- Girardot, R., Viguier, G., Pérez, J. & Ounsy, M. M. FOXTROT: A JAVA-based application to reduce and analyse SAXS and WAXS piles of 2D data at synchrotron SOLEIL, Synchrotron Soleil. In Proc. 8th canSAS Meeting, Tokai, Japan (2015).
- Good, P. Permutation, Parametric, and Bootstrap Tests of Hypotheses (Springer-Verlag, 2005).
Cited by
Sorted by citations
The molecular basis for cellular function of intrinsically disordered protein regions
Holehouse, A. S., & Kragelund, B. B. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00673-0 · Cited by 741
Self-citationPhase Transitions of Associative Biomacromolecules
Pappu, R. V., Cohen, S. R., Dar, F., Farag, M., & Kar, M. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00814 · Cited by 371
Self-citationConformational ensembles of the human intrinsically disordered proteome
Tesei, G., Trolle, A. I., Jonsson, N., Betz, J., Knudsen, F. E., Pesce, F., Johansson, K. E., & Lindorff‐Larsen, K. (2024) · Nature · doi:10.1038/s41586-023-07004-5 · Cited by 331
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
Alderson, T. R., Pritišanac, I., Kolarić, Đ., Moses, A. M., & Forman-Kay, J. D. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304302120 · Cited by 240
Direct prediction of intrinsically disordered protein conformational properties from sequence
Lotthammer, J. M., Ginell, G. M., Griffith, D., Emenecker, R. J., & Holehouse, A. S. (2024) · Nature Methods · doi:10.1038/s41592-023-02159-5 · Cited by 236
Self-citationELM—the Eukaryotic Linear Motif resource—2024 update
Kumar, M., Michael, S., Alvarado-Valverde, J., Zeke, A., Lázár, T., Glavina, J., Nagy‐Kanta, E., Donagh, J. M., Kálmán, Z. E., Pascarelli, S., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1058 · Cited by 185
Self-citationFerrie, J. J., Karr, J. P., Tjian, R., & Darzacq, X. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.021 · Cited by 142
Intrinsically disordered regions are poised to act as sensors of cellular chemistry
MOSES, D. C., Ginell, G. M., Holehouse, A. S., & Sukenik, S. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.08.001 · Cited by 136
Self-citationSequence-based prediction of intermolecular interactions driven by disordered regions
Ginell, G. M., Emenecker, R. J., Lotthammer, J. M., Keeley, A. T., Plassmeyer, S. P., Razo, N. J., Usher, E. T., Pelham, J. F., & Holehouse, A. S. (2025) · Science · doi:10.1126/science.adq8381 · Cited by 123
Self-citationLindorff-Larsen, K., & Kragelund, B. B. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167196 · Cited by 85
Computer-Aided Drug Discovery for Undruggable Targets
Sun, Q., Wang, H., Xie, J., Wang, L., Mu, J., Li, J., Ren, Y., & Lai, L. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00969 · Cited by 72
Structural biases in disordered proteins are prevalent in the cell
MOSES, D. C., Guadalupe, K. C., Yu, F., Flores, E., Perez, A. R., McAnelly, R. L., Shamoon, N. M., Kaur, G., Cuevas-Zepeda, E., Merg, A. D., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01148-8 · Cited by 66
Self-citationZheng, L. L., Li, J. Z., Wen, M., Xi, D., Zhu, Y., Wei, Q. L., Zhang, X., Ke, G., Xia, F., & Gao, Z. F. (2023) · Science Advances · doi:10.1126/sciadv.adf5868 · Cited by 50
Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation
Juyoux, P., Galdadas, I., Gobbo, D., von Velsen, J., Pelosse, M., Tully, M. D., Vadas, O., Gervasio, F. L., Pellegrini, E., & Bowler, M. W. (2023) · Science · doi:10.1126/science.add7859 · Cited by 49
Emergent microenvironments of nucleoli
King, M. R., Ruff, K. M., & Pappu, R. V. (2024) · Nucleus · doi:10.1080/19491034.2024.2319957 · Cited by 47
Self-citationConformational entropy in molecular recognition of intrinsically disordered proteins
Skriver, K., Theisen, F. F., & Kragelund, B. B. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102697 · Cited by 45
