FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies

Intrinsically disordered proteins in cellular signalling and regulation

Wright, P. E., & Dyson, H. J. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3920 · Cited by 2,371 · see citing works

Classification of Intrinsically Disordered Regions and Proteins

van der Lee, R., Buljan, M., Lang, B., Weatheritt, R. J., Daughdrill, G. W., Dunker, A. K., Fuxreiter, M., Gough, J., Gsponer, J., Jones, D. T., et al. (2014) · Chemical Reviews · doi:10.1021/cr400525m · Cited by 2,155 · see citing works

Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering

Bernadó, P., Mylonas, E., Petoukhov, M. V., Blackledge, M. J., & Svergun, D. I. (2007) · Journal of the American Chemical Society · doi:10.1021/ja069124n · Cited by 1,172 · see citing works

Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions

Tompa, P., & Fuxreiter, M. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.10.003 · Cited by 1,080 · see citing works

Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057 · see citing works

Linking folding and binding

Wright, P. E., & Dyson, H. J. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.12.003 · Cited by 1,012 · see citing works

Structural basis for the binding of proline-rich peptides to SH3 domains

Yu, H., Chen, J., Feng, S., Dalgarno, D. C., Brauer, A. W., & Schrelber, S. L. (1994) · Cell · doi:10.1016/0092-8674(94)90367-0 · Cited by 1,003 · see citing works

DisProt: the Database of Disordered Proteins

Sickmeier, M. D., Hamilton, J. A., LeGall, T., Vacic, V., Cortese, M. S., Tantos, Á., Szabó, B., Tompa, P., Chen, J. Y., Uversky, V. N., et al. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl893 · Cited by 796 · see citing works

D2P2: database of disordered protein predictions

Oates, M. E., Romero, P., Ishida, T., Ghalwash, M., Mizianty, M. J., Xue, B., Dosztányi, Z., Uversky, V. N., Obradovic, Z., Kurgan, L., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1226 · Cited by 705 · see citing works

The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules

Wu, H., & Fuxreiter, M. (2016) · Cell · doi:10.1016/j.cell.2016.05.004 · Cited by 352 · see citing works

Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor

Mittag, T., Orlicky, S. M., Choy, W., Tang, X., Lin, H., Sicheri, F., Kay, L. E., Tyers, M., & Forman-Kay, J. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809222105 · Cited by 338 · see citing works

Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors

Milles, S., Mercadante, D., Aramburu, I. V., Jensen, M. R., Banterle, N., Koehler, C., Tyagi, S., Clarke, J., Shammas, S. L., Blackledge, M. J., et al. (2015) · Cell · doi:10.1016/j.cell.2015.09.047 · Cited by 304 · see citing works

Fuzzy Complexes: A More Stochastic View of Protein Function

Fuxreiter, M., & Tompa, P. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4614-0659-4_1 · Cited by 240 · see citing works

Fuzzy complexes: Specific binding without complete folding

Sharma, R., Ráduly, Z., Miskei, M., & Fuxreiter, M. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.07.022 · Cited by 226 · see citing works

pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins

Váradi, M., Kosol, S., Lebrun, P., Valentini, E., Blackledge, M. J., Dunker, A. K., Felli, I. C., Forman-Kay, J. D., Kriwacki, R. W., Pierattelli, R., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt960 · Cited by 211 · see citing works

MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins

Potenza, E., Domenico, T. D., Walsh, I., & Tosatto, S. C. E. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku982 · Cited by 193 · see citing works

Fuzziness: linking regulation to protein dynamics

Fuxreiter, M. (2011) · Molecular BioSystems · doi:10.1039/c1mb05234a · Cited by 180 · see citing works

The intrinsically disordered C‐terminal domain of the measles virus nucleoprotein interacts with the C‐terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded

Bourhis, J., Receveur‐Brechot, V., Oglesbee, M., Zhang, X., Buccellato, M. A., Darbon, H., Canard, B., Finet, S., & Longhi, S. (2005) · Protein Science · doi:10.1110/ps.051411805 · Cited by 147 · see citing works

IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners

Fukuchi, S., Amemiya, T., Sakamoto, S., Nobe, Y., Hosoda, K., Kado, Y., Murakami, S. D., Koike, R., Hiroaki, H., & Ota, M. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1010 · Cited by 122 · see citing works

Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding

Andrésen, C., Helander, S., Lemak, A. S., Farès, C., Csizmók, V., Carlsson, J., Penn, L. Z., Forman-Kay, J. D., Arrowsmith, C. H., Lundström, P., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks263 · Cited by 119 · see citing works

Tail-Mediated Collapse of HMGB1 Is Dynamic and Occurs via Differential Binding of the Acidic Tail to the A and B Domains

Stott, K. M., Watson, M. L., Howe, F. S., Grossmann, J. G., & Thomas, J. O. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.07.045 · Cited by 116 · see citing works

Ensemble modeling of protein disordered states: Experimental restraint contributions and validation

Marsh, J. A., & Forman-Kay, J. D. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23220 · Cited by 114 · see citing works

Intrinsically Disordered Proteins: From Sequence and Conformational Properties toward Drug Discovery

Rezaei‐Ghaleh, N., Blackledge, M. J., & Zweckstetter, M. (2012) · ChemBioChem · doi:10.1002/cbic.201200093 · Cited by 106 · see citing works

NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain

Vise, P. D. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki336 · Cited by 103 · see citing works

Linker length and composition influence the flexibility of Oct‐1 DNA binding

van Leeuwen, H. C., Strating, M., Rensen, M., de Laat, W. L., & van der Vliet, P. C. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.2043 · Cited by 100 · see citing works

Interaction of the Eukaryotic Initiation Factor 4E with 4E-BP2 at a Dynamic Bipartite Interface

Lukhele, S., Bah, A., Lin, H., Sonenberg, N., & Forman-Kay, J. D. (2013) · Structure · doi:10.1016/j.str.2013.08.030 · Cited by 83 · see citing works

Compensatory Adaptations of Structural Dynamics in an Intrinsically Disordered Protein Complex

Kurzbach, D., Schwarz, T. C., Platzer, G., Höfler, S., Hinderberger, D., & Konrat, R. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201308389 · Cited by 63 · see citing works

The Affinity of Ets-1 for DNA is Modulated by Phosphorylation Through Transient Interactions of an Unstructured Region

Lee, G. M., Pufall, M. A., Meeker, C. A., Kang, H.-S., Graves, B. J., & McIntosh, L. P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.064 · Cited by 58 · see citing works

Structural basis for epitope masking and strain specificity of a conserved epitope in an intrinsically disordered malaria vaccine candidate

Morales, R. A. V., MacRaild, C. A., Seow, J., Krishnarjuna, B., Drinkwater, N., Rouet, R., Anders, R. F., Christ, D., McGowan, S., & Norton, R. S. (2015) · Scientific Reports · doi:10.1038/srep10103 · Cited by 31 · see citing works

Interaction of Nonstructural Protein 5A of the Hepatitis C Virus with Src Homology 3 Domains Using Noncanonical Binding Sites

Schwarten, M., Sólyom, Z., Feuerstein, S., Aladağ, A., Hoffmann, S., Willbold, D., & Brutscher, B. (2013) · Biochemistry · doi:10.1021/bi400363v · Cited by 22 · see citing works

IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding

Mészáros, B., Erdős, G., & Dosztányi, Z. (2018) · Nucleic Acids Res. · doi:10.1093/nar/gky384 · Cited by 1,376 · see citing works

AlphaFold and Implications for Intrinsically Disordered Proteins

Ruff, K. M., & Pappu, R. V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167208 · Cited by 635 · see citing works

Analyzing Protein Disorder with IUPred2A

Erdős, G., & Dosztányi, Z. (2020) · Current Protocols in Bioinformatics · doi:10.1002/cpbi.99 · Cited by 336 · see citing works

