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
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
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Many IDPs/IDRs are capable of at least partial ordering upon interaction with specific partners [7–18].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [9]
Citations
Cites
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-citationCoupling 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
Jeffery, C. J. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01335-8 · Cited by 1,016
Yamamoto, K., Ichijo, H., & Korsmeyer, S. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8469 · Cited by 1,003
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-citationImplications 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
Flagged first, then by citations
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
Cited by
Sorted by citations
Items 601–700 of 1,001
Gupta, M. N., & Uversky, V. N. (2024) · Protein Science · doi:10.1002/pro.4968 · Cited by 51
Wu, Z., Hu, G., Yang, J., Peng, Z., Uversky, V. N., & Kurgan, L. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.08.014 · Cited by 49
Intrinsically Disordered Proteins in a Physics-Based World
Click, T. H., Ganguly, D., & Chen, J. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11125292 · Cited by 49
Xue, B., Dunker, A. K., & Uversky, V. N. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11103725 · Cited by 48
Self-citationA biological perspective on the structure and function of caseins and casein micelles
Smyth, E., CLEGG, R. A., & Holt, C. (2004) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.2004.00141.x · Cited by 48
Ikeda, T., Ninomiya, K.-I., Hirota, R., & Kuroda, A. (2009) · Protein Expression and Purification · doi:10.1016/j.pep.2009.12.009 · Cited by 50
DNA-Based Nanodevices Controlled by Purely Entropic Linker Domains
Mariottini, D., Idili, A., Nijenhuis, M. A. D., de Greef, T. F. A., & Ricci, F. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b07640 · Cited by 48
Identifying Disordered Regions in Proteins by Limited Proteolysis
Fontana, A., de Laureto, P. P., Spolaore, B., & Frare, E. (2012) · Methods in molecular biology · doi:10.1007/978-1-4614-3704-8_20 · Cited by 48
Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma
Kulkarni, P., Leite, V. B. P., Roy, S., Bhattacharyya, S., Mohanty, A. R., Achuthan, S., Singh, D., Appadurai, R., Govindan Rangarajan, C., Weninger, K., et al. (2022) · Biophysics Reviews · doi:10.1063/5.0080512 · Cited by 49
Nelson, W. D., Blakely, S. E., Nesmelov, Y. E., & Thomas, D. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401664102 · Cited by 47
Group 3 LEA protein model peptides protect liposomes during desiccation
Furuki, T., & Sakurai, M. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.07.009 · Cited by 47
Energetic Basis of Uncoupling Folding from Binding for an Intrinsically Disordered Protein
Drobnak, I., Jonge, N. D., Haesaerts, S., Vesnaver, G., Loris, R., & Lah, J. (2013) · Journal of the American Chemical Society · doi:10.1021/ja305081b · Cited by 49
Local Flexibility in Molecular Function Paradigm
Bhalla, J., Storchan, G. B., MacCarthy, C. M., Uversky, V. N., & Tcherkasskaya, O. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500315-mcp200 · Cited by 46
svm PRAT: SVM-based Protein Residue Annotation Toolkit
Rangwala, H., Kauffman, C., & Karypis, G. (2009) · BMC Bioinformatics · doi:10.1186/1471-2105-10-439 · Cited by 47
Thermo-resistant intrinsically disordered proteins are efficient 20S proteasome substrates
