Cited by 1,731Protein Structure and DynamicsEnzyme Structure and FunctionProtein Interaction Studies and Fluorescence Analysis

The DOI matches its Crossref record; 89 of the 89 references it cites were found in a registry or an index.

Intrinsic Disorder and Protein Function

Dunker, A. Keith, Brown, Celeste J., Lawson, J. David, Iakoucheva, Lilia M., Obradović, Zoran·2002·Biochemistry

DOI 10.1021/bi012159+

Open this paper in CoChat — free account

Abstract

0196237 to Z.O. and A.K.D and by NIH-1R01-LM06916 to A.K.D. and Z.O. Key words: native protein, random coil, molten globule, intrinsic disorder, protein structurefunction, genomics, proteomics, and bioinformatics Abbreviations: circular dichroism (CD), limited proteolysis (LP), nuclear magnetic resonance

Integrity signals

Registry

Crossref · 10.1021/bi012159+

Cites

89 of 89 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Basic Methods in Molecular Biology
(1986) · Elsevier eBooks · doi:10.1016/b978-0-444-01082-7.x5001-2 · Cited by 3,163
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968
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
Self-citation
Coupling of folding and binding for unstructured proteins
Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex
Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253
Moonlighting proteins
Jeffery, C. J. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01335-8 · Cited by 1,016
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
Methods in molecular biology
Deininger, P. L. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90283-y · Cited by 894
Intrinsic protein disorder in complete genomes.
Dunker, A. K., Zoran Obradovic, A., Romero, P. R., Garner, E. C., & Brown, C. J. (2000) · PubMed · Cited by 661
Self-citation
Implications of macromolecular crowding for protein assembly
Minton, A. P. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00045-7 · Cited by 649