MobiDB: intrinsically disordered proteins in 2021

Piovesan, D., Necci, M., Escobedo, N., Monzón, A. M., Hatos, A., Mičetić, I., Quaglia, F., Paladin, L., Ramasamy, P., Dosztányi, Z., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1058 · Cited by 223 · see citing works

MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins

Piovesan, D., Tabaro, F., Paladin, L., Necci, M., Mičetić, I., Camilloni, C., Davey, N. E., Dosztányi, Z., Mészáros, B., Monzón, A. M., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1071 · Cited by 208 · see citing works

LLPSDB: a database of proteins undergoing liquid–liquid phase separation in vitro

Li, Q., Peng, X., Li, Y.-Q., Tang, W.-Y., Zhu, J., Huang, J., Qi, Y., & Zhang, Z.-Q. (2019) · Nucleic Acids Res. · doi:10.1093/nar/gkz778 · Cited by 179 · see citing works

Fuzziness and Frustration in the Energy Landscape of Protein Folding, Function, and Assembly

Gianni, S., Freiberger, M. I., Jemth, P., Ferreiro, D. U., Wolynes, P. G., & Fuxreiter, M. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.0c00813 · Cited by 156 · see citing works

DisProt in 2022: improved quality and accessibility of protein intrinsic disorder annotation

Quaglia, F., Mészáros, B., Salladini, E., Hatos, A., Pancsa, R., Chemes, L. B., Pajkos, M., Lázár, T., Peña‐Díaz, S., Santos, J., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1082 · Cited by 157 · see citing works

Fuzziness in Protein Interactions—A Historical Perspective

Fuxreiter, M. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.02.015 · Cited by 147 · see citing works

DisProt in 2024: improving function annotation of intrinsically disordered proteins

Aspromonte, M. C., Nugnes, M. V., Quaglia, F., Bouharoua, A., Sagris, V., Promponas, V. J., Chasapi, A., Fichó, E., Balatti, G. E., Parisi, G. D., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad928 · Cited by 142 · see citing works

Behaviour of intrinsically disordered proteins in protein–protein complexes with an emphasis on fuzziness

Olsen, J. G., Teilum, K., & Kragelund, B. B. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2560-7 · Cited by 129 · see citing works

Charge pattern matching as a ‘fuzzy’ mode of molecular recognition for the functional phase separations of intrinsically disordered proteins

Lin, Y., Brady, J. P., Forman-Kay, J. D., & Chan, H. S. (2017) · New Journal of Physics · doi:10.1088/1367-2630/aa9369 · Cited by 124 · see citing works

Sequence-Based Prediction of Fuzzy Protein Interactions

Miskei, M., Horváth, A., Vendruscolo, M., & Fuxreiter, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.017 · Cited by 111 · see citing works

Is protein context responsible for peptide-mediated interactions?

Zhou, P., Miao, Q., Yan, F., Li, Z., Jiang, Q., Wen, L., & Meng, Y. (2019) · Molecular Omics · doi:10.1039/c9mo00041k · Cited by 113 · see citing works

The Unique Domain Forms a Fuzzy Intramolecular Complex in Src Family Kinases

Arbesú, M., Maffei, M., Cordeiro, T. N., Teixeira, J. M. C., Pérez, Y., Bernadó, P., Roche, S., & Pons, M. (2017) · Structure · doi:10.1016/j.str.2017.02.011 · Cited by 93 · see citing works

DIBS: a repository of disordered binding sites mediating interactions with ordered proteins

Schád, É., Fichó, E., Pancsa, R., Simon, I., Dosztányi, Z., & Mészáros, B. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx640 · Cited by 93 · see citing works

MOBIDB in 2025: integrating ensemble properties and function annotations for intrinsically disordered proteins

Piovesan, D., Conte, A. D., Mehdiabadi, M., Aspromonte, M. C., Blum, M., Tesei, G., von Bülow, S., Lindorff‐Larsen, K., & Tosatto, S. C. E. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae969 · Cited by 81 · see citing works

Fuzziness enables context dependence of protein interactions

Miskei, M., Gregus, A., Sharma, R., Duro, N., Zsolyomi, F., & Fuxreiter, M. (2017) · FEBS Letters · doi:10.1002/1873-3468.12762 · Cited by 82 · see citing works

Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains

Arbesú, M., Iruela, G., Fuentes, H., Teixeira, J. M. C., & Pons, M. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00039 · Cited by 79 · see citing works

Fold or not to fold upon binding — does it really matter?