Tsvetkov, P., Myers, N., Moscovitz, O., Sharon, M., Prilusky, J., & Shaul, Y. (2011) · Molecular BioSystems · doi:10.1039/c1mb05283g · Cited by 47
Zambelli, B., Cremades, N., Neyroz, P., Turano, P., Uversky, V. N., & Ciurli, S. (2011) · Molecular BioSystems · doi:10.1039/c1mb05227f · Cited by 47
HIV Vaccine Mystery and Viral Shell Disorder
Goh, G. K., Dunker, A. K., Foster, J. A., & Uversky, V. N. (2019) · Biomolecules · doi:10.3390/biom9050178 · Cited by 48
“Similar failures to obtain antibodies against the host-targeting proteins have been observed for several pathogens not counting the three viral examples discussed herein, suggesting that the evolution and utilization of disorder-to-order transitions for binding to host targets may be a strategy commonly used by pathog…”
BackgroundSelf-citationIntroduction to intrinsically disordered proteins and regions
Oldfield, C. J., Uversky, V. N., Dunker, A. K., & Kurgan, L. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816348-1.00001-6 · Cited by 53
Self-citationSolution Structure and Heparin Interaction of Human Hepatoma-derived Growth Factor
Sue, S., Chen, J.-Y., Lee, S., Wu, W.-G., & Huang, T.-H. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.09.014 · Cited by 47
Influence of Sequence Changes and Environment on Intrinsically Disordered Proteins
Mohan, A., Uversky, V. N., & Predrag Radivojac, A. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000497 · Cited by 50
Bovine Viral Diarrhea Virus Core Is an Intrinsically Disordered Protein That Binds RNA
Murray, C. L., Marcotrigiano, J., & Rice, C. M. (2007) · Journal of Virology · doi:10.1128/jvi.01815-07 · Cited by 47
Folkers, G. E., van Buuren, B. N. M., & Kaptein, R. (2004) · Journal of Structural and Functional Genomics · doi:10.1023/b:jsfg.0000029200.66197.0c · Cited by 47
Conversation of Intrinsic Disorder in Protein Domains and Families
Chen, J. W. (2005) · IUScholarWorks (Indiana University) · doi:10.7912/c2/819 · Cited by 47
Buchko, G. W., Niemann, G., Baker, E. S., Belov, M. E., Smith, R. D., Heffron, F., Adkins, J., & McDermott, J. (2010) · Molecular BioSystems · doi:10.1039/c0mb00097c · Cited by 46
SOD1‐associated ALS: A promising system for elucidating the origin of protein‐misfolding disease
Nordlund, A., & Oliveberg, M. (2008) · HFSP journal · doi:10.2976/1.2995726 · Cited by 48
Conformational changes in redox pairs of protein structures
Fan, S. W., George, R. A., Haworth, N. L., Feng, L. L., Liu, J. Y., & Wouters, M. A. (2009) · Protein Science · doi:10.1002/pro.175 · Cited by 46
Adler, J., Reuven, N. B., Kahana, C., & Shaul, Y. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00899-09 · Cited by 46
Valsecchi, I., Crilat, E., Maldiney, R., Habricot, Y., Lignon, S., Lebrun, R., Miginiac, É., Ruelland, É., Jeannette, E., & Lebreton, S. (2013) · Molecular BioSystems · doi:10.1039/c3mb70128j · Cited by 46
Sun, X., Greenwood, D. R., Templeton, M. D., Libich, D. S., McGhie, T. K., Xue, B., Yoon, M., Cui, W., Kirk, C. A., Jones, W. T., et al. (2014) · FEBS Journal · doi:10.1111/febs.12937 · Cited by 46
Heterotrimeric G protein signaling via GIV/Girdin: Breaking the rules of engagement, space, and time
Aznar, N., Kalogriopoulos, N. A., Midde, K., & Ghosh, P. (2016) · BioEssays · doi:10.1002/bies.201500133 · Cited by 43
Dehydrins: Molecular Biology, Structure and Function
Eriksson, S. K., & Harryson, P. (2011) · Ecological studies · doi:10.1007/978-3-642-19106-0_14 · Cited by 47
“proteins that lack a fixed 3D structure under physiological conditions ( Dunker et al. 2002 ; F ink2005; Uversky et al. 2005).”
