Intrinsic Disorder and Protein Function

Basic Methods in Molecular Biology

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

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Intrinsically disordered protein

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Coupling of folding and binding for unstructured proteins

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Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc ₁ Complex

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Moonlighting proteins

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BCL-2 Is Phosphorylated and Inactivated by an ASK1/Jun N-Terminal Protein Kinase Pathway Normally Activated at G2/M

Yamamoto, K., Ichijo, H., & Korsmeyer, S. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8469 · Cited by 1,003 · see citing works

Methods in molecular biology

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Intrinsic protein disorder in complete genomes.

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Implications of macromolecular crowding for protein assembly

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Evolutionary Rate Heterogeneity in Proteins with Long Disordered Regions

Brown, C. J., Takayama, S., Campen, A., Vise, P., Marshall, T. W., Oldfield, C., Williams, C. J., & Dunker, A. (2002) · Journal of Molecular Evolution · doi:10.1007/s00239-001-2309-6 · Cited by 441 · see citing works

Structure of Human Des(1-45) Factor Xa at 2·2 Å Resolution

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Of urfs and orfs : a primer on how to analyze devised amino acid sequences

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Structure of heparin-binding EGF-like growth factor. Multiple forms, primary structure, and glycosylation of the mature protein

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The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra‐helical deoxyribose at DNA abasic sites

Gorman, M. A., Moréra, S., Rothwell, D. G., Fortelle, E. D. L., Mol, C. D., Tainer, J. A., Hickson, I. D., & Freemont, P. S. (1997) · The EMBO Journal · doi:10.1093/emboj/16.21.6548 · Cited by 323 · see citing works

The Crystal Structure of the DNA-Binding Domain of Yeast RAP1 in Complex with Telomeric DNA

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X-ray Structure of Active Site-inhibited Clotting Factor Xa

Brandstetter, H., Kühne, A., Bode, W., Huber, R., von der Saal, W., Wirthensohn, K., & Engh, R. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.47.29988 · Cited by 279 · see citing works

Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity

Clackson, T., Ultsch, M. H., Wells, J. A., & de Vos, A. M. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1669 · Cited by 278 · see citing works

Titin Extensibility In Situ: Entropic Elasticity of Permanently Folded and Permanently Unfolded Molecular Segments

Trombitás, K., Greaser, M. L., Labeit, S., Jin, J., Kellermayer, M., Helmes, M., & Granzier, H. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.853 · Cited by 239 · see citing works

Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues

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Protein motifs that recognize structural features of DNA

Churchill, M. E. A., & TRAVERS, A. A. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90040-3 · Cited by 201 · see citing works

Probing the conformational state of apomyoglobin by limited proteolysis 1 1Edited by P. E. Wright

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The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with cognate tRNAPhe

Goldgur, Y., Mosyak, L., Reshetnikova, L. S., Ankilova, V. N., Lavrik, O. I., Khodyreva, S. N., & Safro, M. G. (1997) · Structure · doi:10.1016/s0969-2126(97)00166-4 · Cited by 193 · see citing works

Roles of partly unfolded conformations in macromolecular self‐assembly

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Trimethylamine N-Oxide-induced Cooperative Folding of an Intrinsically Unfolded Transcription-activating Fragment of Human Glucocorticoid Receptor

Baskakov, I. V., Kumar, P., Srinivasan, G., Ji, Y., Bolen, D. W., & Thompson, E. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10693 · Cited by 163 · see citing works

The Conformation of Horse Heart Apocytochrome c

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Structural and functional analysis of the NF-kappa B p65 C terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation.

Schmitz, M. L., Silva, M. A. D. S., Altmann, H., Czisch, M., Holak, T. A., & Baeuerle, P. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47294-8 · Cited by 159 · see citing works

X-ray Crystal Structure of Human Dopamine Sulfotransferase, SULT1A3

Dajani, R., Cleasby, A., Neu, M., Wonacott, A. J., Jhoti, H., Hood, A. M., Modi, S. P., Hersey, A., Taskinen, J., Cooke, R. M., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.37862 · Cited by 158 · see citing works

The Conformation of Histone H5

Avilés, F. X., Chapman, G. E., Kneale, G. G., Crane‐Robinson, C., & Bradbury, E. M. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12457.x · Cited by 152 · see citing works

Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site 1 1Edited by I. A. Wilson

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Terminal regions of flagellin are disordered in solution

Vonderviszt, F., Kanto, S., Aizawa, S.-I., & Namba, K. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90176-9 · Cited by 137 · see citing works

Ca2+–calmodulin and protein kinase Cs: a hypothetical synthesis of their conflicting convergences on shared substrate domains

Chakravarthy, B., Morley, P., & Whitfield, J. (1999) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01288-0 · Cited by 135 · see citing works

Distinct structural elements in GDNF mediate binding to GFRα1 and activation of the GFRα1–c‐Ret receptor complex

Eketjäll, S., Fainzilber, M., Murray‐Rust, J., & Ibáñez, C. F. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5901 · Cited by 129 · see citing works

NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein

Penkett, C. J., Redfield, C., Dodd, I. B., Hubbard, J., McBay, D. L., Mossakowska, D. E., Smith, R. A., Dobson, C. M., & Smith, L. J. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1369 · Cited by 125 · see citing works

Crystal structure of glycyl‐tRNA synthetase from Thermus thermophilus.

Logan, D. T., Mazauric, M., Kern, D., & Moras, D. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00089.x · Cited by 122 · see citing works

Crystal structure of human catecholamine sulfotransferase 1 1Edited by R. Huber

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Structure of tomato bushy stunt virus

Hopper, P., Harrison, S. C., & Sauer, R. T. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90045-7 · Cited by 112 · see citing works

Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 Å: evidence for conformational lability 1 1Edited by J. M. Thornton

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Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein 1 1Edited by A. R. Fersht

Geyer, M., Munte, C. E., Schorr, J., Kellner, R., & Kalbitzer, H. R. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2740 · Cited by 101 · see citing works

Human replication protein A: Global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker†

Jacobs, D. M., Lipton, A. S., Isern, N., Daughdrill, G. W., Lowry, D. F., Gomes, X. V., & Wold, M. S. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008373009786 · Cited by 100 · see citing works

Crystal Structure of the Complex of Diphtheria Toxin with an Extracellular Fragment of Its Receptor

Louie, G. V., Yang, W., Bowman, M. E., & Choe, S. (1997) · Molecular Cell · doi:10.1016/s1097-2765(00)80008-8 · Cited by 100 · see citing works

Conformational Changes in the Fibronectin Binding MSCRAMMs Are Induced by Ligand Binding

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Structural Studies on Two High‐Mobility‐Group Proteins from Calf Thymus, HMG‐14 and HMG‐20 (Ubiquitin), and Their Interaction with DNA

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Modular Motif, Structural Folds and Affinity Profiles of the PEVK Segment of Human Fetal Skeletal Muscle Titin

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Purification and characterization of the carboxyl-terminal transactivation domain of Vmw65 from herpes simplex virus type 1.

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Studies on the Conformational Properties of the High‐Mobility‐Group Chromosomal Protein HMG 17 and Its Interaction with DNA

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The Cap-binding Protein eIF4E Promotes Folding of a Functional Domain of Yeast Translation Initiation Factor eIF4G1

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Independent Ligand-Induced Folding of the RNA-Binding Domain and Two Functionally Distinct Antitermination Regions in the Phage λ N Protein

Mogridge, J., Legault, P., Li, J., Oene, M. D. V., Kay, L. E., & Greenblatt, J. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80027-1 · Cited by 88 · see citing works

NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin

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The C-terminal domain of Saccharomyces cerevisiae DNA topoisomerase II.

Caron, P. R., Watt, P. M., & Wang, J. C. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.5.3197 · Cited by 86 · see citing works

High Resolution NMR Solution Structure of the Leucine Zipper Domain of the c-Jun Homodimer*

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The Binding of Calcium to the B-repeat Segment of SdrD, a Cell Surface Protein of Staphylococcus aureus

Josefsson, E., O'Connell, D. W., Foster, T. J., Durussel, I., & Cox, J. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.47.31145 · Cited by 77 · see citing works

Crystal structure of the adenovirus DNA binding protein reveals a hook‐on model for cooperative DNA binding.

