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Identification of intrinsic order and disorder in the DNA repair protein XPA

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Methods for improving protein disorder prediction

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Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

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Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept

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Coupling of folding and binding for unstructured proteins

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PONDR-FIT: A meta-predictor of intrinsically disordered amino acids

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Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins

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Understanding protein non-folding

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

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Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

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Function and structure of inherently disordered proteins

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Length-dependent prediction of protein intrinsic disorder

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Fungal Cellulases

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

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DisProt: the Database of Disordered Proteins

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Intrinsic Disorder in Transcription Factors

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Introducing Protein Intrinsic Disorder

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Analysis of Molecular Recognition Features (MoRFs)

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The interplay between structure and function in intrinsically unstructured proteins

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Intrinsic Disorder and Functional Proteomics

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The DISOPRED server for the prediction of protein disorder

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The unfoldomics decade: an update on intrinsically disordered proteins

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Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes

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

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Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation

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What Macromolecular Crowding Can Do to a Protein

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Functional Anthology of Intrinsic Disorder. 1. Biological Processes and Functions of Proteins with Long Disordered Regions

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Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics

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ESpritz: accurate and fast prediction of protein disorder

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Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)

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A decade and a half of protein intrinsic disorder: Biology still waits for physics

Uversky, V. (2013) · Protein Science · doi:10.1002/pro.2261 · Cited by 478 · see citing works

A Protein-Chameleon: Conformational Plasticity of α-Synuclein, a Disordered Protein Involved in Neurodegenerative Disorders

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OPTIMIZING LONG INTRINSIC DISORDER PREDICTORS WITH PROTEIN EVOLUTIONARY INFORMATION

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Characterization of Molecular Recognition Features, MoRFs, and Their Binding Partners

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Probing protein structure by limited proteolysis.

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Predicting intrinsic disorder from amino acid sequence

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Assessing protein disorder and induced folding

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Intrinsically disordered proteins from A to Z

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TOP-IDP-Scale: A New Amino Acid Scale Measuring Propensity for Intrinsic Disorder

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Identification and functions of usefully disordered proteins

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Flavors of protein disorder

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How Random are Intrinsically Disordered Proteins? A Small Angle Scattering Perspective

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Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding

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Molecular signature of hypersaline adaptation: insights from genome and proteome composition of halophilic prokaryotes

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

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Evolutionary biochemistry: revealing the historical and physical causes of protein properties

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Mining α-Helix-Forming Molecular Recognition Features with Cross Species Sequence Alignments

Cheng, Y., Oldfield, C. J., Meng, J., Romero, P. R., Uversky, V. N., & Dunker, A. K. (2007) · Biochemistry · doi:10.1021/bi7012273 · Cited by 321 · see citing works

Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go?

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Nanomechanical Basis of Selective Gating by the Nuclear Pore Complex

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What’s in a name? Why these proteins are intrinsically disordered

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p27 binds cyclin–CDK complexes through a sequential mechanism involving binding-induced protein folding

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PROSPER: An Integrated Feature-Based Tool for Predicting Protease Substrate Cleavage Sites

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Intrinsic disorder in scaffold proteins: Getting more from less

Cortese, M. S., Uversky, V. N., & Dunker, A. K. (2008) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2008.05.007 · Cited by 292 · see citing works

The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein

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Deep learning methods in protein structure prediction

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Unfoldomics of human diseases: linking protein intrinsic disorder with diseases

Uversky, V. N., Oldfield, C. J., Midic, U., Xie, H. M., Xue, B., Vučetić, S., Iakoucheva, L. M., Zoran Obradovic, A., & Dunker, A. K. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-s1-s7 · Cited by 283 · see citing works

Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter

Darling, A., & Uversky, V. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00158 · Cited by 236 · see citing works

A novel multi-epitope peptide vaccine against cancer: An in silico approach

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The Mysterious Unfoldome: Structureless, Underappreciated, Yet Vital Part of Any Given Proteome

Uversky, V. N. (2009) · BioMed Research International · doi:10.1155/2010/568068 · Cited by 267 · see citing works

Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes

Uversky, V. N. (2010) · Chemical Society Reviews · doi:10.1039/c0cs00057d · Cited by 260 · see citing works

Functional Anthology of Intrinsic Disorder. 2. Cellular Components, Domains, Technical Terms, Developmental Processes, and Coding Sequence Diversities Correlated with Long Disordered Regions

Vučetić, S., Xie, H. M., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2007) · Journal of Proteome Research · doi:10.1021/pr060393m · Cited by 253 · see citing works

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

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Assemblages: Functional units formed by cellular phase separation

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Intrinsically Disordered Proteins: An Overview

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Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase

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Do viral proteins possess unique biophysical features?

Tokuriki, N., Oldfield, C. J., Uversky, V. N., Berezovsky, I. N., & Tawfik, D. S. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.10.009 · Cited by 237 · see citing works

Intrinsic disorder in proteins associated with neurodegenerative diseases

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Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance

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The N-terminal Domain of p53 is Natively Unfolded

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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 · see citing works

Methionine oxidation inhibits fibrillation of human α‐synuclein in vitro

Uversky, V. N., Yamin, G., Souillac, P. O., Goers, J. W. F., Glaser, C. B., & Fink, A. L. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02638-8 · Cited by 222 · see citing works

Interaction sites on human IgG-Fc for FcγR: current models

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Conditionally and Transiently Disordered Proteins: Awakening Cryptic Disorder To Regulate Protein Function

Jakob, U., Kriwacki, R. W., & Uversky, V. N. (2014) · Chemical Reviews · doi:10.1021/cr400459c · Cited by 216 · see citing works

The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation

Константинович, Т. К., Kuznetsova, I. М., & Uversky, V. N. (2010) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2010.01.003 · Cited by 215 · see citing works

Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling

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Structural Changes in the Carboxyl Terminus of the Gap Junction Protein Connexin43 Indicates Signaling between Binding Domains for c-Src and Zonula Occludens-1

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Computational prediction of protein interfaces: A review of data driven methods

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

Uversky, V. N. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111874 · Cited by 193 · see citing works

Natively Disordered Proteins

Daughdrill, G. W., Pielak, G. J., Uversky, V. N., Cortese, M. S., & Dunker, A. K. (2005) · Wiley eBooks · doi:10.1002/9783527619498.ch41 · Cited by 194 · see citing works

Protein flexibility and rigidity predicted from sequence

Schlessinger, A., & Rost, B. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20587 · Cited by 186 · see citing works

Amyloidogenesis of Natively Unfolded Proteins

Uversky, V. N. (2008) · Current Alzheimer Research · doi:10.2174/156720508784533312 · Cited by 187 · see citing works

Loopy Proteins Appear Conserved in Evolution

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Comparison of Secondary Structure Formation Using 10 Different Force Fields in Microsecond Molecular Dynamics Simulations

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