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A Combined Spectroscopic/Molecular Dynamic Study for Investigating a Methyl-Carboxylated PEI as a Potential Uranium Decorporation Agent

Lahrouch, F., Chamayou, A., Creff, G., Duvail, M., Hennig, C., Lozano-Rodríguez, M. J., Auwer, C. D., & Giorgio, C. D. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b02408 · Cited by 20 · see citing works

Conformational tuning of a DNA-bound transcription factor

Sicoli, G., Vezin, H., Ledolter, K., Kress, T., & Kurzbach, D. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz291 · Cited by 20 · see citing works

Structural Insights into the Osteopontin-Aptamer Complex by Molecular Dynamics Simulations

Penna, G. L., & Chelli, R. (2018) · Frontiers in Chemistry · doi:10.3389/fchem.2018.00002 · Cited by 19 · see citing works

Integrating computational and experimental advances in bone multiscale mechanics

Rowe, J., Shen, S. C.-Y., de Alcântara, A. C. S., Skaf, M. S., Dini, D., Harrison, N. M., Hansen, U., Buehler, M. J., & Abel, R. L. (2025) · Progress in Materials Science · doi:10.1016/j.pmatsci.2025.101474 · Cited by 18 · see citing works

Bovine seminal plasma osteopontin: Structural modelling, recombinant expression and its relationship with semen quality

Bustamante‐Filho, I. C., Menegassi, S. R. O., Pereira, G. R., Salton, G. D., Munari, F. M., Schneider, M. R., Mattos, R. C., Barcellos, J. O. J., Laurino, J. P., Lima, E. O. C., et al. (2020) · Andrologia · doi:10.1111/and.13905 · Cited by 18 · see citing works

Hydrophobic Collapse of the Intrinsically Disordered Transcription Factor Myc Associated Factor X

Kızılsavaş, G., Ledolter, K., & Kurzbach, D. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00679 · Cited by 18 · see citing works

Intrinsically disordered proteins (IDPs) studied by EPR and in-cell EPR

Weickert, S., Cattani, J., & Drescher, M. (2018) · Royal Society of Chemistry eBooks · doi:10.1039/9781788013888-00001 · Cited by 18 · see citing works

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 · see citing works

Do “Newly Born” orphan proteins resemble “Never Born” proteins? A study using three deep learning algorithms

Liu, J., Yuan, R., Shao, W., Wang, J., Silman, I., & Sussman, J. L. (2023) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26496 · Cited by 18 · see citing works

Thermodynamic Analysis of the Disorder-to-α-Helical Transition of 18.5-kDa Myelin Basic Protein Reveals an Equilibrium Intermediate Representing the Most Compact Conformation

Vassall, K. A., Jenkins, A. D., Bamm, V. V., & Harauz, G. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.03.011 · Cited by 17 · see citing works

Microglia signaling in health and disease – Implications in sex-specific brain development and plasticity

Pramanik, S., Harini Devi, M., Chakrabarty, S., Paylar, B., Pradhan, A., Thaker, M., Ayyadhury, S., Manavalan, A., Olsson, P., Pramanik, G., et al. (2024) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2024.105834 · Cited by 18 · see citing works

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

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

Assessing SPP1/Osteopontin (OPN) Splice Variants and Their Association to Nonmelanoma Skin Cancer by Absolute Quantification: Identification of OPN-5 Subvariants and Their Protein Coding Potential

Chou, C., Huang, C. C., Dabil, N. B., & Chang, P. (2021) · Cancer Investigation · doi:10.1080/07357907.2021.1933015 · Cited by 14 · see citing works

Nitroxide spin labels: fabulous spy spins for biostructural EPR applications

Martinho, M., Fournier, E., Breton, N. L., Mileo, E., & Belle, V. (2018) · Royal Society of Chemistry eBooks · doi:10.1039/9781788013888-00066 · Cited by 12 · see citing works

Lactoferrin-Based Heteroprotein Systems, From Their Formation Mechanism, Properties, To Applications

Chen, R., Ding, J., Li, Y., Zhang, Y., & Yang, R. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c05298 · Cited by 11 · see citing works

The Multifaceted Role of Osteopontin in Prostate Pathologies

Silver, S. V., & Popovics, P. (2023) · Biomedicines · doi:10.3390/biomedicines11112895 · Cited by 10 · see citing works

Kompensatorische Anpassungen der strukturellen Dynamik eines intrinsisch unstrukturierten Protein‐Komplexes

Kurzbach, D., Schwarz, T. C., Platzer, G., Höfler, S., Hinderberger, D., & Konrat, R. (2014) · Angewandte Chemie · doi:10.1002/ange.201308389 · Cited by 10 · see citing works

Energy dissipation of osteopontin at a HAp mineral interface: Implications for bone biomechanics

Tavakol, M., & Vaughan, T. J. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.12.023 · Cited by 10 · see citing works

