The protein trinity—linking function and disorder

The Protein Data Bank

Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196

Lethality and centrality in protein networks

Jeong, H., Mason, S., Barabási, A., & Oltvai, Z. (2001) · Nature · doi:10.1038/35075138 · Cited by 5,327

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968

Intrinsically disordered protein

Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272

Einfluss der Configuration auf die Wirkung der Enzyme

Fischer, E. (1894) · Berichte der deutschen chemischen Gesellschaft · doi:10.1002/cber.18940270364 · Cited by 1,841

Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex

Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1519061 · Cited by 1,032

Crystal structures of human calcineurin and the human FKBP12–FK506–calcineurin complex

Kissinger, C. R., Parge, H. E., Knighton, D. R., Lewis, C. T., Pelletier, L. A., Tempczyk, A., Kalish, V. J., Tucker, K. D., Showalter, R. E., Moomaw, E. W., et al. (1995) · Nature · doi:10.1038/378641a0 · Cited by 768

Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity.

Kriwacki, R. W., Hengst, L., Tennant, L. L., Reed, S. I., & Wright, P. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11504 · Cited by 576

IEEE International Conference on Neural Networks

(1993) · doi:10.1109/icnn.1993 · Cited by 550

On the Structure of Native, Denatured, and Coagulated Proteins

Mirsky, A. E., & Pauling, L. C. (1936) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.22.7.439 · Cited by 523

The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

Arnold, K., Bordoli, L., Kopp, J., & Schwede, T. F. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti770 · Cited by 7,031

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

Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., & Jones, D. T. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.002 · Cited by 2,010

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

Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125924 · Cited by 1,447

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

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

Xue, B., Dunbrack, R. L., Williams, R. W., Dunker, A. K., & Uversky, V. N. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.01.011 · Cited by 1,239

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

Understanding protein non-folding

Uversky, V. N., & Dunker, A. K. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.01.017 · Cited by 1,221

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

Function and structure of inherently disordered proteins

Dunker, A. K., Silman, I., Uversky, V. N., & Sussman, J. L. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.10.002 · Cited by 963

Length-dependent prediction of protein intrinsic disorder

Peng, K., Predrag Radivojac, A., Vučetić, S., Dunker, A. K., & Zoran Obradovic, A. (2006) · BMC Bioinformatics · doi:10.1186/1471-2105-7-208 · Cited by 940

Fungal Cellulases

Payne, C. M., Knott, B. C., Mayes, H. B., Hansson, H., Himmel, M. E., Sandgren, M. O. J., Ståhlberg, J., & Beckham, G. T. (2015) · Chemical Reviews · doi:10.1021/cr500351c · Cited by 882

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

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

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

Introducing Protein Intrinsic Disorder

Habchi, J., Tompa, P., Longhi, S., & Uversky, V. N. (2014) · Chemical Reviews · doi:10.1021/cr400514h · Cited by 767

Analysis of Molecular Recognition Features (MoRFs)

Mohan, A., Oldfield, C. J., Predrag Radivojac, A., Vacic, V., Cortese, M. S., Dunker, A. K., & Uversky, V. N. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.07.087 · Cited by 769

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

Intrinsic Disorder and Functional Proteomics

Predrag Radivojac, A., Iakoucheva, L. M., Oldfield, C. J., Zoran Obradovic, A., Uversky, V. N., & Dunker, A. K. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.094045 · Cited by 714

The DISOPRED server for the prediction of protein disorder

Ward, J. J., McGuffin, L. J., Bryson, K., Buxton, B. F., & Jones, D. T. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth195 · Cited by 684

The unfoldomics decade: an update on intrinsically disordered proteins

Dunker, A. K., Oldfield, C. J., Meng, J., Romero, P. R., Yang, J. Y., Chen, J. W., Vacic, V., Zoran Obradovic, A., & Uversky, V. N. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-s2-s1 · Cited by 694

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

Haynes, C. A., Oldfield, C. J., Ji, F., Klitgord, N., Cusick, M. E., Predrag Radivojac, A., Uversky, V. N., Vidal, M., & Iakoucheva, L. M. (2006) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0020100 · Cited by 593

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

Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation

Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 593

What Macromolecular Crowding Can Do to a Protein

Kuznetsova, I. М., Константинович, Т. К., & Uversky, V. N. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151223090 · Cited by 573

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

Xie, H. M., Vučetić, S., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Uversky, V. N., & Zoran Obradovic, A. (2007) · Journal of Proteome Research · doi:10.1021/pr060392u · Cited by 572

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

Uversky, V. N. (2019) · Frontiers in Physics · doi:10.3389/fphy.2019.00010 · Cited by 542

ESpritz: accurate and fast prediction of protein disorder

Walsh, I., Martín, A. J. M., Domenico, T. D., & Tosatto, S. C. E. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr682 · Cited by 523