Fuxreiter, M. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.09.008 · Cited by 76 · see citing works

Unique insights to intrinsically disordered proteins provided by ion mobility mass spectrometry

Stuchfield, D., & Barran, P. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.01.007 · Cited by 72 · see citing works

An arsenal of methods for the experimental characterization of intrinsically disordered proteins – How to choose and combine them?

Schramm, A., Bignon, C., Brocca, S., Grandori, R., Santambrogio, C., & Longhi, S. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.07.020 · Cited by 66 · see citing works

Mechanistic roles of protein disorder within transcription

Shammas, S. L. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.02.003 · Cited by 64 · see citing works

Dynamic multivalent interactions of intrinsically disordered proteins

Weng, J., & Wang, W. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.11.001 · Cited by 61 · see citing works

Structural Ensemble Modulation upon Small-Molecule Binding to Disordered Proteins

Heller, G. T., Bonomi, M., & Vendruscolo, M. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.03.015 · Cited by 61 · see citing works

Intrinsically disordered chromatin protein NUPR1 binds to the C-terminal region of Polycomb RING1B

Santofimia‐Castaño, P., Rizzuti, B., Pey, A. L., Soubeyran, P., Vidal, M., Urrutia, R. A., Iovanna, J., & Neira, J. L. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1619932114 · Cited by 56 · see citing works

Sequence-based prediction of protein binding mode landscapes

Horváth, A., Miskei, M., Ambrus, V., Vendruscolo, M., & Fuxreiter, M. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1007864 · Cited by 55 · see citing works

FuzDB: a new phase in understanding fuzzy interactions

Hatos, A., Monzón, A. M., Tosatto, S. C. E., Piovesan, D., & Fuxreiter, M. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1060 · Cited by 54 · see citing works

Modeling disordered protein interactions from biophysical principles

Peterson, L. X., Roy, A., Christoffer, C. W., Terashi, G., & Kihara, D. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005485 · Cited by 54 · see citing works

Analytical Theory for Sequence-Specific Binary Fuzzy Complexes of Charged Intrinsically Disordered Proteins

Amin, A. N., Lin, Y., Das, S., & Chan, H. S. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c04575 · Cited by 54 · see citing works

Moonlighting Proteins in the Fuzzy Logic of Cellular Metabolism

Liu, H., & Jeffery, C. J. (2020) · Molecules · doi:10.3390/molecules25153440 · Cited by 52 · see citing works

How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication

Longhi, S., Bloyet, L.-M., Gianni, S., & Gerlier, D. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2556-3 · Cited by 48 · see citing works

Insights into the conformations and dynamics of intrinsically disordered proteins using single-molecule fluorescence

Gomes, G.-N. W., & Gradinaru, C. C. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.06.008 · Cited by 48 · see citing works

Tutorial: a guide for the selection of fast and accurate computational tools for the prediction of intrinsic disorder in proteins

Kurgan, L., Hu, G., Wang, K., Ghadermarzi, S., Zhao, B., Malhis, N., Erdős, G., Gsponer, J. A., Uversky, V. N., & Dosztányi, Z. (2023) · Nature Protocols · doi:10.1038/s41596-023-00876-x · Cited by 47 · see citing works

A Numb–Mdm2 fuzzy complex reveals an isoform-specific involvement of Numb in breast cancer

Colaluca, I. N., Basile, A., Freiburger, L. A., D'Uva, V., Disalvatore, D., Vecchi, M., Confalonieri, S., Tosoni, D., Cecatiello, V., Malabarba, M. G., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201709092 · Cited by 43 · see citing works