Identification of Patients with Pancreatic Cancer by Electron Paramagnetic Resonance Spectroscopy of Fatty Acid Binding to Human Serum Albumin

Haeri, H. H., Tomaszewski, J., Phytides, B., Schimm, H., Möslein, G., Niedergethmann, M., Hinderberger, D., & Gelos, M. (2020) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00116 · Cited by 10 · see citing works

Intrinsically Disordered Osteopontin Fragment Orders During Interfacial Calcium Oxalate Mineralization

Lü, H., Ng, D. Y. W., Lieberwirth, I., Weidner, T., & Bonn, M. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202105768 · Cited by 10 · see citing works

Quantification of Distributions of Local Proton Concentrations in Heterogeneous Soft Matter and Non-Anfinsen Biomacromolecules

Kuzin, S. V., Stolba, D., Wu, X., Syryamina, V. N., Boulos, S., Jeschke, G., Nyström, L., & Yulikov, M. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.4c00825 · Cited by 9 · see citing works

Effects of Full-Length Phosphorylated Osteopontin and Constituent Acidic Peptides and Amino Acids on Calcite Dissolution

Nelea, V., Chien, Y., Paquette, J., & McKee, M. D. (2014) · Crystal Growth & Design · doi:10.1021/cg4012394 · Cited by 9 · see citing works

Comparison of 30 Cytokines in Human Breast Milk between 1989 and 2013 in Japan

Takahashi, T., Ueno, H., Yamaide, F., Nakano, T., Shiko, Y., Kawasaki, Y., Mitsuishi, C., & Shimojo, N. (2023) · Nutrients · doi:10.3390/nu15071735 · Cited by 8 · see citing works

Magnetic Resonance Access to Transiently Formed Protein Complexes

Sára, T., Schwarz, T. C., Kurzbach, D., Wunderlich, C. H., Kreutz, C., & Konrat, R. (2014) · ChemistryOpen · doi:10.1002/open.201402008 · Cited by 7 · see citing works

1H, 15N, 13C resonance assignment of human osteopontin

Platzer, G., Żerko, S., Saxena, S., Koźmiński, W., & Konrat, R. (2015) · Biomolecular NMR Assignments · doi:10.1007/s12104-014-9594-7 · Cited by 7 · see citing works

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 · see citing works

Deep Learning for Hyperpolarized NMR of Intrinsically Disordered Proteins without Resolution Loss: Access to Short‐Lived Intermediates

Turhan, E., Pötzl, C., Brandis, D., Faglia, F., Zachrdla, M., & Kurzbach, D. (2025) · Chemistry - A European Journal · doi:10.1002/chem.202502067 · Cited by 6 · see citing works

ICOSL: more than a trigger of ICOS function

Stoppa, I., Provera, A., Sacchetti, S., Clemente, N., Pantham, D., Christaki, F., Vecchio, C., Sheferaw, A. N., Rolla, R., Dianzani, C., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02559-4 · Cited by 5 · see citing works

Digested disorder

Reddy, K. D., DeForte, S., & Uversky, V. N. (2014) · Intrinsically Disordered Proteins · doi:10.4161/idp.27833 · Cited by 5 · see citing works

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 · see citing works

Pulse EPR spectroscopy and molecular modeling reveal the origins of the local heterogeneity of dietary fibers

Syryamina, V. N., Wu, X., Boulos, S., Nyström, L., & Yulikov, M. (2023) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2023.121167 · Cited by 5 · see citing works

Protein Folding, Misfolding, Aggregation And Amyloid Formation: Mechanisms of Aβ Oligomer Mediated Toxicities

Salahuddin, P. (2015) · Journal of Biochemistry and Molecular Biology Research · doi:10.17554/j.issn.2313-7177.2015.01.4 · Cited by 5 · see citing works

Conformation and Dynamics of Monomeric, Phase-Separated, and Cross-Linked Resilin Biomaterials

Otis, J., Reichenwallner, J., Reichheld, S. E., Au, A., Yip, C. M., Ernst, O. P., & Sharpe, S. J. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c12305 · Cited by 4 · see citing works

Exploring the separation power of mixed‐modal resins for purification of recombinant osteopontin from clarified Escherichia coli lysates

Guo, S., Ravi, A., Mayfield, S. P., & Nikolov, Z. L. (2018) · Biotechnology Progress · doi:10.1002/btpr.2722 · Cited by 4 · see citing works

Human apo-metallothionein 1a is not a random coil: Evidence from guanidinium chloride, high temperature, and acidic pH unfolding studies

Korkola, N. C., & Stillman, M. J. (2024) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2024.141010 · Cited by 3 · see citing works

Compendium of lactopontin: Molecular structure, manufacturing process and biological functions

Lyu, Y. F., Wen, X., Hu, J., Huang, Y., Qiao, Y., & Zhang, J. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.106155 · Cited by 3 · see citing works

An intrinsically disordered protein, osteopontin, driving neuropathology in Alzheimer’s dementia

Steinman, L. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2221816120 · Cited by 3 · see citing works

