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FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies
Open accessAbstract
FuzDB (http://protdyn-database.org) compiles experimentally observed fuzzy protein complexes, where intrinsic disorder (ID) is maintained upon interacting with a partner (protein, nucleic acid or small molecule) and directly impacts biological function. Entries in the database have both (i) structural evidence demonstrating the structural multiplicity or dynamic disorder of the ID region(s) in the partner bound form of the protein and (ii) in vitro or in vivo biological evidence that indicates the significance of the fuzzy region(s) in the formation, function or regulation of the assembly. Unlike the other intrinsically disordered or unfolded protein databases, FuzDB focuses on ID regions within a biological context, including higher-order assemblies and presents a detailed analysis of the structural and functional data. FuzDB also provides interpretation of experimental results to elucidate the molecular mechanisms by which fuzzy regions-classified on the basis of topology and mechanism-interfere with the structural ensembles and activity of protein assemblies. Regulatory sites generated by alternative splicing (AS) or post-translational modifications (PTMs) are also collected. By assembling all this information, FuzDB could be utilized to develop stochastic structure-function relationships for proteins and could contribute to the emergence of a new paradigm.
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“since many (not all) IDRs can undergo coupled folding and binding into context-specific threedimensional structures, 26,45”
From AlphaFold and Implications for Intrinsically Disordered Proteins (2021) · cites this paper as [26]
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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 2,482
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 2,249
Self-citationStructural 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
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
Self-citationIntrinsically 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
Wright, P. E., & Dyson, H. J. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.12.003 · Cited by 1,012
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
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
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
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
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Bioinformatical Approaches to Unstructured/Disordered Proteins and Their Complexes
Mészáros, B., Dosztányi, Z., Fichó, E., Magyar, C., & Simon, I. (2018) · Springer series on bio- and neurosystems · doi:10.1007/978-3-319-95843-9_17
Amin, A. N., Lin, Y., Das, S., & Chan, H. S. (2019) · arXiv (Cornell University)
Orders of disorder: computational analysis of the interactions of intrinsically disordered proteins
Fichó, E. (2019) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2018.256
A tumormetasztázisban szerepet játszó néhány fehérje vizsgálata NMR spektroszkópiával
Pálfy, G. (2019) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2019.142
Chakraborty, R., & Hasija, Y. (2022) · Soft Computing · doi:10.1007/s00500-022-07085-w
Forman-Kay, J. D., & Chong, A. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736585742.793566654
A tumormetasztázisban szerepet játszó néhány fehérje vizsgálata NMR spektroszkópiával
Pálfy, G. (2019) · Eötvös Loránd Tudományegyetem · doi:10.15476/q1ms-3e22
Majila, K., & Viswanath, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.22.609111
Meghatározatlan (2018) · Nyelvtudományi Közlemények · doi:10.15776/nyk.2018.114.10
Yang, T., Zhang, R.-R., Lv, X.-R., Lv, T., Wang, B., Zhang, Y., Wang, P., Zhou, Q., Jiang, D., Liu, Z., et al. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.112002
A Comprehensive Atlas and Machine-Learning Framework for Predicting IDR-Protein Binding AffinityPreprint
Adhikari, S., Choudhuri, S., & Mondal, J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.21.707165
Molecular mechanisms of folding of intrinsically disordered proteins
Troilo, F. (2018) · theses.fr (ABES) · doi:10.70675/e70e7c51zcde2z4e24z8fd6z79d2d48d8c88
Structural and functional investigation of the C-terminal intrinsically disordered fragment of ErbB2
Pinet, L. (2019) · theses.fr (ABES) · doi:10.70675/475c3429zc6c3z40ffz8928zcf02d751d48d · Cited by 1
Caractérisation d’une famille de protéines intrinsèquement désordonnées, les syndécans
Gondelaud, F. (2020) · theses.fr (ABES) · doi:10.70675/a43fb43bzced0z479cz9a50z4fc7530e838d
Fernández, M. L., Bastien, M. C., Tavolaro, F. G., & Marino‐Buslje, C. (2026) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2026.1907936
Shape-shifting proteins and the subtlety in their form and function
Kulkarni, P., Bhattacharya, S., Mohanty, A. R., Ramisetty, S. K., Pisick, E., Orban, J. P., Uversky, V. N., Weninger, K., Huang, S., Chou, T., et al. (2026) · iScience · doi:10.1016/j.isci.2026.117386
Berilo, A., Odobašić, N., Husić, M., Hromić‐Jahjefendić, A., Adilović, M., & Uversky, V. N. (2026) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6c05122
FAIRsharing record for: MobiDB
FAIRsharing Team, & Mičetić, I. (2015) · FAIRsharing.org · doi:10.25504/fairsharing.jwra3e
Metadata
- Authors
- Miskei, M., Antal, C., & Fuxreiter, M.
- Affiliations
- University of Debrecen (HU)
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2016-10-28
- Volume
- 45
- Issue
- D1
- Pages
- D228-D235
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC5210525
- OpenAlex
- W2541950838
- Cited by
- 119
- References
- 30
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 6 · 2023: 11 · 2022: 8 · 2021: 9 · 2020: 20 · 2019: 21 · 2018: 19 · 2017: 15
- FWCI
- 9.53
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nucleic Acids Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion, other-oa)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
- HighWire Press Open Archive (submittedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- Magyar Tudományos Akadémia
- Debreceni Egyetem
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- fuzzy complexes, intrinsically disordered proteins, protein complexes, structural ensembles, protein-protein interaction, alternative splicing, post-translational modification, protein-ligand interactions
- MeSH terms
- Carrier Proteins, Models, Molecular, Protein Binding, Proteins, Software, Structure-Activity Relationship, Computational Biology, Databases, Protein, Multiprotein Complexes, Web Browser
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