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Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2

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Termini of Salmonella flagellin are disordered and become organized upon polymerization into flagellar filament

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Phosphorylation and N‐terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2

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Acetylation of Novel Sites in the Nucleosomal Binding Domain of Chromosomal Protein HMG-14 by p300 Alters Its Interaction with Nucleosomes

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Conformation of bovine myelin basic protein purified with bound lipids

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Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine 1 1Edited by R. Huber

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High-resolution solution structure of the retinoid X receptor DNA-binding domain

Holmbeck, S. M. A., Foster, M. P., Casimiro, D. R., Sem, D. S., Dyson, H. J., & Wright, P. E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1908 · Cited by 61 · see citing works

Locations of terminal segments of flagellin in the filament structure and their roles in polymerization and polymorphism

Mimori‐Kiyosue, Y., Vonderviszt, F., & Namba, K. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1111 · Cited by 56 · see citing works

Yeast heat shock transcription factor N‐terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy

Cho, H. S., Liu, C. W., Damberger, F. F., Pelton, J. G., Nelson, H. C. M., & Wemmer, D. E. (1996) · Protein Science · doi:10.1002/pro.5560050210 · Cited by 56 · see citing works

The refinement of southern bean mosaic virus in reciprocal space

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Mapping of a major surface-exposed site in herpes simplex virus protein Vmw65 to a region of direct interaction in a transcription complex assembly

Hayes, S., & O'Hare, P. (1993) · Journal of Virology · doi:10.1128/jvi.67.2.852-862.1993 · Cited by 50 · see citing works

Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes

Huang, Y., Komoto, J., Konishi, K., Takata, Y., Ogawa, H., Gomi, T., Fujioka, M., & Takusagawa, F. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3637 · Cited by 49 · see citing works

Structural and functional characterization of the HPV16 E7 protein expressed in bacteria.

Pahel, G. L., AULABAUGH, A. E., Short, S. A., Barnes, J. A., Painter, G. R., Ray, P. H., & Phelps, W. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74487-1 · Cited by 43 · see citing works

NMR Structure and Functional Characteristics of the Hydrophilic N Terminus of the Potassium Channel β-Subunit Kvβ1.1

Wissmann, R., Baukrowitz, T., Kalbacher, H., Kalbitzer, H. R., Ruppersberg, J. P., Pongs, O., Antz, C., & Fakler, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35521 · Cited by 41 · see citing works

Comparing predictors of disordered protein.

Li, X., Zoran Obradovic, A., Brown, C. J., Garner, E. C., & Dunker, A. K. (2000) · PubMed · Cited by 39 · see citing works

Intelligent Data Analysis for Protein Disorder Prediction

Romero, P. R., Zoran Obradovic, A., & Dunker, A. K. (2000) · Artificial Intelligence Review · doi:10.1023/a:1006678623815 · Cited by 38 · see citing works

A folding transition and novel zinc finger accessory domain in the transcription factor ADR1.

Klevit, R. E., Bowers, P. M., & Schaufler, L. E. (1999) · Nature Structural Biology · doi:10.1038/8283 · Cited by 38 · see citing works

Role of the outermost subdomain of Salmonella flagellin in the filament structure revealed by electron cryomicroscopy 1 1Edited by M. F. Moody

Mimori‐Kiyosue, Y., Yamashita, I., Fujiyoshi, Y., Yamaguchi, S., & Namba, K. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2184 · Cited by 38 · see citing works

Structural and functional properties of the N transcriptional activation domain of thyroid transcription factor-1: similarities with the acidic activation domains

Tell, G., Perrone, L., Fabbro, D., Pellizzari, L., Pucillo, C. E. M., Felice, M. D., Acquaviva, R., Formisano, S., & Damante, G. (1998) · Biochemical Journal · doi:10.1042/bj3290395 · Cited by 38 · see citing works

Nuclear magnetic resonance studies of the structure of B50/neuromodulin and its interaction with calmodulin

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Assembly of a Ternary Complex by the Predicted Minimal Coiled-coil-forming Domains of Syntaxin, SNAP-25, and Synaptobrevin

Cánaves, J. M., & Montal, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.34214 · Cited by 30 · see citing works

Domain III of Elongation Factor G from Thermus thermophilus Is Essential for Induction of GTP Hydrolysis on the Ribosome

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Dimerization and DNA Binding Facilitate aaa-Helix Formation of Max in Solution

Horiuchi, M., Kurihara, Y., Katahira, M., Maeda, T., Saito, T., & Uesugi, S. (1997) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021813 · Cited by 26 · see citing works

