Fuzzy Complexes: A More Stochastic View of Protein Function

Translating the Histone Code

Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756

Crystal structure of the nucleosome core particle at 2.8 Å resolution

Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466

Protein Misfolding, Functional Amyloid, and Human Disease

Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968

Intrinsically unstructured proteins

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

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

Intrinsic Disorder and Protein Function

Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731

Electrostatic Basis for Enzyme Catalysis

Warshel, A., Sharma, P. K., Kato, M., Xiang, Y., Liu, H., & Olsson, M. H. M. (2006) · Chemical Reviews · doi:10.1021/cr0503106 · Cited by 1,487

The importance of intrinsic disorder for protein phosphorylation

Iakoucheva, L. M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh253 · Cited by 1,429

Integrating mRNA Processing with Transcription

Proudfoot, N. J., Furger, A., & Dye, M. J. (2002) · Cell · doi:10.1016/s0092-8674(02)00617-7 · Cited by 1,084

Single-Molecule FRET Reveals the Native-State Dynamics of the IκBα Ankyrin Repeat Domain

Lamboy, J. A., Kim, H., Dembinski, H. E., Ha, T., & Komives, E. A. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.04.015 · Cited by 27

Conformational Plasticity of Hepatitis C Virus Core Protein Enables RNA-Induced Formation of Nucleocapsid-like Particles

Holmstrom, E. D., Nettels, D., & Schuler, B. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.10.010 · Cited by 26

Fluorescence Depolarization Kinetics to Study the Conformational Preference, Structural Plasticity, Binding, and Assembly of Intrinsically Disordered Proteins

Majumdar, A., & Mukhopadhyay, S. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.09.031 · Cited by 24

Investigation of the impact of PTMs on the protein backbone conformation

Craveur, P., Narwani, T., Rebehmed, J., & de Brevern, A. G. (2019) · Amino Acids · doi:10.1007/s00726-019-02747-w · Cited by 26

Modulation of Correlated Segment Fluctuations in IDPs upon Complex Formation as an Allosteric Regulatory Mechanism

Beier, A., Schwarz, T. C., Kurzbach, D., Platzer, G., Tribuzio, F., & Konrat, R. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.04.035 · Cited by 26

Japanese encephalitis virus – exploring the dark proteome and disorder–function paradigm

Bhardwaj, T., Saumya, K. U., Kumar, P., Sharma, N., Gadhave, K., Uversky, V. N., & Giri, R. (2020) · FEBS Journal · doi:10.1111/febs.15427 · Cited by 25

On the Roles of Protein Intrinsic Disorder in the Origin of Life and Evolution

Uversky, V. N. (2024) · Life · doi:10.3390/life14101307 · Cited by 24

Structural features and interfacial properties of WH2, β‐thymosin domains and other intrinsically disordered domains in the regulation of actin cytoskeleton dynamics

Renault, L., Deville, C., & van Heijenoort, C. (2013) · Cytoskeleton · doi:10.1002/cm.21140 · Cited by 27

Intrinsic disorder and metal binding in UreG proteins from Archae hyperthermophiles: GTPase enzymes involved in the activation of Ni(II) dependent urease

Miraula, M., Ciurli, S., & Zambelli, B. (2015) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-015-1261-7 · Cited by 24

Recognition of the HIV Capsid by the TRIM5α Restriction Factor Is Mediated by a Subset of Pre-Existing Conformations of the TRIM5α SPRY Domain

Kovalskyy, D. B., & Ivanov, D. N. (2014) · Biochemistry · doi:10.1021/bi4014962 · Cited by 24

Protein plasticity driven by disorder and collapse governs the heterogeneous binding of CytR to DNA

Munshi, S., Gopi, S., Subramanian, S., Campos, L. A., & Naganathan, A. N. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky176 · Cited by 23

Intrinsically disordered proteins and phenotypic switching: Implications in cancer

Kulkarni, V., & Kulkarni, P. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.03.013 · Cited by 23

Interaction of Nonstructural Protein 5A of the Hepatitis C Virus with Src Homology 3 Domains Using Noncanonical Binding Sites

Schwarten, M., Sólyom, Z., Feuerstein, S., Aladağ, A., Hoffmann, S., Willbold, D., & Brutscher, B. (2013) · Biochemistry · doi:10.1021/bi400363v · Cited by 23

Structural Characterization of N-WASP Domain V Using MD Simulations with NMR and SAXS Data

Chan-Yao-Chong, M., Deville, C., Pinet, L., van Heijenoort, C., Christiane, D. D., & Ha‐Duong, T. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.02.015 · Cited by 22

