The importance of being unfolded

From Levinthal to pathways to funnels

Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293 · see citing works

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Booth, D. R., Sunde, M., Bellotti, V., Robinson, C. V., Hutchinson, W. L., Fraser, P. E., Hawkins, P. N., Dobson, C. M., Radford, S. E., Blake, C., et al. (1997) · Nature · doi:10.1038/385787a0 · Cited by 1,049 · 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

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

The concept of a random coil: Residual structure in peptides and denatured proteins

Smith, L. J., Fiebig, K. M., Schwalbe, H., & Dobson, C. M. (1996) · Folding and Design · doi:10.1016/s1359-0278(96)00046-6 · Cited by 350 · see citing works

Comparison of the Backbone Dynamics of a Folded and an Unfolded SH3 Domain Existing in Equilibrium in Aqueous Buffer

Farrow, N. A., Zhang, O., Forman-Kay, J. D., & Kay, L. E. (1995) · Biochemistry · doi:10.1021/bi00003a021 · Cited by 297 · see citing works

The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, σ28

Daughdrill, G. W., Chadsey, M. S., Karlinsey, J. E., Hughes, K. T., & Dahlquist, F. W. (1997) · Nature Structural Biology · doi:10.1038/nsb0497-285 · Cited by 196 · see citing works

Structural Characterization of Folded and Unfolded States of an SH3 Domain in Equilibrium in Aqueous Buffer

Zhang, O., & Forman-Kay, J. D. (1995) · Biochemistry · doi:10.1021/bi00020a025 · Cited by 174 · see citing works

The Bacterial Flagellar Motor

Schuster, S. C., & Khan, S. (1994) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.23.060194.002453 · Cited by 114 · see citing works

Conformational Changes in the Fibronectin Binding MSCRAMMs Are Induced by Ligand Binding

House‐Pompeo, K., Xu, Y., Joh, D., Speziale, P., & Höök, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1379 · Cited by 99 · see citing works

The Structure, Stability, and Folding Process of Amyloidogenic Mutant Human Lysozyme

Funahashi, J., Takano, K., Ogasahara, K., Yamagata, Y., & Yutani, K. (1996) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021544 · Cited by 87 · 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

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

Helix nucleation kinetics from molecular simulations in explicit solvent

Hummer, G., Garcı́a, A. E., & Garde, S. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20010101)42:1 · Cited by 107 · 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

Electrochemical interrogation of conformational changes as a reagentless method for the sequence-specific detection of DNA

Fan, C., Plaxco, K. W., & Heeger, A. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1633515100 · Cited by 1,046 · 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

Intrinsic protein disorder in complete genomes.

Dunker, A. K., Zoran Obradovic, A., Romero, P. R., Garner, E. C., & Brown, C. J. (2000) · PubMed · Cited by 661 · 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

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

Folding-Based Electrochemical Biosensors: The Case for Responsive Nucleic Acid Architectures

Lubin, A. A., & Plaxco, K. W. (2010) · Accounts of Chemical Research · doi:10.1021/ar900165x · Cited by 506 · 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

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

The fundamentals of protein folding: bringing together theory and experiment

Dobson, C. M., & Karplus, M. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80012-8 · Cited by 410 · see citing works

Protein disorder and the evolution of molecular recognition: theory, predictions and observations.

Dunker, A. K., Garner, E. C., Guilliot, S., Romero, P. R., Albrecht, K., Hart, J., Zoran Obradovic, A., Kissinger, C. R., & Villafranca, J. E. (1998) · PubMed · Cited by 378 · 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

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

THE ANTI-SIGMA FACTORS

Hughes, K. T., & Mathee, K. (1998) · Annual Review of Microbiology · doi:10.1146/annurev.micro.52.1.231 · Cited by 341 · 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

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

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

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Harauz, G., Ishiyama, N., Hill, C. M. D., Bates, I. R., Libich, D. S., & Farès, C. (2004) · Micron · doi:10.1016/j.micron.2004.04.005 · Cited by 256 · see citing works

THE PROTEIN NON-FOLDING PROBLEM: AMINO ACID DETERMINANTS OF INTRINSIC ORDER AND DISORDER

Williams, R. M., Zoran Obradovic, A., Mathura, V. S., Braun, W. A., Garner, E. C., Young, J. K., Takayama, S., Brown, C. J., & Dunker, A. K. (2000) · Pacific Symposium on Biocomputing (PSB) · doi:10.1142/9789814447362_0010 · Cited by 244 · see citing works

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 · see citing works

Titin Extensibility In Situ: Entropic Elasticity of Permanently Folded and Permanently Unfolded Molecular Segments