Protein Databases Related to Liquid–Liquid Phase Separation

Li, Q., Wang, X., Dou, Z., Yang, W., Huang, B., Lou, J., & Zhang, Z. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186796 · Cited by 44 · see citing works

Biotin proximity tagging favours unfolded proteins and enables the study of intrinsically disordered regions

Minde, D. P., Ramakrishna, M., & Lilley, K. (2020) · Communications Biology · doi:10.1038/s42003-020-0758-y · Cited by 35 · see citing works

Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins

Bhattarai, A., & Emerson, I. A. (2020) · Journal of Biosciences · doi:10.1007/s12038-020-0010-4 · Cited by 39 · see citing works

Rational drug design targeting intrinsically disordered proteins

Wang, H., Xiong, R., & Lai, L. (2023) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1685 · Cited by 39 · see citing works

Fuzzy protein theory for disordered proteins

Fuxreiter, M. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200239 · Cited by 37 · see citing works

Advanced Sampling Methods for Multiscale Simulation of Disordered Proteins and Dynamic Interactions

Gong, X., Zhang, Y., & Chen, J. (2021) · Biomolecules · doi:10.3390/biom11101416 · Cited by 37 · see citing works

Characterization of Dynamic IDP Complexes by NMR Spectroscopy

Prestel, A., Bugge, K., Staby, L., Hendus-Altenburger, R., & Kragelund, B. B. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.08.026 · Cited by 34 · see citing works

Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions

Zhao, B., & Kurgan, L. (2022) · Biomolecules · doi:10.3390/biom12070888 · Cited by 36 · see citing works

Amphipathic helical peptides hamper protein-protein interactions of the intrinsically disordered chromatin nuclear protein 1 (NUPR1)

Santofimia‐Castaño, P., Rizzuti, B., Abián, O., Velázquez‐Campoy, A., Iovanna, J., & Neira, J. L. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.03.009 · Cited by 33 · see citing works

IDPology of the living cell: intrinsic disorder in the subcellular compartments of the human cell

Zhao, B., Katuwawala, A., Uversky, V. N., & Kurgan, L. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03654-0 · Cited by 33 · see citing works

Machine Learning Generation of Dynamic Protein Conformational Ensembles

Zheng, L.-E., Barethiya, S., Nordquist, E. B., & Chen, J. (2023) · Molecules · doi:10.3390/molecules28104047 · Cited by 32 · see citing works

Protein–Protein Interactions Mediated by Intrinsically Disordered Protein Regions Are Enriched in Missense Mutations

Wong, E. T. C., So, V., Guron, M., Kuechler, E. R., Malhis, N., Bui, J. M., & Gsponer, J. A. (2020) · Biomolecules · doi:10.3390/biom10081097 · Cited by 31 · see citing works

Toward Accurate Coarse-Grained Simulations of Disordered Proteins and Their Dynamic Interactions

Zhang, Y., Liu, X., & Chen, J. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c00974 · Cited by 31 · see citing works

Advanced computational approaches to understand protein aggregation

Ghosh, D., Biswas, A., & Radhakrishna, M. (2024) · Biophysics Reviews · doi:10.1063/5.0180691 · Cited by 31 · see citing works

Electrostatic interactions in molecular recognition of intrinsically disordered proteins

Yang, J., Zeng, Y., Liu, Y., Gao, M., Liu, S., Su, Z., & Huang, Y. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1692073 · Cited by 30 · see citing works

Resources for computational prediction of intrinsic disorder in proteins

Kurgan, L. (2022) · Methods · doi:10.1016/j.ymeth.2022.03.018 · Cited by 28 · see citing works

Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model

Sisk, T. R., & Robustelli, P. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313360121 · Cited by 26 · see citing works

Extreme Fuzziness: Direct Interactions between Two IDPs

Wang, W., & Wang, D. (2019) · Biomolecules · doi:10.3390/biom9030081 · Cited by 27 · see citing works

Partner-Mediated Polymorphism of an Intrinsically Disordered Protein

Bignon, C., Troilo, F., Gianni, S., & Longhi, S. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.11.012 · Cited by 24 · see citing works