Show all 89 references

Research works printed but not linked: 133

Sigler P. B., 1988, Nature 333, 210−212
Frankel A. D., 1991, Cell 65, 717−719
Romero P., 1997, IEEE Intl. Conf. Neural Networks 1, 90−95
Li X., 1999, Gen. Inform., 10, 40
Romero P., 2001, Funct., Gen. 42, 38−48.
Vucetic S., 2001, Intl
Romero P., 1998, PSB 1998 3, 437−448
Romero P., 1997, Gen. Inform. 8, 110−124
Li X., 2000, Gen. Inform. 11, 172−184
Dunker A. K., 2000, Gen. Inform. 11, 161−171
Dunker A. K., 2001, Nat. Biotech. 19, 805−806
Karush F., 1950, J. Am. Chem. Soc., 72
Meador W. E., 1992, Science 257, 1251−1255
Choo Y., 1998, Nat. Struct. Biol. 5, 253−255
Morar A. S., 2001, Biochemistry 40, 281−285
Flaugh S. L., 2001, Biomacromolecules 2, 538−540
Zurdo J., 1997, Biochemistry 36, 9625−9635
Zurdo J., 2000, Biochemistry 39, 8935−8943
Johansson J., 1998, J. Biol. Chem., 273
Mogridge J., 1998, Mol. Cell 1, 265−275
Legault P., 1998, Cell 93, 289−299
Mol C. D., 2000, Nature 403, 451−456
Chang J. F., 1999, J. Mol. Biol., 288
Yamamoto K., 1999, Mol. Cell. Biol. 19, 8469−8478
Cheng E. H., 1997, Science 278
Chang B. S., 1997, EMBO J., 16
Clem R. J., 1998, Proc. Natl. Acad. Sci. U.S.A. 95, 554−559
Rodi D. J., 1999, J. Mol. Biol., 285
Rodi D. J., 1999, Pacific Symp. Biocomputing 4, 532−541
Fang G., 1998, Cancer Res. 58, 3202−3208
Kissinger C. R., 1995, Nature 378, 641−644
Yang S. A., 2000, Biochemistry 39, 16147−16154
Bhattacharyya J., 1999, J. Biol. Chem., 274
Ostedgaard L. S., 2000, Proc. Natl. Acad. Sci. U.S.A. 97, 5657−5662
Lapthorn A. J., 1994, Nature 369, 455−461
Wu H., 1994, Structure 2, 545−558
Bailey R. W., 2001, Biochemistry 40, 11828−11840
Brandstetter H., 1995, Proc. Natl. Acad. Sci. U.S.A. 92, 9796−9800
Thomas J., 1991, J. Biol. Chem., 266
Knighton D. R., 1991, Science 253, 414−420
Kriwacki R. W., 1996, Proc. Natl. Acad. Sci. U.S.A. 93, 11504−11509
Russo A. A., 1996, Nature 382, 325−331
Evarsson A., 1994, EMBO J., 13
Eom J., 1996, Plant Sci., 115, 24
Ghosh D., 1995, Structure 3, 503−513
Penkett C. J., 1998, Biochemistry 37, 17054−17067
Penkett C. J., 2000, Biochemistry 39, 2887−2893
Samatey F. A., 2001, Nature 410, 331−337
Daughdrill G. W., 1997, Nat. Struct. Biol. 4, 285−291
Daughdrill G. W., 1998, Biochemistry 37, 1076−1082
Fletcher C. M., 1998, Biochemistry, 37, 15
Fletcher C. M., 1998, Protein Sci. 7, 1639−1642
Gingras A. C., 1999, Genes Dev. 13, 1422−1437
Eigenbrot C., 1997, Nat. Struct. Biol. 4, 435−438
Clackson T., 1995, Science 267, 383−386
Holliger P., 1997, Structure 5, 265−275
Coleman D. E., 1994, Science 265, 1405−1412
Coleman D. E., 1999, J. Biol. Chem., 274
Cary P. D., 1980, Eur. J. Biochem., 112
Louie D. F., 2000, Protein Sci. 9, 170−179
Huth J. R., 1997, Nat. Struct. Biol. 4, 657−665
Pierantoni G. M., 2001, Oncogene 20, 6132−6141
Munshi N., 2001, Science 293, 1133−1136
Cary P. D., 1981, Eur. J. Biochem., 119
Nakayama J., 2001, Science 292, 110−113
Ramakrishnan V., 1993, Nature 362, 219−223
Focia P. J., 1998, Biochemistry 37, 15066−15075
Love J. J., 1995, Nature 376, 791−795
Lee C. H., 1996, Cell 85, 931−942
Arold S., 1997, Structure 5, 1361−1372
Arold S. T., 2001, Trends Biochem. Sci. 26, 356−363
Berkovits H. J., 1999, Biochemistry 38, 16826−168230
Brown H. G., 1997, Biochemistry 36, 15035−15040
Hoh J. H., 1998, Proteins 32, 223−228
Zhang M., 1994, Biochem. Cell Biol. 72, 109−116
Grishin N. V., 1999, Biochemistry 38, 15174−15184
Mosyak L., 1995, Nat. Struct. Biol. 2, 537−547
Rao V. D., 1998, Cell 94, 829−839
Grobler J. A., 1996, Nat. Struct. Biol. 3, 788−795
Essen L. O., 1996, Nature 380, 595−602
Lopez Garcia F., 2000, Proc. Natl. Acad. Sci. U.S.A. 97, 8334−8339
Gatewood J. M., 1990, J. Biol. Chem., 265
Gast K., 1995, Biochemistry 34, 13211−13218
McEwan I. J., 1996, Biochemistry 35, 9584−93
Gong W., 1997, Nucleic Acids Res. 25, 2702−2715
Ban N., 1999, Nature 400, 841−847
Tesmer J. J., 1997, Cell 89, 251−261
Moy F. J., 2000, Biochemistry 39, 7063−7073
Chatterjee T. K., 2000, J. Biol. Chem., 275
Choi H. K., 1996, J. Mol. Biol., 262
Kim K. K., 1998, Nature 394, 595−599
Kim R., 1998, Proc. Natl. Acad. Sci. U.S.A. 95, 9129−9133
Fasshauer D., 1997, J. Biol. Chem., 272
Fasshauer D., 1997, J. Biol. Chem., 272
Fasshauer D., 1998, Biochemistry 37, 10354−10362
Sutton R. B., 1998, Nature 395, 347−353
Weinreb P. H., 1996, Biochemistry 35, 13709−13715
Nielsen M. S., 2001, J. Biol. Chem., 18, 18
Labeit S., 1995, Science 270, 293−296
Kellermayer M. S. Z., 1997, Science 276, 1112−1116
Helmes M., 1999, Circ. Res. 84, 1339−1352
Stewart L., 1996, J. Biol. Chem., 271
Shaiu W. L., 1999, Pacific Symp. Biocomput. 4, 578−589
Berger J. M., 1996, Nature 379, 225−232
Caron P. R., 1994, Mol. Cell Biol. 14, 3197−3207
Parraga G., 1988, Science 241, 1489−1492
Klevit R. E., 1990, Proteins 7, 215−226
Hyre D. E., 1998, J. Mol. Biol., 279
Bowers P. M., 1999, Nat. Struct. Biol. 6, 478−485
Campbell K. M., 2000, Biochemistry 39, 2708−2713
John M., 1996, Pept. Res., 9, 78
Glover J. N., 1995, Nature 373, 257−61
Chen L., 1998, Nature, 392, 48
Richards J. P., 1996, J. Biol. Chem., 271
Liu D., 1998, Cell 94, 573−583
Weiss M. A., 1990, Nature 347, 575−578
Chang J., 1995, J. Biol. Chem., 270
Kussie P. H., 1996, Science 274, 948−953
Shen F., 1996, J. Biol. Chem., 271
Uesugi M., 1997, Science 277, 1310−1313
Liu Y., 1999, Genes Dev. 13, 1692−1703
O'Hare P., 1992, Biochemistry 31, 4150−4156
Wilmanns M., 1995, Proc. Natl. Acad. Sci. U.S.A. 92, 11955−11959
Abramson J., 2000, Nat. Struct. Biol. 7, 910−917
Iakoucheva L. M., 2001, Protein Sci. 10, 560−571
Schulz G. E., 1979, Molecular Mechanism of Biological Recognition
Meador W. E., 1993, Science 262, 1718−1721
Pontius B. W., 1993, Trends Biochem. Sci. 18, 181−186
Pappu R. V., 2000, Proc. Natl. Acad. Sci. U.S.A. 97, 12565−12570
Fontana A., 1997, R17−R26.
Hubbard S. J., 1994, Protein Sci. 3, 757−768
Ban N., 2000, Science 289, 905−920
Treiber D. K., 2001, Curr. Opin. Struct. Biol. 11, 309−314

