Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

Collective dynamics of ‘small-world’ networks

Watts, D. J., & Strogatz, S. H. (1998) · Nature · doi:10.1038/30918 · Cited by 43,060 · see citing works

Emergence of Scaling in Random Networks

Barabási, A.-L., & Albert, R. (1999) · Science · doi:10.1126/science.286.5439.509 · Cited by 36,135 · see citing works

Network biology: understanding the cell's functional organization

Barabási, A.-L., & Oltvai, Z. N. (2004) · Nature Reviews Genetics · doi:10.1038/nrg1272 · Cited by 7,903 · see citing works

p53, the cellular gatekeeper for growth and division

Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693 · see citing works

Genetic regulatory mechanisms in the synthesis of proteins

Jacob, F., & Monod, J. (1961) · Journal of Molecular Biology · doi:10.1016/s0022-2836(61)80072-7 · Cited by 6,605 · see citing works

The interpretation of protein structures: Estimation of static accessibility

Lee, B., & Richards, F. M. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90324-x · Cited by 5,884 · see citing works

Protein secondary structure prediction based on position-specific scoring matrices.

Jones, D. C. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3091 · Cited by 5,741 · see citing works

The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.

Wade Harper, J. (1993) · Cell · doi:10.1016/0092-8674(93)90499-g · Cited by 5,651 · see citing works

Lethality and centrality in protein networks

Jeong, H., Mason, S., Barabási, A., & Oltvai, Z. (2001) · Nature · doi:10.1038/35075138 · Cited by 5,327 · see citing works

Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B

Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244 · see citing works

p53, guardian of the genome

Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138 · see citing works

A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae

Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., Lockshon, D., Narayan, V., Srinivasan, M., Pochart, P., et al. (2000) · Nature · doi:10.1038/35001009 · Cited by 4,706 · see citing works

Small Angle X-ray Scattering

Hart, M., & Deutsch, M. (1983) · Physics Bulletin · doi:10.1088/0031-9112/34/7/032 · Cited by 4,587 · see citing works

Identification of c- <i>MYC</i> as a Target of the APC Pathway

He, T.-C., Sparks, A. B., Rago, C., Hermeking, H., Zawel, L., da Costa, L. T., Morin, P. J., Vogelstein, B., & Kinzler, K. W. (1998) · Science · doi:10.1126/science.281.5382.1509 · Cited by 4,566 · see citing works

Predicting coiled coils from protein sequences.

Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953 · see citing works

Intrinsically unstructured proteins and their functions

Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871 · see citing works

Small-Angle X-Ray Scattering

Bhushan, B. (2016) · Springer eBooks · doi:10.1007/978-94-017-9780-1_101037 · Cited by 3,789 · see citing works

Prediction of protein antigenic determinants from amino acid sequences.

Hopp, T. P., & Woods, K. R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.6.3824 · Cited by 3,726 · see citing works

From molecular to modular cell biology.

Hartwell, L. H., Hopfield, J. J., Leibler, S., & Murray, A. W. (1999) · Nature · doi:10.1038/35011540 · Cited by 3,632 · see citing works

The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution

Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327 · see citing works

Wnt signaling and cancer

Polakis, P. (2000) · Genes &amp; Development · doi:10.1101/gad.14.15.1837 · Cited by 3,183 · see citing works

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 · see citing works

Solvent-Accessible Surfaces of Proteins and Nucleic Acids

Connolly, M. L. (1983) · Science · doi:10.1126/science.6879170 · Cited by 2,759 · see citing works

Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations

Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,559 · cited 2× · see citing works

Scale-Free Networks

Barabási, A.-L., & Bonabeau, E. (2003) · Scientific American · doi:10.1038/scientificamerican0503-60 · Cited by 2,494 · see citing works

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 · see citing works

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

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

Estimation of globular protein secondary structure from circular dichroism

Provencher, S. W., & Gloeckner, J. (1981) · Biochemistry · doi:10.1021/bi00504a006 · Cited by 2,167 · see citing works

Stability of Proteins Small Globular Proteins

Privalov, P. L. (1979) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60460-x · Cited by 2,163 · see citing works

Control of β-Catenin Phosphorylation/Degradation by a Dual-Kinase Mechanism

Liu, C., Li, Y., Semënov, M. V., Han, C., Baeg, G., Tan, Y., Zhang, Z., Lin, X., & He, X. (2002) · Cell · doi:10.1016/s0092-8674(02)00685-2 · Cited by 2,066 · see citing works

Intrinsically unstructured proteins

Tompa, P. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02169-2 · Cited by 2,056 · see citing works

MECHANISMS OF WNT SIGNALING IN DEVELOPMENT

Wodarz, A., & Nusse, R. (1998) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.14.1.59 · Cited by 2,017 · see citing works

Prediction 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 · see citing works

Crystal structure of the ribosome at 5.5 Å resolution

Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944 · see citing works

Circular Dichroism and the Conformational Analysis of Biomolecules

Fasman, G. D. (1996) · Springer eBooks · doi:10.1007/978-1-4757-2508-7 · Cited by 1,936 · see citing works

Natively unfolded proteins: A point where biology waits for physics

Uversky, V. N. (2002) · Protein Science · doi:10.1110/ps.4210102 · Cited by 1,815 · see citing works

Evidence for dynamically organized modularity in the yeast protein–protein interaction network

Han, J. J., Bertin, N., Hao, T., Goldberg, D. S., Berriz, G. F., Zhang, L. V., Dupuy, D., Walhout, A. J. M., Cusick, M. E., Roth, F. P., et al. (2004) · Nature · doi:10.1038/nature02555 · Cited by 1,789 · see citing works

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 · see citing works

Intrinsically Disordered Proteins

Uversky, V. N. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-374984-0.01698-3 · Cited by 1,646 · see citing works

Biophysical and Molecular Mechanisms of Shaker Potassium Channel Inactivation

Hoshi, T., Zagotta, W. N., & Aldrich, R. W. (1990) · Science · doi:10.1126/science.2122519 · Cited by 1,527 · see citing works

NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded

Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., & Lansbury, P. T. (1996) · Biochemistry · doi:10.1021/bi961799n · Cited by 1,524 · see citing works

Inactivation of the sodium channel. I. Sodium current experiments.

Bezanilla, F., & Armstrong, C. M. (1977) · The Journal of General Physiology · doi:10.1085/jgp.70.5.549 · Cited by 1,489 · see citing works

Association of BRCA1 with Rad51 in Mitotic and Meiotic Cells

Scully, R., Chen, J., Plug, A., Xiao, Y., Weaver, D., Feunteun, J., Ashley, T., & Livingston, D. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81847-4 · Cited by 1,459 · see citing works

Coupling of Local Folding to Site-Specific Binding of Proteins to DNA

Spolar, R. S., & Record, M. T. (1994) · Science · doi:10.1126/science.8303294 · Cited by 1,402 · see citing works

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 · see citing works

Functional Interaction of an Axin Homolog, Conductin, with β-Catenin, APC, and GSK3β

Behrens, J., Jerchow, B., Würtele, M., Grimm, J., Asbrand, C., Wirtz, R. M., Kühl, M., Wedlich, D., & Birchmeier, W. (1998) · Science · doi:10.1126/science.280.5363.596 · Cited by 1,255 · see citing works

Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK‐3β and β‐catenin and promotes GSK‐3β‐dependent phosphorylation of β‐catenin

Ikeda, S., Kishida, S., Yamamoto, H., Murai, H., Koyama, S., & Kikuchi, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.5.1371 · Cited by 1,248 · see citing works

Molten Globule and Protein Folding

Ptitsyn, O. B. (1995) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60546-x · Cited by 1,222 · see citing works

Shape Complementarity at Protein/Protein Interfaces

Lawrence, M. C., & Colman, P. M. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1648 · Cited by 1,219 · see citing works

Protein Disorder Prediction

Linding, R., Jensen, L. J., Diella, F., Peer Bork, B., Gibson, T. J., & Russell, R. B. (2003) · Structure · doi:10.1016/j.str.2003.10.002 · Cited by 1,214 · see citing works

Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins

Iakoucheva, L. M., Brown, C. J., Lawson, J. D., Obradović, Z., & Dunker, A. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00969-5 · Cited by 1,214 · see citing works

Connectivity of Growing Random Networks

Krapivsky, P. L., Redner, S., & Leyvraz, F. (2000) · Physical Review Letters · doi:10.1103/physrevlett.85.4629 · Cited by 1,210 · see citing works

Shape complementarity at protein–protein interfaces

Norel, R., Lin, S. L., Wolfson, H. J., & Nussinov, R. (1994) · Biopolymers · doi:10.1002/bip.360340711 · Cited by 1,208 · see citing works

MSCRAMM-MEDIATED ADHERENCE OF MICROORGANISMS TO HOST TISSUES

Patti, J. M., Allen, B. L., McGavin, M. J., & Höök, M. (1994) · Annual Review of Microbiology · doi:10.1146/annurev.mi.48.100194.003101 · Cited by 1,191 · see citing works

CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5

Wu, L., Gerard, N. P., Wyatt, R. T., Choe, H., Parolin, C., Ruffing, N., Borsetti, A., Cardoso, A. A., Desjardin, E., Newman, W., et al. (1996) · Nature · doi:10.1038/384179a0 · Cited by 1,168 · see citing works

Prediction of chain flexibility in proteins

Karplus, P. A., & Schulz, G. E. (1985) · Die Naturwissenschaften · doi:10.1007/bf01195768 · Cited by 1,153 · see citing works

The Specificity of Serological Reactions

(1945) · Harvard University Press eBooks · doi:10.4159/harvard.9780674184220 · Cited by 1,097 · see citing works

[4] Circular dichroism

Woody, R. W. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)46006-3 · Cited by 1,040 · see citing works

CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5

Trkola, A., Dragic, T., Arthos, J. A., Binley, J. Μ., Olson, W. C., Allaway, G. P., Cheng‐Mayer, C., Robinson, J. E., Maddon, P. J., & Moore, J. P. (1996) · Nature · doi:10.1038/384184a0 · Cited by 1,034 · see citing works

Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex

Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1519061 · Cited by 1,032 · see citing works

Inhibition of cyclin-dependent kinases by p21.

Harper, J. W., Elledge, S. J., Keyomarsi, K., Dynlacht, B. D., Tsai, L., Zhang, P., Dobrowolski, S. F., Bai, C., Connell‐Crowley, L., & Swindell, E. C. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.4.387 · Cited by 1,025 · see citing works

The Pairwise Energy Content Estimated from Amino Acid Composition Discriminates between Folded and Intrinsically Unstructured Proteins

Dosztányi, Z., Csizmók, V., Tompa, P., & Simon, I. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.01.071 · Cited by 1,021 · see citing works

Requirement of ATM-Dependent Phosphorylation of Brca1 in the DNA Damage Response to Double-Strand Breaks

Cortez, D., Wang, Y., Qin, J., & Elledge, S. J. (1999) · Science · doi:10.1126/science.286.5442.1162 · Cited by 1,020 · see citing works

Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon

MEURS, E. F., Chong, K. L., GALABRU, J., Thomas, N. S. B., Kerr, I. M., Williams, B. R. G., & Hovanessian, A. G. (1990) · Cell · doi:10.1016/0092-8674(90)90374-n · Cited by 1,017 · see citing works

What does it mean to be natively unfolded?

Uversky, V. N. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02649.x · Cited by 985 · see citing works

GlobPlot: exploring protein sequences for globularity and disorder

Linding, R. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg519 · Cited by 985 · see citing works

A sperm ion channel required for sperm motility and male fertility

Ren, D., Navarro, B., Perez, G. I., Jackson, A. C., Battaglia-Hsu, S.-F., Shi, Q., Tilly, J. L., & Clapham, D. E. (2001) · Nature · doi:10.1038/35098027 · Cited by 957 · see citing works

Inactivation of the sodium channel. II. Gating current experiments.

Armstrong, C. M., & Bezanilla, F. (1977) · The Journal of General Physiology · doi:10.1085/jgp.70.5.567 · Cited by 953 · see citing works

High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium

Harms, J. M., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Franceschi, F. J., & Yonath, A. (2001) · Cell · doi:10.1016/s0092-8674(01)00546-3 · Cited by 899 · see citing works

The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution

Acharya, R., Fry, E. E., Stuart, D. I., Fox, G., Rowlands, D. J., & Brown, F. (1989) · Nature · doi:10.1038/337709a0 · Cited by 866 · see citing works

How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices

O’Neil, K. T., & DeGrado, W. F. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90177-d · Cited by 845 · see citing works

A Theory of the Structure and Process of Formation of Antibodies*

Pauling, L. C. (1940) · Journal of the American Chemical Society · doi:10.1021/ja01867a018 · Cited by 843 · see citing works

Downregulation of β-catenin by human Axin and its association with the APC tumor suppressor, β-catenin and GSK3β

Hart, M. J., Santos, R. D. L., Albert, I., Rubinfeld, B., & Polakis, P. G. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70226-x · Cited by 836 · see citing works

Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor

Lasky, L. A., Nakamura, G. R., Smith, D. H., Fennie, C., Shimasaki, C. D., Patzer, E. J., Berman, P. W., Gregory, T. J., & Capon, D. J. (1987) · Cell · doi:10.1016/0092-8674(87)90524-1 · Cited by 828 · see citing works

Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence

Bittle, J. L., Houghten, R. A., Alexander, H., Shinnick, T. M., Sutcliffe, J. G., Lerner, R. A., Rowlands, D. J., & Brown, F. (1982) · Nature · doi:10.1038/298030a0 · Cited by 820 · see citing works

Centrosome Amplification and a Defective G2–M Cell Cycle Checkpoint Induce Genetic Instability in BRCA1 Exon 11 Isoform–Deficient Cells

Xu, X., Ohler, Z. W., Linke, S. P., Li, C., Gotay, J., Wang, X. W., Harris, C. C., Ried, T., & Deng, C. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80466-9 · Cited by 819 · see citing works

HMG domain proteins: architectural elements in the assembly of nucleoprotein structures

Grosschedl, R., Giese, K., & Pagel, J. M. (1994) · Trends in Genetics · doi:10.1016/0168-9525(94)90232-1 · Cited by 817 · see citing works

Crystal Structure of the Lactose Operon Repressor and Its Complexes with DNA and Inducer

Lewis, M., Chang, G. A., Horton, N. C., Kercher, M. A., Pace, H. C., Schumacher, M. A., Brennan, R. G., & Lu, P. (1996) · Science · doi:10.1126/science.271.5253.1247 · Cited by 790 · see citing works

A Third Recognition Element in Bacterial Promoters: DNA Binding by the α Subunit of RNA Polymerase

Ross, W., Gosink, K. K., Salomon, J., Igarashi, K., Zou, C., Ishihama, A., Severinov, K., & Gourse, R. L. (1993) · Science · doi:10.1126/science.8248780 · Cited by 789 · see citing works

High-Mobility-Group Chromosomal Proteins: Architectural Components That Facilitate Chromatin Function

Bustin, M., & Reeves, R. (1996) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60360-8 · Cited by 769 · see citing works

Restoration of Inactivation in Mutants of Shaker Potassium Channels by a Peptide Derived from ShB

Zagotta, W. N., Hoshi, T., & Aldrich, R. W. (1990) · Science · doi:10.1126/science.2122520 · Cited by 762 · see citing works

[33] Analysis of compositionally biased regions in sequence databases

Wootton, J. C., & Federhen, S. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)66035-2 · Cited by 745 · see citing works

Statistics of local complexity in amino acid sequences and sequence databases

Wootton, J. C., & Federhen, S. (1993) · Computers & Chemistry · doi:10.1016/0097-8485(93)85006-x · Cited by 721 · see citing works

Antibody Multispecificity Mediated by Conformational Diversity

James, L. C., Roversi, P., & Tawfik, D. S. (2003) · Science · doi:10.1126/science.1079731 · Cited by 719 · see citing works

A Common Phosphate Binding Site Explains the Unique Substrate Specificity of GSK3 and Its Inactivation by Phosphorylation

Frame, S., Cohen, P., & Biondi, R. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00253-2 · Cited by 703 · see citing works

Natively unfolded proteins

Fink, A. L. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.01.002 · Cited by 700 · see citing works

The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure.