Cancer-Associated Mutations Perturb the Disordered Ensemble and Interactions of the Intrinsically Disordered p53 Transactivation Domain

Schrag, L. G., Liu, X., Thevarajan, I., Prakash, O., Žółkiewski, M., & Chen, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167048 · Cited by 25 · see citing works

FuzPred: a web server for the sequence-based prediction of the context-dependent binding modes of proteins

Hatos, A., Teixeira, J. M. C., Barrera-Vilarmau, S., Horváth, A., Tosatto, S. C. E., Vendruscolo, M., & Fuxreiter, M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad214 · Cited by 24 · see citing works

The intrinsically disordered nature of the peroxisomal protein translocation machinery

Barros‐Barbosa, A., Rodrigues, T. A., Ferreira, M. J., Pedrosa, A. G., Teixeira, N. R., Francisco, T., & Azevedo, J. E. (2018) · FEBS Journal · doi:10.1111/febs.14704 · Cited by 24 · see citing works

Probing Surfaces in Dynamic Protein Interactions

Spreitzer, E., Usluer, S., & Madl, T. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.032 · Cited by 23 · see citing works

Amino acid polymorphisms in the fibronectin-binding repeats of fibronectin-binding protein A affect bond strength and fibronectin conformation

Casillas-Ituarte, N. N., da Cruz, C. H. B., Lins, R. D., DiBartola, A. C., Howard, J., Liang, X., Höök, M., Viana, I. F. T., Sierra‐Hernández, M. R., & Lower, S. K. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.786012 · Cited by 19 · see citing works

Integrating disorder in globular multidomain proteins: Fuzzy sensors and the role of SH3 domains

Arbesú, M., & Pons, M. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108161 · Cited by 19 · see citing works

Concomitant disorder and high‐affinity zinc binding in the human zinc‐ and iron‐regulated transport protein 4 intracellular loop

Bafaro, E. M., Maciejewski, M. W., Hoch, J. C., & Dempski, R. E. (2019) · Protein Science · doi:10.1002/pro.3591 · Cited by 19 · see citing works

Tumor‐Suppressor p53TAD1–60 Forms a Fuzzy Complex with Metastasis‐Associated S100A4: Structural Insights and Dynamics by an NMR/MD Approach

Dudás, E. F., Pálfy, G., Menyhárd, D. K., Sebák, F., Ecsédi, P., Nyitray, L., & Bodor, A. (2020) · ChemBioChem · doi:10.1002/cbic.202000348 · Cited by 18 · see citing works

Functions of intrinsically disordered proteins through evolutionary lenses

Pajkos, M., & Dosztányi, Z. (2021) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2021.06.017 · Cited by 18 · see citing works

Intrinsically disordered protein NUPR1 binds to the armadillo-repeat domain of Plakophilin 1

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Intrinsically Disordered Chromatin Protein NUPR1 Binds to the Enzyme PADI4

Araujo‐Abad, S., Neira, J. L., Rizzuti, B., García-Morales, P., Romero, C. D. J., Santofimia‐Castaño, P., & Iovanna, J. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168033 · Cited by 17 · see citing works

Altered dynamics may drift pathological fibrillization in membraneless organelles

Tüű-Szabó, B., Hoffka, G., Duro, N., Koczy, L., & Fuxreiter, M. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.04.005 · Cited by 17 · see citing works

Databases for intrinsically disordered proteins

Piovesan, D., Monzón, A. M., Quaglia, F., & Tosatto, S. C. E. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321012109 · Cited by 16 · see citing works

The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes

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FLIPPER: Predicting and Characterizing Linear Interacting Peptides in the Protein Data Bank

Monzón, A. M., Bonato, P., Necci, M., Tosatto, S. C. E., & Piovesan, D. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166900 · Cited by 16 · see citing works

Binding and folding in transcriptional complexes

Smith, N. C., Kuravsky, M. L., Shammas, S. L., & Matthews, J. M. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.026 · Cited by 15 · see citing works