Sorted by citations

Items 901–1,000 of 1,001

Functional Analysis of Kinases and Transcription Factors in Saccharomyces cerevisiae Using an Integrated Overexpression Library
Youn, J., Friesen, H., Ba, A. N. N., Liang, W., Messier, V., Cox, M. J., Moses, A. M., & Andrews, B. (2017) · G3 Genes Genomes Genetics · doi:10.1534/g3.116.038471 · Cited by 26
“…involved in protein–protein interactions (PPIs) (Dunker et al. 2001), protein degradation (Brocca et al. 2009), and post-translational modifications (Dunker et al. 2002), and these functions are mediated by short (2– 10 aa long) linear motifs that are often conserved (Obenauer et al. 2003; Nguyen…”
Background
An Effective Recombinant Protein Expression and Purification System in Saccharomyces cerevisiae
Xie, Y., Han, X., & Miao, Y. (2018) · Current Protocols in Molecular Biology · doi:10.1002/cpmb.62 · Cited by 23
Structural and Dynamical Order of a Disordered Protein: Molecular Insights into Conformational Switching of PAGE4 at the Systems Level
Lin, X., Kulkarni, P., Bocci, F., Schafer, N. P., Roy, S., Tsai, M., He, Y., Chen, Y., Rajagopalan, K., Mooney, S. M., et al. (2019) · Biomolecules · doi:10.3390/biom9020077 · Cited by 23
Intrinsically disordered proteins and phenotypic switching: Implications in cancer
Kulkarni, V., & Kulkarni, P. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.03.013 · Cited by 23
PRISMA and BioID disclose a motifs-based interactome of the intrinsically disordered transcription factor C/EBPα
Ramberger, E., Sapozhnikova, V., Kowenz‐Leutz, E., Zimmermann, K., Nicot, N., Nazarov, P. V., Pérez-Hernández, D., Reimer, U., Mertins, P., Dittmar, G., et al. (2021) · iScience · doi:10.1016/j.isci.2021.102686 · Cited by 24
“These are typical hallmarks of gene regulatory proteins that integrate signal transmission, gene regulation, and epigenetic regulation through promiscuous interactomes (Dunker et al., 2002; Dyson andWright, 2005; Tompa, 2012; Uversky et al., 2005; van der Lee et al., 2014; Ward et al., 2004; Wright and Dyson, 1999).”
Background
How disorder influences order and vice versa – mutual effects in fusion proteins containing an intrinsically disordered and a globular protein
Sambi, I., Gatti‐Lafranconi, P., Longhi, S., & Lotti, M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07825.x · Cited by 23
RVCaB, a Calcium-binding Protein in Radish Vacuoles, is Predominantly an Unstructured Protein with a Polyproline Type II Helix
Ishijima, J., Nagasaki, N., Maeshima, M., & Miyano, M. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvm130 · Cited by 23
Dissecting physical structure of calreticulin, an intrinsically disordered Ca2+-buffering chaperone from endoplasmic reticulum
Migliaccio, A. R., & Uversky, V. N. (2017) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2017.1330224 · Cited by 23
Unraveling the role of the nucleocapsid protein in SARS-CoV-2 pathogenesis: From viral life cycle to vaccine development
El‐Maradny, Y. A., Badawy, M. A., Mohamed, K. I., Ragab, R. F., Moharm, H. M., Abdallah, N. A., Elgammal, E. M., Rubio‐Casillas, A., Uversky, V. N., & Redwan, E. M. M. M. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135201 · Cited by 26
Molecular mechanisms of the anomalous thermal aggregation of green fluorescent protein
Melnik, B. S., Molochkov, N. V., Prokhorov, D. A., Uversky, V. N., & Kutyshenko, V. P. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.07.017 · Cited by 22
Developments and Applications of Coil-Library-Based Residue-Specific Force Fields for Molecular Dynamics Simulations of Peptides and Proteins
Jiang, F., Wu, H., Kang, W., & Wu, Y. (2019) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.8b00794 · Cited by 22
Evolutionary Approach of Intrinsically Disordered CIP/KIP Proteins
Fahmi, M., & Ito, M. (2019) · Scientific Reports · doi:10.1038/s41598-018-37917-5 · Cited by 22
The Effect of Multisite Phosphorylation on the Conformational Properties of Intrinsically Disordered Proteins
Rieloff, E., & Skepö, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011058 · Cited by 21
A mobile loop order–disorder transition modulates the speed of chaperonin cycling
Shewmaker, F. P., Kerner, M. J., Hayer-Hartl, M. K., Klein, G., Georgopoulos, C. P., & Landry, S. J. (2004) · Protein Science · doi:10.1110/ps.04773204 · Cited by 22
A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1
Kennedy, J. A., Daughdrill, G. W., & Schmidt, K. H. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt817 · Cited by 22
Characterization of Essential Domains and Plasticity of the Classical Swine Fever Virus Core Protein
Riedel, C., Lamp, B., Heimann, M., & Rümenapf, T. (2010) · Journal of Virology · doi:10.1128/jvi.00699-10 · Cited by 22
Uncertainty analysis in protein disorder prediction
Ghalwash, M. F., Dunker, A. K., & Zoran Obradovic, A. (2011) · Molecular BioSystems · doi:10.1039/c1mb05373f · Cited by 22
Self-citation
Testing the transferability of a coarse-grained model to intrinsically disordered proteins