Reeves, R., & Nissen, M. S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38926-4 · Cited by 685 · see citing works

The DISOPRED server for the prediction of protein disorder

Ward, J. J., McGuffin, L. J., Bryson, K., Buxton, B. F., & Jones, D. T. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth195 · Cited by 684 · see citing works

Crystal Structure of Glycogen Synthase Kinase 3β

Dajani, R., Fraser, E., Roe, S. M., Young, N., Good, V. M., Dale, T. C., & Pearl, L. H. (2001) · Cell · doi:10.1016/s0092-8674(01)00374-9 · Cited by 678 · see citing works

BRCT Repeats As Phosphopeptide-Binding Modules Involved in Protein Targeting

Manke, I. A., Lowery, D. M., Nguyen, A., & Yaffe, M. B. (2003) · Science · doi:10.1126/science.1088877 · Cited by 651 · see citing works

Conserved Sequence and Structural Elements in the HIV-1 Principal Neutralizing Determinant

LaRosa, G. J., Davide, J. P., Weinhold, K. J., Waterbury, J. A., Profy, A. T., Lewis, J. A., Langlois, A. J., Dreesman, G. R., Boswell, R. N., Shadduck, P. P., et al. (1990) · Science · doi:10.1126/science.2392685 · Cited by 650 · see citing works

In search of the tumour-suppressor functions of BRCA1 and BRCA2

Scully, R., & Livingston, D. M. (2000) · Nature · doi:10.1038/35044000 · Cited by 643 · see citing works

Stable Interaction between the Products of the BRCA1 and BRCA2 Tumor Suppressor Genes in Mitotic and Meiotic Cells

Chen, J., Silver, D. P., Walpita, D., Cantor, S. B., Gazdar, A. F., Tomlinson, G. E., Couch, F. J., Weber, B. L., Ashley, T., Livingston, D. M., et al. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80276-2 · Cited by 635 · see citing works

Unfolded Proteins and Protein Folding Studied by NMR

Dyson, H. J., & Wright, P. E. (2004) · Chemical Reviews · doi:10.1021/cr030403s · Cited by 628 · see citing works

Association of BRCA1 with the hRad50-hMre11-p95 Complex and the DNA Damage Response

Zhong, Q., Chen, C.-F., Li, S., Chen, Y., Wang, C.-C., Xiao, J., Chen, P.-L., Sharp, Z. D., & Lee, W.-H. (1999) · Science · doi:10.1126/science.285.5428.747 · Cited by 626 · see citing works

Antibodies that inhibit fusion of human immunodeficiency virus-infected cells bind a 24-amino acid sequence of the viral envelope, gp120.

Rusche, J. R., Javaherian, K., McDanal, C. B., Petro, J., Lynn, D. L., Grimaila, R., Langlois, A. J., Gallo, R. C., Arthur, L. O., & Fischinger, P. J. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.9.3198 · Cited by 619 · see citing works

Principal neutralizing domain of the human immunodeficiency virus type 1 envelope protein.

Javaherian, K., Langlois, A. J., McDanal, C. B., Ross, K. L., Eckler, L., Jellis, C. L., Profy, A. T., Rusche, J. R., Bolognesi, D. P., & Putney, S. D. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.17.6768 · Cited by 618 · see citing works

Sequence-Dependent Correction of Random Coil NMR Chemical Shifts

Schwarzinger, S., Kroon, G. J. A., Foss, T. R., Chung, J., Wright, P. E., & Dyson, H. J. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003760i · Cited by 604 · see citing works

Correlation between segmental mobility and the location of antigenic determinants in proteins

Westhof, É., Altschuh, D., Moras, D., Bloomer, A. C., Mondragón, A., Klug, A., & Regenmortel, M. H. V. V. (1984) · Nature · doi:10.1038/311123a0 · Cited by 587 · see citing works

Alpha-crystallin

Horwitz, J. (2003) · Experimental Eye Research · doi:10.1016/s0014-4835(02)00278-6 · Cited by 587 · see citing works

The protein trinity—linking function and disorder

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

Conformational diversity and protein evolution – a 60-year-old hypothesis revisited

James, L. C., & Tawfik, D. S. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00135-x · Cited by 579 · see citing works

Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity.

Kriwacki, R. W., Hengst, L., Tennant, L. L., Reed, S. I., & Wright, P. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11504 · Cited by 576 · see citing works

Major Glycoprotein Antigens That Induce Antibodies in AIDS Patients Are Encoded by HTLV-III

Allan, J. D., Coligan, J. E., Barin, F., McLane, M. F., Sodroski, J., Rosen, C., Haseltine, W. A., Lee, T. H., & Essex, M. (1985) · Science · doi:10.1126/science.2986290 · Cited by 572 · see citing works

Calcium-Binding Proteins

Kretsinger, R. H. (2011) · Springer eBooks · doi:10.1007/978-3-642-16483-5_778 · Cited by 571 · see citing works

Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure.

Schweers, O., Schönbrunn, E., Marx, A., & Mandelkow�, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51080-8 · Cited by 569 · see citing works

[27] Circular dichroism and optical rotatory dispersion of proteins and polypeptides

Adler, A. J., Greenfield, N. J., & Fasman, G. D. (1973) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(73)27030-1 · Cited by 561 · see citing works

The role of structural disorder in the function of RNA and protein chaperones

Tompa, P., & Csermely, P. (2004) · The FASEB Journal · doi:10.1096/fj.04-1584rev · Cited by 555 · see citing works

Interactions of protein antigens with antibodies.

Davies, D. R., & Cohen, G. H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.7 · Cited by 553 · see citing works

Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms

Jeffrey, P. D., Gorina, S. S., & Pavletich, N. P. (1995) · Science · doi:10.1126/science.7878469 · Cited by 548 · see citing works

Structural Insights into the Evolution of an Antibody Combining Site

Wedemayer, G. J., Patten, P. A., Wang, L. H., Schultz, P. G., & Stevens, R. C. (1997) · Science · doi:10.1126/science.276.5319.1665 · Cited by 547 · see citing works

Comparing and Combining Predictors of Mostly Disordered Proteins

Oldfield, C. J., Cheng, Y., Cortese, M. S., Brown, C. J., Uversky, V. N., & Dunker, A. K. (2005) · Biochemistry · doi:10.1021/bi047993o · Cited by 544 · see citing works

Molecular biology of HMGA proteins: hubs of nuclear function

Reeves, R. (2001) · Gene · doi:10.1016/s0378-1119(01)00689-8 · Cited by 535 · see citing works

Structural Evidence for Induced Fit as a Mechanism for Antibody-Antigen Recognition

Rini, J. M., Schulze‐Gahmen, U., & Wilson, I. A. (1992) · Science · doi:10.1126/science.1546293 · Cited by 530 · see citing works

hCds1-mediated phosphorylation of BRCA1 regulates the DNA damage response

Lee, J., Collins, K. M., Brown, A. L., Lee, C. H., & Chung, J. H. (2000) · Nature · doi:10.1038/35004614 · Cited by 529 · see citing works

Non-globular domains in protein sequences: Automated segmentation using complexity measures

Wootton, J. C. (1994) · Computers & Chemistry · doi:10.1016/0097-8485(94)85023-2 · Cited by 524 · see citing works

Antibody-antigen interactions: new structures and new conformational changes

Wilson, I. A., & Stanfield, R. L. (1994) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(94)90267-4 · Cited by 517 · see citing works

Functional interactions between BRCA1 and the checkpoint kinase ATR during genotoxic stress

Tibbetts, R. S., Cortez, D., Brumbaugh, K. M., Scully, R., Livingston, D., Elledge, S. J., & Abraham, R. T. (2000) · Genes &amp; Development · doi:10.1101/gad.851000 · Cited by 512 · see citing works

[29] Osmotic stress for the direct measurement of intermolecular forces

Parsegian, V. A., Rand, R. P., Fuller, N. L., & Rau, D. C. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)27032-9 · Cited by 503 · see citing works

A Protein-Chameleon: Conformational Plasticity of α-Synuclein, a Disordered Protein Involved in Neurodegenerative Disorders

Uversky, V. N. (2003) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2003.10506918 · Cited by 502 · see citing works

OPTIMIZING LONG INTRINSIC DISORDER PREDICTORS WITH PROTEIN EVOLUTIONARY INFORMATION

PENG, K., Vučetić, S., Predrag Radivojac, A., Brown, C. J., Dunker, A. K., & Zoran Obradovic, A. (2005) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720005000886 · Cited by 497 · see citing works

Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.