Intrinsic disorder and flexibility in proteins: a challenge for structural biology and drug design

Zanotti, G. (2023) · Crystallography Reviews · doi:10.1080/0889311x.2023.2208518 · Cited by 15 · see citing works

Measuring Intrinsic Disorder and Tracking Conformational Transitions Using Rosetta ResidueDisorder

Seffernick, J. T., Ren, H., Kim, S. S., & Lindert, S. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b04333 · Cited by 12 · see citing works

Intrinsically Disordered Transactivation Domains Bind to TAZ1 Domain of CBP via Diverse Mechanisms

Gao, M., Yang, J., Liu, S., Su, Z., & Huang, Y. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.08.026 · Cited by 11 · see citing works

Versatile roles of disordered transcription factor effector domains in transcriptional regulation

Datta, R. R., Akdogan, D., Tezcan, E. B., & Önal, P. (2025) · FEBS Journal · doi:10.1111/febs.17424 · Cited by 10 · see citing works

Predicting Protein–Protein Interfaces that Bind Intrinsically Disordered Protein Regions

Wong, E. T. C., & Gsponer, J. A. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.06.010 · Cited by 10 · see citing works

Predicting Protein Conformational Disorder and Disordered Binding Sites

Tamburrini, K. C., Pesce, G., Nilsson, J. F., Gondelaud, F., Kajava, A. V., Berrin, J., & Longhi, S. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2095-3_4 · Cited by 10 · see citing works

Where differences resemble: sequence-feature analysis in curated databases of intrinsically disordered proteins

Necci, M., Piovesan, D., & Tosatto, S. C. E. (2018) · Database · doi:10.1093/database/bay127 · Cited by 10 · see citing works

Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery

Luo, S., Wohl, S., Zheng, W., & Yang, S. (2023) · Biomolecules · doi:10.3390/biom13030530 · Cited by 9 · see citing works

Engagement of intrinsic disordered proteins in protein–protein interaction

Roterman, I., Stąpor, K., & Konieczny, L. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1230922 · Cited by 9 · see citing works

Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional Partners

Troilo, F., Bignon, C., Gianni, S., Fuxreiter, M., & Longhi, S. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.08.006 · Cited by 9 · see citing works

NoLogo: a new statistical model highlights the diversity and suggests new classes of Crm1-dependent nuclear export signals

Liku, M. E., Legere, E.-A., & Moses, A. M. (2018) · BMC Bioinformatics · doi:10.1186/s12859-018-2076-7 · Cited by 9 · see citing works

New insights into disordered proteins and regions according to the FOD-M model

Roterman, I., Stąpor, K., Fabian, P., & Konieczny, L. (2022) · PLoS ONE · doi:10.1371/journal.pone.0275300 · Cited by 8 · see citing works

When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes

Sacquin‐Mora, S., & Prévost, C. (2021) · Biomolecules · doi:10.3390/biom11101529 · Cited by 8 · see citing works

Intrinsically disordered proteins in biology: One for all, all for one

Yruela, I., & Neira, J. L. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108328 · Cited by 8 · see citing works

Conformational Characterization of Intrinsically Disordered Proteins and Its Biological Significance

Delaforge, E., Cordeiro, T. N., Bernadó, P., & Sibille, N. (2018) · Modern Magnetic Resonance · doi:10.1007/978-3-319-28388-3_52 · Cited by 7 · see citing works

Specific and Fuzzy Interactions Cooperate in Modulating Protein Half-Life

Sharma, R., Demény, M. Á., Ambrus, V., Király, S. B., Kurtán, T., Gatti‐Lafranconi, P., & Fuxreiter, M. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.02.006 · Cited by 7 · see citing works

Disobind: A sequence-based, partner-dependent contact map and interface residue predictor for intrinsically disordered regions

Majila, K., Ullanat, V., & Viswanath, S. (2026) · Cell Systems · doi:10.1016/j.cels.2025.101486 · Cited by 8 · see citing works