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

Theillet, F., Binolfi, A., Frembgen-Kesner, T., Hingorani, K. S., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L. M., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 521

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

Uversky, V. N. (2013) · Protein Science · doi:10.1002/pro.2261 · Cited by 512

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

Uversky, V. N. (2003) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2003.10506918 · Cited by 516

OPTIMIZING LONG INTRINSIC DISORDER PREDICTORS WITH PROTEIN EVOLUTIONARY INFORMATION

PENG, K., Vučetić, S., Predrag Radivojac, A., Brown, C. J., Dunker, A. K., & Zoran Obradovic, A. (2005) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720005000886 · Cited by 499

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

Vacic, V., Oldfield, C. J., Mohan, A., Predrag Radivojac, A., Cortese, M. S., Uversky, V. N., & Dunker, A. K. (2007) · Journal of Proteome Research · doi:10.1021/pr0701411 · Cited by 499

Probing protein structure by limited proteolysis.

Fontana, A., de Laureto, P. P., Spolaore, B., Frare, E., Picotti, P., & Zambonin, M. (2004) · Acta Biochimica Polonica · doi:10.18388/abp.2004_3573 · Cited by 476

Predicting intrinsic disorder from amino acid sequence

Zoran Obradovic, A., Peng, K., Vučetić, S., Predrag Radivojac, A., Brown, C. J., & Dunker, A. K. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10532 · Cited by 455

Assessing protein disorder and induced folding

Receveur‐Brechot, V., Bourhis, J., Uversky, V. N., Canard, B., & Longhi, S. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20750 · Cited by 458

Intrinsically disordered proteins from A to Z

Uversky, V. N. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.04.001 · Cited by 457

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

Campen, A., Williams, R. M., Brown, C. J., Meng, J., Uversky, V. N., & Dunker, A. K. (2008) · Protein and Peptide Letters · doi:10.2174/092986608785849164 · Cited by 422

Identification and functions of usefully disordered proteins

Dunker, A. K., Brown, C. J., & Zoran Obradovic, A. (2002) · Advances in protein chemistry · doi:10.1016/s0065-3233(02)62004-2 · Cited by 410

Flavors of protein disorder

Vučetić, S., Brown, C. J., Dunker, A. K., & Zoran Obradovic, A. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10437 · Cited by 381

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

Receveur‐Brechot, V., & Christiane, D. D. (2012) · Current Protein and Peptide Science · doi:10.2174/138920312799277901 · Cited by 357

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

Uversky, V. N. (2009) · The Protein Journal · doi:10.1007/s10930-009-9201-4 · Cited by 367

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

Paul, S., Bag, S. K., Das, S., Harvill, E. T., & Dutta, C. (2008) · Genome biology · doi:10.1186/gb-2008-9-4-r70 · Cited by 377

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

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

Harms, M. J., & Thornton, J. W. (2013) · Nature Reviews Genetics · doi:10.1038/nrg3540 · Cited by 330

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 324

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

Uversky, V. N. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3096-6 · Cited by 322

Nanomechanical Basis of Selective Gating by the Nuclear Pore Complex

Lim, R. Y. H., Fahrenkrog, B., Köser, J., Schwarz-Herion, K., Deng, J., & Aebi, U. (2007) · Science · doi:10.1126/science.1145980 · Cited by 307

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

Dunker, A. K., Babu, M. M., Barbar, E. J., Blackledge, M. J., Bondos, S. E., Dosztányi, Z., Dyson, H. J., Forman-Kay, J. D., Fuxreiter, M., Gsponer, J. A., et al. (2013) · Intrinsically Disordered Proteins · doi:10.4161/idp.24157 · Cited by 308

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

Lacy, E. R., Filippov, I. V., Lewis, W. S., Otieno, S. B., Xiao, L., Weiß, S. B., Hengst, L., & Kriwacki, R. W. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb746 · Cited by 305

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

Song, J., Tan, H., Perry, A., Akutsu, T., Webb, G. I., Whisstock, J. C., & Pike, R. N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050300 · Cited by 297

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 301

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

Longhi, S., Receveur‐Brechot, V., Karlin, D., Johansson, K., Darbon, H., Bhella, D., Yeo, R. P., Finet, S., & Canard, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300518200 · Cited by 292

Deep learning methods in protein structure prediction

Torrisi, M., Pollastri, G., & Le, Q. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.12.011 · Cited by 297

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

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

Darling, A. L., & Uversky, V. N. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00158 · Cited by 271

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

Nezafat, N., Ghasemi, Y., Javadi, G., Khoshnoud, M. J., & Omidinia, E. (2014) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2014.01.018 · Cited by 262

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 274

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 264

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 256

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

Harauz, G., Ishiyama, N., Hill, C. M. D., Bates, I. R., Libich, D. S., & Farès, C. (2004) · Micron · doi:10.1016/j.micron.2004.04.005 · Cited by 256