Brzović, P. S., Rajagopal, P., Hoyt, D. W., King, M., & Klevit, R. E. (2001) · Nature Structural Biology · doi:10.1038/nsb1001-833 · Cited by 494 · see citing works

BRCA1 physically associates with p53 and stimulates its transcriptional activity

Zhang, H., Somasundaram, K., Peng, Y., Tian, H., Zhang, H., Bi, D., Weber, B. L., & El‐Deiry, W. S. (1998) · Oncogene · doi:10.1038/sj.onc.1201932 · Cited by 492 · see citing works

Osmotic stress, crowding, preferential hydration, and binding: A comparison of perspectives

Parsegian, V. A., Rand, R. P., & Rau, D. C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.3987 · Cited by 491 · see citing works

Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator

Hughes, K. T., Gillen, K., Semon, M., & Karlinsey, J. E. (1993) · Science · doi:10.1126/science.8235660 · Cited by 484 · see citing works

Intrinsic and Extrinsic Factors in Protein Antigenic Structure

Berzofsky, J. A. (1985) · Science · doi:10.1126/science.2410982 · Cited by 482 · see citing works

The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a protein

Tainer, J. A., Getzoff, E. D., Alexander, H., Houghten, R. A., Olson, A. J., Lerner, R. A., & Hendrickson, W. A. (1984) · Nature · doi:10.1038/312127a0 · Cited by 479 · see citing works

Probing protein structure by limited proteolysis.

Fontana, A., de Laureto, P. P., Spolaore, B., Frare, E., Picotti, P., & Zambonin, M. (2004) · Acta Biochimica Polonica · doi:10.18388/abp.2004_3573 · Cited by 467 · see citing works

Predicting intrinsic disorder from amino acid sequence

Zoran Obradovic, A., Peng, K., Vučetić, S., Predrag Radivojac, A., Brown, C. J., & Dunker, A. K. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10532 · Cited by 455 · see citing works

Acid blobs and negative noodles

Sigler, P. B. (1988) · Nature · doi:10.1038/333210a0 · Cited by 438 · see citing works

Characterization of gp41 as the Transmembrane Protein Coded by the HTLV-III/LAV Envelope Gene

Veronese, F. D. M., DeVico, A. L., Copeland, T. D., Oroszlan, S. I., Gallo, R. C., & Sarngadharan, M. G. (1985) · Science · doi:10.1126/science.2994223 · Cited by 437 · see citing works

Translational control

(1991) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240470805 · Cited by 433 · see citing works

Regulation of β-Catenin Signaling by the B56 Subunit of Protein Phosphatase 2A

Seeling, J. M., Miller, J. R., Gil, R., Moon, R. T., White, R. L., & Virshup, D. M. (1999) · Science · doi:10.1126/science.283.5410.2089 · Cited by 421 · see citing works

Multiple diverse ligands binding at a single protein site: A matter of pre‐existing populations

Ma, B., Shatsky, M., Wolfson, H. J., & Nussinov, R. (2002) · Protein Science · doi:10.1110/ps.21302 · Cited by 420 · see citing works

Induced fit in RNA-protein recognition.

Williamson, J. R. (2000) · Nature Structural Biology · doi:10.1038/79575 · Cited by 419 · see citing works

Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies

Petros, A. M., Nettesheim, D. G., Wang, Y., Olejniczak, E. T., Meadows, R. P., Mack, J. C., Swift, K. M., Matayoshi, E. D., Zhang, H., Thompson, C. B., et al. (2000) · Protein Science · doi:10.1110/ps.9.12.2528 · Cited by 413 · see citing works

Identification and functions of usefully disordered proteins

Dunker, A. K., Brown, C. J., & Zoran Obradovic, A. (2002) · Advances in protein chemistry · doi:10.1016/s0065-3233(02)62004-2 · Cited by 410 · see citing works

The solution structure of an HMG-I(Y)–DNA complex defines a new architectural minor groove binding motif

Huth, J. R., Bewley, C. A., Nissen, M. S., Evans, J. N. S., Reeves, R., Gronenborn, A. M., & Clore, G. M. (1997) · Nature Structural Biology · doi:10.1038/nsb0897-657 · Cited by 404 · see citing works

Structural basis for Hif-1α/CBP recognition in the cellular hypoxic response

Dames, S. A., Martinez‐Yamout, M. A., Guzman, R. N. D., Dyson, H. J., & Wright, P. E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082121399 · Cited by 404 · see citing works

Axin and Frat1 interact with Dvl and GSK, bridging Dvl to GSK in Wnt‐mediated regulation of LEF‐1

Li, L., Yuan, H., Weaver, C. D., Mao, J., Farr, G. H., Sussman, D. J., Jonkers, J., Kimelman, D., & Wu, D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.15.4233 · Cited by 403 · see citing works

Protection of Cattle Against Foot-and-Mouth Disease by a Synthetic Peptide

DiMarchi, R. D., Brooke, G. S., GALE, C. C., Cracknell, V., Doel, T. R., & Mowat, N. (1986) · Science · doi:10.1126/science.3008333 · Cited by 402 · see citing works

[3] Macromolecules and water: Probing with osmotic stress

Parsegian, V. A., Rand, R. P., & Rau, D. C. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)59039-0 · Cited by 395 · see citing works

Structure of Factor-inhibiting Hypoxia-inducible Factor (HIF) Reveals Mechanism of Oxidative Modification of HIF-1α

Elkins, J. M., Hewitson, K. S., McNeill, L. A., Seibel, J. F., Schlemminger, I., Pugh, C. W., Ratcliffe, P. J., & Schofield, C. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200644200 · Cited by 391 · see citing works

The Cell Attachment Site on Foot-and-Mouth Disease Virus Includes the Amino Acid Sequence RGD (Arginine-Glycine-Aspartic Acid)

Fox, G., Parry, N. R., Barnett, P. V., McGinn, B., Rowlands, D. J., & Brown, F. (1989) · Journal of General Virology · doi:10.1099/0022-1317-70-3-625 · Cited by 389 · see citing works

Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides.