BackgroundSelection and Slippage Creating Serine Homopolymers
Huntley, M. A., & Golding, G. B. (2006) · Molecular Biology and Evolution · doi:10.1093/molbev/msl073 · Cited by 46
Gazi, A. D., Charova, S. N., Panopoulos, N. J., & Kokkinidis, M. (2009) · Cellular Microbiology · doi:10.1111/j.1462-5822.2009.01297.x · Cited by 45
Phosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein
Chin, A. F., Toptygin, D. D., Elam, W. A., Schrank, T. P., & Hilser, V. J. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.12.013 · Cited by 43
Choice of Force Field for Proteins Containing Structured and Intrinsically Disordered Regions
Zapletal, V., Mládek, A., Melková, K., Louša, P., Nomilner, E., Jaseňáková, Z., Kubáň, V., Makovická, M., Laníková, A., Žı́dek, L., et al. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.02.019 · Cited by 45
Single-Molecule Dynamics Reveals Cooperative Binding-Folding in Protein Recognition
Wang, J., Lu, Q., & Lu, H. P. (2006) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0020078 · Cited by 45
The YoeB Toxin Is a Folded Protein That Forms a Physical Complex with the Unfolded YefM Antitoxin
Cherny, I., Rockah-Shmuel, L., & Gazit, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506220200 · Cited by 45
Prediction of Protein Cleavage Site with Feature Selection by Random Forest
Li, B., Cai, Y., Feng, K., & Zhao, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045854 · Cited by 45
Meirelles, G. V., Lanza, D. C. F., da Silva, J. C., Bernachi, J. S., Leme, A. F. P., & Kobarg, J. (2010) · Journal of Proteome Research · doi:10.1021/pr100562w · Cited by 46
Hu, D., Qin, Z., Xue, B., Fink, A. L., & Uversky, V. N. (2008) · Biochemistry · doi:10.1021/bi800806d · Cited by 44
Conformational Flexibility of α-Lactalbumin Related to its Membrane Binding Capacity
Halskau, Ø., Underhaug, J., Frøystein, N. Å., & Martı́nez, A. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.04.020 · Cited by 44
The calpain‐system of Drosophila melanogaster: coming of age
Friedrich, P., Tompa, P., & Farkas, A. E. (2004) · BioEssays · doi:10.1002/bies.20106 · Cited by 44
Huang, K.-L., Chadee, A. B., Chen, C. A., Zhang, Y., & Shyu, A. (2013) · RNA · doi:10.1261/rna.037317.112 · Cited by 44
Prediction of Intrinsic Disorder and Its Use in Functional Proteomics
Uversky, V. N., Predrag Radivojac, A., Iakoucheva, L. M., Zoran Obradovic, A., & Dunker, A. K. (2007) · Methods in molecular biology · doi:10.1007/978-1-59745-547-3_5 · Cited by 47
Self-citationMulti-chain immune recognition receptors: spatial organization and signal transduction
Sigalov, A. B. (2004) · Seminars in Immunology · doi:10.1016/j.smim.2004.09.003 · Cited by 44
Nanoimaging for protein misfolding and related diseases
Lyubchenko, Y. L., Sherman, S., Shlyakhtenko, L. S., & Uversky, V. N. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20989 · Cited by 43
Conformational Dynamics of the Partially Disordered Yeast Transcription Factor GCN4
Robustelli, P., Trbovic, N., Friesner, R. A., & Palmer, A. G. I. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct400654r · Cited by 46
Paddock, C. M., Lytle, B. L., Peterson, F. C., Holyst, T., Newman, P. J., Volkman, B. F., & Newman, D. K. (2011) · Blood · doi:10.1182/blood-2010-11-317867 · Cited by 43
Comparative Genomics and Disorder Prediction Identify Biologically Relevant SH3 Protein Interactions
Beltrão, P., & Serrano, L. G. (2005) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0010026 · Cited by 43
