Intrinsically Disordered Proteins

Principles that Govern the Folding of Protein Chains

Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096

Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes

Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116

The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent Motility

Kozielski, F., Sack, S., Marx, A., Thormählen, M., Schönbrunn, E., Biou, V, Thompson, A., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80489-4 · Cited by 408

Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association

Pontius, B. W. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90111-y · Cited by 183

The importance of being unfolded

Plaxco, K. W., & Groβ, M. (1997) · Nature · doi:10.1038/386657a0 · Cited by 121

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).

Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894

Intrinsically unstructured proteins and their functions

Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897

Coupling of folding and binding for unstructured proteins

Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327

Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins

Iakoucheva, L. M., Brown, C. J., Lawson, J. D., Obradović, Z., & Dunker, A. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00969-5 · Cited by 1,214

Flexible nets: The roles of intrinsic disorder in protein interaction networks

Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., & Uversky, V. N. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04948.x · Cited by 1,122

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

Plasma membrane phosphoinositide organization by protein electrostatics

McLaughlin, S., & Murray, D. (2005) · Nature · doi:10.1038/nature04398 · Cited by 868

Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847

Intrinsic Disorder in Transcription Factors

Liu, J., Perumal, N. B., Oldfield, C. J., Su, E. W., Uversky, V. N., & Dunker, A. K. (2006) · Biochemistry · doi:10.1021/bi0602718 · Cited by 792

The interplay between structure and function in intrinsically unstructured proteins

Tompa, P. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.072 · Cited by 717

Preformed structural elements feature in partner recognition by intrinsically unstructured proteins

Fuxreiter, M., Simon, I., Friedrich, P., & Tompa, P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.03.017 · Cited by 518

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

Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins

Hilser, V. J., & Thompson, E. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700329104 · Cited by 406

Molecular properties of food allergens

Breiteneder, H., & Mills, E. N. C. (2005) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2004.10.022 · Cited by 359

Clusterin promotes amyloid plaque formation and is critical for neuritic toxicity in a mouse model of Alzheimer's disease

DeMattos, R. B., O'dell, M. A., Parsadanian, M., Taylor, J. W., Harmony, J. A. K., Bales, K. R., Paul, S. M., Aronow, B. J., & Holtzman, D. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162228299 · Cited by 359

The structural and functional signatures of proteins that undergo multiple events of post‐translational modification

Pejaver, V., Hsu, W., Xin, F., Dunker, A. K., Uversky, V. N., & Radivojac, P. (2014) · Protein Science · doi:10.1002/pro.2494 · Cited by 349

Deubiquitinase-targeting chimeras for targeted protein stabilization

Henning, N. J., Boike, L., Spradlin, J. N., Ward, C. C., Liu, G., Zhang, E., Belcher, B. P., Brittain, S. M., Hesse, M. J., Dovala, D., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-00971-2 · Cited by 344

Disorder and Sequence Repeats in Hub Proteins and Their Implications for Network Evolution

Dosztányi, Z., Chen, J., Dunker, A. K., Simon, I., & Tompa, P. (2006) · Journal of Proteome Research · doi:10.1021/pr060171o · Cited by 341

Human Transcription Factors Contain a High Fraction of Intrinsically Disordered Regions Essential for Transcriptional Regulation

Minezaki, Y., Homma, K., Kinjo, A. R., & Nishikawa, K. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.04.016 · Cited by 297

Beyond modules and hubs: the potential of gene coexpression networks for investigating molecular mechanisms of complex brain disorders

Gaiteri, C., Ding, Y., French, B., Tseng, G. C., & Sibille, E. (2014) · Genes, Brain and Behavior · doi:10.1111/gbb.12106 · Cited by 289

Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases

Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288

Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity

Borg, M., Mittag, T., Pawson, T., Tyers, M., Forman-Kay, J. D., & Chan, H. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702580104 · Cited by 245

Intrinsically disordered proteins play diverse roles in cell signaling

Bondos, S. E., Dunker, A. K., & Uversky, V. N. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00821-7 · Cited by 222

The Acidic Transcription Activator Gcn4 Binds the Mediator Subunit Gal11/Med15 Using a Simple Protein Interface Forming a Fuzzy Complex

Brzovic, P. S., Heikaus, C. C., Kisselev, L., Vernon, R., Herbig, E., Pacheco, D., Warfield, L., Littlefield, P., Baker, D., Klevit, R. E., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.11.008 · Cited by 203

AlphaFold2: A Role for Disordered Protein/Region Prediction?

Wilson, C. J., Choy, W.-Y., & Karttunen, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094591 · Cited by 173

Improved amino acid flexibility parameters

Smith, D. K., Radivojac, P., Obradovic, Z., Dunker, A. K., & Zhu, G. (2003) · Protein Science · doi:10.1110/ps.0236203 · Cited by 164

Active promoters give rise to false positive ‘Phantom Peaks’ in ChIP-seq experiments

Jain, D., Baldi, S., Zabel, A., Straub, T., & Becker, P. B. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv637 · Cited by 156

Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity

Wilson, M. R., Yerbury, J. J., & Poon, S. (2007) · Molecular BioSystems · doi:10.1039/b712728f · Cited by 142

Describing sequence–ensemble relationships for intrinsically disordered proteins

Mao, A. H., Lyle, N., & Pappu, R. V. (2013) · Biochemical Journal · doi:10.1042/bj20121346 · Cited by 135

The structural coverage of the human proteome before and after AlphaFold

Porta-Pardo, E., Ruiz-Serra, V., Valentini, S., & Valencia, A. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1009818 · Cited by 131

Finding Our Way in the Dark Proteome

Bhowmick, A., Brookes, D. H., Yost, S. R., Dyson, H. J., Forman-Kay, J. D., Gunter, D., Head-Gordon, M., Hura, G. L., Pande, V. S., Wemmer, D. E., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06543 · Cited by 128

Natively unfolded C‐terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin

Permyakov, S. E., Millett, I. S., Doniach, S., Permyakov, E. A., & Uversky, V. N. (2003) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10481 · Cited by 113

The MiDAC histone deacetylase complex is essential for embryonic development and has a unique multivalent structure

Turnbull, R. E., Fairall, L., Saleh, A., Kelsall, E., Morris, K. L., Ragan, T. J., Savva, C. G., Chandru, A., Millard, C. J., Makarova, O. V., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17078-8 · Cited by 108

MeCP2: the long trip from a chromatin protein to neurological disorders

Ausió, J., Paz, A. M. D., & Esteller, M. (2014) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.03.004 · Cited by 108

Multi-functionality of proteins involved in GPCR and G protein signaling: making sense of structure–function continuum with intrinsic disorder-based proteoforms

Fonin, A. V., Darling, A. L., Kuznetsova, I. M., Turoverov, K. K., & Uversky, V. N. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03276-1 · Cited by 91

On the Potential of Machine Learning to Examine the Relationship Between Sequence, Structure, Dynamics and Function of Intrinsically Disordered Proteins

Lindorff-Larsen, K., & Kragelund, B. B. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167196 · Cited by 85

A quantitative measure for protein conformational heterogeneity

Lyle, N., Das, R. K., & Pappu, R. V. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4812791 · Cited by 85

AlphaFold illuminates half of the dark human proteins

Binder, J. L., Berendzen, J., Stevens, A. O., He, Y., Wang, J., Dokholyan, N. V., & Oprea, T. I. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102372 · Cited by 81

Transcriptome profiling of a TGF-β-induced epithelial-to-mesenchymal transition reveals extracellular clusterin as a target for therapeutic antibodies

Lenferink, A. E. G., Cantin, C., Nantel, A., Wang, E., Durocher, Y., Banville, M., Paul-Roc, B., Marcil, A., Wilson, M. R., & O'Connor-McCourt, M. D. (2010) · Oncogene · doi:10.1038/onc.2009.399 · Cited by 81

Diffusing protein binders to intrinsically disordered proteins

Liu, C., Wu, K., Choi, H., Han, H. L., Zhang, X., Watson, J. L., Ahn, G., Zhang, J. Z., Shijo, S., Good, L. L., et al. (2025) · Nature · doi:10.1038/s41586-025-09248-9 · Cited by 79

Sequence-to-conformation relationships of disordered regions tethered to folded domains of proteins

Mittal, A., Holehouse, A. S., Cohan, M. C., & Pappu, R. V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.012 · Cited by 72

Quantifying the topography of the intrinsic energy landscape of flexible biomolecular recognition

Chu, X., Gan, L., Wang, E., & Wang, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220699110 · Cited by 62

Structure of a P element transposase–DNA complex reveals unusual DNA structures and GTP-DNA contacts

Ghanim, G. E., Kellogg, E. H., Nogales, E., & Rio, D. C. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0319-6 · Cited by 37

Presence and utility of intrinsically disordered regions in kinases

Kathiriya, J. J., Pathak, R. R., Clayman, E., Xue, B., Uversky, V. N., & Davé, V. (2014) · Molecular BioSystems · doi:10.1039/c4mb00224e · Cited by 30

Networks of Networks: An Essay on Multi-Level Biological Organization

Uversky, V. N., & Giuliani, A. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.706260 · Cited by 28

Structural Preferences Shape the Entropic Force of Disordered Protein Ensembles

(2023) · doi:10.1021/acs.jpcb.3c00698 · Cited by 25

Diffusing protein binders to intrinsically disordered proteins

Liu, C., Wu, K., Choi, H., Han, H., Zhang, X., Watson, J. L., Shijo, S., Bera, A. K., Kang, A., Brackenbrough, E., et al. (2024) · doi:10.1101/2024.07.16.603789 · Cited by 24

Differential occurrence of protein intrinsic disorder in the cytoplasmic signaling domains of cell receptors

Sigalov, A. B., & Uversky, V. N. (2011) · Self/Nonself · doi:10.4161/self.2.1.14790 · Cited by 23

Protein intrinsically disordered regions have a non-random, modular architecture

McConnell, B. S., & Parker, M. W. (2023) · Bioinformatics · doi:10.1093/bioinformatics/btad732 · Cited by 17

Integration of Nanometer-Range Label-to-Label Distances and Their Distributions into Modelling Approaches

Jeschke, G. (2022) · Biomolecules · doi:10.3390/biom12101369 · Cited by 13

The Rapid Evolution of De Novo Proteins in Structure and Complex

(2024) · doi:10.1093/gbe/evae107 · Cited by 13

Looking at the Pathogenesis of the Rabies Lyssavirus Strain Pasteur Vaccins through a Prism of the Disorder-Based Bioinformatics

Dhulipala, S., & Uversky, V. N. (2022) · Biomolecules · doi:10.3390/biom12101436 · Cited by 6