Rutter, G. O., Brown, A. H., Quigley, D., Walsh, T. R., & Allen, M. P. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp05652g · Cited by 22
Direct Prediction of NMR Residual Dipolar Couplings from the Primary Sequence of Unfolded Proteins
Huang, J., Ozenne, V., Jensen, M. R., & Blackledge, M. J. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201206585 · Cited by 22
Population genetic structure and natural selection of apical membrane antigen-1 in Plasmodium vivax Korean isolates
Kang, J., Lee, J., Cho, P.-Y., Moon, S.-U., Ju, H., Ahn, S. K., Sohn, W., Lee, H.-W., Kim, T., & Na, B. (2015) · Malaria Journal · doi:10.1186/s12936-015-0942-6 · Cited by 22
Protein dynamics of bovine dentin phosphophoryn
Cross, K. J., Huq, N. L., & Reynolds, E. C. (2005) · Journal of Peptide Research · doi:10.1111/j.1399-3011.2005.00273.x · Cited by 22
Simulation of coupled folding and binding of an intrinsically disordered protein in explicit solvent with metadynamics
Han, M., Xu, J., Ren, Y., & Li, J. (2016) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2016.06.015 · Cited by 22
Circular Dichroism Spectroscopy of Folding in a Protein Monolayer
Keegan, N., Wright, N. G., & Lakey, J. H. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200462977 · Cited by 22
Novel Sensors of the Regulatory Switch on the Regulatory Light Chain of Smooth Muscle Myosin
Mazhari, S. M., Selser, C. T., & Cremo, C. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407062200 · Cited by 22
Time-Resolved FRET Detection of Subtle Temperature-Induced Conformational Biases in Ensembles of α-Synuclein Molecules
Grupi, A., & Haas, E. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.056 · Cited by 21
Secondary Structure and Dynamics of an Intrinsically Unstructured Linker Domain
Olson, K. E., Narayanaswami, P., Vise, P. D., Lowry, D. F., Wold, M. S., & Daughdrill, G. W. (2005) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2005.10507052 · Cited by 21
From sequence to structural analysis in protein phosphorylation motifs
Via, A. (2010) · Frontiers in bioscience · doi:10.2741/3787 · Cited by 21
Anchoring Intrinsically Disordered Proteins to Multiple Targets: Lessons from N-Terminus of the p53 Protein
Huang, Y., & Liu, Z. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12021410 · Cited by 21
Enhanced transcriptional heterogeneity mediated by NF-κB super-enhancers
Wibisana, J. N., Inaba, T., Shinohara, H., Yumoto, N., Hayashi, T., Umeda, M., Ebisawa, M., Nikaido, I., Sako, Y., & Okada, M. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010235 · Cited by 21
“Earlier experimental approaches examined the presence of IDRs in RelA [28].”
Background
Role of C-terminal domain of Mycobacterium tuberculosis PE6 (Rv0335c) protein in host mitochondrial stress and macrophage apoptosis
Medha, M., Priyanka, P., Bhatt, P., Sharma, S., & Sharma, M. (2022) · APOPTOSIS · doi:10.1007/s10495-022-01778-1 · Cited by 21
The N-Terminal Domain of the Drosophila Histone mRNA Binding Protein, SLBP, Is Intrinsically Disordered with Nascent Helical Structure,
Thapar, R., Mueller, G. A., & Marzluff, W. F. (2004) · Biochemistry · doi:10.1021/bi036314r · Cited by 21
Foldamer Structuring by Covalently Bound Macromolecules
Ghosh, K., & Moore, J. S. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2087163 · Cited by 21
Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain
Takahashi, M., Mizuguchi, M., Shinoda, H., Aizawa, T., Demura, M., Okazawa, H., & Kawano, K. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.03.007 · Cited by 21
“Intrinsically unstructured proteins carry out important functions in key biological processes, such as regulation of transcription and signal transduction [24–27].”
BackgroundInfluential
Large‐scale analysis of secondary structure changes in proteins suggests a role for disorder‐to‐order transitions in nucleotide binding proteins
Dan, A. D., Ofran, Y., & Kliger, Y. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22531 · Cited by 20
Back to the Future: Nuclear Magnetic Resonance and Bioinformatics Studies on Intrinsically Disordered Proteins
Dunker, A. K., & Oldfield, C. J. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-20164-1_1 · Cited by 21
Self-citation
Functional correlations of respiratory syncytial virus proteins to intrinsic disorder
Whelan, J. N., Reddy, K. D., Uversky, V. N., & Teng, M. N. (2016) · Molecular BioSystems · doi:10.1039/c6mb00122j · Cited by 22
Analytical methods for structural ensembles and dynamics of intrinsically disordered proteins
Schor, M., Mey, A. S. J. S., & MacPhee, C. E. (2016) · Biophysical Reviews · doi:10.1007/s12551-016-0234-6 · Cited by 21
“However, over the past two decades, it has become clear that many proteins contain long disordered regions or are completely disordered under physiological conditions (Wright and Dyson 2015; Dyson and Wright 2005; Tompa 2005; Dunker et al. 2002; Uversky 2002; Tompa 2011).”
Background
Time, space, and disorder in the expanding proteome universe