Gazi, A. D., Bastaki, M. N., Charova, S. N., Gkougkoulia, E. A., Kapellios, E. A., Panopoulos, N. J., & Kokkinidis, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803408200 · Cited by 43
Popelka, H., Uversky, V. N., & Klionsky, D. J. (2014) · Autophagy · doi:10.4161/auto.28616 · Cited by 41
Agnati, L. F., Leo, G., Genedani, S., Andreoli, N., Marcellino, D. J., Woods, A. S., Piron, L., Guidolin, D., & Fuxé, K. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2007.10.003 · Cited by 43
Dominant Kinetic Paths on Biomolecular Binding-Folding Energy Landscape
Wang, J., Zhang, K., Lu, H., & Wang, E. (2006) · Physical Review Letters · doi:10.1103/physrevlett.96.168101 · Cited by 42
p25α is flexible but natively folded and binds tubulin with oligomeric stoichiometry
Otzen, D. E., Lundvig, D. M. S., Wimmer, R., Nielsen, L. H., Pedersen, J. R., & Jensen, P. H. (2005) · Protein Science · doi:10.1110/ps.041285605 · Cited by 43
On the properties and sequence context of structurally ambivalent fragments in proteins
Kuznetsov, I. B., & Rackovsky, S. R. (2003) · Protein Science · doi:10.1110/ps.03209703 · Cited by 43
Occupancy of chromatin organizers in the Epstein–Barr virus genome
Holdorf, M. M., Cooper, S., Yamamoto, K. R., & Miranda, J. L. (2011) · Virology · doi:10.1016/j.virol.2011.04.004 · Cited by 42
Occurrence of disordered patterns and homorepeats in eukaryotic and bacterial proteomes
Lobanov, M. Y., & Galzitskaya, O. V. (2011) · Molecular BioSystems · doi:10.1039/c1mb05318c · Cited by 42
Mosaic, self-similarity logic and biological attraction principles
Agnati, L. F., Baluška, F., Barlow, P. W., & Guidolin, D. (2009) · Communicative & Integrative Biology · doi:10.4161/cib.2.6.9644 · Cited by 41
Correlations between predicted protein disorder and post-translational modifications in plants
Kurotani, A., Tokmakov, A. A., Kuroda, Y., Fukami, Y., Shinozaki, K., & Sakurai, T. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btt762 · Cited by 45
“The proteins with IDRs are also widespread in plant proteomes with the overall proteome disorder content in different plant species being typical for other eukaryotes (Dunker et al., 2001; Fukuchi et al., 2011; Xue et al., 2012).”
BackgroundInfluentialLocal control of a disorder–order transition in 4E-BP1 underpins regulation of translation via eIF4E
Tait, S., Dutta, K., Cowburn, D., Warwicker, J., Doig, A. J., & McCarthy, J. E. G. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008242107 · Cited by 42
Cordeiro, T. N., Chen, P., Biasio, A. D., Sibille, N., Blanco, F. J., Hub, J. S., Crehuet, R., & Bernadó, P. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1183 · Cited by 41
Advances in studying protein disorder with solid-state NMR
Siemer, A. B. (2020) · Solid State Nuclear Magnetic Resonance · doi:10.1016/j.ssnmr.2020.101643 · Cited by 41
Testa, L., Brocca, S., Santambrogio, C., D’Urzo, A., Habchi, J., Longhi, S., Uversky, V. N., & Grandori, R. (2013) · Intrinsically Disordered Proteins · doi:10.4161/idp.25068 · Cited by 43
Uversky, V. N. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-20164-1_7 · Cited by 42
Zbilut, J. P., Colosimo, A., Conti, F., Colafranceschi, M., Manetti, C., Valerio, M., Webber, C. L., & Giuliani, A. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74774-2 · Cited by 42
“Group E proteins come from the Dunker list of natively unfolded systems (Dunker et al., 2002).”