Disorder Mediated Oligomerization of DISC1 Proteins Revealed by Coarse-Grained Molecular Dynamics Simulations

Roche, J., & Potoyan, D. A. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b07467 · Cited by 5 · see citing works

Sequence and Structure Properties Uncover the Natural Classification of Protein Complexes Formed by Intrinsically Disordered Proteins via Mutual Synergistic Folding

Mészáros, B., Dobson, L., Fichó, E., & Simon, I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215460 · Cited by 6 · see citing works

The Role of Med15 Sequence Features in Transcription Factor Interactions

Cooper, D. G., Liu, S., Grunkemeyer, E., & Fassler, J. S. (2024) · Molecular and Cellular Biology · doi:10.1080/10985549.2024.2436672 · Cited by 5 · see citing works

Simulations of Higher‐Order Protein Organizations Using a Fuzzy Framework

Tüű-Szabó, B., Kóczy, L. T., & Fuxreiter, M. (2018) · Complexity · doi:10.1155/2018/6360846 · Cited by 5 · see citing works

Cellular labelling favours unfolded proteinsPreprint

Minde, D. P., Ramakrishna, M., & Lilley, K. (2018) · bioRxiv · doi:10.1101/274761 · Cited by 3 · see citing works

Exploring Protein Intrinsic Disorder with MobiDB

Monzón, A. M., Hatos, A., Necci, M., Piovesan, D., & Tosatto, S. C. E. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0524-0_6 · Cited by 4 · see citing works

Coarse-Grained Simulations of Phosphorylation Regulation of p53 Autoinhibition

Barethiya, S., Schultz, S., Zhang, Y., & Chen, J. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00668 · Cited by 3 · see citing works

FuzDrop: sequence-based prediction of the propensity of proteins for liquid–liquid phase separation and aggregation

Vendruscolo, M., & Fuxreiter, M. (2026) · Nature Protocols · doi:10.1038/s41596-025-01267-0 · Cited by 3 · see citing works

DNA-binding, multivalent interactions and phase separation in transcriptional activation

Smith, N. C., & Matthews, J. M. (2023) · Australian Journal of Chemistry · doi:10.1071/ch22269 · Cited by 3 · see citing works

Conformational Characterization of Intrinsically Disordered Proteins and Its Biological Significance

Delaforge, E., Cordeiro, T. N., Bernadó, P., & Sibille, N. (2017) · Springer eBooks · doi:10.1007/978-3-319-28275-6_52-1 · Cited by 3 · see citing works

Simulations of higher-order protein assemblies using a fuzzy frameworkPreprint

Tüű-Szabó, B., Kóczy, L. T., & Fuxreiter, M. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/248062 · Cited by 3 · see citing works

Guidelines for experimental characterization of liquid–liquid phase separation in vitro

Pattanashetty, S. G., Joshi, A., Walimbe, A., & Mukhopadhyay, S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00012-9 · Cited by 2 · see citing works

A Deep Learning Method for Predicting Interactions for Intrinsically Disordered Regions of ProteinsPreprint

Majila, K., Ullanat, V., & Viswanath, S. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5133412 · Cited by 1 · see citing works

Fuzziness: linking regulation to protein dynamics

Fuxreiter, M. (2011) · Molecular BioSystems · doi:10.1039/c1mb05234a · Cited by 180 · see citing works

Fuzziness in Protein Interactions—A Historical Perspective

Fuxreiter, M. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.02.015 · Cited by 147 · see citing works

Fuzziness ‐ Disorder in Protein Complexes ‐ Imparts Versatility on Signalling

Fuxreiter, M. (2015) · The FASEB Journal · doi:10.1096/fasebj.29.1_supplement.372.1

Fuzzy Complexes: A More Stochastic View of Protein Function

Fuxreiter, M., & Tompa, P. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4614-0659-4_1 · Cited by 240 · see citing works

Fuzziness : structural disorder in protein complexes

Fuxreiter, M., & Tompa, P. (2012) · doi:10.1007/978-1-4614-0659-4 · Cited by 28 · see citing works