Trombitás, K., Greaser, M. L., Labeit, S., Jin, J., Kellermayer, M., Helmes, M., & Granzier, H. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.853 · Cited by 239 · see citing works

Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis

Jaikaran, E. T. A. S., Higham, C. E., Serpell, L. C., Zurdo, J., Gross, M., Clark, A., & Fraser, P. E. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4593 · Cited by 236 · 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

Methionine oxidation inhibits fibrillation of human α‐synuclein in vitro

Uversky, V. N., Yamin, G., Souillac, P. O., Goers, J. W. F., Glaser, C. B., & Fink, A. L. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02638-8 · Cited by 222 · see citing works

Equilibrium NMR studies of unfolded and partially folded proteins

Dyson, H. J., & Wright, P. E. (1998) · Nature Structural Biology · doi:10.1038/739 · Cited by 207 · see citing works

Predicting Binding Regions within Disordered Proteins.

Garner, E. C., Romero, P. R., Dunker, K., Brown, C. J., & Zoran Obradovic, A. (1999) · PubMed · Cited by 182 · see citing works

Nitration inhibits fibrillation of human α‐synuclein in vitro by formation of soluble oligomers

Yamin, G., Uversky, V. N., & Fink, A. L. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00367-3 · Cited by 167 · 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

Toward a taxonomy of the denatured state: Small angle scattering studies of unfolded proteins

Millett, I. S., Doniach, S., & Plaxco, K. W. (2002) · Advances in protein chemistry · doi:10.1016/s0065-3233(02)62009-1 · Cited by 159 · see citing works

A simple model for polyproline II structure in unfolded states of alanine‐based peptides

Pappu, R. V., & Rose, G. D. (2002) · Protein Science · doi:10.1110/ps.0217402 · Cited by 154 · see citing works

Molecular Mechanics of Cardiac Titin's PEVK and N2B Spring Elements

Watanabe, K., Nair, P., Labeit, D., Kellermayer, M., Greaser, M. L., Labeit, S., & Granzier, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200356200 · Cited by 135 · see citing works

4E Binding Proteins Inhibit the Translation Factor eIF4E without Folded Structure

Fletcher, C. M., Manson, A. L., Gingras, A., Li, H., Matsuo, H., Sonenberg, N., & Wagner, G. (1998) · Biochemistry · doi:10.1021/bi972494r · Cited by 121 · see citing works

Regulation of the Cystic Fibrosis Transmembrane Conductance Regulator Cl− Channel by Its R Domain

Ostedgaard, L. S., Baldursson, Ó., & Welsh, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100001200 · Cited by 121 · see citing works

Defining the molecular basis of Arf and Hdm2 interactions

Bothner, B. B., Lewis, W. S., DiGiammarino, E. L., Weber, J. D., Bothner, S. J., & Kriwacki, R. W. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5110 · Cited by 122 · see citing works

Polycation‐induced oligomerization and accelerated fibrillation of human α‐synuclein in vitro

Goers, J. W. F., Uversky, V. N., & Fink, A. L. (2003) · Protein Science · doi:10.1110/ps.0230903 · Cited by 118 · see citing works

A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution

Ostedgaard, L. S., Baldursson, Ó., Vermeer, D. W., Welsh, M. J., & Robertson, A. D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100588797 · Cited by 118 · see citing works

Intrinsic Disorder, Protein–Protein Interactions, and Disease

Uversky, V. N. (2017) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2017.06.005 · Cited by 118 · see citing works

Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo

Fonin, A. V., Darling, A. L., Kuznetsova, I. М., Константинович, Т. К., & Uversky, V. N. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2894-9 · Cited by 107 · see citing works

Reconciling Observations of Sequence-Specific Conformational Propensities with the Generic Polymeric Behavior of Denatured Proteins

Tran, H. T., Wang, X., & Pappu, R. V. (2005) · Biochemistry · doi:10.1021/bi050196l · Cited by 107 · see citing works

Protein disorder prediction by condensed PSSM considering propensity for order or disorder

Su, C.-T., Chen, C., & Ou, Y. (2006) · BMC Bioinformatics · doi:10.1186/1471-2105-7-319 · Cited by 101 · see citing works

High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins

Kamatari, Y. O. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.010 · Cited by 94 · see citing works

Proteome-wide analysis of human disease mutations in short linear motifs: neglected players in cancer?