SOURSOP: A Python Package for the Analysis of Simulations of Intrinsically Disordered Proteins
Lalmansingh, J. M., Keeley, A. T., Ruff, K. M., Pappu, R. V., & Holehouse, A. S. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.3c00190 · Cited by 42
Self-citationMolecular grammars of predicted intrinsically disordered regions that span the human proteome
Ruff, K. M., King, M. R., Ying, A. W., Liu, V., Pant, A., Lieberman, W. E., Shinn, M. K., Su, X., Kadoch, C., & Pappu, R. V. (2025) · Cell · doi:10.1016/j.cell.2025.10.019 · Cited by 59
Self-citationAlston, J. J., Ginell, G. M., Soranno, A., & Holehouse, A. S. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c01619 · Cited by 38
Self-citationDynamics and interactions of intrinsically disordered proteins
Arai, M., Suetaka, S., & Ooka, K. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102734 · Cited by 38
A functional map of the human intrinsically disordered proteome
Pritišanac, I., Alderson, T. R., Kolarić, Đ., Zarin, T., Xie, S., Lu, A. X., Alam, A., Maqsood, A., Youn, J., Forman-Kay, J. D., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2604562123 · Cited by 38
Accurate predictions of disordered protein ensembles with STARLING
Novak, B., Lotthammer, J. M., Emenecker, R. J., & Holehouse, A. S. (2026) · Nature · doi:10.1038/s41586-026-10141-2 · Cited by 66
Self-citationOrand, T., & Jensen, M. R. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102958 · Cited by 34
Multivalency emerges as a common feature of intrinsically disordered protein interactions
Sipko, E. L., Chappell, G. F., & Berlow, R. B. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102742 · Cited by 30
Holla, A., Martin, E. W., Dannenhoffer-Lafage, T. P., Ruff, K. M., König, S. L. B., Nüesch, M. F., Chowdhury, A., Louis, J. M., Soranno, A., Nettels, D., et al. (2024) · JACS Au · doi:10.1021/jacsau.4c00673 · Cited by 29
Self-citationShinn, M. K., Cohan, M. C., Bullock, J. L., Ruff, K. M., Levin, P. A., & Pappu, R. V. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2211178119 · Cited by 29
Self-citationStringer, M. A., Cubuk, J., Incicco, J. J., Roy, D., Hall, K. B., Stuchell‐Brereton, M. D., & Soranno, A. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c02356 · Cited by 28
Machine learning methods to study sequence–ensemble–function relationships in disordered proteins
von Bülow, S., Tesei, G., & Lindorff‐Larsen, K. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103028 · Cited by 27
Synapsin Condensation is Governed by Sequence-Encoded Molecular Grammars
Hoffmann, C., Ruff, K. M., Edu, I. A., Shinn, M. K., Tromm, J. V., King, M. R., Pant, A., Ausserwöger, H., Morgan, J. R., Knowles, T. P. J., et al. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.168987 · Cited by 27
Self-citationEntropy, enthalpy, and evolution: Adaptive trade-offs in protein binding thermodynamics
Georgelin, R., & Jackson, C. J. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103080 · Cited by 25
Rational design of disordered proteins for systematic sequence-to-function investigationPreprint
Hunter, K., Brandt, T., Guadalupe, K. C., Kolamunna, K., Lotthammer, J. M., Shamoon, N. M., Nicholson, B., Day, L. M., Martinez, A., Holehouse, A. S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.29.564547 · Cited by 22
Self-citationDirect prediction of intermolecular interactions driven by disordered regionsPreprint
Ginell, G. M., Emenecker, R. J., Lotthammer, J. M., Usher, E. T., & Holehouse, A. S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.03.597104 · Cited by 22
Self-citationUncovering the Contributions of Charge Regulation to the Stability of Single Alpha Helices**
Fossat, M. J., Posey, A. E., & Pappu, R. V. (2023) · ChemPhysChem · doi:10.1002/cphc.202200746 · Cited by 21
