Natively unfolded proteins: A point where biology waits for physics

Crystal structure of the ribosome at 5.5 Å resolution

Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944

Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation

Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010907200 · Cited by 1,096

The active form of the steroidogenic acute regulatory protein, StAR, appears to be a molten globule

Bose, H. S., Whittal, R. M., Baldwin, M. A., & Miller, W. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7250 · Cited by 227

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

The importance of being unfolded

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

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

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

Kato, M., Han, T. W., Xie, S., Shi, K., Du, X., Wu, L. C., Mirzaei, H., Goldsmith, E. J., Longgood, J., Pei, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.017 · Cited by 2,012

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

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

D2P2: database of disordered protein predictions

Oates, M. E., Romero, P., Ishida, T., Ghalwash, M., Mizianty, M. J., Xue, B., Dosztányi, Z., Uversky, V. N., Obradovic, Z., Kurgan, L., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1226 · Cited by 705

Myelin basic protein: a multifunctional protein

Boggs, J. M. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6094-7 · Cited by 687

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

Globular amyloid β‐peptide 1−42 oligomer − a homogenous and stable neuropathological protein in Alzheimer's disease

Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559

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

Global Hairpin Folding of Tau in Solution

Jeganathan, S., von Bergen, M., Brutlach, H., Steinhoff, H.-J., & Mandelkow, E. (2006) · Biochemistry · doi:10.1021/bi0521543 · Cited by 432

Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins

Hilser, V. J., & Thompson, E. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700329104 · Cited by 406

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367

Active promoters give rise to false positive ‘Phantom Peaks’ in ChIP-seq experiments

Jain, D., Baldi, S., Zabel, A., Straub, T., & Becker, P. B. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv637 · Cited by 156

Describing sequence–ensemble relationships for intrinsically disordered proteins

Mao, A. H., Lyle, N., & Pappu, R. V. (2013) · Biochemical Journal · doi:10.1042/bj20121346 · Cited by 135

Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form

Sigalov, A. B., Zhuravleva, A. V., & Orekhov, V. Y. (2007) · Biochimie · doi:10.1016/j.biochi.2006.11.003 · Cited by 128

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

The multiple effects of amino acids on the early stages of calcium carbonate crystallization

Picker, A., Kellermeier, M., Seto, J., Gebauer, D., & Cölfen, H. (2012) · Zeitschrift für Kristallographie - Crystalline Materials · doi:10.1524/zkri.2012.1569 · Cited by 103

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

Preprotein mature domains contain translocase targeting signals that are essential for secretion.

Chatzi, K. E., Sardis, M. F., Tsirigotaki, A., Koukaki, M., Šoštarić, N., Konijnenberg, A., Sobott, F., Kalodimos, C. G., Karamanou, S., & Economou, A. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201609022 · Cited by 72

How multisite phosphorylation impacts the conformations of intrinsically disordered proteins

Jin, F., & Gräter, F. (2021) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1008939 · Cited by 77

Evaluation of scFv protein recovery from E. coli by in vitro refolding and mild solubilization process

Sarker, A., Rathore, A. S., & Gupta, R. D. (2019) · Microbial Cell Factories · doi:10.1186/s12934-019-1053-9 · Cited by 75

Sequence-to-conformation relationships of disordered regions tethered to folded domains of proteins

Mittal, A., Holehouse, A. S., Cohan, M. C., & Pappu, R. V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.012 · Cited by 72

Quantifying the topography of the intrinsic energy landscape of flexible biomolecular recognition

Chu, X., Gan, L., Wang, E., & Wang, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220699110 · Cited by 62

Machines vs. Ensembles: Effective MAPK Signaling through Heterogeneous Sets of Protein Complexes

Suderman, R., & Deeds, E. J. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003278 · Cited by 52

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

Role of Ordered Proteins in the Folding-Upon-Binding of Intrinsically Disordered Proteins

Lawrence, C. W., Kumar, S., Noid, W. G., & Showalter, S. A. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz402729x · Cited by 25

AlphaFold2 modeling and molecular dynamics simulations of an intrinsically disordered protein

Guo, H.-B., Huntington, B., Perminov, A., Smith, K., Hastings, N., Dennis, P., Kelley-Loughnane, N., & Berry, R. (2024) · PLOS ONE · doi:10.1371/journal.pone.0301866 · Cited by 13

Intrinsically disordered regions regulate RhlE RNA helicase functions in bacteria

Hausmann, S., Geiser, J., Allen, G. E., Geslain, S. A. M., & Valentini, M. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae511 · Cited by 9

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

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

The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction

(2024) · doi:10.1016/j.isci.2024.111259 · Cited by 3