Uyar, B., Weatheritt, R. J., Dinkel, H., Davey, N. E., & Gibson, T. J. (2014) · Molecular BioSystems · doi:10.1039/c4mb00290c · Cited by 87 · see citing works

Independent Ligand-Induced Folding of the RNA-Binding Domain and Two Functionally Distinct Antitermination Regions in the Phage λ N Protein

Mogridge, J., Legault, P., Li, J., Oene, M. D. V., Kay, L. E., & Greenblatt, J. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80027-1 · Cited by 88 · see citing works

Unfolded, yes, but random? Never!

Plaxco, K. W., & Gross, M. (2001) · Nature Structural Biology · doi:10.1038/90349 · Cited by 87 · see citing works

Proline Zwitterion Dynamics in Solution, Glass, and Crystalline State

Kapitán, J., Baumruk, V., Kopecký, V., Pohl, R., & Bouř, P. (2006) · Journal of the American Chemical Society · doi:10.1021/ja062958l · Cited by 85 · see citing works

Regulated unfolding of proteins in signaling

Mitrea, D. M., & Kriwacki, R. W. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.02.024 · Cited by 81 · see citing works

The interaction of eIF4E with 4E‐BP1 is an induced fit to a completely disordered protein

Fletcher, C., & Wagner, G. (1998) · Protein Science · doi:10.1002/pro.5560070720 · Cited by 86 · see citing works

Reduction in Structural Disorder and Functional Complexity in the Thermal Adaptation of Prokaryotes

Burra, P. V. L. S., Kalmár, L., & Tompa, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012069 · Cited by 79 · see citing works

Further Biochemical and Kinetic Characterization of Human Eukaryotic Initiation Factor 4H

Richter, N. J., Rogers, G. W., Hensold, J. O., & Merrick, W. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35415 · Cited by 77 · see citing works

Sequence-Specific Resonance Assignment of Soluble Nonglobular Proteins by 7D APSY-NMR Spectroscopy

Hiller, S., Wasmer, C., Wider, G., & Kurt Wüthrich, A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072564+ · Cited by 75 · see citing works

Computational Prediction of MoRFs, Short Disorder-to-order Transitioning Protein Binding Regions

Katuwawala, A., Peng, Z., Yang, J., & Kurgan, L. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.03.013 · Cited by 73 · see citing works

Intrinsically Disordered Proteins: Where Computation Meets Experiment

Burger, V., Gurry, T., & Stultz, C. M. (2014) · Polymers · doi:10.3390/polym6102684 · Cited by 68 · see citing works

High-resolution structure of an archaeal zinc ribbon defines a general architectural motif in eukaryotic RNA polymerases

Wang, B., Jones, D. N. M., Kaine, B. P., & Weiss, M. A. (1998) · Structure · doi:10.1016/s0969-2126(98)00058-6 · Cited by 69 · see citing works

Nanometer‐Sized Gold‐Loaded Gelatin/Silica Nanocapsules

Liu, S., Zhang, Z., & Han, M. (2005) · Advanced Materials · doi:10.1002/adma.200500124 · Cited by 67 · see citing works

Dynamics of Unfolded Proteins: Incorporation of Distributions of Correlation Times in the Model Free Analysis of NMR Relaxation Data

Buevich, A. V., & Baum, J. (1999) · Journal of the American Chemical Society · doi:10.1021/ja9910412 · Cited by 55 · see citing works

Nonrandom Structure in the Urea-UnfoldedEscherichia coliOuter Membrane Protein X (OmpX)

Tafer, H., Hiller, S., Hilty, C., Fernández, C. F., & Kurt Wüthrich, A. (2004) · Biochemistry · doi:10.1021/bi0356606 · Cited by 48 · see citing works

Polymorphism of β2-Microglobulin Amyloid Fibrils Manifested by Ultrasonication-enhanced Fibril Formation in Trifluoroethanol

Chatani, E., Yagi, H., Naiki, H., & Goto, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.333310 · Cited by 45 · see citing works

Protein intrinsic disorder within the Potyvirus genus: from proteome-wide analysis to functional annotation

Charon, J., Theil, S., Nicaise, V., & Michon, T. (2015) · Molecular BioSystems · doi:10.1039/c5mb00677e · Cited by 45 · see citing works

A Complete Set of NMR Chemical Shifts and Spin−Spin Coupling Constants for l -Alanyl- l -alanine Zwitterion and Analysis of Its Conformational Behavior

Bouř, P., Buděšı́nský, M., Špirko, V., Kapitán, J., Šebestı́k, J., & Sychrovský, V. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0552343 · Cited by 41 · see citing works