Self-citationForsberg, Z., Stepnov, A. A., Tesei, G., Wang, Y., Buchinger, E., Kristiansen, S. K., Aachmann, F. L., Arleth, L., Eijsink, V. G. H., Lindorff‐Larsen, K., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105262 · Cited by 21
Tesei, G., Trolle, A. I., Jonsson, N., Betz, J., Pesce, F., Johansson, K. E., & Lindorff‐Larsen, K. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.08.539815 · Cited by 21
DelRosso, N. V., Suzuki, P., Griffith, D., Lotthammer, J. M., Novak, B., Kocalar, S., Sheth, M. U., Holehouse, A. S., Bintu, L., & Fordyce, P. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.19.608698 · Cited by 23
Self-citationAccurate predictions of conformational ensembles of disordered proteins with STARLINGPreprint
Novak, B., Lotthammer, J. M., Emenecker, R. J., & Holehouse, A. S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.14.638373 · Cited by 17
Self-citationGeneralized design of sequence–ensemble–function relationships for intrinsically disordered proteins
Krueger, R., Brenner, M. P., & Shrinivas, K. (2025) · Nature Computational Science · doi:10.1038/s43588-025-00881-y · Cited by 20
Impact of Linker Length on Biomolecular Condensate Formation
GrandPre, T., Zhang, Y., Pyo, A. G. T., Weiner, B., Li, J.-L., Jonikas, M. C., & Wingreen, N. S. (2023) · PRX Life · doi:10.1103/prxlife.1.023013 · Cited by 16
Wang, Q., Liu, Y., Ma, Y., Lu, Y., Huang, L., & Wang, Z. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.106068 · Cited by 15
Evolution of SLiM-mediated hijack functions in intrinsically disordered viral proteins
Glavina, J., Palópoli, N., & Chemes, L. B. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220059 · Cited by 15
Self-citationDesign of functional intrinsically disordered proteins
Garg, A., Foutel, N. S. G., Gielnik, M. B., & Kjærgaard, M. (2024) · Protein Engineering Design and Selection · doi:10.1093/protein/gzae004 · Cited by 15
Rudinskiy, M., Galli, C., Raimondi, A., & Molinari, M. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01728-4 · Cited by 17
Dasmeh, P., Doronin, R., & Wagner, A. (2021) · Genetics · doi:10.1093/genetics/iyab184 · Cited by 15
Alston, J. J., Soranno, A., & Holehouse, A. S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.06.552128 · Cited by 14
Self-citationCagliani, R., Forni, D., Mozzi, A., Fuchs, R., Tussia-Cohen, D., Arrigoni, F., Pozzoli, U., GIOIA, L. D., Hagai, T., & Sironi, M. (2024) · Molecular Biology and Evolution · doi:10.1093/molbev/msae154 · Cited by 12
Nanotechnology and nano-sized tools: Newer approaches to circumvent oncolytic adenovirus limitations
Shirazi, M. M. A., Saedi, T. A., Moghaddam, Z. S., Nemati, M., شیری, ر., Negahdari, B., & Goradel, N. H. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108611 · Cited by 12
Decoding intrinsically disordered regions in biomolecular condensates
Shi, M., Wu, Z., Zhang, Y., & Li, T. (2025) · Fundamental Research · doi:10.1016/j.fmre.2025.01.013 · Cited by 12
Single-point mutations in disordered proteins: Linking sequence, ensemble, and function
Flores, E., Acharya, N., Castañeda, C. A., & Sukenik, S. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.102987 · Cited by 14
The MDMX Acidic Domain Uses Allovalency to Bind Both p53 and MDMX
Fenton, M. J., Borcherds, W. M., Chen, L., Anbanandam, A., Levy, R., Chen, J., & Daughdrill, G. W. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167844 · Cited by 12
Self-citationDynamic Implications of Noncovalent Interactions in Amphiphilic Single-Chain Polymer Nanoparticles
Dykeman-Bermingham, P. A., Stingaciu, L. R., Do, C., & Knight, A. (2024) · ACS Macro Letters · doi:10.1021/acsmacrolett.4c00269 · Cited by 11
Protein binding and folding through an evolutionary lens
Jemth, P. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102980 · Cited by 11