Minde, D., Dunker, A. K., & Lilley, K. S. (2017) · PROTEOMICS · doi:10.1002/pmic.201600399 · Cited by 21
Self-citation
The rheumatic disease-associated FAM167A-BLK locus encodes DIORA-1, a novel disordered protein expressed highly in bronchial epithelium and alveolar macrophages
Mentlein, L., Thorlacius, G. E., Meneghel, L., Aqrawi, L. A., Sepúlveda, J. I. R., Grünewald, J., Espinosa, A., & Wahren‐Herlenius, M. (2018) · Clinical & Experimental Immunology · doi:10.1111/cei.13138 · Cited by 21
Heme interaction of the intrinsically disordered N-terminal peptide segment of human cystathionine-β-synthase
Kumar, A., Wißbrock, A., Goradia, N., Bellstedt, P., Ramachandran, R., Imhof, D., & Ohlenschläger, O. (2018) · Scientific Reports · doi:10.1038/s41598-018-20841-z · Cited by 21
Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins
Anbo, H., Sato, M., Okoshi, A., & Fukuchi, S. (2019) · Biomolecules · doi:10.3390/biom9030088 · Cited by 20
Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder
Hong, S., Choi, S., Kim, R., & Koh, J. (2020) · Molecules and Cells · doi:10.14348/molcells.2020.0186 · Cited by 23
Intrinsic Disorder is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes
Haynes, C. A., Oldfield, C. J., Ji, F., Klitgord, N., Cusick, M. E., Predrag Radivojac, A., Uversky, V. N., Vidal, M., & Iakoucheva, L. M. (2005) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0020100.eor · Cited by 20
Self-citation
Prediction of natively unfolded regions in protein chains
Galzitskaya, O. V., Garbuzynskiy, S. O., & Lobanov, M. Y. (2006) · Molecular Biology · doi:10.1134/s0026893306020166 · Cited by 21
STABILITY OF INTERCELLULAR EXCHANGE OF BIOCHEMICAL SUBSTANCES AFFECTED BY VARIABILITY OF ENVIRONMENTAL PARAMETERS
MIHAILOVIĆ, D. T., BUDINČEVIĆ, M., Balaž, I., & MIHAILOVIĆ, A. (2011) · Modern Physics Letters B · doi:10.1142/s0217984911027431 · Cited by 20
Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins
Borcherds, W. M., & Daughdrill, G. W. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.09.011 · Cited by 20
Oxidation of proteins
Heinonen, M., Gürbüz, G., & Ertbjerg, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-817380-0.00003-8 · Cited by 21
Development and Validation of AMBER-FB15-Compatible Force Field Parameters for Phosphorylated Amino Acids
Stoppelman, J. P., Ng, T. T., Nerenberg, P. S., & Wang, L. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c07547 · Cited by 18
Encoding and decoding NF-κB nuclear dynamics
Wibisana, J. N., & Okada, M. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.102103 · Cited by 22
A Unifying Theory
Fantini, J., & Yahi, N. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800111-0.00013-8 · Cited by 21
Novel mechanistic concept of platelet inhibition
Sigalov, A. B. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.6.677 · Cited by 20
Homodimerization propensity of the intrinsically disordered N-terminal domain of Ultraspiracle from Aedes aegypti
Pieprzyk, J., Zbela, A., Jakób, M., Ożyhar, A., & Orłowski, M. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.03.010 · Cited by 20
Phosphorylation in intrinsically disordered regions regulates the activity of Neurogenin2
McDowell, G. S., Hindley, C. J., Lippens, G. M., Landrieu, I., & Philpott, A. (2014) · BMC Biochemistry · doi:10.1186/s12858-014-0024-3 · Cited by 20
Bayesian statistical modelling of human protein interaction network incorporating protein disorder information
Bulashevska, S., Bulashevska, A., & Eils, R. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-46 · Cited by 19
The DEAD-Box Protein CYT-19 Uses Arginine Residues in Its C‑Tail To Tether RNA Substrates
Busa, V. F., Rector, M. J., & Russell, R. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00362 · Cited by 20
Discovery of Cryoprotective Activity in Human Genome-Derived Intrinsically Disordered Proteins
Matsuo, N., Goda, N., Shimizu, K., Fukuchi, S., Ota, M., & Hiroaki, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020401 · Cited by 20
Fesselin is a Natively Unfolded Protein
Khaymina, S. S., Kenney, J. M., Schroeter, M. M., & Chalovich, J. M. (2007) · Journal of Proteome Research · doi:10.1021/pr070237v · Cited by 20
Estimation of Position Specific Energy as a Feature of Protein Residues from Sequence Alone for Structural Classification
Iqbal, S., & Hoque, M. T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0161452 · Cited by 20
Designed Mutations Alter the Binding Pathways of an Intrinsically Disordered Protein
Wu, D., & Zhou, H. (2019) · Scientific Reports · doi:10.1038/s41598-019-42717-6 · Cited by 19
NMR of unfolded proteins
Chatterjee, A., Kumar, A., Chugh, J., Srivastava, S., Bhavesh, N. S., & Hosur, R. V. (2005) · Journal of Chemical Sciences · doi:10.1007/bf02704356 · Cited by 20
NMR Studies on the Substrate-binding Domains of the Thermosome: Structural Plasticity in the Protrusion Region
Heller, M., John, M., Coles, M. P., Bosch, G., Baumeister, W. P., & Kessler, H. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.12.035 · Cited by 20
