The DOI matches its Crossref record; 86 of the 86 references it cites were found in a registry or an index.
Fuzzy Complexes: A More Stochastic View of Protein Function
Abstract
Intrinsically disordered proteins (IDPs) are widespread in eukaryotic proteomes and challenge the classical structure-function paradigm that equates a folded 3-D structure with protein function. However, IDPs often function by molecular recognition, in which they bind a partner molecule and undergo "induced folding" or "disorder-to-order transition" upon binding, which apparently suggests that in a functional context IDPs become ordered. Whereas this observation would restore the "prestige" of the classical structure-function paradigm, a closer inspection of the complexes of IDPs reveals that they do not always become fully ordered, but preserve functionally significant disorder in the complex with their binding partner(s). This phenomenon, which we termed "fuzziness", is the ultimate extension of structural disorder to the functional native state of proteins. In this introductory chapter, we outline the most important aspects of fuzziness, such as its structural categories, molecular mechanisms of function it mediates and the biological processes, in which it plays a distinguished role. As confirmed by all the other chapters of the book, we will show that new cases of fuzziness pop up at an accelerating pace, underscoring that this phenomenon presents a widespread novel paradigm of protein structure and function.
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
“Some IDPs/IDRs may remain unfolded and dynamic even in the bound state [19–23], creating fuzzy complexes (Fig. 1) [24, 25].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [25]
Citations
Cites
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497
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 unstructured proteins
Tompa, P. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02169-2 · Cited by 2,056
Self-citationPrediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., & Jones, D. T. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.002 · Cited by 2,010
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
Electrostatic Basis for Enzyme Catalysis
Warshel, A., Sharma, P. K., Kato, M., Xiang, Y., Liu, H., & Olsson, M. H. M. (2006) · Chemical Reviews · doi:10.1021/cr0503106 · Cited by 1,487
The importance of intrinsic disorder for protein phosphorylation
Iakoucheva, L. M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh253 · Cited by 1,429
Integrating mRNA Processing with Transcription
Proudfoot, N. J., Furger, A., & Dye, M. J. (2002) · Cell · doi:10.1016/s0092-8674(02)00617-7 · Cited by 1,084
Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions
Tompa, P., & Fuxreiter, M. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.10.003 · Cited by 1,080
Self-citationWright, P. E., & Dyson, H. J. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.12.003 · Cited by 1,012
Structural basis for the binding of proline-rich peptides to SH3 domains
Yu, H., Chen, J., Feng, S., Dalgarno, D. C., Brauer, A. W., & Schrelber, S. L. (1994) · Cell · doi:10.1016/0092-8674(94)90367-0 · Cited by 1,003
Intrinsic motions along an enzymatic reaction trajectory
Henzler‐Wildman, K. A., Thai, V., Lei, M., Ott, M., Wolf‐Watz, M., Fenn, T. D., Pozharski, E. V., Wilson, M. A., Petsko, G. A., Karplus, M., et al. (2007) · Nature · doi:10.1038/nature06410 · Cited by 893
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
DisProt: the Database of Disordered Proteins
Sickmeier, M. D., Hamilton, J. A., LeGall, T., Vacic, V., Cortese, M. S., Tantos, Á., Szabó, B., Tompa, P., Chen, J. Y., Uversky, V. N., et al. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl893 · Cited by 796
Self-citationAntibody Multispecificity Mediated by Conformational Diversity
James, L. C., Roversi, P., & Tawfik, D. S. (2003) · Science · doi:10.1126/science.1079731 · Cited by 719
The interplay between structure and function in intrinsically unstructured proteins
Tompa, P. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.072 · Cited by 717
Self-citationIntrinsic 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
Xie, H. M., Vučetić, S., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Uversky, V. N., & Zoran Obradovic, A. (2007) · Journal of Proteome Research · doi:10.1021/pr060392u · Cited by 572