Structure and Functional Characterization of the Conserved JAK Interaction Region in the Intrinsically Disordered N-Terminus of SOCS5

Chandrashekaran, I. R., Mohanty, B., Linossi, E. M., Dagley, L. F., Leung, E. W. W., Murphy, J. M., Babon, J. J., Nicholson, S. E., & Norton, R. S. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00619 · Cited by 21

Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments

Graether, S. P. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00118 · Cited by 20

Functional benefit of structural disorder for the replication of measles, Nipah and Hendra viruses

Gondelaud, F., Pesce, G., Nilsson, J. F., Bignon, C., Ptchelkine, D., Gerlier, D., Mathieu, C., & Longhi, S. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220045 · Cited by 21

The Robustness of a Signaling Complex to Domain Rearrangements Facilitates Network Evolution

Sato, P. M., Yoganathan, K., Jung, J. H., & Peisajovich, S. G. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1002012 · Cited by 18

Conformational editing of intrinsically disordered protein by α-methylation

Bauer, V., Schmidtgall, B., Gógl, G., Dolenc, J., Ősz, J., Nominé, Y., Kostmann, C., Cousido-Siah, A., Mitschler, A., Rochel, N., et al. (2020) · Chemical Science · doi:10.1039/d0sc04482b · Cited by 20

‘Nonlinear’ Biochemistry of Nucleosome Detergents

Erkine, A. M. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.09.006 · Cited by 19

The Sec61/SecY complex is inherently deficient in translocating intrinsically disordered proteins

Gonsberg, A., Jung, S., Ulbrich, S., Origi, A., Ziska, A., Baier, M., Koch, H., Zimmermann, R., Winklhofer, K. F., & Tatzelt, J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.788067 · Cited by 18

Functions of intrinsically disordered proteins through evolutionary lenses

Pajkos, M., & Dosztányi, Z. (2021) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2021.06.017 · Cited by 19

Dynamic footprint of sequestration in the molecular fluctuations of osteopontin

Lenton, S., Seydel, T., Nylander, T., Holt, C., Haertlein, M., Teixeira, S. C. M., & Zaccaı̈, G. (2015) · Journal of The Royal Society Interface · doi:10.1098/rsif.2015.0506 · Cited by 18

Functionality of intrinsic disorder in tumor necrosis factor‐α and its receptors

Uversky, V. N., El‐Baky, N. A., El‐Fakharany, E. M., Sabry, A., Mattar, E. H., Uversky, A. V., & Redwan, E. M. M. M. (2017) · FEBS Journal · doi:10.1111/febs.14182 · Cited by 18

How to drug a cloud? Targeting intrinsically disordered proteins

Uversky, V. N. (2024) · Pharmacological Reviews · doi:10.1124/pharmrev.124.001113 · Cited by 22

Intrinsic, Functional, and Structural Properties of β-Thymosins and β-Thymosin/WH2 Domains in the Regulation and Coordination of Actin Self-Assembly Dynamics and Cytoskeleton Remodeling

Renault, L. (2016) · Vitamins and hormones · doi:10.1016/bs.vh.2016.04.006 · Cited by 17

Orchestration of algal metabolism by protein disorder

Launay, H., Receveur-Bréchot, V., Carrière, F., & Gontero, B. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.108070 · Cited by 16

The α-Helical Structure of Prodomains Promotes Translocation of Intrinsically Disordered Neuropeptide Hormones into the Endoplasmic Reticulum

Dirndorfer, D., Seidel, R. P., Nimrod, G., Miesbauer, M., Ben‐Tal, N., Engelhard, M., Zimmermann, R., Winklhofer, K. F., & Tatzelt, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.430264 · Cited by 16

The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complexin vitro

Avila, M. D., Vassall, K. A., Smith, G. S. T., Bamm, V. V., & Harauz, G. (2014) · Bioscience Reports · doi:10.1042/bsr20140149 · Cited by 16

Activation of gene expression by detergent-like protein domains

Broyles, B. K., Gutierrez, A. T., Maris, T. P., Coil, D. A., Wagner, T. M., Wang, X., Kihara, D., Class, C. A., & Erkine, A. M. (2021) · iScience · doi:10.1016/j.isci.2021.103017 · Cited by 14

Disordered regions tune order in chromatin organization and function

Shukla, S., Agarwal, P., & Kumar, A. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106716 · Cited by 16

Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum

Burger, V., Nolasco, D. O., & Stultz, C. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.692590 · Cited by 17

Engineering Order and Cooperativity in a Disordered Protein

Munshi, S., Subramanian, S., Ramesh, S., Golla, H., Divakar, K., Madhurima, K., Campos, L. A., Sekhar, A., & Naganathan, A. N. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00182 · Cited by 15

Protein interactions: anything new?