Predicting the Energetics of Conformational Fluctuations in Proteins from Sequence: A Strategy for Profiling the Proteome
Gu, J., & Hilser, V. J. (2008) · Structure · doi:10.1016/j.str.2008.08.016 · Cited by 20
‘Intelligent’ proteins
Tripathi, T., Uversky, V. N., & Giuliani, A. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05770-1 · Cited by 21
Conformational Ensembles of an Intrinsically Disordered Protein pKID with and without a KIX Domain in Explicit Solvent Investigated by All-Atom Multicanonical Molecular Dynamics
Umezawa, K., Ikebe, J., Takano, M., Nakamura, H., & Higo, J. (2012) · Biomolecules · doi:10.3390/biom2010104 · Cited by 19
Integrating disorder in globular multidomain proteins: Fuzzy sensors and the role of SH3 domains
Arbesú, M., & Pons, M. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108161 · Cited by 19
Taurine Induces an Ordered but Functionally Inactive Conformation in Intrinsically Disordered Casein Proteins
Bhat, M. Y., Singh, L. R., & Dar, T. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-60430-7 · Cited by 19
Characterization of the Connexin45 Carboxyl-Terminal Domain Structure and Interactions with Molecular Partners
Kopanic, J. L., Al‐Mugotir, M., Kieken, F., Zach, S., Trease, A. J., & Sorgen, P. L. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.03.045 · Cited by 19
Direct Observations of Conformational Distributions of Intrinsically Disordered p53 Peptides Using UV Raman and Explicit Solvent Simulations
Xiong, K., Zwier, M. C., Myshakina, N. S., Burger, V., Asher, S. A., & Chong, L. T. (2011) · The Journal of Physical Chemistry A · doi:10.1021/jp112235d · Cited by 19
C-terminal acidic domain of ubiquitin-conjugating enzymes: A multi-functional conserved intrinsically disordered domain in family 3 of E2 enzymes
Arrigoni, A., Grillo, B., Vitriolo, A., GIOIA, L. D., & Papaleo, E. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.04.003 · Cited by 19
Genome-Wide Survey of Natural Selection on Functional, Structural, and Network Properties of Polymorphic Sites in Saccharomyces paradoxus
Vishnoi, A., Sethupathy, P., Simola, D. F., Plotkin, J. B., & Hannenhalli, S. S. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msr085 · Cited by 22
Intrinsic disorder of the bacterial cell division protein ZipA: coil‐to‐brush conformational transition
López‐Montero, I., López‐Navajas, P., Mingorance, J., Rivas, G., Vélez, M., Vicente, M., & Monroy, F. (2013) · The FASEB Journal · doi:10.1096/fj.12-224337 · Cited by 19
Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4
Hibino, E., Inoue, R., Sugiyama, M., Kuwahara, J., Matsuzaki, K., & Hoshino, M. (2016) · Protein Science · doi:10.1002/pro.3013 · Cited by 19
Protein/Peptide Aggregation and Amyloidosis on Biointerfaces
Lu, Q., Tang, Q., Xiong, Y., Qing, G., & Sun, T. (2016) · Materials · doi:10.3390/ma9090740 · Cited by 19
Structural Characterization of the SMRT Corepressor Interacting with Histone Deacetylase 7
Desravines, D. C., Martin, I. S., Schneider, R., Mas, P. J., Aleksandrova, N., Jensen, M. R., Blackledge, M. J., & Hart, D. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-03718-5 · Cited by 19
Intrinsic Disorder in Proteins Associated with Neurodegenerative Diseases
Uversky, V. N. (2008) · Focus on structural biology · doi:10.1007/978-1-4020-9434-7_2 · Cited by 20
TransDFL: Identification of Disordered Flexible Linkers in Proteins by Transfer Learning
Pang, Y., & Liu, B. (2022) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2022.10.004 · Cited by 18
“DFLs serve as the linkers in multidomain proteins characterized by extremely structural ﬂexibility, and can be located between inter-and intra-domain, which are different from generic linkers [5,7– 10].”
Background
Crystal structure of the tetrameric inositol 1‐phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima
Stieglitz, K. A., Roberts, M. F., Li, W., & Stec, B. (2007) · FEBS Journal · doi:10.1111/j.0014-2956.2007.05779.x · Cited by 19
Caprice/ MISP is a novel F ‐actin bundling protein critical for actin‐based cytoskeletal reorganizations
Kumeta, M., Gilmore, J. L., Umeshima, H., Ishikawa, M.-A., Kitajiri, S., Horigome, T., Kengaku, M., & Takeyasu, K. (2014) · Genes to Cells · doi:10.1111/gtc.12131 · Cited by 19
“Recent studies have revealed the disordered regions as active sites for adaptive molecular interactions, rather than only serving as a spacer among rigid domains (Dunker et al. 2002).”
Background
Monitoring the conformational changes of an intrinsically disordered peptide using a quartz crystal microbalance
Shur, O., Wu, J., Cropek, D. M., & Banta, S. A. (2011) · Protein Science · doi:10.1002/pro.625 · Cited by 19
Thermodynamics of Conformational Transitions in a Disordered Protein Backbone Model
Drake, J. A., & Pettitt, B. M. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.04.027 · Cited by 19
Molecular and in silico analyses validates pathogenicity of homozygous mutations in the NPR2 gene underlying variable phenotypes of Acromesomelic dysplasia, type Maroteaux
