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Archaic chaos: intrinsically disordered proteins in Archaea

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Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo

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Disease-Associated Mutations Disrupt Functionally Important Regions of Intrinsic Protein Disorder

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Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes

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Isoindolinone Inhibitors of the Murine Double Minute 2 (MDM2)-p53 Protein−Protein Interaction: Structure−Activity Studies Leading to Improved Potency

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Selective Inhibition of c-Myc/Max Dimerization and DNA Binding by Small Molecules

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Intrinsically disordered proteins in overcrowded milieu: Membrane-less organelles, phase separation, and intrinsic disorder

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The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches

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Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

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Protein intrinsic disorder-based liquid–liquid phase transitions in biological systems: Complex coacervates and membrane-less organelles

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New insights into protein–protein interaction modulators in drug discovery and therapeutic advance

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Drugging Undruggable Molecular Cancer Targets

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Intrinsically Disordered Proteome of Human Membrane‐Less Organelles

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The new (dis)order in RNA regulation

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p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept

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Force field development and simulations of intrinsically disordered proteins

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Stochasticity of Biological Soft Matter: Emerging Concepts in Intrinsically Disordered Proteins and Biological Phase Separation

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Rapid prediction and analysis of protein intrinsic disorder

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Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell

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General Purpose Water Model Can Improve Atomistic Simulations of Intrinsically Disordered Proteins

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Liquid–liquid phase separation as an organizing principle of intracellular space: overview of the evolution of the cell compartmentalization concept

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Disordered Proteinaceous Machines

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Potential lactoferrin activity against pathogenic viruses

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Intrinsic Disorder, Protein–Protein Interactions, and Disease

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Recent Developments in the Field of Intrinsically Disordered Proteins: Intrinsic Disorder–Based Emergence in Cellular Biology in Light of the Physiological and Pathological Liquid–Liquid Phase Transitions

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How Closely Related Are Conformations of Protein Ions Sampled by IM-MS to Native Solution Structures?

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Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators

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Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo

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Functional Analysis of Human Hub Proteins and Their Interactors Involved in the Intrinsic Disorder-Enriched Interactions

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Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies

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Targeting intrinsically disordered proteins in rational drug discovery

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Order, Disorder, and Everything in Between

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

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In Aqua Veritas: The Indispensable yet Mostly Ignored Role of Water in Phase Separation and Membrane-less Organelles

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Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding

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MyelStones: the executive roles of myelin basic protein in myelin assembly and destabilization in multiple sclerosis

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PTEN proteoforms in biology and disease

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Biological soft matter: intrinsically disordered proteins in liquid–liquid phase separation and biomolecular condensates

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The roles of intrinsic disorder-based liquid-liquid phase transitions in the “Dr. Jekyll–Mr. Hyde” behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

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Regulation of PTEN expression by noncoding RNAs

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The Pathophysiological Significance of Fibulin-3

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Intrinsically Disordered Proteins in Chronic Diseases

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Membrane-Bound Selenoproteins

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Therapeutic Interventions of Cancers Using Intrinsically Disordered Proteins as Drug Targets: c-Myc as Model System

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Progress toward Alzheimer's disease treatment: Leveraging the Achilles' heel of Aβ oligomers?

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Ascorbate Oxidation by Cu(Amyloid-β) Complexes: Determination of the Intrinsic Rate as a Function of Alterations in the Peptide Sequence Revealing Key Residues for Reactive Oxygen Species Production

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Exploiting Transient Protein States for the Design of Small-Molecule Stabilizers of Mutant p53

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Methods of probing the interactions between small molecules and disordered proteins

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DEPICTER: Intrinsic Disorder and Disorder Function Prediction Server

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Intrinsic disorder in proteins involved in amyotrophic lateral sclerosis

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How accurate are your simulations? Effects of confined aqueous volume and AMBER FF99SB and CHARMM22/CMAP force field parameters on structural ensembles of intrinsically disordered proteins: Amyloid-β42in water

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Quantitative Biophysical Characterization of Intrinsically Disordered Proteins

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Evolutionary Features in the Structure and Function of Bacterial Toxins

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The solvent side of proteinaceous membrane-less organelles in light of aqueous two-phase systems

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Direct inhibition of c-Myc-Max heterodimers by celastrol and celastrol-inspired triterpenoids

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Accuracy of protein-level disorder predictions

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How do disordered regions achieve comparable functions to structured domains?