Signäs, C., Raucci, G., Jönsson, K., Lindgren, P., Anantharamaiah, G. M., Höök, M., & Lindberg, M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.2.699 · Cited by 383 · see citing works

Flavors of protein disorder

Vučetić, S., Brown, C. J., Dunker, A. K., & Zoran Obradovic, A. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10437 · Cited by 381 · see citing works

Folding transition in the DMA-binding domain of GCN4 on specific binding to DNA

Weiss, M. A., Ellenberger, T. E., Wobbe, C. R., Lee, J. P., Harrison, S. C., & Struhl, K. (1990) · Nature · doi:10.1038/347575a0 · Cited by 379 · see citing works

Classification of scale-free networks

Goh, K.-I., Oh, E., Jeong, H., Kahng, B., & Kim, D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202301299 · Cited by 378 · see citing works

Glycogen synthase kinase-3: functions in oncogenesis and development

Plyte, S. E. (1992) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(92)90012-n · Cited by 377 · see citing works

Characterization of a human immunodeficiency virus neutralizing monoclonal antibody and mapping of the neutralizing epitope

Matsushita, S., Robert-Guroff, M., Rusche, J. R., Koito, A., Hattori, T., Hoshino, H., Javaherian, K., Takatsuki, K., & Putney, S. D. (1988) · Journal of Virology · doi:10.1128/jvi.62.6.2107-2114.1988 · Cited by 376 · see citing works

Revised nomenclature for high mobility group (HMG) chromosomal proteins

Bustin, M. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01777-1 · Cited by 371 · see citing works

Structure of a major immunogenic site on foot-and-mouth disease virus

Logan, D. T., ABU-GHAZALEH, R., Blakemore, W. E., Curry, S., Jackson, T., King, A. J., Lea, S. M., Lewis, R., Newman, J. W. I., Parry, N. R., et al. (1993) · Nature · doi:10.1038/362566a0 · Cited by 366 · see citing works

Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus.

Pfaff, E., Mussgay, M., Böhm, H. O., Schulz, G. E., & Schaller, H. (1982) · The EMBO Journal · doi:10.1002/j.1460-2075.1982.tb01262.x · Cited by 361 · see citing works

HMGI/Y proteins: flexible regulators of transcription and chromatin structure

Reeves, R., & Beckerbauer, L. (2001) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(01)00215-9 · Cited by 358 · see citing works

Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems

Sobue, K., & Sellers, J. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98864-2 · Cited by 354 · see citing works

Characterization of Envelope and Core Structural Gene Products of HTLV-III with Sera from AIDS Patients

Robey, W. G., Safai, B., Oroszlan, S. I., Arthur, L. O., Gonda, M. A., Gallo, R. C., & Fischinger, P. J. (1985) · Science · doi:10.1126/science.2984774 · Cited by 349 · see citing works

Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function.

Frelinger, A. L., Du, X., Plow, E. F., & Ginsberg, M. H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47346-8 · Cited by 348 · see citing works

Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex

Brzovic, P. S., Keeffe, J. R., Nishikawa, H., Miyamoto, K., Fox, D., Fukuda, M., Ohta, T., & Klevit, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0836054100 · Cited by 346 · see citing works

Protein flexibility and intrinsic disorder

Predrag Radivojac, A., Zoran Obradovic, A., Smith, D. K., Zhu, G., Vučetić, S., Brown, C. J., Lawson, J. D., & Dunker, A. K. (2003) · Protein Science · doi:10.1110/ps.03128904 · Cited by 341 · see citing works

Extended disordered proteins: targeting function with less scaffold

Gunasekaran, K., Tsai, C., Kumar, S., Zanuy, D., & Nussinov, R. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00003-3 · Cited by 338 · see citing works

HTLV-III/LAV-Neutralizing Antibodies to an E. coli -Produced Fragment of the Virus Envelope

Putney, S. D., Matthews, T. J., Robey, W. G., Lynn, D. L., Robert-Guroff, M., Mueller, W. T., Langlois, A. J., Ghrayeb, J., Petteway, S. R., Weinhold, K. J., et al. (1986) · Science · doi:10.1126/science.2431482 · Cited by 332 · see citing works

Local Structural Elements in the Mostly Unstructured Transcriptional Activation Domain of Human p53

Lee, H., Mok, K. H., Muhandiram, R., Park, K.-H., Suk, J.-E., Kim, D., Chang, J., Sung, Y. C., Choi, K. Y., & Han, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003107200 · Cited by 329 · see citing works

GBP, an Inhibitor of GSK-3, Is Implicated in Xenopus Development and Oncogenesis

Yost, C., Farr, G. H., Pierce, S. B., Ferkey, D. M., Chen, M. M., & Kimelman, D. (1998) · Cell · doi:10.1016/s0092-8674(00)81208-8 · Cited by 328 · see citing works

Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation

Agrawal, R. K., Penczek, P. A., Grassucci, R. A., & Frank, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6134 · Cited by 325 · see citing works

Protein-protein interfaces: Analysis of amino acid conservation in homodimers

Valdar, W. S. J., & Thornton, J. M. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20010101)42:1 · Cited by 322 · see citing works

A computer program for predicting protein antigenic determinants

Hopp, T. P., & Woods, K. R. (1983) · Molecular Immunology · doi:10.1016/0161-5890(83)90029-9 · Cited by 320 · see citing works

FlgM gains structure in living cells

Dedmon, M. M., Patel, C. N., Young, G. B., & Pielak, G. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202331299 · Cited by 317 · see citing works

Structural basis for recruitment of glycogen synthase kinase 3β to the axin—APC scaffold complex

Dajani, R., Fraser, E., Roe, S. M., Yeo, M., Good, V. M., Thompson, V., Dale, T. C., & Pearl, L. H. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg068 · Cited by 315 · see citing works

Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go?

Uversky, V. N. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3096-6 · Cited by 314 · see citing works

Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers.

Frelinger, A. L., Cohen, I., Plow, E. F., Smith, M. A., Roberts, J. R., Lam, S. C., & Ginsberg, M. H. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39332-9 · Cited by 313 · see citing works

Structure of the negative regulatory domain of p53 bound to S100B(betabeta).

Weber, D. J., Rust, R. R., & Baldisseri, D. M. (2000) · Nature Structural Biology · doi:10.1038/76797 · Cited by 313 · see citing works

Structure of the double‐stranded RNA‐binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA‐mediated activation

Nanduri, S., Carpick, B. W., Yang, Y., Williams, B. R. G., & Qin, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.18.5458 · Cited by 312 · see citing works

Accuracy of protein flexibility predictions

Vihinen, M., Torkkila, E., & Riikonen, P. T. (1994) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340190207 · Cited by 312 · see citing works

High level expression of the HMGI (Y) gene during embryonic development.

Chiappetta, G., Avantaggiato, V., Visconti, R., Fedele, M., Battista, S., Trapasso, F., Merciai, B. M., Fidanza, V., Giancotti, V., Santoro, M., et al. (1996) · PubMed · Cited by 309 · see citing works

Probing the partly folded states of proteins by limited proteolysis

Fontana, A., de Laureto, P. P., Filippis, V. D., Scaramella, E., & Zambonin, M. (1997) · Folding and Design · doi:10.1016/s1359-0278(97)00010-2 · Cited by 309 · see citing works

EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome.

Agrawal, R. K., Heagle, A. B., Penczek, P. A., Grassucci, R. A., & Frank, J. (1999) · Nature Structural Biology · doi:10.1038/10695 · Cited by 298 · see citing works

Design of DNA-Binding Peptides Based on the Leucine Zipper Motif

O’Neil, K. T., Hoess, R. H., & DeGrado, W. F. (1990) · Science · doi:10.1126/science.2389143 · Cited by 296 · see citing works

Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1.