Irfanullah, I., Zeb, A., Shinwari, N., Shah, K., Gilani, S. Z. T., Khan, S., Lee, K. W., Raza, S. I., Hussain, S., Liaqat, K., et al. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.07.004 · Cited by 19
Efficient expression of isotopically labeled peptides for high resolution NMR studies: Application to the Cdc42/Rac binding domains of virulent kinases in Candida albicans *
Osborne, M. J., Su, Z., Sridaran, V., & Ni, F. (2003) · Journal of Biomolecular NMR · doi:10.1023/a:1024043620972 · Cited by 19
According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of a protein. Is this correct?
Dyson, H. J., & Wright, P. E. (2006) · IUBMB Life · doi:10.1080/15216540500484376 · Cited by 19
Structured proteins and proteins with intrinsic disorder
Serdyuk, I. N. (2007) · Molecular Biology · doi:10.1134/s0026893307020082 · Cited by 19
Expression and properties of the recombinant murine Golli‐myelin basic protein isoform J37
Kaur, J., Libich, D. S., Campagnoni, C. W., Wood, D. D., Moscarello, M. A., Campagnoni, A. T., & Harauz, G. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10547 · Cited by 19
Novel Enzymes Through Design and Evolution
Woycechowsky, K. J., Vamvaca, K., & Hilvert, D. (2010) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780471224464.ch4 · Cited by 19
Towards understanding the crosstalk between protein post‐translational modifications: Homo‐ and heterotypic PTM pair distances on protein surfaces are not random
Korkuć, P., & Walther, D. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25200 · Cited by 19
Bridging the Molecular-Cellular Gap in Understanding Ion Channel Clustering
Nirenberg, V. A., & Yifrach, O. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01644 · Cited by 18
New genotypes of Helicobacter Pylori VacA d-region identified from global strains
Soyfoo, M. D., Doomah, Y. H., Xu, D. H., Zhang, C., Sang, H., Liu, Y.-Y., Zhang, G., Jiang, J., & Xu, S. (2021) · BMC Molecular and Cell Biology · doi:10.1186/s12860-020-00338-2 · Cited by 18
Mechanism of Ligand-Induced Folding of a Natively Unfolded Helixless Variant of Rabbit I-BABP
Rea, A. M., Thurston, V., & Searle, M. S. (2009) · Biochemistry · doi:10.1021/bi900805s · Cited by 18
“In many cases, it has been observed that the folding of the natively unstructured polypeptide chain, or a partially structured state, is coupled to a ligand binding event (4).”
Background
Degradation of gap junction connexins is regulated by the interaction with Cx43-interacting protein of 75 kDa (CIP75)
Kopanic, J. L., Schlingmann, B., Koval, M. H., Lau, A. F., Sorgen, P. L., & Su, V. (2015) · Biochemical Journal · doi:10.1042/bj20141042 · Cited by 18
“An intrinsically disordered connexin CT domain would be ideal for cell signalling events by allowing many different binding partners with both high specificity and low affinity to rapidly switch between molecular partners, thereby activating alternative signalling pathways [15,16].”
Background
Intrinsically disordered proteins: structural and functional dynamics
Wallin, S. (2017) · Research and Reports in Biology · doi:10.2147/rrb.s57282 · Cited by 19
Intrinsically Disordered Proteins as Important Players during Desiccation Stress of Soybean Radicles
Liu, Y., Wu, J., Sun, N., Tu, C., Shi, X., Cheng, H., Liu, S., Li, S., Wang, Y., Zheng, Y., et al. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b01045 · Cited by 17
Formation of Heterotypic Amyloids: α‐Synuclein in Co‐Aggregation
Bhasne, K., & Mukhopadhyay, S. (2018) · PROTEOMICS · doi:10.1002/pmic.201800059 · Cited by 17
The Hypervariable Region of K-Ras4B Governs Molecular Recognition and Function
Abdelkarim, H., Banerjee, A., Grudzien, P. K., Leschinsky, N., Abushaer, M., & Gaponenko, V. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225718 · Cited by 18
The exquisite structural biophysics of the Golgi Reassembly and Stacking Proteins
Mendes, L. F. S., Fontana, N. A., Reddy, S. T., Uversky, V. N., & Costa-Filho, A. J. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.08.203 · Cited by 15
Functions of intrinsically disordered proteins through evolutionary lenses
Pajkos, M., & Dosztányi, Z. (2021) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2021.06.017 · Cited by 19
Self-assembling layers created by membrane proteins on gold
Shah, D. S. H., Thomas, M. B., Phillips, S. R., Cisneros, D. A., Brun, A. P. L., Holt, S. A., & Lakey, J. H. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350522 · Cited by 18
Physiological and genetical adaptation to temperature in fish populations
Colosimo, A., Giuliani, A., Maranghi, F., Brix, O., Thorkildsen, S., Fischer, T., Knust, R., & Pörtner, H. (2003) · Continental Shelf Research · doi:10.1016/j.csr.2003.06.012 · Cited by 18
Structural studies of human Naked2: A biologically active intrinsically unstructured protein
Hu, T., Krezel, A. M., Li, C., & Coffey, R. J. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.09.121 · Cited by 18