Intrinsically disordered proteins: Chronology of a discovery

Uversky, V. N., & Kulkarni, P. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106694 · Cited by 41 · see citing works

Refolding and structural characterization of the human p53 tumor suppressor protein

Bell, S. J., Hansen, S., & Büchner, J. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00011-x · Cited by 40 · see citing works

Understanding the interactability of chikungunya virus proteinsviamolecular recognition feature analysis

Singh, A., Kumar, A., Uversky, V. N., & Giri, R. (2018) · RSC Advances · doi:10.1039/c8ra04760j · Cited by 38 · see citing works

Structure, Orientation, and Dynamics of the C-Terminal Hexapeptide of LRAP Determined Using Solid-State NMR

Shaw, W. J., & Ferris, K. F. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp808012g · Cited by 38 · see citing works

A gradual disruption of tight side-chain packing: 2D 1H-NMR characterization of acid-induced unfolding of CHABII.

Song, J., Ménèz, A., Jamin, N., Gilquin, B., & Vita, C. (1999) · Nature Structural Biology · doi:10.1038/5815 · Cited by 38 · see citing works

Intelligent Data Analysis for Protein Disorder Prediction

Romero, P. R., Zoran Obradovic, A., & Dunker, A. K. (2000) · Artificial Intelligence Review · doi:10.1023/a:1006678623815 · Cited by 38 · see citing works

Structural dissection of alkaline‐denatured pepsin

Kamatari, Y. O., Dobson, C. M., & Konno, T. (2003) · Protein Science · doi:10.1110/ps.0219903 · Cited by 36 · see citing works

Functional unfoldomics: Roles of intrinsic disorder in protein (multi)functionality

Uversky, V. N. (2023) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2023.11.001 · Cited by 29 · see citing works

Characterization of NMR relaxation-active motions of a partially folded A-state analogue of ubiquitin

Prompers, J. J., Scheurer, C., & Brüschweiler, R. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4353 · Cited by 29 · see citing works

M1 RNA is important for the in-cell solubility of its cognate C5 protein: Implications for RNA-mediated protein folding

Son, A., Choi, S. I., Han, G., & Seong, B. L. (2015) · RNA Biology · doi:10.1080/15476286.2015.1096487 · Cited by 28 · see citing works

Functions of short lifetime biological structures at large: the case of intrinsically disordered proteins

Uversky, V. N. (2018) · Briefings in Functional Genomics · doi:10.1093/bfgp/ely023 · Cited by 26 · see citing works

New technologies to analyse protein function: an intrinsic disorder perspective

Uversky, V. (2020) · F1000Research · doi:10.12688/f1000research.20867.1 · Cited by 20 · see citing works

Testing the transferability of a coarse-grained model to intrinsically disordered proteins

Rutter, G. O., Brown, A. H., Quigley, D., Walsh, T. R., & Allen, M. P. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp05652g · Cited by 22 · see citing works

Back to the Future: Nuclear Magnetic Resonance and Bioinformatics Studies on Intrinsically Disordered Proteins

Dunker, A. K., & Oldfield, C. J. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-20164-1_1 · Cited by 21 · see citing works

NMR of unfolded proteins

Chatterjee, A., Kumar, A., Chugh, J., Srivastava, S., Bhavesh, N. S., & Hosur, R. V. (2005) · Journal of Chemical Sciences · doi:10.1007/bf02704356 · Cited by 20 · see citing works

Structured proteins and proteins with intrinsic disorder

Serdyuk, I. N. (2007) · Molecular Biology · doi:10.1134/s0026893307020082 · Cited by 19 · see citing works

Automated Projection Spectroscopy and Its Applications

Hiller, S., & Wider, G. (2011) · Topics in current chemistry · doi:10.1007/128_2011_189 · Cited by 18 · see citing works

Protein Folding and Evolution are Driven by the Maxwell Demon Activity of Proteins

Balbín, A., & Andrade, E. (2004) · Acta Biotheoretica · doi:10.1023/b:acbi.0000043441.74099.0c · Cited by 16 · see citing works

Isolation of chloroform-resistant mutants of filamentous phage: localization in models of phage structure

Oh, J. S., Davies, D. R., Lawson, J. D., Arnold, G. E., & Dunker, A. K. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2599 · Cited by 15 · see citing works

Molecular Interactions of the Gβ Binding Domain of the Ste20p/PAK Family of Protein Kinases

Song, J., Chen, Z., Xu, P., Gingras, R., Ng, A., Leberer, E., Thomas, D. Y., & Ni, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103449200 · Cited by 15 · see citing works

Protein conformational transitions coupled to binding in molecular recognition of unstructured proteins: Deciphering the effect of intermolecular interactions on computational structure prediction of the p27Kip1 protein bound to the cyclin A–cyclin‐dependent kinase 2 complex

Verkhivker, G. M. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20351 · Cited by 15 · see citing works

Origins of globular structure in proteins

Doi, N., & Yanagawa, H. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00674-7 · Cited by 14 · see citing works

Quantitative proteome-based guidelines for intrinsic disorder characterization

Vincent, M. P., Whidden, M. E., & Schnell, S. D. (2016) · Biophysical Chemistry · doi:10.1016/j.bpc.2016.03.005 · Cited by 11 · see citing works

Expression, Purification and Structural Analysis of a Fibrinogen Receptor FbsA from Streptococcus agalactiae

Ragunathan, P. T., & Ponnuraj, K. (2011) · The Protein Journal · doi:10.1007/s10930-011-9317-1 · Cited by 11 · see citing works

Why are we Interested in the Unfolded Peptides and Proteins?

Uversky, V. N., & Dunker, A. K. (2012) · doi:10.1002/9781118183373.ch1 · Cited by 11 · see citing works

The N-terminal domain of elastin-binding protein of Staphylococcus aureus changes its secondary structure in a membrane-mimetic environment

Nakakido, M., Tanaka, Y., & Tsumoto, K. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvm131 · Cited by 9 · see citing works

Functional diversity of intrinsically disordered proteins and their structural heterogeneity: Protein structure-function continuum

Uversky, V. N. (2025) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.11.006 · Cited by 8 · see citing works

Partially Folded Bovine Pancreatic Trypsin Inhibitor Analogues Attain Fully Native Structures when Co-Crystallized with S195A Rat Trypsin

Getun, I. V., Brown, C. K., Tulla‐Puche, J., Ohlendorf, D. H., Woodward, C. K., & Bárány, G. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.084 · Cited by 7 · see citing works

What's in the BAGs? Intrinsic disorder angle of the multifunctionality of the members of a family of chaperone regulators

Marzullo, L., Turco, M. C., & Uversky, V. N. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30123 · Cited by 8 · see citing works

DSC Studies of a Family of Natively Disordered Fragments from Escherichia coli Thioredoxin: Surface Burial in Intrinsic Coils

Mendoza, C., Figueirido, F. E., & Tasayco, M. L. (2003) · Biochemistry · doi:10.1021/bi0271906 · Cited by 7 · see citing works

Protein conformational transitions coupled to binding in molecular recognition of unstructured proteins: Hierarchy of structural loss from all‐atom Monte Carlo simulations of p27Kip1 unfolding–unbinding and structural determinants of the binding mechanism

Verkhivker, G. M. (2004) · Biopolymers · doi:10.1002/bip.20149 · Cited by 7 · see citing works

Ab initio- and density-functional studies of conformational behaviour of N-formylmethionine in gaseous phase

Das, G., & Mandal, S. (2014) · Chemical Papers · doi:10.2478/s11696-014-0614-y · Cited by 6 · see citing works

Protein Intrinsic Disorder and Adaptation to Extreme Environments: Resilience of Chaos

Uversky, V. N. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169547 · Cited by 5 · see citing works

Zwitterionic conformers of pyrrolysine and their interactions with metal ions—a theoretical study

Das, G. (2013) · Journal of Molecular Modeling · doi:10.1007/s00894-013-1829-5 · Cited by 5 · see citing works

Analysis of Conformational Variation in Macromolecular Structural Models

Srivastava, S. K., Gayathri, S., Manjasetty, B. A., & Gopal, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039993 · Cited by 5 · see citing works

Rotational aspects of non-ionized creatine in the gas phase

Das, G. (2014) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-014-1210-0 · Cited by 5 · see citing works

Conformational States and Protein Stability from a Proteomic Perspective

Prosinecki, V., Faísca, P. F. N., & Gomes, C. M. (2007) · Current Proteomics · doi:10.2174/157016407781387375 · Cited by 5 · see citing works

Binding of a substrate (“lock and key”) and conformational adaption (“induced fit”) are different stages of enzyme action

Gupta, M. N., Tripathi, T., & Uversky, V. N. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21809-5.00017-x · Cited by 4 · 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

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 674 · see citing works

intrinsically disordered and of unfolded proteins

Varadi, M., Kosol, S., Lebrun, P., Valentini, E., Blackledge, M. J., Dunker, A. K., Felli, I. C., Forman-Kay, J. D., Kriwacki, R. W., Pierattelli, R., et al. (2013)

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

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