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Deep learning in prediction of intrinsic disorder in proteins

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Survey of Similarity-Based Prediction of Drug-Protein Interactions

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15 N detection harnesses the slow relaxation property of nitrogen: Delivering enhanced resolution for intrinsically disordered proteins

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Multiple Regulatory Intrinsically Disordered Motifs Control FOXO4 Transcription Factor Binding and Function

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Ramachandran mapping of peptide conformation using a large database of computed Raman and Raman optical activity spectra

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Inexpensive Radical Methylation and Related Alkylations of Heteroarenes

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Molecular recognition of peptides and proteins by cucurbit[ n ]urils: systems and applications

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Identification of Inhibitors of Biological Interactions Involving Intrinsically Disordered Proteins

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Femtosecond Hydration Map of Intrinsically Disordered α-Synuclein

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SUR1 Receptor Interaction with Hesperidin and Linarin Predicts Possible Mechanisms of Action of Valeriana officinalis in Parkinson

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Learning to evolve structural ensembles of unfolded and disordered proteins using experimental solution data

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Residual Structures and Transient Long-Range Interactions of p53 Transactivation Domain: Assessment of Explicit Solvent Protein Force Fields

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Transient Secondary Structures as General Target-Binding Motifs in Intrinsically Disordered Proteins

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Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities

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Understanding the interactability of chikungunya virus proteinsviamolecular recognition feature analysis

Singh, A., Kumar, A., Uversky, V. N., & Giri, R. (2018) · RSC Advances · doi:10.1039/c8ra04760j · Cited by 38 · see citing works

NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins

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Tracing the Evolution of the p53 Tetramerization Domain

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Zooming into the Dark Side of Human Annexin-S100 Complexes: Dynamic Alliance of Flexible Partners

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HyRes: a coarse-grained model for multi-scale enhanced sampling of disordered protein conformations

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Intrinsic Disorder of the BAF Complex: Roles in Chromatin Remodeling and Disease Development

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A Unique Mdm2-Binding Mode of the 3-Pyrrolin-2-one- and 2-Furanone-Based Antagonists of the p53-Mdm2 Interaction

Surmiak, E., Twarda‐Clapa, A., Żak, K. M., Musielak, B., Tomala, M. D., Kubica, K., Grudnik, P., Madej, M., Jabłoński, M., Potempa, J., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00596 · Cited by 36 · see citing works

Intrinsic Disorder in Tetratricopeptide Repeat Proteins

Bibber, N. W. V., Haerle, C., Khalife, R., Xue, B., & Uversky, V. N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103709 · Cited by 35 · see citing works

Water Rearrangements upon Disorder-to-Order Amyloid Transition

Arya, S., Singh, A. K., Khan, T., Bhattacharya, M., Datta, A., & Mukhopadhyay, S. (2016) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.6b02088 · Cited by 35 · see citing works

Orcein-Related Small Molecule O4 Destabilizes hIAPP Protofibrils by Interacting Mostly with the Amyloidogenic Core Region

Zou, Y. F., Qian, Z., Sun, Y., Wei, G., & Zhang, Q. (2017) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b08652 · Cited by 35 · see citing works

The roles of intrinsically disordered proteins in neurodegeneration

Utami, K. H., Morimoto, S., Mitsukura, Y., & Okano, H. (2025) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2025.130772 · Cited by 34 · see citing works

Rational design and synthesis of 1,5-disubstituted tetrazoles as potent inhibitors of the MDM2-p53 interaction

Surmiak, E., Neochoritis, C. G., Musielak, B., Twarda‐Clapa, A., Kurpiewska, K., Dubin, G., Camacho, C. J., Holak, T. A., & Dömling, A. S. S. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.11.029 · Cited by 34 · see citing works

Binding of protofibrillar Aβ trimers to lipid bilayer surface enhances Aβ structural stability and causes membrane thinning

Dong, X., Sun, Y., Wei, G., Nussinov, R., & Ma, B. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp05959k · Cited by 34 · see citing works

Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins

Gupta, M. N., & Uversky, V. N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032424 · Cited by 33 · see citing works

Binding mechanisms of intrinsically disordered proteins: Insights from experimental studies and structural predictions

Orand, T., & Jensen, M. R. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102958 · Cited by 33 · see citing works

The dark side of Alzheimer’s disease: unstructured biology of proteins from the amyloid cascade signaling pathway

Gadhave, K., Gehi, B. R., Kumar, P., Xue, B., Uversky, V. N., & Giri, R. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03414-9 · 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

Increasing the Chemical‐Shift Dispersion of Unstructured Proteins with a Covalent Lanthanide Shift Reagent