Combining All-Atom Molecular Dynamics Simulation and NMR to Analyze Conformational Ensemble of Intrinsically Disordered Proteins

Song, X., & Wang, W. (2025) · Communications in Computational Chemistry · doi:10.4208/cicc.2025.217.02 · Cited by 2 · see citing works

Confidence limits in pulse dipolar EPR spectroscopy: estimates for individual measurements

Syryamina, V. N., Матвеева, А. Г., & Bowman, M. K. (2024) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp05797f · Cited by 2 · see citing works

A set of cross-correlated relaxation experiments to probe the correlation time of two different and complementary spin pairs

Ceccolini, I., Kauffmann, C., Holzinger, J., Konrat, R., & Zawadzka‐Kazimierczuk, A. (2024) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2024.107661 · Cited by 2 · see citing works

Alternative polyadenylation mechanism links secreted phosphoprotein 1 gene to glioblastoma

Mehravar, M., Ghaemimanesh, F., & Poursani, E. (2022) · Cancer Biomarkers · doi:10.3233/cbm-210135 · Cited by 1 · see citing works

Probing Macromolecular and Supramolecular Structure, Dynamics, and Function by Magnetic Resonance

Spiess, H. W. (2013) · Advances in polymer science · doi:10.1007/12_2013_255 · Cited by 2 · see citing works

Hyperpolarized water via dissolution dynamic nuclear polarization: Applications in biomolecular NMR

Lee, Y., & Kim, J. (2024) · Applied Spectroscopy Reviews · doi:10.1080/05704928.2024.2324821 · Cited by 1 · see citing works

In search of shape in the unshaped: Constructing ensembles of intrinsically disordered proteins

Saha, D., Yang, W., & Zheng, W. (2026) · Biophysics Reviews · doi:10.1063/5.0307183 · Cited by 1 · see citing works

Encounter Complexes Between the N-terminal of Neurotensin with the Extracellular Loop 2 of the Neurotensin Receptor 1 Steer Neurotensin to the Orthosteric Binding Pocket

Asadollahi, K., Rajput, S., Jameson, G. N. L., Scott, D. J., & Gooley, P. R. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168244 · Cited by 1 · see citing works

Osteopontin (Spp1)

Bawage, S., Weeks, S. E., Shevde, L. A., & Samant, R. S. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101771 · Cited by 1 · see citing works

The molecular mechanism of Hsp90-induced oligomerization of TauPreprint

Weickert, S., Wawrzyniuk, M., John, L., Rüdiger, S., & Drescher, M. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/614289

Intrinsisch ungeordnete Osteopontin‐Fragmente ordnen sich während der interfazialen Calciumoxalat‐Mineralisierung

Lü, H., Ng, D. Y. W., Lieberwirth, I., Weidner, T., & Bonn, M. (2021) · Angewandte Chemie · doi:10.1002/ange.202105768

Η κλινική αξία της οστεοποντίνης στον καρκίνο του πνεύμονα

Καζάκου, Α. (2016) · doi:10.12681/eadd/39378

Osteopontin (Spp1)

Bawage, S., Weeks, S. E., Shevade, L. A., & Samant, R. S. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101771-1

BRCA1 inhibits MYC:MAX heterodimerization by modulating the availability of transient MAX monomersPreprint

Kurzbach, D., Epasto, L. M., Pötzl, C., Peterlik, H., Khalil, M., Saint‐Pierre, C., Gasparutto, D., & Sicoli, G. (2023) · Research Square · doi:10.21203/rs.3.rs-3114406/v1

Studying Molecular Chaperones and Their Client Interactions by Nanometer Distance Restraints from Electron Paramagnetic Resonance Spectroscopy

Dröden, J., & Drescher, M. (2023) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781839165986-00217

Interactions among the three protein states

Kadeřávek, P., Kubíček, K., & Žı́dek, L. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21809-5.00022-3

The hidden order of intrinsically disordered proteins and its role in molecular recognition

Mateos, B. (2019) · University of Vienna · doi:10.25365/thesis.60692

Structural, dynamic and thermodynamic description of IDPs and their interactions by NMR

Schwarz, T. (2015)

Denaturant-Induced Conformational Transitions in Intrinsically Disordered Proteins

Neyroz, P., Ciurli, S., & Uversky, V. N. (2012) · Methods in molecular biology · doi:10.1007/978-1-4614-3704-8_12 · Cited by 4 · see citing works

The intrinsically „not-so-unfolded“ protein Osteopontin

Platzer, G. (2009) · University of Vienna · doi:10.25365/thesis.7854

The Ambivalent Role of Proline Residues in an Intrinsically Disordered Protein: From Disorder Promoters to Compaction Facilitators

Mateos, B., Conrad‐Billroth, C., Schiavina, M., Beier, A., Kontaxis, G., Konrat, R., Felli, I. C., & Pierattelli, R. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.11.015 · Cited by 100 · see citing works