Assemblages: Functional units formed by cellular phase separation

Toretsky, J. A., & Wright, P. E. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201404124 · Cited by 251

Intrinsically Disordered Proteins: An Overview

Trivedi, R., & Nagarajaram, H. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214050 · Cited by 277

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

Fontana, A., Spolaore, B., Mero, A., & Veronese, F. M. (2007) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.06.015 · Cited by 249

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

Intrinsic disorder in proteins associated with neurodegenerative diseases

Vladimir, N. (2009) · Frontiers in bioscience · doi:10.2741/3594 · Cited by 241

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

Dyson, H. J., & Wright, P. E. (2002) · Advances in protein chemistry · doi:10.1016/s0065-3233(02)62012-1 · Cited by 230

The N-terminal Domain of p53 is Natively Unfolded

Dawson, R. J. P., Müller, L., Dehner, A., Klein, C., Kessler, H., & Büchner, J. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.08.008 · Cited by 233

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

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 224

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

Jefferis, R., & Lund, J. (2002) · Immunology Letters · doi:10.1016/s0165-2478(02)00019-6 · Cited by 222

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 218

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 221

Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling

Csizmók, V., Follis, A. V., Kriwacki, R. W., & Forman-Kay, J. D. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00548 · Cited by 210

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

Sorgen, P. L., Duffy, H. S., Sahoo, P. P., Coombs, W., Delmar, M., & Spray, D. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409552200 · Cited by 194

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

Xue, L. C., Dobbs, D. L., Bonvin, A. M. J. J., & Honavar, V. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.003 · Cited by 184

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 196

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 196

Protein flexibility and rigidity predicted from sequence

Schlessinger, A., & Rost, B. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20587 · Cited by 191

Amyloidogenesis of Natively Unfolded Proteins

Uversky, V. N. (2008) · Current Alzheimer Research · doi:10.2174/156720508784533312 · Cited by 188

Loopy Proteins Appear Conserved in Evolution

Liu, J., Tan, H., & Rost, B. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00736-2 · Cited by 192

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

Cino, E. A., Choy, W., & Karttunen, M. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300323g · Cited by 191

Improved Disorder Prediction by Combination of Orthogonal Approaches

Schlessinger, A., Punta, M., Yachdav, G., Kaján, L., & Rost, B. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004433 · Cited by 178

Structural disorder and modular organization in Paramyxovirinae N and P

Karlin, D., Ferrón, F., Canard, B., & Longhi, S. (2003) · Journal of General Virology · doi:10.1099/vir.0.19451-0 · Cited by 178

The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner

Bourhis, J., Johansson, K., Receveur‐Brechot, V., Oldfield, C. J., Dunker, A. K., Canard, B., & Longhi, S. (2004) · Virus Research · doi:10.1016/j.virusres.2003.11.007 · Cited by 175

The roles of intrinsic disorder in protein interaction networks

Uversky, V. N. (2013) · The biomedical & life sciences collection. · doi:10.69645/bdro2797 · Cited by 175

Expanding the proteome: disordered and alternatively folded proteins

Dyson, H. J. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583511000060 · Cited by 181

Intrinsic Disorder in the Protein Data Bank

LeGall, T., Romero, P. R., Cortese, M. S., Uversky, V. N., & Dunker, A. K. (2007) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2007.10507123 · Cited by 167

Nitration inhibits fibrillation of human α‐synuclein in vitro by formation of soluble oligomers

Yamin, G., Uversky, V. N., & Fink, A. L. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00367-3 · Cited by 171

Molecular recognition features (MoRFs) in three domains of life

Yan, J. R., Dunker, A. K., Uversky, V. N., & Kurgan, L. (2015) · Molecular BioSystems · doi:10.1039/c5mb00640f · Cited by 167

Cementum proteins: role in cementogenesis, biomineralization, periodontium formation and regeneration

Arzate, H., Zeichner‐David, M., & Mercado, G. (2014) · Periodontology 2000 · doi:10.1111/prd.12062 · Cited by 164

Comprehensive large-scale assessment of intrinsic protein disorder

Walsh, I., Giollo, M., Domenico, T. D., Ferrari, C., Zimmermann, O., & Tosatto, S. C. E. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu625 · Cited by 159

PROFbval: predict flexible and rigid residues in proteins

Schlessinger, A., Yachdav, G., & Rost, B. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl032 · Cited by 154

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Experimental investigation of protein folding and misfolding

Dobson, C. M. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.002 · Cited by 156

Role of intrinsic disorder in transient interactions of hub proteins

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Pe’er, I., Felder, C. E., Man, O., Silman, I., Sussman, J. L., & Beckmann, J. S. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10559 · Cited by 152

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The intrinsically disordered C‐terminal domain of the measles virus nucleoprotein interacts with the C‐terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded

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The importance of being unfolded

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

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