Williams, R. S., Green, R., & Glover, J. N. M. (2001) · Nature Structural Biology · doi:10.1038/nsb1001-838 · Cited by 292 · see citing works

The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein

Longhi, S., Receveur‐Brechot, V., Karlin, D., Johansson, K., Darbon, H., Bhella, D., Yeo, R. P., Finet, S., & Canard, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300518200 · Cited by 292 · see citing works

Intrinsically unstructured proteins evolve by repeat expansion

Tompa, P. (2003) · BioEssays · doi:10.1002/bies.10324 · Cited by 283 · see citing works

Direct DNA binding by Brca1

Paull, T. T., Cortez, D., Bowers, B., Elledge, S. J., & Gellert, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111125998 · Cited by 282 · see citing works

Polyreactivity of antibody molecules

Notkins, A. L. (2004) · Trends in Immunology · doi:10.1016/j.it.2004.02.004 · Cited by 281 · see citing works

Cooperative Signals Governing ARF-Mdm2 Interaction and Nucleolar Localization of the Complex

Weber, J. D., Kuo, M.-L., Bothner, B. B., DiGiammarino, E. L., Kriwacki, R. W., Roussel, M. F., & Sherr, C. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2517-2528.2000 · Cited by 273 · see citing works

Double-strand breaks and tumorigenesis

Pierce, A. J., Stark, J. M., Araujo, F. D., Moynahan, M. E., Berwick, M., & Jasin, M. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02149-3 · Cited by 269 · see citing works

The structure and antigenicity of a type C foot-and-mouth disease virus

Lea, S. M., Hernéndez, J., Blakemore, W. E., Brocchi, E., Curry, S., Domingo, E., Fry, E. E., ABU-GHAZALEH, R., King, A., Newman, J., et al. (1994) · Structure · doi:10.1016/s0969-2126(00)00014-9 · Cited by 267 · see citing works

Comparing function and structure between entire proteomes

Liu, J., & Rost, B. (2001) · Protein Science · doi:10.1110/ps.10101 · Cited by 266 · see citing works

Gene fliA encodes an alternative sigma factor specific for flagellar operons in Salmonella typhimurium

Ohnishi, K., Kutsukake, K., Suzuki, H., & Iino, T. (1990) · Molecular and General Genetics MGG · doi:10.1007/bf00261713 · Cited by 265 · see citing works

Caseins as rheomorphic proteins: interpretation of primary and secondary structures of the α S1 -, β- and κ-caseins

Holt, C., & Sawyer, L. (1993) · Journal of the Chemical Society Faraday Transactions · doi:10.1039/ft9938902683 · Cited by 265 · see citing works

Conformational isomerism and the diversity of antibodies.

Foote, J., & Milstein, C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10370 · Cited by 264 · see citing works

Identification of a Domain of Axin That Binds to the Serine/Threonine Protein Phosphatase 2A and a Self-binding Domain

Hsu, W., Zeng, L., & Costantini, F. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3439 · Cited by 262 · see citing works

Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease

Dev, K. K. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00140-0 · Cited by 262 · see citing works

Insufficiently dehydrated hydrogen bonds as determinants of protein interactions

Fernández, A., & Scheraga, H. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0136888100 · Cited by 258 · see citing works

Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR.

Morellet, N., Jullian, N., de ROCQUIGNY, H., Maigret, B., Darlix, J., & Roques, B. P. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05377.x · Cited by 256 · see citing works

Dynamics of Proteins in Crystals: Comparison of Experiment with Simple Models

Kundu, S., Melton, J. S., Sorensen, D. C., & Phillips, G. N. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75203-x · Cited by 254 · see citing works

An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo

Midgley, C., Desterro, J. M. P., Saville, M. K., Howard, S. F., Sparks, A., Hay, R. T., & Lane, D. P. (2000) · Oncogene · doi:10.1038/sj.onc.1203593 · Cited by 250 · see citing works

Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation

Allain, F. H. ‐., Gubser, C. C., Howe, P. W. A., Nagai, K., Neuhaus, D., & Varani, G. (1996) · Nature · doi:10.1038/380646a0 · Cited by 249 · see citing works

The C‐terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo

Lopez, P. J., Marchand, I., Joyce, S. A., & Dreyfus, M. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01465.x · Cited by 249 · see citing works

Role for ATM in DNA damage-induced phosphorylation of BRCA1.

Gatei, M. H., Scott, S. P., Filippovitch, I., Soronika, N., Lavin, M. F., Weber, B. L., & Khanna, K. K. (2000) · PubMed · Cited by 247 · see citing works

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.

Todd, M. J., Lorimer, G., & Thirumalai, D. (1996) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.93.9.4030 · Cited by 244 · see citing works

Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept

Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125924 · Cited by 1,406 · see citing works

The ensemble nature of allostery

Motlagh, H. N., Wrabl, J. O., Li, J., & Hilser, V. J. (2014) · Nature · doi:10.1038/nature13001 · Cited by 1,247 · see citing works

Understanding protein non-folding

Uversky, V. N., & Dunker, A. K. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.01.017 · Cited by 1,188 · see citing works

Flexible nets: The roles of intrinsic disorder in protein interaction networks

Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., & Uversky, V. N. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04948.x · Cited by 1,122 · see citing works

Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057 · see citing works

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 · see citing works

Intrinsic Disorder in Transcription Factors

Liu, J., Perumal, N. B., Oldfield, C. J., Su, E. W., Uversky, V. N., & Dunker, A. K. (2006) · Biochemistry · doi:10.1021/bi0602718 · Cited by 792 · see citing works

Introducing Protein Intrinsic Disorder

Habchi, J., Tompa, P., Longhi, S., & Uversky, V. N. (2014) · Chemical Reviews · doi:10.1021/cr400514h · Cited by 744 · see citing works

Analysis of Molecular Recognition Features (MoRFs)

Mohan, A., Oldfield, C. J., Predrag Radivojac, A., Vacic, V., Cortese, M. S., Dunker, A. K., & Uversky, V. N. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.07.087 · Cited by 746 · see citing works

Intrinsic Disorder and Functional Proteomics

Predrag Radivojac, A., Iakoucheva, L. M., Oldfield, C. J., Zoran Obradovic, A., Uversky, V. N., & Dunker, A. K. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.094045 · Cited by 705 · see citing works

Myelin basic protein: a multifunctional protein

Boggs, J. M. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6094-7 · Cited by 687 · see citing works

The unfoldomics decade: an update on intrinsically disordered proteins

Dunker, A. K., Oldfield, C. J., Meng, J., Romero, P. R., Yang, J. Y., Chen, J. W., Vacic, V., Zoran Obradovic, A., & Uversky, V. N. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-s2-s1 · Cited by 673 · see citing works

Prediction of Protein Binding Regions in Disordered Proteins

Mészáros, B., Simon, I., & Dosztányi, Z. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000376 · Cited by 621 · see citing works

Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners

Oldfield, C. J., Meng, J., Yang, J. Y., Yang, M. Q., Uversky, V. N., & Dunker, A. K. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-s1-s1 · Cited by 594 · see citing works

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. (2006) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0020100 · Cited by 583 · see citing works

Unusual biophysics of intrinsically disordered proteins.

Uversky, V. (2013) · Biochimica et Biophysica Acta · doi:10.1016/j.bbapap.2012.12.008 · Cited by 536 · see citing works

Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation

Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 567 · see citing works

What Macromolecular Crowding Can Do to a Protein

Kuznetsova, I. М., Константинович, Т. К., & Uversky, V. N. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151223090 · Cited by 560 · see citing works

Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life

Xue, B., Dunker, A. K., & Uversky, V. N. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2012.675145 · Cited by 557 · see citing works

Functional Anthology of Intrinsic Disorder. 1. Biological Processes and Functions of Proteins with Long Disordered Regions

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 556 · see citing works

Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics

Uversky, V. (2019) · Frontiers of Physics · doi:10.3389/fphy.2019.00010 · Cited by 449 · see citing works

A decade and a half of protein intrinsic disorder: Biology still waits for physics

Uversky, V. (2013) · Protein Science · doi:10.1002/pro.2261 · Cited by 478 · see citing works

Characterization of Molecular Recognition Features, MoRFs, and Their Binding Partners

Vacic, V., Oldfield, C. J., Mohan, A., Predrag Radivojac, A., Cortese, M. S., Uversky, V. N., & Dunker, A. K. (2007) · Journal of Proteome Research · doi:10.1021/pr0701411 · Cited by 483 · see citing works

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

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

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

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

Assessing protein disorder and induced folding

Receveur‐Brechot, V., Bourhis, J., Uversky, V. N., Canard, B., & Longhi, S. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20750 · Cited by 442 · see citing works

Intrinsically disordered proteins from A to Z

Uversky, V. N. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.04.001 · Cited by 434 · see citing works

TOP-IDP-Scale: A New Amino Acid Scale Measuring Propensity for Intrinsic Disorder