Domain Mapping of Human Apurinic/Apyrimidinic Endonuclease

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Origin of the Napoleon's hat nebula around SN1987A and implications for the progenitor

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The Phage Infection Process: a Functional Role for the Distal Linker Region of Bacteriophage Protein 3

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ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1 1Edited by M. Yaniv

Dekker, J., Kanellopoulos, P. N., van Oosterhout, J. A. W. M., Stier, G., Tucker, P. A., & van der Vliet, P. C. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1652 · Cited by 23 · see citing works

Crystallization of the globular domain of histone H5

Graziano, V., Gerchman, S. E., Wonacott, A. J., Sweet, R. M., Wells, J. R. E., White, S. W., & Ramakrishnan, V. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90122-3 · Cited by 23 · see citing works

The Formation of a Flexible DNA-binding Protein Chain Is Required for Efficient DNA Unwinding and Adenovirus DNA Chain Elongation

van Breukelen, B., Kanellopoulos, P. N., Tucker, P. A., & van der Vliet, P. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005745200 · Cited by 17 · see citing works

Inter-Domain Interaction and the Structural Flexibility of Calmodulin in the Connecting Region of the Terminal Two Domains

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THE HYDROPHILIC, PROTEAS E-SENSITIVE TERMINAL DOMAINS OF EUCARYOTIC DNA TOPOISOMERASES HAVE ESSENTIAL INTRACELLULAR FUNCTIONS

Shaiu, W.-L., Tao, H., & Hsieh, T. S. (1998) · Pacific Symposium on Biocomputing (PSB) · doi:10.1142/9789814447300_0057 · Cited by 15 · see citing works

Biological Research Center

Martinson, J. (1962) · Science · doi:10.1126/science.137.3533.900-a · Cited by 10 · see citing works

Purification of histone core octamers and 2.15 Å X-ray analysis of crystals in KCl/phosphate

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The basic subdomain of the c-Jun oncoprotein. A joint CD, Fourier-transform infrared and NMR study.

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Biological Research Center

Martinson, J. (1962) · Science · doi:10.1126/science.137.3533.900 · Cited by 7 · see citing works

Quality of the electron density map

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

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

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Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins

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Protein Disorder Prediction

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Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering

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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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Colicin Biology

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The Pairwise Energy Content Estimated from Amino Acid Composition Discriminates between Folded and Intrinsically Unstructured Proteins

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Conformational constraints for amyloid fibrillation: the importance of being unfolded

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GlobPlot: exploring protein sequences for globularity and disorder

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Targeting transcription factors in cancer — from undruggable to reality

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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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FoldIndex(C): a simple tool to predict whether a given protein sequence is intrinsically unfolded

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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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PrDOS: prediction of disordered protein regions from amino acid sequence

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DisProt: the Database of Disordered Proteins

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Introducing Protein Intrinsic Disorder

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Analysis of Molecular Recognition Features (MoRFs)

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Phosphorylated Proteins and Control over Apatite Nucleation, Crystal Growth, and Inhibition

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The interplay between structure and function in intrinsically unstructured proteins

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Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations

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Intrinsic Disorder and Functional Proteomics

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The unfoldomics decade: an update on intrinsically disordered proteins

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Coupled Folding and Binding with α-Helix-Forming Molecular Recognition Elements

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Unfolded Proteins and Protein Folding Studied by NMR

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Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners

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Identification, analysis, and prediction of protein ubiquitination sites

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

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Unusual biophysics of intrinsically disordered proteins.

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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 567 · see citing works

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 560 · see citing works

Net charge per residue modulates conformational ensembles of intrinsically disordered proteins

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Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life

Xue, B., Dunker, A. K., & Uversky, V. N. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2012.675145 · Cited by 557 · see citing works

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

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The role of structural disorder in the function of RNA and protein chaperones

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Exploiting heterogeneous sequence properties improves prediction of protein disorder

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

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The SARS coronavirus nucleocapsid protein – Forms and functions

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Preformed structural elements feature in partner recognition by intrinsically unstructured proteins

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Raman Spectroscopic Characterization of Secondary Structure in Natively Unfolded Proteins: α-Synuclein

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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

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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

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 497 · see citing works

Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms

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Structural disorder throws new light on moonlighting

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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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PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites

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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 442 · see citing works

Intrinsically disordered proteins from A to Z

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A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering

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Predicting intrinsic disorder in proteins: an overview

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

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POPP the question: what do LEA proteins do?