Toward a unified framework for determining conformational ensembles of disordered proteins
Ghafouri, H., Kadeřávek, P., Melo, A. M., Aspromonte, M. C., Bernadó, P., Cortés, J., Dosztányi, Z., Erdős, G., Feig, M., Janson, G., et al. (2026) · Nature Methods · doi:10.1038/s41592-026-03003-2 · Cited by 15
Self-citationLuo, S., Wohl, S., Zheng, W., & Yang, S. (2023) · Biomolecules · doi:10.3390/biom13030530 · Cited by 10
Mihalič, F., Arcila, D., Pettersson, M. E., Farkhondehkish, P., Andersson, E., Andersson, L., Betancur‐R, R., & Jemth, P. (2024) · Molecular Biology and Evolution · doi:10.1093/molbev/msae018 · Cited by 8
Karlsson, E., Ottoson, C., Ye, W., Andersson, E., & Jemth, P. (2023) · Biochemistry · doi:10.1021/acs.biochem.3c00285 · Cited by 8
Oh, C., Buckley, P. M., Choi, J., Hierro, A., & DiMaio, D. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2307721120 · Cited by 6
Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1
Orand, T., Delaforge, E., Lee, A., Kragelj, J., Tengo, M., Tengo, L., Blackledge, M. J., Erba, E. B., Davis, R. J., Palencia, A., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2419915122 · Cited by 6
LeBlanc, C. J., Stefani, J., Soriano, M., Lam, A., Zintel, M. A., Kotha, S. R., Chase, E., Pimentel-Solorio, G., Vunnum, A., Hu, G. F., et al. (2026) · PLoS Genetics · doi:10.1371/journal.pgen.1012069 · Cited by 9
Host diversification is concurrent with linear motif evolution in a Mastadenovirus hub protein
Glavina, J., de la Vega, R. C. R., Risso, V. A., Leonetti, C. O., Chemes, L. B., & Sanchez, I. E. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167563 · Cited by 6
Self-citationAdvances in the determination of disordered protein ensemble
Ghafouri, H., Tosatto, S. C. E., & Monzón, A. M. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103198 · Cited by 5
Simonsen, S., Larsen, F. B., Søgaard, C. K., Jonsson, N., Lindorff‐Larsen, K., Bruheim, P., Otterlei, M., Hartmann‐Petersen, R., & Kragelund, B. B. (2025) · FEBS Journal · doi:10.1111/febs.70133 · Cited by 6
Carey, O., Fehilly, J., O’Leary, E. T., O’Shea, S., Juda, K., Fitzel, R., Selvaraj, P., Burk, K., Lindsay, A. J., Young, P. W., et al. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169314 · Cited by 6
Badyaev, A. V., Moreno, C. S., Lee, C. A., Britton, S. E., Johnstone, L. M., & Duckworth, R. A. (2026) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2025.2393 · Cited by 4
Krokengen, O. C., Raasakka, A., & Kursula, P. (2023) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2023.101474 · Cited by 7
The Disorderly Nature of Caliciviruses
Young, V. L., McSweeney, A. M., Edwards, M. J., & Ward, V. K. (2024) · Viruses · doi:10.3390/v16081324 · Cited by 5
Correlating disordered activation domain ensembles with gene expression levels
Flores, E., Camacho, A. R., Cuevas-Zepeda, E., McCoy, M., Yu, F., Staller, M. V., & Sukenik, S. (2025) · Biophysical Reports · doi:10.1016/j.bpr.2024.100195 · Cited by 6
Functional and Structural Determinants of Long- and Short-Term Evolution of Herpesvirus Proteins
Fuchs, R., Mozzi, A., Forni, D., Naim, B., Schor, O., Sironi, M., & Hagai, T. (2025) · Molecular Biology and Evolution · doi:10.1093/molbev/msaf256 · Cited by 4
Pozzoli, U., Forni, D., Arrigoni, F., Cagliani, R., GIOIA, L. D., & Sironi, M. (2025) · Genome biology · doi:10.1186/s13059-025-03854-6 · Cited by 4
STI1 domain engages transient helices to mediate Dsk2 phase separation and proteasome condensation
Acharya, N., Daniel, E. A., Dao, T. P., Niblo, J. K., Mulvey, E. O., Sukenik, S., Kraut, D. A., Roelofs, J., & Castañeda, C. A. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00696-1 · Cited by 7
Rational design of disordered proteins for sequence–function investigation
Hunter, K., Brandt, T., Guadalupe, K. C., Kolamunna, K. C., Lotthammer, J. M., Shamoon, N. M., Niblo, J. K., Nicholson, B., Day, L. M., Martinez, A., et al. (2026) · Nature · doi:10.1038/s41586-026-10849-1 · Cited by 26
Self-citationAssessment of Disordered Linker Predictions in the CAID2 Experiment
Wang, K., Hu, G., Wu, Z., Uversky, V. N., & Kurgan, L. (2024) · Biomolecules · doi:10.3390/biom14030287 · Cited by 5
Disentangling Folding from Energetic Traps in Simulations of Disordered Proteins
Lotthammer, J. M., & Holehouse, A. S. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c02005 · Cited by 4
Self-citationPhosphorylation modulates secondary structure of intrinsically disorder regions in RNA polymerase II
Chen, W., Laremore, T. N., Yennawar, N. H., & Showalter, S. A. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108533 · Cited by 4
Dynamic protein interactions probed by NMR spectroscopy
Lee, J., & Lee, J. H. (2025) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.70036 · Cited by 3
Dynamical Buffering of Reconfiguration Dynamics in Intrinsically Disordered Proteins
Ivanović, M. T., Holla, A., Nüesch, M. F., von Roten, V., Schuler, B., & Best, R. B. (2026) · JACS Au · doi:10.1021/jacsau.5c01753 · Cited by 3
The evolution and exploration of intrinsically disordered and phase-separated protein states
Chow, C. F. W., & Tóth-Petróczy, Á. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21809-5.00014-4 · Cited by 3
From molecular descriptions to cellular functions of intrinsically disordered protein regions
Chen, W., Fraser, O. A., George, C., & Showalter, S. A. (2024) · Biophysics Reviews · doi:10.1063/5.0225900 · Cited by 3
Wohl, S., Gilron, Y., & Zheng, W. (2025) · ACS Physical Chemistry Au · doi:10.1021/acsphyschemau.5c00005 · Cited by 5
Zafar, A., Hou, C., Amirani, N., & Shen, Y. (2026) · Human Genetics and Genomics Advances · doi:10.1016/j.xhgg.2026.100618 · Cited by 2
Due, A. D., Davey, N. E., Thomasen, F. E., Morffy, N., Prestel, A., Brakti, I., O’Shea, C., Strader, L. C., Lindorff‐Larsen, K., Skriver, K., et al. (2025) · Protein Science · doi:10.1002/pro.70142 · Cited by 3
Modeling of flexible membrane-bound biomolecular complexes for solution small-angle scattering
Barclay, A., Kragelund, B. B., Arleth, L., & Pedersen, M. C. (2022) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2022.12.024 · Cited by 3
Giudice, A. D., Gurrieri, L., Galantini, L., Fanti, S., Trost, P., Sparla, F., & Fermani, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119308 · Cited by 3
Cagliani, R., Forni, D., Mozzi, A., Fuchs, R., Hagai, T., & Sironi, M. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.07.022 · Cited by 3
Conserved linker length in double dsRBD proteins from plants restricts interdomain motion
Mascali, F. C., Crespo, R., Tabares, L. C., & Rasia, R. M. (2023) · Journal of Magnetic Resonance Open · doi:10.1016/j.jmro.2023.100109 · Cited by 3
Acharya, N., Daniel, E. A., Dao, T. P., Niblo, J. K., Mulvey, E., Sukenik, S., Kraut, D. A., Roelofs, J., & Castañeda, C. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.14.643327 · Cited by 3
Nanopore based single-molecule temporal omics
Li, M., Jiang, J., Niu, H., Ying, Y., & Long, Y. (2023) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2023-0082 · Cited by 2
Structural Adaptation of Secondary P53 Binding Sites on Mdm2 and Mdmx
Higbee, P. S., Dayhoff, G. W., Anbanandam, A., Varma, S., & Daughdrill, G. W. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168626 · Cited by 2
Self-citationKrokengen, O. C., Raasakka, A., & Kursula, P. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.13.507838 · Cited by 2
Holehouse, A. S., Alston, J. J., & Soranno, A. (2024) · Research Square · doi:10.21203/rs.3.rs-4477977/v1 · Cited by 3