Natively Unfolded Nucleoporins Gate Protein Diffusion across the Nuclear Pore Complex
Patel, S. S., Belmont, B. J., Sante, J. M., & Rexach, M. F. (2007) · Cell · doi:10.1016/j.cell.2007.01.044 · Cited by 566
Molecular biology of HMGA proteins: hubs of nuclear function
Reeves, R. (2001) · Gene · doi:10.1016/s0378-1119(01)00689-8 · Cited by 541
Gill, G., Pascal, E., Tseng, Z. H., & Tjian, R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.192 · Cited by 531
Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
Fuxreiter, M., Simon, I., Friedrich, P., & Tompa, P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.03.017 · Cited by 518
Self-citationStructural insights into a yeast prion illuminate nucleation and strain diversity
Krishnan, R., & Lindquist, S. L. (2005) · Nature · doi:10.1038/nature03679 · Cited by 477
Acid blobs and negative noodles
Sigler, P. B. (1988) · Nature · doi:10.1038/333210a0 · Cited by 438
Local structural disorder imparts plasticity on linear motifs
Fuxreiter, M., Tompa, P., & Simon, I. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm035 · Cited by 420
Self-citationThe Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways
del Sol, A., Tsai, C., Ma, B., & Nussinov, R. (2009) · Structure · doi:10.1016/j.str.2009.06.008 · Cited by 367
Linear motifs: Evolutionary interaction switches
Neduva, V., & Russell, R. B. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.04.005 · Cited by 352
Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor
Mittag, T., Orlicky, S. M., Choy, W., Tang, X., Lin, H., Sicheri, F., Kay, L. E., Tyers, M., & Forman-Kay, J. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809222105 · Cited by 347
Corden, J. L. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90236-5 · Cited by 332
Hope, I. A., Mahadevan, S., & Struhl, K. (1988) · Nature · doi:10.1038/333635a0 · Cited by 325
Lacy, E. R., Filippov, I. V., Lewis, W. S., Otieno, S. B., Xiao, L., Weiß, S. B., Hengst, L., & Kriwacki, R. W. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb746 · Cited by 305
Ha, N., Tonozuka, T., Stamos, J. L., Choi, H., & Weis, W. I. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.010 · Cited by 304
CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices
Baker, J. M., Hudson, R. P., Kanelis, V., Choy, W., Thibodeau, P. H., Thomas, P., & Forman-Kay, J. D. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1278 · Cited by 288
The Ste5 Scaffold Allosterically Modulates Signaling Output of the Yeast Mating Pathway
Bhattacharyya, R. P., Reményi, A., Good, M. C., Bashor, C. J., Falick, A. M., & Lim, W. A. (2006) · Science · doi:10.1126/science.1120941 · Cited by 281
Billeter, M., Qian, Y., Otting, G., Müller, M., Gehring, W., & Kurt Wüthrich, A. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1661 · Cited by 273
Intrinsic Protein Disorder, Amino Acid Composition, and Histone Terminal Domains
Hansen, J. C., Lu, X., Ross, E. D., & Woody, R. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.r500022200 · Cited by 265
Galea, C. A., Wang, Y., Sivakolundu, S. G., & Kriwacki, R. W. (2008) · Biochemistry · doi:10.1021/bi8006803 · Cited by 258
Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity
Borg, M., Mittag, T., Pawson, T., Tyers, M., Forman-Kay, J. D., & Chan, H. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702580104 · Cited by 245
Thousands of proteins likely to have long disordered regions.
Romero, P. R., Zoran Obradovic, A., Kissinger, C. R., Villafranca, J. E., Garner, E. C., Guilliot, S., & Dunker, A. K. (1998) · PubMed · Cited by 242
Investigation of α-Synuclein Fibril Structure by Site-directed Spin Labeling
Chen, M., Margittai, M., Chen, J., & Langen, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700368200 · Cited by 238
Tcf4 can specifically recognize beta-catenin using alternative conformations.
Graham, T. A., Ferkey, D. M., Mao, F., Kimelman, D., & Xu, W. (2001) · Nature Structural Biology · doi:10.1038/nsb718 · Cited by 219
Structural Basis for the Molecular Recognition between Human Splicing Factors U2AF65 and SF1/mBBP
Selenko, P., Gregorovic, G., Sprangers, R., Stier, G., Rhani, Z., Krämer, A., & Sattler, M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00115-1 · Cited by 212
Malleable machines take shape in eukaryotic transcriptional regulation
Fuxreiter, M., Tompa, P., Simon, I., Uversky, V. N., Hansen, J. C., & Asturias, F. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.127 · Cited by 211
