Analysis of Molecular Recognition Features (MoRFs)

Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features

Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320

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

Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain

Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206

Intrinsic Disorder and Protein Function

Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731

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 protein trinity—linking function and disorder

Dunker, A. K., & Obradovic, Z. (2001) · Nature Biotechnology · doi:10.1038/nbt0901-805 · Cited by 581

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

Romero, P. R., Zaidi, S., Fang, Y. Y., Uversky, V. N., Radivojac, P., Oldfield, C. J., Cortese, M. S., Sickmeier, M., LeGall, T., Obradovic, Z., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507916103 · Cited by 480

Proteasomal degradation of tau protein

David, D. C., Layfield, R., Serpell, L., Narain, Y., Goedert, M., & Spillantini, M. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01137.x · Cited by 327

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,897

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

Identification of slow molecular order parameters for Markov model construction

Pérez-Hernández, G., Paul, F., Giorgino, T., De Fabritiis, G., & Noé, F. (2013) · The Journal of Chemical Physics · doi:10.1063/1.4811489 · Cited by 990

Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation

Gsponer, J., Futschik, M. E., Teichmann, S. A., & Babu, M. M. (2008) · Science · doi:10.1126/science.1163581 · Cited by 466

The structural and functional signatures of proteins that undergo multiple events of post‐translational modification

Pejaver, V., Hsu, W., Xin, F., Dunker, A. K., Uversky, V. N., & Radivojac, P. (2014) · Protein Science · doi:10.1002/pro.2494 · Cited by 349

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

Intrinsically disordered proteins and multicellular organisms

Dunker, A. K., Bondos, S. E., Huang, F., & Oldfield, C. J. (2015) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.09.025 · Cited by 150

Finding Our Way in the Dark Proteome

Bhowmick, A., Brookes, D. H., Yost, S. R., Dyson, H. J., Forman-Kay, J. D., Gunter, D., Head-Gordon, M., Hura, G. L., Pande, V. S., Wemmer, D. E., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06543 · Cited by 128

PepNN: a deep attention model for the identification of peptide binding sites

Abdin, O., Nim, S., Wen, H., & Kim, P. M. (2022) · Communications Biology · doi:10.1038/s42003-022-03445-2 · Cited by 104

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

A Computational Investigation of Allostery in the Catabolite Activator Protein

Li, L., Uversky, V. N., Dunker, A. K., & Meroueh, S. O. (2007) · Journal of the American Chemical Society · doi:10.1021/ja076046a · Cited by 71

Stochastic machines as a colocalization mechanism for scaffold protein function

Xue, B., Romero, P. R., Noutsou, M., Maurice, M. M., Rüdiger, S. G. D., William, A. M., Mizianty, M. J., Kurgan, L., Uversky, V. N., & Dunker, A. K. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.04.006 · Cited by 47

PRISMA: Protein Interaction Screen on Peptide Matrix Reveals Interaction Footprints and Modifications- Dependent Interactome of Intrinsically Disordered C/EBPβ

Dittmar, G., Hernandez, D. P., Kowenz-Leutz, E., Kirchner, M., Kahlert, G., Wesolowski, R., Baum, K., Knoblich, M., Hofstätter, M., Muller, A., et al. (2019) · iScience · doi:10.1016/j.isci.2019.02.026 · Cited by 41

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

Differential occurrence of protein intrinsic disorder in the cytoplasmic signaling domains of cell receptors

Sigalov, A. B., & Uversky, V. N. (2011) · Self/Nonself · doi:10.4161/self.2.1.14790 · Cited by 23

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

Exploring the evolution and function of Canoe’s intrinsically disordered region in linking cell-cell junctions to the cytoskeleton during embryonic morphogenesis

Gurley, N. J., Szymanski, R. A., Dowen, R. H., Butcher, T. A., Ishiyama, N., & Peifer, M. (2023) · PLOS ONE · doi:10.1371/journal.pone.0289224 · Cited by 15

Chaotic aging: intrinsically disordered proteins in aging-related processes

Manyilov, V. D., Ilyinsky, N. S., Nesterov, S. V., Saqr, B. M. G. A., Dayhoff, G. W., Zinovev, E. V., Matrenok, S. S., Fonin, A. V., Kuznetsova, I. M., Turoverov, K. K., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04897-3 · Cited by 14

T and Z , partial seed coat patterning genes in common bean, provide insight into the structure and protein interactions of a plant MBW complex

McClean, P. E., Roy, J., Colbert, C. L., Osborne, C., Lee, R., Miklas, P. N., & Osorno, J. M. (2024) · G3: Genes, Genomes, Genetics · doi:10.1093/g3journal/jkae184 · Cited by 13

RLIP76: A Structural and Functional Triumvirate

Cornish, J., Owen, D., & Mott, H. R. (2021) · Cancers · doi:10.3390/cancers13092206 · Cited by 8