Self-citationVu, Q. V., Sitarik, I. M., Li, M. S., & O’Brien, E. P. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c01260 · Cited by 1
Tahzima, R., Charon, J., Díaz, A., Jonghe, K. D., Massart, S., Michon, T., & Vranken, W. (2025) · Frontiers in Virology · doi:10.3389/fviro.2025.1501616 · Cited by 1
Ghafouri, H., Janson, G., Tosatto, S. C. E., & Monzón, A. M. (2025) · Protein Science · doi:10.1002/pro.70427 · Cited by 1
Forni, D., Cagliani, R., & Sironi, M. (2026) · FEBS Letters · doi:10.1002/1873-3468.70368 · Cited by 2
AF ‐ CALVADOS : AlphaFold ‐guided simulations of multi‐domain proteins at the proteome level
von Bülow, S., Johansson, K. E., & Lindorff‐Larsen, K. (2026) · Protein Science · doi:10.1002/pro.70694 · Cited by 12
Cook, C. B. R., Ramsey, K. M., & Barrick, D. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2501607122 · Cited by 1
Meng, D., Glavina, J., Alvarez, H. M. G., Leonetti, C. O., Pollastri, G., & Chemes, L. B. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.169994 · Cited by 1
Self-citationForsberg, Z., Stepnov, A. A., Tesei, G., Wang, Y., Buchinger, E., Kristiansen, S. K., Aachmann, F. L., Arleth, L., Eijsink, V. G. H., Lindorff‐Larsen, K., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.01.543078 · Cited by 1
GrandPre, T., Zhang, Y., Pyo, A. G. T., Weiner, B., Li, J.-L., Jonikas, M. C., & Wingreen, N. S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.11.544494 · Cited by 1
Metadata
- Authors
- González-Foutel, N. S., Glavina, J., Borcherds, W. M., Safranchik, M., Barrera-Vilarmau, S., Sagar, A., Estaña, A., Barozet, A., Garrone, N. A., Fernandez-Ballester, G., Blanes-Mira, C., Sánchez, I. E., de Prat-Gay, G., Cortés, J., Bernadó, P., Pappu, R. V., Holehouse, A. S., Daughdrill, G. W., & Chemes, L. B.
- Affiliations
- Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
- University of South Florida (US)
- Consejo Superior de Investigaciones Científicas (ES)
- Centre National de la Recherche Scientifique (FR)
- Universitat de Miguel Hernández d'Elx (ES)
- Washington University in St. Louis (US)
- Corresponding author
- Pappu, Rohit V.
- Holehouse, Alex S.
- Daughdrill, Gary W.
- ORCID
- Venue
- Nature Structural & Molecular Biology
- Published
- 2022-08
- Volume
- 29
- Issue
- 8
- Pages
- 781-790
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC10262780
- OpenAlex
- W4291018995
- Cited by
- 118
- References
- 106
- Citations by year
- 2026: 22 · 2025: 34 · 2024: 22 · 2023: 30 · 2022: 8
- FWCI
- 7.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
- HAL (submittedVersion, other-oa)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, other-oa)
- Funders
- National Science Foundation (1614766)
- Florida Department of Health (20B17)
- Agence Nationale de la Recherche (2017-, 10-LABX-12-01, ANR-10-INBS-04-01, ANR-10- INBS-05, ANR-10-LABX-12-01, 10-INBS-04-01, ANR‐10_INBS‐04, ANR-10, ANR-10-LABX-0012, ANR-10-INBS-0004, ANR-10-INBS-0005)
- Consejo Nacional de Investigaciones Científicas y Técnicas
- Ministerio de Ciencia e Innovación (RTI2018-097189-C2-1)
- Laboratoire d'Excellence EpiGenMed (ANR-10-LABX-12-01)
- National Institutes of Health
- Deutsches Elektronen-Synchrotron
- Agencia Nacional de Promoción Científica y Tecnológica (2017/1924, CONICET)
- National Cancer Institute (R01CA141244)
- National Institute of General Medical Sciences (R01GM115556)
- National Institute of Neurological Disorders and Stroke (R01NS056114)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- intrinsically disordered proteins, functional selection, adenovirus E1A, retinoblastoma protein, protein-protein binding, cell cycle regulation, protein coevolution
- MeSH terms
- Protein Domains, Amino Acid Sequence, Protein Binding, Retinoblastoma Protein, Adenovirus E1A Proteins, Intrinsically Disordered Proteins
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
