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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
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“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]
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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
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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
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