Barrera-Vilarmau, S., Teixeira, J. M. C., & Fuxreiter, M. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220044 · Cited by 15

Side chain electrostatic interactions and pH‐dependent expansion of the intrinsically disordered, highly acidic carboxyl‐terminus of γ‐tubulin

Payliss, B. J., Vogel, J., & Mittermaier, A. (2019) · Protein Science · doi:10.1002/pro.3618 · Cited by 15

A new type of flexible CP12 protein in the marine diatom Thalassiosira pseudonana

Shao, H., Huang, W., Avilán, L., Receveur‐Brechot, V., Puppo, C., Puppo, R., Lebrun, R., Gontero, B., & Launay, H. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00718-x · Cited by 15

Molecular Dynamics of "Fuzzy" Transcriptional Activator-Coactivator Interactions

Scholes, N. S., & Weinzierl, R. O. J. (2016) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004935 · Cited by 15

Network representation of protein interactions: Theory of graph description and analysis

Kurzbach, D. (2016) · Protein Science · doi:10.1002/pro.2963 · Cited by 15

Structural determinants governing S100A4‐induced isoform‐selective disassembly of nonmuscle myosin II filaments

Kiss, B., Kalmár, L., Nyitray, L., & Pál, G. (2016) · FEBS Journal · doi:10.1111/febs.13728 · Cited by 14

The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N

Johnson, C., Solovyova, A. S., Hecht, O., Macdonald, C., Waller, H., Grossmann, J. G., Moore, G. R., & Lakey, J. H. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.08.030 · Cited by 14

Prediction and Analysis of Intrinsically Disordered Proteins

Punta, M., Simon, I., & Dosztányi, Z. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2230-7_3 · Cited by 14

Transient antibody-antigen interactions mediate the strain-specific recognition of a conserved malaria epitope

Krishnarjuna, B., Sugiki, T., Morales, R. A. V., Seow, J., Fujiwara, T., Wilde, K. L., Norton, R. S., & MacRaild, C. A. (2018) · Communications Biology · doi:10.1038/s42003-018-0063-1 · Cited by 14

Current concepts of casein and casein micelle structure, interactions, and dynamics

Carver, J. A., & Holt, C. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15836-0.00002-0 · Cited by 13

Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6

Russo, L., Giller, K., Pfitzner, E., Griesinger, C., & Becker, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-17088-5 · Cited by 13

Modulation of the HIV nucleocapsid dynamics finely tunes its RNA-binding properties during virion genesis

Mouhand, A., Belfetmi, A., Catala, M., Larue, V., Zargarian, L., Brachet, F., Gorelick, R. J., van Heijenoort, C., Mirambeau, G., Barraud, P., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky612 · Cited by 16

The protein disorder cycle

Uversky, V. N. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00853-2 · Cited by 10

Cellular ATP Levels Determine the Stability of a Nucleotide Kinase

Brylski, O., Shrestha, P., Gnutt, P., Gnutt, D., Mueller, J. W., & Ebbinghaus, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.790304 · Cited by 13

Lighting up Nobel Prize-winning studies with protein intrinsic disorder

Piersimoni, L., el Malek, M. A., Bhatia, T., Bender, J., Brankatschk, C., Sánchez, J. C., Dayhoff, G. W., Ianni, A. D., Parra, J. O. F., Martínez, D. G., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04468-y · Cited by 11

Intrinsic disorder perspective of an interplay between the renin-angiotensin-aldosterone system and SARS-CoV-2

Elrashdy, F., Redwan, E. M., & Uversky, V. N. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104510 · Cited by 11

High avidity drives the interaction between the streptococcal C1 phage endolysin, PlyC, with the cell surface carbohydrates of Group A Streptococcus

Broendum, S. S., Williams, D. E., Hayes, B. K., Kraus, F., Fodor, J., Clifton, B. E., Volbeda, A. G., Codée, J. D. C., Riley, B. T., Drinkwater, N., et al. (2021) · Molecular Microbiology · doi:10.1111/mmi.14719 · Cited by 11

NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B

Bessa, L. M., Launay, H. M. M., Dujardin, M., Cantrelle, F., Lippens, G. M., Landrieu, I., Schneider, R., & Hanoulle, X. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.813766 · Cited by 11

Functional in vitro diversity of an intrinsically disordered plant protein during freeze–thawing is encoded by its structural plasticity

Hernández-Sánchez, I. E., Rindfleisch, T., Alpers, J., Dulle, M., Garvey, C. J., Knox‐Brown, P., Miettinen, M. S., Nagy, G., Pusterla, J. M., Rekas, A., et al. (2024) · Protein Science · doi:10.1002/pro.4989 · Cited by 10

Intrinsic Disorder in the Host Proteins Entrapped in Rabies Virus Particles

Ashraf, H. N., & Uversky, V. N. (2024) · Viruses · doi:10.3390/v16060916 · Cited by 9

Identification of a novel transcript isoform of the TTLL12 gene in human cancers

Wen, R., Yingying, X., Zhang, Y., Yang, M., Lin, Y., & Tang, J. (2016) · Oncology Reports · doi:10.3892/or.2016.5135 · Cited by 10

The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure

Uversky, V. N., & Dunker, A. K. (2013) · F1000 Biology Reports · doi:10.3410/b5-01 · Cited by 10

Native disorder mediates binding of dynein to NudE and dynactin

Barbar, E. J. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120180 · Cited by 10

Dynamic Allostery in PLCγ1 and Its Modulation by a Cancer Mutation Revealed by MD Simulation and NMR

Koss, H., Bunney, T. D., Esposito, D., Martins, M., Katan, M., & Driscoll, P. C. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.05.031 · Cited by 10

Intrinsic Disorder in Human Proteins Encoded by Core Duplicon Gene Families

Bibber, N. W. V., Haerle, C., Khalife, R., Dayhoff, G. W., & Uversky, V. N. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c07676 · Cited by 9

Deciphering the cause of evolutionary variance within intrinsically disordered regions in human proteins

Banerjee, S., Chakraborty, S., & De, R. K. (2016) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2016.1143877 · Cited by 9

Experimental Characterization of Fuzzy Protein Assemblies: Interactions of Paramyxoviral NTAIL Domains With Their Functional Partners

Troilo, F., Bignon, C., Gianni, S., Fuxreiter, M., & Longhi, S. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.08.006 · Cited by 9

The Disordered Cellular Multi-Tasker WIP and Its Protein–Protein Interactions: A Structural View

Sokolik, C. G., Qassem, N., & Chill, J. H. (2020) · Biomolecules · doi:10.3390/biom10071084 · Cited by 9

Intrinsically Disordered Proteins: Insights from Poincaré, Waddington, and Lamarck

Kulkarni, P. (2020) · Biomolecules · doi:10.3390/biom10111490 · Cited by 10

Tales of Dihydrofolate Binding to R67 Dihydrofolate Reductase

Duff, M. R., Chopra, S., Strader, M. B., Agarwal, P. K., & Howell, E. E. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00981 · Cited by 9

A finely balanced order–disorder equilibrium sculpts the folding–binding landscape of an antibiotic sequestering protein

Natarajan, L., Sciscio, M. L. D., Nardi, A. N., Sekhar, A., Giudice, A. D., D’Abramo, M., & Naganathan, A. N. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318855121 · Cited by 8

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 9

Activation of p53: How phosphorylated Ser15 triggers sequential phosphorylation of p53 at Thr18 by CK1δ

Nicolaou, S. T., Kannan, S., Warwicker, J., & Verma, C. S. (2022) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26393 · Cited by 8

Molecular recognition and packing frustration in a helical protein

Huynh, L., Neale, C., Pomès, R., & Chan, H. S. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005909 · Cited by 8

Sequence-Specific DNA Binding by Noncovalent Peptide–Azocyclodextrin Dimer Complex as a Suitable Model for Conformational Fuzziness

Quirolo, Z., Sequeira, M. A., Martins, J. C., & Dodero, V. (2019) · Molecules · doi:10.3390/molecules24132508 · Cited by 6

When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes

Sacquin‐Mora, S., & Prévost, C. (2021) · Biomolecules · doi:10.3390/biom11101529 · Cited by 8

Contribution of protein phosphorylation to binding‐induced folding of the SLBP–histone mRNA complex probed by phosphorus‐31 NMR

Thapar, R. (2014) · FEBS Open Bio · doi:10.1016/j.fob.2014.10.002 · Cited by 8

Digested disorder

Uversky, V. N. (2013) · Intrinsically Disordered Proteins · doi:10.4161/idp.25496 · Cited by 8

Studying the Structures of Relaxed and Fuzzy Interactions: The Diverse World of S100 Complexes

Ecsédi, P., Gógl, G., & Nyitray, L. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.749052 · Cited by 8

MFIB 2.0: a major update of the database of protein complexes formed by mutual folding of the constituting protein chains

Fichó, E., Pancsa, R., Magyar, C., Kálmán, Z. E., Schád, É., Németh, B. Z., Simon, I., Dobson, L., & Tusnády, G. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae976 · Cited by 7

Untersuchung von intrinsisch unstrukturierten Proteinen mithilfe des Austausches mit hyperpolarisiertem Wasser

Kurzbach, D., Canet, E., Flamm, A. G., Jhajharia, A., Weber, E. M. M., Konrat, R., & Bodenhausen, G. (2016) · Angewandte Chemie · doi:10.1002/ange.201608903 · Cited by 7

The Enigma of Transcriptional Activation Domains

Erkine, A. M., Oliveira, M., & Class, C. A. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168766 · Cited by 6

Neuronal splicing regulator RBFOX3 (NeuN) distribution and organization are modified in response to monosodium glutamate in rat brain at postnatal day 14

Juarez, A., González, N., Campos-Ordoñez, T., Martínez, Y. G., & Gudiño‐Cabrera, G. (2024) · Acta Histochemica · doi:10.1016/j.acthis.2024.152207 · Cited by 7

Role of structural flexibility in the evolution of emerin

Jia, Y., & Xue, B. (2015) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2015.08.009 · Cited by 6

Digested disorder

DeForte, S., Reddy, K. D., & Uversky, V. N. (2013) · Intrinsically Disordered Proteins · doi:10.4161/idp.27454 · Cited by 6

Experimental studies of binding of intrinsically disordered proteins to their partners

Schneider, R., Jensen, M. R., & Blackledge, M. J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816348-1.00005-3 · Cited by 6

Network representation of protein interactions—Experimental results

Kurzbach, D., Flamm, A. G., & Sára, T. (2016) · Protein Science · doi:10.1002/pro.2964 · Cited by 5

Modulation of α-synuclein aggregation amid diverse environmental perturbation

Wasim, A., Menon, S., & Mondal, J. (2024) · eLife · doi:10.7554/elife.95180 · Cited by 17

Crowders Steal Dihydrofolate Reductase Ligands through Quinary Interactions

Duff, M. R., Desai, N., Craig, M. A., Agarwal, P. K., & Howell, E. E. (2019) · Biochemistry · doi:10.1021/acs.biochem.8b01110 · Cited by 5

Simulations of Higher‐Order Protein Organizations Using a Fuzzy Framework

Tüű-Szabó, B., Kóczy, L. T., & Fuxreiter, M. (2018) · Complexity · doi:10.1155/2018/6360846 · Cited by 8

Biochemical and structural biology aspects of liquid–liquid phase separation: protein side of liquid–liquid phase separation, membrane-less organelles, and biomolecular condensates

Uversky, V. N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00011-7 · Cited by 4

NMR ‐identification of the interaction between BRCA1 and the intrinsically disordered monomer of the Myc‐associated factor X

Epasto, L. M., Pötzl, C., Peterlik, H., Khalil, M., Saint‐Pierre, C., Gasparutto, D., Sicoli, G., & Kurzbach, D. (2023) · Protein Science · doi:10.1002/pro.4849 · Cited by 3

Effects of flexibility and electrostatic interactions on the coupled binding–folding mechanisms of Chz.core and H2A.z–H2B

Shang, X., Chu, W., Chu, X., Liu, C., Xu, L., & Wang, J. (2017) · Molecular BioSystems · doi:10.1039/c7mb00103g · Cited by 4

Effects of Osmolytes on Ligand Binding to Dihydropteroate Synthase from Bacillus anthracis

Nambiar, D., Sharma, O., Duff, M. R., & Howell, E. E. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c03311 · Cited by 4

New type of interaction between the SARAH domain of the tumour suppressor RASSF1A and its mitotic kinase Aurora A

Szimler, T., Gráczer, É., Györffy, D., Végh, B. M., Szilágyi, A., Hajdú, I., Závodszky, P., & Vas, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-41972-x · Cited by 4

Diffusion of the disordered E-cadherin tail on β-cateninPreprint

Wiggers, F., Wohl, S., Dubovetskyi, A., Rosenblum, G., Zheng, W., & Hofmann, H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.03.429507 · Cited by 4

Multivalency in Tau–Microtubule Interactions: Heterogeneous Association and Functional Implications

Naveh-Tassa, S., & Levy, Y. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169600 · Cited by 3

Intrinsic disorder and salt-dependent conformational changes of the N-terminal region of TFIP11 splicing factor

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