Intrinsically unstructured proteins

Intrinsic Disorder and Protein Function

Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731

Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions

Radhakrishnan, I., Pérez-Alvarado, G. C., Parker, D., Dyson, H. J., Montminy, M. R., & Wright, P. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80463-8 · Cited by 728

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

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

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

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

Induced fit, conformational selection and independent dynamic segments: an extended view of binding events

Csermely, P., Palotai, R., & Nussinov, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.009 · Cited by 821

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

Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000034 · Cited by 652

Conformational diversity and protein evolution – a 60-year-old hypothesis revisited

James, L. C., & Tawfik, D. S. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00135-x · Cited by 579

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

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

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

Specific Knockdown of Endogenous Tau Protein by Peptide-Directed Ubiquitin-Proteasome Degradation

Chu, T.-T., Gao, N., Li, Q.-Q., Chen, P.-G., Yang, X.-F., Chen, Y.-X., Zhao, Y.-F., & Li, Y.-M. (2016) · Cell Chemical Biology · doi:10.1016/j.chembiol.2016.02.016 · Cited by 247

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

Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in Escherichia coli

Idicula‐Thomas, S., & Balaji, P. V. (2005) · Protein Science · doi:10.1110/ps.041009005 · Cited by 175

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

Sequence‐similar, structure‐dissimilar protein pairs in the PDB

Kosloff, M., & Kolodny, R. (2008) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21770 · Cited by 124

Why do eukaryotic proteins contain more intrinsically disordered regions?

Basile, W., Salvatore, M., Bassot, C., & Elofsson, A. (2019) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1007186 · Cited by 113

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

Cooperative Unfolding of Compact Conformations of the Intrinsically Disordered Protein Osteopontin

Kurzbach, D., Platzer, G., Schwarz, T. C., Henen, M. A., Konrat, R., & Hinderberger, D. (2013) · Biochemistry · doi:10.1021/bi400502c · Cited by 105

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

Hydrophobic tagging-mediated degradation of Alzheimer's disease related Tau

Gao, N., Chu, T.-T., Li, Q.-Q., Lim, Y.-J., Qiu, T., Ma, M.-R., Hu, Z.-W., Yang, X.-F., Chen, Y.-X., Zhao, Y.-F., et al. (2017) · RSC Advances · doi:10.1039/c7ra05347a · Cited by 62

Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22

Kazakov, A. S., Markov, D. I., Gusev, N. B., & Levitsky, D. I. (2009) · Biophysical Chemistry · doi:10.1016/j.bpc.2009.09.003 · Cited by 43

SpatialPPI: Three-dimensional space protein-protein interaction prediction with AlphaFold Multimer

(2024) · doi:10.1016/j.csbj.2024.03.009 · Cited by 29

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

Equilibrium Conformational Ensemble of the Intrinsically Disordered Peptide n16N: Linking Subdomain Structures and Function in Nacre

Brown, A. H., Rodger, P. M., Evans, J. S., & Walsh, T. R. (2014) · Biomacromolecules · doi:10.1021/bm501263s · Cited by 28

Prediction of Quality-control Degradation Signals in Yeast Proteins

Johansson, K. E., Mashahreh, B., Hartmann-Petersen, R., Ravid, T., & Lindorff-Larsen, K. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167915 · Cited by 24

Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14

Murvai, N., Kalmar, L., Szalaine Agoston, B., Szabo, B., Tantos, A., Csikos, G., Micsonai, A., Kardos, J., Vertommen, D., Nguyen, P. N., et al. (2020) · Cells · doi:10.3390/cells9081856 · Cited by 13

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

The intrinsically disordered transcriptional activation domain of CIITA is functionally tuneable by single substitutions: An exception or a new paradigm?

Sreenivasan, S., Heffren, P., Suh, K., Rodnin, M. V., Kosa, E., Fenton, A. W., Ladokhin, A. S., Smith, P. E., Fontes, J. D., & Swint‐Kruse, L. (2024) · Protein Science · doi:10.1002/pro.4863 · Cited by 11

Hydration of Intrinsically Disordered Proteins from Wide‐Line NMR

Tompa, K., Bokor, M., & Tompa, P. (2010) · Instrumental Analysis of Intrinsically Disordered Proteins · doi:10.1002/9780470602614.ch12 · Cited by 8

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

TAFPred: Torsion Angle Fluctuations Prediction from Protein Sequences

Kabir, M. W. U., Alawad, D. M., Mishra, A., & Hoque, M. T. (2023) · Biology · doi:10.3390/biology12071020 · Cited by 5

Navigating the unstructured by evaluating alphafold’s efficacy in predicting missing residues and structural disorder in proteins

Zheng, S. (2025) · PLOS ONE · doi:10.1371/journal.pone.0313812 · Cited by 4