Campen, A., Williams, R. M., Brown, C. J., Meng, J., Uversky, V. N., & Dunker, A. K. (2008) · Protein and Peptide Letters · doi:10.2174/092986608785849164 · Cited by 422 · see citing works

Large Potentials of Small Heat Shock Proteins

Mymrikov, E. V., Seit‐Nebi, A. S., & Gusev, N. B. (2011) · Physiological Reviews · doi:10.1152/physrev.00023.2010 · Cited by 409 · see citing works

Local structural disorder imparts plasticity on linear motifs

Fuxreiter, M., Tompa, P., & Simon, I. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm035 · Cited by 405 · see citing works

Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins

Hilser, V. J., & Thompson, E. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700329104 · Cited by 406 · see citing works

Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life

Peng, Z., Yan, J. R., Fan, X., Mizianty, M. J., Xue, B., Wang, K., Hu, G., Uversky, V. N., & Kurgan, L. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1661-9 · Cited by 382 · see citing works

Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding

Uversky, V. N. (2009) · The Protein Journal · doi:10.1007/s10930-009-9201-4 · Cited by 360 · see citing works

Disorder and Sequence Repeats in Hub Proteins and Their Implications for Network Evolution

Dosztányi, Z., Chen, J., Dunker, A. K., Simon, I., & Tompa, P. (2006) · Journal of Proteome Research · doi:10.1021/pr060171o · Cited by 341 · see citing works

Mining α-Helix-Forming Molecular Recognition Features with Cross Species Sequence Alignments

Cheng, Y., Oldfield, C. J., Meng, J., Romero, P. R., Uversky, V. N., & Dunker, A. K. (2007) · Biochemistry · doi:10.1021/bi7012273 · Cited by 321 · see citing works

Human Transcription Factors Contain a High Fraction of Intrinsically Disordered Regions Essential for Transcriptional Regulation

Minezaki, Y., Homma, K., Kinjo, A. R., & Nishikawa, K. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.04.016 · Cited by 297 · see citing works

Intrinsic disorder in scaffold proteins: Getting more from less

Cortese, M. S., Uversky, V. N., & Dunker, A. K. (2008) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2008.05.007 · Cited by 292 · see citing works

Improving protein disorder prediction by deep bidirectional long short-term memory recurrent neural networks

Hanson, J., Yang, Y., Paliwal, K. K., & Zhou, Y. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw678 · Cited by 286 · see citing works

The alphabet of intrinsic disorder

Theillet, F., Kalmár, L., Tompa, P., Han, K., Selenko, P., Dunker, A. K., Daughdrill, G. W., & Uversky, V. N. (2013) · Intrinsically Disordered Proteins · doi:10.4161/idp.24360 · Cited by 283 · see citing works

The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments

Jeganathan, S., von Bergen, M., Mandelkow, E.-M., & Mandelkow, E. (2008) · Biochemistry · doi:10.1021/bi800783d · Cited by 286 · see citing works

Unfoldomics of human diseases: linking protein intrinsic disorder with diseases

Uversky, V. N., Oldfield, C. J., Midic, U., Xie, H. M., Xue, B., Vučetić, S., Iakoucheva, L. M., Zoran Obradovic, A., & Dunker, A. K. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-s1-s7 · Cited by 283 · see citing works

Small heat shock proteins HSP27 (HspB1), αB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death

Acunzo, J., Katsogiannou, M., & Rocchi, P. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.04.002 · Cited by 280 · see citing works

The amyloid‐β precursor protein: integrating structure with biological function

Reinhard, C., Hébert, S. S., & de Strooper, B. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600860 · Cited by 276 · see citing works

Molecular Principles of the Interactions of Disordered Proteins

Mészáros, B., Tompa, P., Simon, I., & Dosztányi, Z. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.07.004 · Cited by 277 · see citing works

Functional aspects of protein flexibility

Teilum, K., Olsen, J. G., & Kragelund, B. B. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0014-6 · Cited by 273 · see citing works

Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter

Darling, A., & Uversky, V. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00158 · Cited by 236 · see citing works

Kinetic Advantage of Intrinsically Disordered Proteins in Coupled Folding–Binding Process: A Critical Assessment of the “Fly-Casting” Mechanism

Huang, Y., & Liu, Z. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.09.010 · Cited by 266 · see citing works

The Mysterious Unfoldome: Structureless, Underappreciated, Yet Vital Part of Any Given Proteome

Uversky, V. N. (2009) · BioMed Research International · doi:10.1155/2010/568068 · Cited by 267 · see citing works

Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes

Uversky, V. N. (2010) · Chemical Society Reviews · doi:10.1039/c0cs00057d · Cited by 260 · see citing works

Close encounters of the third kind: disordered domains and the interactions of proteins

Tompa, P., Fuxreiter, M., Oldfield, C. J., Simon, I., Dunker, A. K., & Uversky, V. N. (2009) · BioEssays · doi:10.1002/bies.200800151 · Cited by 258 · see citing works

Functional Anthology of Intrinsic Disorder. 2. Cellular Components, Domains, Technical Terms, Developmental Processes, and Coding Sequence Diversities Correlated with Long Disordered Regions

Vučetić, S., Xie, H. M., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2007) · Journal of Proteome Research · doi:10.1021/pr060393m · Cited by 253 · see citing works

Intrinsically Disordered Proteins: An Overview

Trivedi, R., & Nagarajaram, H. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214050 · Cited by 253 · see citing works

Prediction of disordered regions in proteins based on the meta approach

Ishida, T., & Kinoshita, K. (2008) · Bioinformatics · doi:10.1093/bioinformatics/btn195 · Cited by 249 · see citing works

Do viral proteins possess unique biophysical features?

Tokuriki, N., Oldfield, C. J., Uversky, V. N., Berezovsky, I. N., & Tawfik, D. S. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.10.009 · Cited by 237 · see citing works

Fuzzy Complexes: A More Stochastic View of Protein Function

Fuxreiter, M., & Tompa, P. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4614-0659-4_1 · Cited by 240 · see citing works

Versatility from Protein Disorder

Babu, M. M., Kriwacki, R. W., & Pappu, R. V. (2012) · Science · doi:10.1126/science.1228775 · Cited by 235 · see citing works

Intrinsic disorder in proteins associated with neurodegenerative diseases

Vladimir, N. (2009) · Frontiers in bioscience · doi:10.2741/3594 · Cited by 234 · see citing works

Multiple Independent Binding Sites for Small-Molecule Inhibitors on the Oncoprotein c-Myc

Hammoudeh, D. I., Follis, A. V., Prochownik, E. V., & Metallo, S. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja900616b · Cited by 232 · see citing works

The structural basis of allosteric regulation in proteins

Laskowski, R. A., Gerick, F., & Thornton, J. M. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.03.019 · Cited by 231 · see citing works

Protein intrinsic disorder-based liquid–liquid phase transitions in biological systems: Complex coacervates and membrane-less organelles

Uversky, V. N. (2016) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2016.05.012 · Cited by 233 · see citing works

Intrinsically disordered proteins play diverse roles in cell signaling

Bondos, S. E., Dunker, A. K., & Uversky, V. N. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00821-7 · Cited by 222 · see citing works

Protein synthesis rate is the predominant regulator of protein expression during differentiation

Kristensen, A. R., Gsponer, J., & Foster, L. J. (2013) · Molecular Systems Biology · doi:10.1038/msb.2013.47 · Cited by 217 · see citing works

Intrinsically Disordered Proteome of Human Membrane‐Less Organelles

Darling, A. L., Liu, Y., Oldfield, C. J., & Uversky, V. N. (2017) · PROTEOMICS · doi:10.1002/pmic.201700193 · Cited by 218 · see citing works

Conditionally and Transiently Disordered Proteins: Awakening Cryptic Disorder To Regulate Protein Function

Jakob, U., Kriwacki, R. W., & Uversky, V. N. (2014) · Chemical Reviews · doi:10.1021/cr400459c · Cited by 216 · see citing works

The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation

Константинович, Т. К., Kuznetsova, I. М., & Uversky, V. N. (2010) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2010.01.003 · Cited by 215 · see citing works

What Is a B-Cell Epitope?

Regenmortel, M. H. V. V. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-450-6_1 · Cited by 214 · see citing works

Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins

Uversky, V. N. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.685859 · Cited by 212 · see citing works

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 206 · see citing works

Abundance of Intrinsic Disorder in Protein Associated with Cardiovascular Disease

Cheng, Y., LeGall, T., Oldfield, C. J., Dunker, A. K., & Uversky, V. N. (2006) · Biochemistry · doi:10.1021/bi060981d · Cited by 203 · see citing works

Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders

Uversky, V. N. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00018 · Cited by 204 · see citing works

Structural Disorder in Viral Proteins

Xue, B., Blocquel, D., Habchi, J., Uversky, A. V., Kurgan, L., Uversky, V. N., & Longhi, S. (2014) · Chemical Reviews · doi:10.1021/cr4005692 · Cited by 201 · see citing works

GRAS proteins: the versatile roles of intrinsically disordered proteins in plant signalling

Sun, X., Jones, W. T., & Rikkerink, E. H. A. (2012) · Biochemical Journal · doi:10.1042/bj20111766 · Cited by 198 · see citing works

The rules of disorder or why disorder rules

Gsponer, J. A., & Babu, M. M. (2009) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2009.03.001 · Cited by 198 · see citing works

Reflections on the construction of anion receptors

Schmidtchen, F. P. (2006) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2006.07.009 · Cited by 196 · see citing works

Liquid–Liquid Phase Separation by Intrinsically Disordered Protein Regions of Viruses: Roles in Viral Life Cycle and Control of Virus–Host Interactions

Brocca, S., Grandori, R., Longhi, S., & Uversky, V. N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239045 · Cited by 189 · see citing works

Amyloidogenesis of Natively Unfolded Proteins

Uversky, V. N. (2008) · Current Alzheimer Research · doi:10.2174/156720508784533312 · Cited by 187 · see citing works

A functionally required unfoldome from the plant kingdom: intrinsically disordered N-terminal domains of GRAS proteins are involved in molecular recognition during plant development

Sun, X., Xue, B., Jones, W. T., Rikkerink, E. H. A., Dunker, A. K., & Uversky, V. N. (2011) · Plant Molecular Biology · doi:10.1007/s11103-011-9803-z · Cited by 186 · see citing works

Structural Rationale for the Coupled Binding and Unfolding of the c-Myc Oncoprotein by Small Molecules

Follis, A. V., Hammoudeh, D. I., Wang, H., Prochownik, E. V., & Metallo, S. J. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.09.011 · Cited by 183 · see citing works

Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions

Meng, F., Uversky, V. N., & Kurgan, L. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2555-4 · Cited by 176 · see citing works

SPINE-D: Accurate Prediction of Short and Long Disordered Regions by a Single Neural-Network Based Method

Zhang, T., Faraggi, E., Xue, B., Dunker, A. K., Uversky, V. N., & Zhou, Y. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/073911012010525022 · Cited by 177 · see citing works

The roles of intrinsic disorder in protein interaction networks

Uversky, V. N. (2013) · The biomedical & life sciences collection. · doi:10.69645/bdro2797 · Cited by 175 · see citing works

Multifarious Roles of Intrinsic Disorder in Proteins Illustrate Its Broad Impact on Plant Biology

Sun, X., Rikkerink, E. H. A., Jones, W. T., & Uversky, V. N. (2013) · The Plant Cell · doi:10.1105/tpc.112.106062 · Cited by 170 · see citing works

Intrinsic Disorder in the Protein Data Bank

LeGall, T., Romero, P. R., Cortese, M. S., Uversky, V. N., & Dunker, A. K. (2007) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2007.10507123 · Cited by 167 · see citing works

SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning

Hanson, J., Paliwal, K. K., Litfin, T., & Zhou, Y. (2019) · Genomics, Proteomics &amp; Bioinformatics · doi:10.1016/j.gpb.2019.01.004 · Cited by 165 · see citing works

Molecular recognition features (MoRFs) in three domains of life

Yan, J. R., Dunker, A. K., Uversky, V. N., & Kurgan, L. (2015) · Molecular BioSystems · doi:10.1039/c5mb00640f · Cited by 164 · see citing works

A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome

Peng, Z., Oldfield, C. J., Xue, B., Mizianty, M. J., Dunker, A. K., Kurgan, L., & Uversky, V. N. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1446-6 · Cited by 159 · see citing works

Disease-Associated Mutations Disrupt Functionally Important Regions of Intrinsic Protein Disorder

Vacic, V., Markwick, P. R. L., Oldfield, C. J., Zhao, X., Haynes, C. A., Uversky, V. N., & Iakoucheva, L. M. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002709 · Cited by 157 · see citing works

Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes

Mohan, A., Sullivan, W. J., Predrag Radivojac, A., Dunker, A. K., & Uversky, V. N. (2008) · Molecular BioSystems · doi:10.1039/b719168e · Cited by 155 · see citing works

Small-molecule inhibitors of the Myc oncoprotein

Fletcher, S., & Prochownik, E. V. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.005 · Cited by 153 · see citing works

Therapeutic Targeting of Myc

Prochownik, E. V., & Vogt, P. K. (2010) · Genes & Cancer · doi:10.1177/1947601910377494 · Cited by 150 · see citing works

Depletion interactions modulate the binding between disordered proteins in crowded environments

Zosel, F., Soranno, A., Buholzer, K., Nettels, D., & Schuler, B. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921617117 · Cited by 150 · see citing works

The most important thing is the tail: Multitudinous functionalities of intrinsically disordered protein termini

Uversky, V. N. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.04.042 · Cited by 144 · see citing works

Thermodynamics of Neutral Protein Evolution

Bloom, J. D., Raval, A., & Wilke, C. O. (2006) · Genetics · doi:10.1534/genetics.106.061754 · Cited by 147 · see citing works

Protein disorder in the human diseasome: unfoldomics of human genetic diseases

Midic, U., Oldfield, C. J., Dunker, A. K., Zoran Obradovic, A., & Uversky, V. N. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-s1-s12 · Cited by 144 · see citing works

CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions

Xue, B., Oldfield, C. J., Dunker, A. K., & Uversky, V. N. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.03.070 · Cited by 142 · see citing works

Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell

Deiana, A., Forcelloni, S., Porrello, A., & Giansanti, A. (2019) · PLoS ONE · doi:10.1371/journal.pone.0217889 · Cited by 137 · see citing works

Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D2concept

Uversky, V. N. (2010) · Expert Review of Proteomics · doi:10.1586/epr.10.36 · Cited by 141 · see citing works

Conservation of Intrinsic Disorder in Protein Domains and Families: II. Functions of Conserved Disorder

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Protein Intrinsic Disorder and Human Papillomaviruses: Increased Amount of Disorder in E6 and E7 Oncoproteins from High Risk HPVs

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POODLE-L: a two-level SVM prediction system for reliably predicting long disordered regions

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Interactions via intrinsically disordered regions: What kind of motifs?

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Intrinsically disordered proteins in molecular recognition and structural proteomics

Oldfield, C. J. (2014) · IUScholarWorks (Indiana University) · doi:10.7912/c2/934

On the roles of intrinsically disordered proteins and regions in cell communication and signaling

Bondos, S. E., Dunker, A. K., & Uversky, V. N. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00774-3 · Cited by 109 · see citing works

Intrinsic disorder in scaffold proteins: Getting more from less

Cortese, M. S., Uversky, V. N., & Dunker, A. K. (2008) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2008.05.007 · Cited by 292 · see citing works

Intrinsically disordered proteins/regions and insight into their biomolecular interactions

Chakrabarti, P., & Chakravarty, D. (2022) · Biophysical Chemistry · doi:10.1016/j.bpc.2022.106769 · Cited by 90 · see citing works