Wise, M. J., & Tunnacliffe, A. (2003) · Trends in Plant Science · doi:10.1016/j.tplants.2003.10.012 · Cited by 418 · see citing works

O-linked β-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress

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Relating sequence encoded information to form and function of intrinsically disordered proteins

Das, R. K., Ruff, K. M., & Pappu, R. V. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.03.008 · Cited by 400 · see citing works

Identification and functions of usefully disordered proteins

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Local structural disorder imparts plasticity on linear motifs

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Filming Biomolecular Processes by High-Speed Atomic Force Microscopy

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Recent atomic models of amyloid fibril structure

Nelson, R. A., & Eisenberg, D. S. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.03.007 · Cited by 393 · see citing works

The Phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites’ boundaries

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A Comparative Study of the Relationship Between Protein Structure and β-Aggregation in Globular and Intrinsically Disordered Proteins

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Flavors of protein disorder

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Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life

Peng, Z., Yan, J. R., Fan, X., Mizianty, M. J., Xue, B., Wang, K., Hu, G., Uversky, V. N., & Kurgan, L. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1661-9 · Cited by 382 · see citing works

Functional Anthology of Intrinsic Disorder. 3. Ligands, Post-Translational Modifications, and Diseases Associated with Intrinsically Disordered Proteins

Xie, H. M., Vučetić, S., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2007) · Journal of Proteome Research · doi:10.1021/pr060394e · Cited by 382 · see citing works

What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?

Ekman, D. S., Light, S., Björklund, Å. K., & Elofsson, A. (2006) · Genome biology · doi:10.1186/gb-2006-7-6-r45 · Cited by 377 · see citing works

How do intrinsically disordered protein regions encode a driving force for liquid-liquid phase separation?

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Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables

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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

Uversky, V. N. (2009) · The Protein Journal · doi:10.1007/s10930-009-9201-4 · Cited by 360 · see citing works

Oncogenic Mutations Counteract Intrinsic Disorder in the EGFR Kinase and Promote Receptor Dimerization

Shan, Y., Eastwood, M. P., Zhang, X., Kim, E. T., Arkhipov, A. S., Dror, R. O., Jumper, J., Kuriyan, J., & Shaw, D. E. (2012) · Cell · doi:10.1016/j.cell.2012.02.063 · Cited by 360 · see citing works

High-speed atomic force microscopy coming of age

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Protein flexibility and intrinsic disorder

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

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Understanding eukaryotic linear motifs and their role in cell signaling and regulation

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Extended disordered proteins: targeting function with less scaffold

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Determination of Membrane Protein Structure and Dynamics by Magic-Angle-Spinning Solid-State NMR Spectroscopy

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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

FlgM gains structure in living cells

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Cross-Linking Mass Spectrometry for Investigating Protein Conformations and Protein–Protein Interactions─A Method for All Seasons

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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 314 · see citing works

NMR Characterization of Long-Range Order in Intrinsically Disordered Proteins

Salmon, L., Nodet, G., Ozenne, V., Yin, G., Jensen, M. R., Zweckstetter, M., & Blackledge, M. J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja101645g · Cited by 304 · see citing works

flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions

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Evolution and Disorder

Brown, C. J., Johnson, A. K., Dunker, A., & Daughdrill, G. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.02.005 · Cited by 288 · see citing works

Intrinsic disorder in scaffold proteins: Getting more from less

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Insights into SARS-CoV transcription and replication from the structure of the nsp7–nsp8 hexadecamer

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The importance of intrinsic disorder for protein

Iakoucheva, L. M., Predrag Radivojac, A., Brown, C. J., O'connor, T. R., Sikes, J. G., Zoran Obradovic, A., & Dunker, A. K. (2003)

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 · see citing works

Intrinsically Disordered Proteins

Uversky, V. N. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-374984-0.01698-3 · Cited by 1,646 · see citing works

Identification and functions of usefully disordered proteins

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Functional anthology of intrinsic disorder. III. Ligands, postranslational modifications and diseases associated with long disordered regions

Vučetić, S., Xie, H. M., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2013)