BackgroundMethodYamamoto, M. P. (2004) · Springer eBooks · doi:10.1007/978-3-662-10360-9_19 · Cited by 41
Multivalent IDP assemblies: Unique properties of LC8‐associated, IDP duplex scaffolds
Clark, S. A., Jespersen, N. E., Woodward, C. K., & Barbar, E. J. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.07.032 · Cited by 43
Johnson, D. E., Xue, B., Sickmeier, M. D., Meng, J., Cortese, M. S., Oldfield, C. J., LeGall, T., Dunker, A. K., & Uversky, V. N. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.05.013 · Cited by 41
Self-citationModulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements
Picotti, P., Marabotti, A., Negro, A., Musi, V., Spolaore, B., Zambonin, M., & Fontana, A. (2004) · Protein Science · doi:10.1110/ps.04635304 · Cited by 44
Ribeiro, M. D. L. C., Espinosa, J., Islam, S., Martinez, O., Thanki, J. J., Mazariegos, S., Nguyen, T., Larina, M., Xue, B., & Uversky, V. N. (2013) · PeerJ · doi:10.7717/peerj.2 · Cited by 41
The polyserine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization
Wolf, A., Mantri, M., Heim, A., Müller, U., Fichter, E., Mackeen, M. M., Schermelleh, L., Dadie, G., Leonhardt, H., Vénien‐Bryan, C., et al. (2013) · Biochemical Journal · doi:10.1042/bj20130529 · Cited by 41
Prediction of Tyrosine Sulfation with mRMR Feature Selection and Analysis
Niu, S., Huang, T., Feng, K., Cai, Y., & Li, Y. (2010) · Journal of Proteome Research · doi:10.1021/pr1007152 · Cited by 41
A Clostridium difficile -Specific, Gel-Forming Protein Required for Optimal Spore Germination
Donnelly, M. L., Li, W., Li, Y.-Q., Hinkel, L. A., Setlow, P., & Shen, A. (2017) · mBio · doi:10.1128/mbio.02085-16 · Cited by 41
Structural Characterization of Highly Flexible Proteins by Small-Angle Scattering
Cordeiro, T. N., Herranz-Trillo, F., Urbanek, A., Estaña, A., Cortés, J., Sibille, N., & Bernadó, P. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6038-0_7 · Cited by 39
The inactivating factor of glutamine synthetase, IF7, is a “natively unfolded” protein
Muro‐Pastor, M. I., Barrera, F. N., Reyes, J. C., Florencio, F. J., & Neira, J. L. (2003) · Protein Science · doi:10.1110/ps.0303203 · Cited by 41
Guida, V., Ferese, R., Rocchetti, M., Bonetti, M., Sárközy, A., Cecchetti, S., Gelmetti, V., Lepri, F. R., Copetti, M., Lamorte, G., et al. (2012) · European Journal of Human Genetics · doi:10.1038/ejhg.2012.109 · Cited by 41
Duvignaud, J., Savard, C., Fromentin, R., Majeau, N., Leclerc, D., & Gagné, S. M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.141 · Cited by 41
“from PONDR is indicated by a D [14].”
BackgroundMethodFast folding of a helical protein initiated by the collision of unstructured chains
Meisner, W. K., & Sosnick, T. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404057101 · Cited by 41
Liu, X., & Chen, J. (2019) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.9b00397 · Cited by 40
Proteasome Activation to Combat Proteotoxicity
Jones, C. L., & Tepe, J. J. (2019) · Molecules · doi:10.3390/molecules24152841 · Cited by 43
“The development of Dunker and co-workers original 28 functions of IDPs [59] has resulted in 6 distinct IDP and intrinsically disordered protein region (IDPR) functions being in common usage [56].”