Göbl, C., Moritz, R., Strickland, M., Hartlmüller, C., Viertler, M., Tjandra, N., & Madl, T. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201607261 · Cited by 32 · see citing works

Intrinsically Disordered Proteins

Uversky, V. N. (2020) · Wiley eBooks · doi:10.1002/9781118681121.ch25 · Cited by 32 · see citing works

A link between STK signalling and capsular polysaccharide synthesis in Streptococcus suis

Tang, J., Guo, M., Chen, M., Xu, B., Ran, T., Wang, W., Ma, Z., Lin, H., & Fan, H. (2023) · Nature Communications · doi:10.1038/s41467-023-38210-4 · Cited by 31 · see citing works

DEPICTER2: a comprehensive webserver for intrinsic disorder and disorder function prediction

Basu, S., Gsponer, J. A., & Kurgan, L. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad330 · Cited by 31 · see citing works

flDPnn2: Accurate and Fast Predictor of Intrinsic Disorder in Proteins

Wang, K., Hu, G., Basu, S., & Kurgan, L. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168605 · Cited by 31 · see citing works

1,4,5-Trisubstituted Imidazole-Based p53–MDM2/MDMX Antagonists with Aliphatic Linkers for Conjugation with Biological Carriers

Twarda‐Clapa, A., Krzanik, S., Kubica, K., Guzik, K., Łabuzek, B., Neochoritis, C. G., Khoury, K., Kowalska, K., Czub, M., Dubin, G., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00104 · Cited by 31 · see citing works

Comparative Assessment of Intrinsic Disorder Predictions with a Focus on Protein and Nucleic Acid-Binding Proteins

Katuwawala, A., & Kurgan, L. (2020) · Biomolecules · doi:10.3390/biom10121636 · Cited by 31 · see citing works

Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae

Keefer, K. M., Stein, K. C., & True, H. L. (2017) · Scientific Reports · doi:10.1038/s41598-017-05829-5 · Cited by 31 · see citing works

Sequence-Derived Markers of Drug Targets and Potentially Druggable Human Proteins

Ghadermarzi, S., Li, X., Li, M., & Kurgan, L. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.01075 · Cited by 30 · see citing works

Intrinsically Disordered Regions in Serum Albumin: What Are They For?

Андреевна, Л. Е., Permyakov, S. E., Uversky, V. N., & Permyakov, E. A. (2017) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-017-0785-6 · Cited by 30 · see citing works

Arrestins: structural disorder creates rich functionality

Gurevich, V. V., Gurevich, E. V., & Uversky, V. N. (2018) · Protein & Cell · doi:10.1007/s13238-017-0501-8 · Cited by 28 · see citing works

Discriminating changes in protein structure using tyrosine conjugation

Moinpour, M., Barker, N. K., Guzmán, L. E., Jewett, J. C., Langlais, P. R., & Schwartz, J. C. (2020) · Protein Science · doi:10.1002/pro.3897 · Cited by 27 · see citing works

Alteration of Microstructure in Biopolymeric Hydrogels via Compositional Modification of Resilin-Like Polypeptides

Garcia, C. G., Patkar, S. S., Jovic, N., Mittal, J., & Kiick, K. L. (2021) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.0c01543 · Cited by 27 · see citing works

Erythropoietin and co.: intrinsic structure and functional disorder

Uversky, V. N., & Redwan, E. M. M. M. (2016) · Molecular BioSystems · doi:10.1039/c6mb00657d · Cited by 27 · see citing works

Performance of CHARMM36m with modified water model in simulating intrinsically disordered proteins: a case study

Pineda, L. I. G., Milko, L. N., & He, Y. J. (2020) · Biophysics Reports · doi:10.1007/s41048-020-00107-w · Cited by 26 · see citing works

Unfoldomics of human diseases: Linking protein intrinsic disorder with diseases

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Unfoldomics of Human Genetic Diseases: Illustrative Examples of Ordered and Intrinsically Disordered Members of the Human Diseasome

Midic, U., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2009) · Protein and Peptide Letters · doi:10.2174/092986609789839377 · Cited by 65 · see citing works

Intrinsically Disordered Proteins in Human Diseases.

Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2007) · Bioinformatics and Bioengineering · Cited by 3 · see citing works

Protein disorder in the human diseasome: unfoldomics of human genetic diseases

Midic, U., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2009) · TUScholarShare (Temple University) · Cited by 2 · see citing works

intrinsically disordered and of unfolded proteins

Varadi, 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)