Self-citationPrimary sequence independence for prion formation
Ross, E. D., Edskes, H. K., Terry, M. J., & Wickner, R. B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506136102 · Cited by 204
Structural basis for negative regulation of hypoxia-inducible factor-1α by CITED2
Freedman, S. J., Sun, Z.-Y. J., Kung, A. L., France, D. S., Wagner, G., & Eck, M. J. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb936 · Cited by 200
Structural Basis for Regulation of Protein Phosphatase 1 by Inhibitor-2
Hurley, T. D., Yang, J., Zhang, L., Goodwin, K. D., Zou, Q., Cortese, M. S., Dunker, A. K., & DePaoli-Roach, A. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703472200 · Cited by 189
Scrambled Prion Domains Form Prions and Amyloid
Ross, E. D., Baxa, U., & Wickner, R. B. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7206-7213.2004 · Cited by 179
Margittai, M., & Langen, R. (2008) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583508004733 · Cited by 176
Zor, T., Mayr, B. M., Dyson, H. J., Montminy, M., & Wright, P. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207361200 · Cited by 169
Plasticity of enzyme active sites
Todd, A. E., Orengo, C. A., & Thornton, J. M. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02158-8 · Cited by 167
Unusual bipartite mode of interaction between the nonsense‐mediated decay factors, UPF1 and UPF2
Clerici, M., Mourão, A., Gutsche, I., Gehring, N. H., Hentze, M. W., Kulozik, A. E., Kadlec, J., Sattler, M., & Cusack, S. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.175 · Cited by 156
Regulatory diversity among metazoan co-activator complexes
Taatjes, D. J., Marr, M. T., & Tjian, R. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1369 · Cited by 146
The C‐terminal domain of full‐length E. coli SSB is disordered even when bound to DNA
Savvides, S. N., Raghunathan, S., Fütterer, K., Kozlov, A. G., Lohman, T. M., & Waksman, G. (2004) · Protein Science · doi:10.1110/ps.04661904 · Cited by 145
Sigalov, A. B., Aivazian, D., & Stern, L. J. (2004) · Biochemistry · doi:10.1021/bi035900h · Cited by 141
Mouse Hsp25, a small heat shock protein
Lindner, R. A., Carver, J. A., Ehrnsperger, M., Büchner, J., Esposito, G., Behlke, J., Lutsch, G., Kotlyarov, A., & Gaestel, M. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01188.x · Cited by 127
Quantitative Observation of Backbone Disorder in Native Elastin
Pometun, M. S., Chekmenev, E. Y., & Wittebort, R. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310948200 · Cited by 124
Prevalent Structural Disorder inE.coliandS.cerevisiaeProteomes
Tompa, P., Dosztányi, Z., & Simon, I. (2006) · Journal of Proteome Research · doi:10.1021/pr0600881 · Cited by 124
Self-citationRole of Intrinsic Flexibility in Signal Transduction Mediated by the Cell Cycle Regulator, p27Kip1
Galea, C. A., Nourse, A., Wang, Y., Sivakolundu, S. G., Heller, W. T., & Kriwacki, R. W. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.12.016 · Cited by 123
Fontes, M. R. M., Teh, T., Tóth, G. K., John, A., Pavo, I. J., Jans, D. A., & Kobe, B. (2003) · Biochemical Journal · doi:10.1042/bj20030510 · Cited by 110
Ng, K. P., Potikyan, G., Savene, R. O. V., Denny, C. T., Uversky, V. N., & Lee, K. A. W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607007104 · Cited by 104
Lu, X., Hamkalo, B. A., Parseghian, M. H., & Hansen, J. C. (2008) · Biochemistry · doi:10.1021/bi801636y · Cited by 100
Linker length and composition influence the flexibility of Oct‐1 DNA binding
van Leeuwen, H. C., Strating, M., Rensen, M., de Laat, W. L., & van der Vliet, P. C. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.2043 · Cited by 100
A Flexible Domain Is Essential for the Large Step Size and Processivity of Myosin VI
Rock, R. S., Ramamurthy, B., Dunn, A. R., Beccafico, S., Rami, B. R., Morris, C. A., Spink, B. J., Franzini‐Armstrong, C., Spudich, J. A., & Sweeney, H. L. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.01.015 · Cited by 98
Liu, Y., Matthews, K. S., & Bondos, S. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800375200 · Cited by 97
RNA polymerase II/TFIIF structure and conserved organization of the initiation complex.
Chung, W.-H., Craighead, J. L., Chang, W.-H., Ezeokonkwo, C., Bareket-Samish, A., Kornberg, R., & Asturias, F. (2003) · Molecules and Cells · doi:10.1016/s1097-2765(03)00387-3 · Cited by 96
A molecular code dictates sequence‐specific DNA recognition by homeodomains.
Damante, G., Pellizzari, L., Esposito, G., Fogolari, F., Viglino, P., Fabbro, D., Tell, G., Formisano, S., & Lauro, R. D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00879.x · Cited by 93
Structural disorder within the replicative complex of measles virus: Functional implications
Bourhis, J., Canard, B., & Longhi, S. (2005) · Virology · doi:10.1016/j.virol.2005.09.025 · Cited by 92
Protein Disorder: Conformational Distribution of the Flexible Linker in a Chimeric Double Cellulase
von Ossowski, I., Eaton, J. T., Czjzek, M., Perkins, S. J., Frandsen, T. P., Schülein, M., Panine, P., Henrissat, B., & Receveur‐Brechot, V. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.050146 · Cited by 89
Spire and Cordon-bleu: multifunctional regulators of actin dynamics
Renault, L., Bugyi, B., & Carlier, M. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.07.008 · Cited by 77
Conformational Diversity in the TPR Domain-Mediated Interaction of Protein Phosphatase 5 with Hsp90
Cliff, M. J., Harris, R., Barford, D., Ladbury, J. E., & Williams, M. A. (2006) · Structure · doi:10.1016/j.str.2005.12.009 · Cited by 76
Simon, S. M., Sousa, F. J. R., Mohana‐Borges, R., & Walker, G. C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706067105 · Cited by 76
Polverini, E., Rangaraj, G., Libich, D. S., Boggs, J. M., & Harauz, G. (2007) · Biochemistry · doi:10.1021/bi701336n · Cited by 76
Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins
Tompa, P. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07250.x · Cited by 73
Self-citationSchwarz‐Linek, U., Pilka, E. S., Pickford, A. R., Kim, J. H., Höök, M., Campbell, I. D., & Potts, J. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405083200 · Cited by 66
Tóth-Petróczy, Á., Simon, I., Fuxreiter, M., & Levy, Y. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9052784 · Cited by 66
Self-citationLee, G. M., Pufall, M. A., Meeker, C. A., Kang, H.-S., Graves, B. J., & McIntosh, L. P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.064 · Cited by 58
Interaction between the C‐terminal domains of N and P proteins of measles virus investigated by NMR
Bernard, C., Gely, S., Bourhis, J., Morelli, X., Longhi, S., & Darbon, H. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.03.004 · Cited by 50
Haarmann, C., GREEN, D. J., Casarotto, M. G., Laver, D. R., & Dulhunty, A. F. (2003) · Biochemical Journal · doi:10.1042/bj20021763 · Cited by 44
Phylip, L. H., Lees, W. E., Brownsey, B. G., Bur, D., Dunn, B. M., Winther, J. R., Gustchina, A., Li, M., Copeland, T., Wlodawer, A., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008520200 · Cited by 44
Shi, W., Huang, Y., Sutton‐Smith, M., Tissot, B., Panico, M., Morris, H. R., Dell, A., Haslam, S. M., Boyington, J. C., Graham, B. S., et al. (2008) · Journal of Virology · doi:10.1128/jvi.02731-07 · Cited by 39
Determinants of Histone H4 N-terminal Domain Function during Nucleosomal Array Oligomerization
McBryant, S. J., Klonoski, J. M., Sorensen, T. C., Norskog, S. S., Williams, S., Resch, M. G., Toombs, J. A., Hobdey, S. E., & Hansen, J. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.011288 · Cited by 35
Ahmed, M. A. M., Bamm, V. V., Shi, L., Steiner‐Mosonyi, M., Dawson, J., Brown, L. S., Harauz, G., & Ladizhansky, V. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.10.003 · Cited by 29
Kövér, K. E., Bruix, M., Santoro, J., Batta, G., Laurents, D. V., & Rico, M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.04.042 · Cited by 28
The length of the interdomain region of the L7/L12 protein is important for its function
Bubunenko, M. G., Chuikov, S., & Gudkov, A. T. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81198-u · Cited by 21
Cited by
Sorted by citations
AlphaFold and Implications for Intrinsically Disordered Proteins
Ruff, K. M., & Pappu, R. V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167208 · Cited by 635
Unusual biophysics of intrinsically disordered proteins
Uversky, V. N. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.008 · Cited by 581
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics
Uversky, V. N. (2019) · Frontiers in Physics · doi:10.3389/fphy.2019.00010 · Cited by 542
A decade and a half of protein intrinsic disorder: Biology still waits for physics
Uversky, V. N. (2013) · Protein Science · doi:10.1002/pro.2261 · Cited by 512
Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour
Fusco, G., Simone, A. D., Gopinath, T., Vostrikov, V. V., Vendruscolo, M., Dobson, C. M., & Veglia, G. (2014) · Nature Communications · doi:10.1038/ncomms4827 · Cited by 493
Metadata
- Authors
- Fuxreiter, M., & Tompa, P.
- Venue
- Advances in Experimental Medicine and Biology
- Publisher
- Springer US
- Published
- 2012
- Volume
- 725
- Pages
- 1-14
- ISSN
- 0065-2598 (ISSN-L)
- OpenAlex
- W2243182195
- Cited by
- 240
- References
- 86
- Citations by year
- 2026: 9 · 2025: 10 · 2024: 24 · 2023: 7 · 2022: 12 · 2021: 20 · 2020: 19 · 2019: 18 · 2018: 20 · 2017: 17 · 2016: 19 · 2015: 23 · 2014: 13 · 2013: 24 · 2012: 5
- FWCI
- 35.58
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Advances in experimental medicine and biology (publishedVersion)
- PubMed (publishedVersion)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- intrinsically disordered proteins, fuzziness, protein complexes, induced folding, disorder-to-order transition, protein function, structure-function relationship, molecular recognition, protein-protein interaction
- MeSH terms
- Animals, Humans, Models, Molecular, Protein Binding, Proteins, Protein Structure, Tertiary, Protein Folding
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