Authors: Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z.
Affiliations: Washington State University (US)
School of Molecular Biosciences, Washington State University, Pullman, Washington 99164 and Center for Information Science and Technology, Temple University, Philadelphia, Pennsylvania 19122
Corresponding author: Dunker, A. Keith
ORCID: Dunker, A. Keith
Brown, Celeste J.
Lawson, J. David
Iakoucheva, Lilia M.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2002-05-01
Volume: 41
Issue: 21
Pages: 6573-6582
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi012159+
OpenAlex: W2073745520
Cited by: 1,731
References: 89
Citations by year: 2026: 16 · 2025: 33 · 2024: 40 · 2023: 39 · 2022: 64 · 2021: 52 · 2020: 70 · 2019: 71 · 2018: 60 · 2017: 69 · 2016: 89 · 2015: 78 · 2014: 97 · 2013: 96 · 2012: 109
FWCI: 25.50
Type: journal article
Language: en
Open access: closed
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. National Library of Medicine (1R01-LM06916, R01LM006916)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Keywords: intrinsic disorder, protein function, random coil, molten globule, protein structure-function relationship, native proteins, limited proteolysis, circular dichroism, nuclear magnetic resonance
MeSH terms: Apoproteins, Cytochrome c Group, DNA Helicases, Glycoproteins, Proteins, Structure-Activity Relationship, Molecular Structure, Protein Folding, Molecular Chaperones, Computational Biology, Cytochromes c, Clusterin

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Intrinsic Disorder and Protein Function

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks