Intrinsically disordered proteins: regulation and disease

Selective inhibition of BET bromodomains

Filippakopoulos, P., Qi, J., Picaud, S., Shen, Y., Smith, W. B., Fedorov, O., Morse, E. M., Keates, T., Hickman, T. T., Felletar, I., et al. (2010) · Nature · doi:10.1038/nature09504 · Cited by 4,262

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

Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149

Targeting proteins for degradation.

Schrader, E. K., Harstad, K. G., & Matouschek, A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.250 · Cited by 287

Recurrent design patterns in the feedback regulation of the mammalian signalling network

Legewie, S., Herzel, H., Westerhoff, H. V., & Blüthgen, N. (2008) · Molecular Systems Biology · doi:10.1038/msb.2008.29 · Cited by 112

Pfam: the protein families database

Finn, R. D., Bateman, A., Clements, J., Coggill, P., Eberhardt, R. Y., Eddy, S. R., Heger, A., Hetherington, K., Holm, L., Mistry, J., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1223 · Cited by 6,148

Harnessing protein folding neural networks for peptide–protein docking

Tsaban, T., Varga, J. K., Avraham, O., Ben-Aharon, Z., Khramushin, A., & Schueler-Furman, O. (2022) · Nature Communications · doi:10.1038/s41467-021-27838-9 · Cited by 1,205

Applications of Deep Learning in Biomedicine

Mamoshina, P., Vieira, A., Lane, E., & Zhavoronkov, A. (2016) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5b00982 · Cited by 701

Dynamic integration of splicing within gene regulatory pathways

Braunschweig, U., Gueroussov, S., Plocik, A. M., Graveley, B. R., & Blencowe, B. J. (2013) · Cell · doi:10.1016/j.cell.2013.02.034 · Cited by 406

Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases

Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288

Allosteric Modulators of Steroid Hormone Receptors: Structural Dynamics and Gene Regulation

Kumar, R., & McEwan, I. J. (2012) · Endocrine Reviews · doi:10.1210/er.2011-1033 · Cited by 135

Targeting intrinsically disordered proteins at the edge of chaos

Ruan, H., Sun, Q., Zhang, W., Liu, Y., & Lai, L. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2018.09.017 · Cited by 133

MeCP2: the long trip from a chromatin protein to neurological disorders

Ausió, J., Paz, A. M. D., & Esteller, M. (2014) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.03.004 · Cited by 108

Intrinsically Disordered Proteins Link Alternative Splicing and Post-translational Modifications to Complex Cell Signaling and Regulation

Zhou, J., Zhao, S., & Dunker, A. K. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.03.028 · Cited by 90

AlphaFold and the amyloid landscape

Pinheiro, F., Santos, J., & Ventura, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167059 · Cited by 88

On the Potential of Machine Learning to Examine the Relationship Between Sequence, Structure, Dynamics and Function of Intrinsically Disordered Proteins

Lindorff-Larsen, K., & Kragelund, B. B. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167196 · Cited by 85

A kinetic ensemble of the Alzheimer’s Aβ peptide

Löhr, T., Kohlhoff, K., Heller, G. T., Camilloni, C., & Vendruscolo, M. (2021) · Nature Computational Science · doi:10.1038/s43588-020-00003-w · Cited by 57

Conformational Characterization and Classification of Intrinsically Disordered Proteins by Native Mass Spectrometry and Charge‐State Distribution Analysis

Santambrogio, C., Natalello, A., Brocca, S., Ponzini, E., & Grandori, R. (2019) · PROTEOMICS · doi:10.1002/pmic.201800060 · Cited by 51

Structural determinants of co-translational protein complex assembly

Mallik, S., Venezian, J., Lobov, A., Heidenreich, M., Garcia-Seisdedos, H., Yeates, T. O., Shiber, A., & Levy, E. D. (2025) · Cell · doi:10.1016/j.cell.2024.11.013 · Cited by 42

Matching protein surface structural patches for high-resolution blind peptide docking

(2022) · doi:10.1073/pnas.2121153119 · Cited by 41

The designability of protein switches by chemical rescue of structure: mechanisms of inactivation and reactivation

Xia, Y., DiPrimio, N., Keppel, T. R., Vo, B., Fraser, K., Battaile, K. P., Egan, C., Bystroff, C., Lovell, S., Weis, D. D., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja407644b · Cited by 33

Presence and utility of intrinsically disordered regions in kinases

Kathiriya, J. J., Pathak, R. R., Clayman, E., Xue, B., Uversky, V. N., & Davé, V. (2014) · Molecular BioSystems · doi:10.1039/c4mb00224e · Cited by 30

Identification of intrinsically disordered regions in PTEN and delineation of its function via a network approach

Malaney, P., Uversky, V. N., & Davé, V. (2015) · Methods · doi:10.1016/j.ymeth.2014.10.005 · Cited by 18

Orchestration of algal metabolism by protein disorder

Launay, H., Receveur-Bréchot, V., Carrière, F., & Gontero, B. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108070 · Cited by 16

Diversity of hydrodynamic radii of intrinsically disordered proteins

Białobrzewski, M. K., Klepka, B. P., Michaś, A., Cieplak-Rotowska, M. K., Staszałek, Z., & Niedźwiecka, A. (2023) · European Biophysics Journal · doi:10.1007/s00249-023-01683-8 · Cited by 12

BAGEL: Protein engineering via exploration of an energy landscape

(2025) · doi:10.1371/journal.pcbi.1013774 · Cited by 7

Utilizing the scale-invariant feature transform algorithm to align distance matrices facilitates systematic protein structure comparison

Guo, Z., Wang, Y., & Ou, G. (2024) · Bioinformatics · doi:10.1093/bioinformatics/btae064 · Cited by 6

Characterizing Structural and Kinetic Ensembles of Intrinsically Disordered Proteins Using Writhe

(2025) · doi:10.1021/acs.jctc.5c01133 · Cited by 5

TAFPred: Torsion Angle Fluctuations Prediction from Protein Sequences

Kabir, M. W. U., Alawad, D. M., Mishra, A., & Hoque, M. T. (2023) · Biology · doi:10.3390/biology12071020 · Cited by 5