BackgroundIntrinsically disordered proteins: Chronology of a discovery
Uversky, V. N., & Kulkarni, P. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106694 · Cited by 44
MacRaild, C. A., Zachrdla, M., Andrew, D. W., Krishnarjuna, B., Nováček, J., Žı́dek, L., Sklenář, V., Richards, J. S., Beeson, J. G., Anders, R. F., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119899 · Cited by 40
Length of tandem repeats in fibrin’s αC region correlates with fiber extensibility
Falvo, M. R., Millard, D. C., O'Brien, E. T., Superfine, R., & Lord, S. T. (2008) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2008.03147.x · Cited by 40
Tomar, S., Narwal, M., Harms, E., Smith, J. L., & Kuhn, R. J. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.05.022 · Cited by 40
Digestive versus regulatory proteases: on calpain action in vivo
Friedrich, P., & Bozóky, Z. (2005) · Biological Chemistry · doi:10.1515/bc.2005.071 · Cited by 40
Secretory Granule to the Nucleus
Rajagopal, C., Stone, K. L., Francone, V. P., Mains, R. E., & Eipper, B. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035782 · Cited by 40
Cheng, H., Li, J., Fazlieva, R., Dai, Z., Bu, Z., & Röder, H. (2009) · Structure · doi:10.1016/j.str.2009.03.009 · Cited by 39
Carl, P. L., Temple, B. R. S., & Cohen, P. L. (2005) · Arthritis Research & Therapy · doi:10.1186/ar1832 · Cited by 40
[Prediction of natively unfolded regions in protein chain].
Galzitskaia, O. V., Garbuzinskiĭ, S. A., & Lobanov, M. I. (2006) · PubMed · Cited by 40
Solt, I., Magyar, C., Simon, I., Tompa, P., & Fuxreiter, M. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21032 · Cited by 40
Natively unfolded regions of the vertebrate fibrinogen molecule
Doolittle, R. F., & Kollman, J. M. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20758 · Cited by 40
Structural study of the H/ACA snoRNP components Nop10p and the 3′ hairpin of U65 snoRNA
Khanna, M., Wu, H., Johansson, C. A., Caizergues‐Ferrer, M., & Feigon, J. F. (2005) · RNA · doi:10.1261/rna.2221606 · Cited by 40
“Thus, Nop10p belongs to the growing www.rnajournal.org 43 family of proteins that are partially disordered or unfolded in the absence of their binding partners (Wright and Dyson 1999; Dunker et al. 2002; Dyson and Wright 2002).”
BackgroundCirculating extracellular vesicles and rheumatoid arthritis: a proteomic analysis
Alghamdi, M., Alamry, S. A., Bahlas, S. M., Uversky, V. N., & Redwan, E. M. M. M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04020-4 · Cited by 41
Molecular evolution of dihydrouridine synthases
Kasprzak, J. M., Czerwoniec, A., & Bujnicki, J. M. (2012) · BMC Bioinformatics · doi:10.1186/1471-2105-13-153 · Cited by 39
Characterization of Recombinant Lysyl Oxidase Propeptide
Vora, S. R., Guo, Y., Stephens, D. N., Salih, E., Vu, E. D., Kirsch, K. H., Sonenshein, G. E., & Trackman, P. C. (2010) · Biochemistry · doi:10.1021/bi902218p · Cited by 39
Wang, Y., Trewhella, J., & Goldenberg, D. P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.02.009 · Cited by 39
Natural protein sequences are more intrinsically disordered than random sequences
Yu, J., Cao, Z., Yang, Y., Wang, C., Su, Z.-D., Zhao, Y.-W., Wang, J., & Zhou, Y. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2138-9 · Cited by 38
Intrinsically disordered domains: Sequence ➔ disorder ➔ function relationships
Jianhong, Z., Oldfield, C. J., Yan, W., Shen, B., & Dunker, A. K. (2019) · Protein Science · doi:10.1002/pro.3680 · Cited by 40
Self-citationUversky, V. N. (2019) · Molecules · doi:10.3390/molecules24183265 · Cited by 39
Heme binds to an intrinsically disordered region of Bach2 and alters its conformation
Watanabe‐Matsui, M., Matsumoto, T., Matsui, T., Ikeda‐Saito, M., Muto, A., Murayama, K., & Igarashi, K. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.11.005 · Cited by 39
Metadata
- 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
- 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
- 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