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Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer?

Minde, D., Anvarian, Z., Rüdiger, S., & Maurice, M. M. (2011) · Molecular Cancer · doi:10.1186/1476-4598-10-101 · Cited by 166

Disease-Associated Mutations Disrupt Functionally Important Regions of Intrinsic Protein Disorder

Vacic, V., Markwick, P. R. L., Oldfield, C. J., Zhao, X., Haynes, C. A., Uversky, V. N., & Iakoucheva, L. M. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002709 · Cited by 165

Regulation by phosphorylation of the relative affinities of the N-terminal transactivation domains of p53 for p300 domains and Mdm2

Teufel, D. P., Bycroft, M., & Fersht, A. R. (2009) · Oncogene · doi:10.1038/onc.2009.71 · Cited by 164

Specificity Determinants of Recruitment Peptides Bound to Phospho-CDK2/Cyclin A,

Lowe, E. D., Tews, I., Cheng, K. Y., Brown, N. R., Gul, S., Noble, M. E. M., Gamblin, S. J., & Johnson, L. N. (2002) · Biochemistry · doi:10.1021/bi0268910 · Cited by 163

Regulation of PTEN Activity by Its Carboxyl-terminal Autoinhibitory Domain

Odriozola, L., Singh, G., Hoang, T., & Chan, A. M.-L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611240200 · Cited by 160

Crystal Structure of the p53 Core Domain Bound to a Full Consensus Site as a Self-Assembled Tetramer

Chen, Y., Dey, R., & Chen, L. (2010) · Structure · doi:10.1016/j.str.2009.11.011 · Cited by 156

Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes

Mohan, A., Sullivan, W. J., Predrag Radivojac, A., Dunker, A. K., & Uversky, V. N. (2008) · Molecular BioSystems · doi:10.1039/b719168e · Cited by 155

Isoindolinone Inhibitors of the Murine Double Minute 2 (MDM2)-p53 Protein−Protein Interaction: Structure−Activity Studies Leading to Improved Potency

Hardcastle, I. R., Liu, J., Valeur, E., Watson, A. F., Ahmed, S. U., Blackburn, T. J., Bennaceur, K., Clegg, W., Drummond, C. J., Endicott, J., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm1011929 · Cited by 153

The Chaperone-assisted E3 Ligase C Terminus of Hsc70-interacting Protein (CHIP) Targets PTEN for Proteasomal Degradation

Ahmed, S. F., Deb, S., Paul, I., Chatterjee, A., Mandal, T., Chatterjee, U., & Ghosh, M. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.321083 · Cited by 152

Selective Inhibition of c-Myc/Max Dimerization and DNA Binding by Small Molecules

Kiessling, A., Sperl, B., Hollis, A., Eick, D., & Berg, T. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.05.011 · Cited by 152

Sintokamides A to E, Chlorinated Peptides from the Sponge Dysidea sp. that Inhibit Transactivation of the N-Terminus of the Androgen Receptor in Prostate Cancer Cells

Sadar, M. D., Williams, D. E., Mawji, N. R., Patrick, B. O., Wikanta, T., Chasanah, E., Irianto, H. E., van Soest, R. W. M., & Andersen, R. J. (2008) · Organic Letters · doi:10.1021/ol802021w · Cited by 152

Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation

Zhou, H., & Pang, X. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00305 · Cited by 1,214

Intrinsically disordered proteins in overcrowded milieu: Membrane-less organelles, phase separation, and intrinsic disorder

Uversky, V. N. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.10.015 · Cited by 707

The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches

Joerger, A. C., & Fersht, A. R. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014710 · Cited by 675

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436

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

Hu, G., Katuwawala, A., Wang, K., Wu, Z., Ghadermarzi, S., Gao, J., & Kurgan, L. (2021) · Nature Communications · doi:10.1038/s41467-021-24773-7 · Cited by 292

Unfoldomics of human diseases: Linking protein intrinsic disorder with diseases

(2009) · TUScholarShare (Temple University) · doi:10.34944/dspace/5554

Unfoldomics of Human Genetic Diseases: Illustrative Examples of Ordered and Intrinsically Disordered Members of the Human Diseasome

Midic, U., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2009) · Protein and Peptide Letters · doi:10.2174/092986609789839377 · Cited by 65

Intrinsically Disordered Proteins in Human Diseases.

Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2007) · Bioinformatics and Bioengineering · Cited by 3

Protein disorder in the human diseasome: unfoldomics of human genetic diseases

Midic, U., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2009) · TUScholarShare (Temple University) · Cited by 2

intrinsically disordered and of unfolded proteins

Varadi, M., Kosol, S., Lebrun, P., Valentini, E., Blackledge, M. J., Dunker, A. K., Felli, I. C., Forman-Kay, J. D., Kriwacki, R. W., Pierattelli, R., et al. (2013)