CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates

Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy

Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416

Accurate assessment of mass, models and resolution by small-angle scattering

Rambo, R. P., & Tainer, J. A. (2013) · Nature · doi:10.1038/nature12070 · Cited by 750

Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR

Tang, C., Schwieters, C. D., & Clore, G. M. (2007) · Nature · doi:10.1038/nature06232 · Cited by 416

Structure of the Autoinhibited Kinase Domain of CaMKII and SAXS Analysis of the Holoenzyme

Rosenberg, O. S., Deindl, S., Sung, R.-J., Nairn, A. C., & Kuriyan, J. (2005) · Cell · doi:10.1016/j.cell.2005.10.029 · Cited by 333

SOCS3 binds specific receptor–JAK complexes to control cytokine signaling by direct kinase inhibition

Kershaw, N. J., Murphy, J. M., Liau, N. P. D., Varghese, L. N., Laktyushin, A., Whitlock, E. L., Lucet, I. S., Nicola, N. A., & Babon, J. J. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2519 · Cited by 301

Force interacts with macromolecular structure in activation of TGF-β

Dong, X., Zhao, B., Iacob, R. E., Zhu, J., Koksal, A. C., Lu, C., Engen, J. R., & Springer, T. A. (2017) · Nature · doi:10.1038/nature21035 · Cited by 273

Suprafacial Orientation of the SCFCdc4 Dimer Accommodates Multiple Geometries for Substrate Ubiquitination

Tang, X., Orlicky, S., Lin, Z., Willems, A., Neculai, D., Ceccarelli, D., Mercurio, F., Shilton, B. H., Sicheri, F., & Tyers, M. (2007) · Cell · doi:10.1016/j.cell.2007.04.042 · Cited by 209

Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax

Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., et al. (2018) · Science · doi:10.1126/science.aan1078 · Cited by 212

Full-length extracellular region of the var2CSA variant of PfEMP1 is required for specific, high-affinity binding to CSA

Srivastava, A., Gangnard, S., Round, A., Dechavanne, S., Juillerat, A., Raynal, B., Faure, G., Baron, B., Ramboarina, S., Singh, S. K., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000951107 · Cited by 149

Domain Motion in Cytochrome P450 Reductase

Ellis, J., Gutierrez, A., Barsukov, I. L., Huang, W.-C., Grossmann, J. G., & Roberts, G. C. K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054304 · Cited by 140

Cyclic nucleotide-induced helical structure activates a TIR immune effector

Hogrel, G., Guild, A., Graham, S., Rickman, H., Grüschow, S., Bertrand, Q., Spagnolo, L., & White, M. F. (2022) · Nature · doi:10.1038/s41586-022-05070-9 · Cited by 129

Conformational buffering underlies functional selection in intrinsically disordered protein regions

González-Foutel, N. S., Glavina, J., Borcherds, W. M., Safranchik, M., Barrera-Vilarmau, S., Sagar, A., Estaña, A., Barozet, A., Garrone, N. A., Fernandez-Ballester, G., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00811-w · Cited by 118

On the Potential of Machine Learning to Examine the Relationship Between Sequence, Structure, Dynamics and Function of Intrinsically Disordered Proteins

Lindorff-Larsen, K., & Kragelund, B. B. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167196 · Cited by 85

In-depth analysis of subclass-specific conformational preferences of IgG antibodies

Tian, X., Vestergaard, B., Thorolfsson, M., Yang, Z., Rasmussen, H. B., & Langkilde, A. E. (2015) · IUCrJ · doi:10.1107/s205225251402209x · Cited by 78

Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation

Bernadó, P., Modig, K., Grela, P., Svergun, D. I., Tchorzewski, M., Pons, M., & Akke, M. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.02.012 · Cited by 77

Structural and Functional Consequences of Three Cancer-Associated Mutations of the Oncogenic Phosphatase SHP2

LaRochelle, J. R., Fodor, M., Xu, X., Durzynska, I., Fan, L., Stams, T., Chan, H. M., LaMarche, M. J., Chopra, R., Wang, P., et al. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01287 · Cited by 70

Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition

Liu, Z., Gong, Z., Jiang, W.-X., Yang, J., Zhu, W.-K., Guo, D.-C., Zhang, W.-P., Liu, M.-L., & Tang, C. (2015) · eLife · doi:10.7554/elife.05767 · Cited by 60

The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc

Ilari, A., Alaleona, F., Tria, G., Petrarca, P., Battistoni, A., Zamparelli, C., Verzili, D., Falconi, M., & Chiancone, E. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.010 · Cited by 55

Characterization of ANGPT2 mutations associated with primary lymphedema

Leppänen, V.-M., Brouillard, P., Korhonen, E. A., Sipilä, T., Jha, S. K., Revencu, N., Labarque, V., Fastré, E., Schlögel, M., Ravoet, M., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aax8013 · Cited by 49

Design of a Cereblon construct for crystallographic and biophysical studies of protein degraders

Kroupova, A., Spiteri, V. A., Rutter, Z. J., Furihata, H., Darren, D., Ramachandran, S., Chakraborti, S., Haubrich, K., Pethe, J., Gonzales, D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52871-9 · Cited by 47

A switch point in the molecular chaperone Hsp90 responding to client interaction

Rutz, D. A., Luo, Q., Freiburger, L., Madl, T., Kaila, V. R. I., Sattler, M., & Buchner, J. (2018) · Nature Communications · doi:10.1038/s41467-018-03946-x · Cited by 37

Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice.

Vance, T. D. R., Olijve, L. L. C., Campbell, R. L., Voets, I. K., Davies, P. L., & Guo, S. (2014) · Bioscience Reports · doi:10.1042/bsr20140083 · Cited by 40

Multi-scale Ensemble Modeling of Modular Proteins with Intrinsically Disordered Linker Regions: Application to p53

Terakawa, T., Higo, J., & Takada, S. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.06.026 · Cited by 32

Dimerization of Tie2 mediated by its membrane-proximal FNIII domains

Moore, J. O., Lemmon, M. A., & Ferguson, K. M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617800114 · Cited by 30

Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases

Keppel, T. R., Sarpong, K., Murray, E. M., Monsey, J., Zhu, J., & Bose, R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.747485 · Cited by 29

AlphaFold-predicted protein structures and small-angle X-ray scattering: insights from an extended examination of selected data in the Small-Angle Scattering Biological Data Bank

Brookes, E., Rocco, M., Vachette, P., & Trewhella, J. (2023) · Journal of Applied Crystallography · doi:10.1107/s1600576723005344 · Cited by 21

Allosteric HIV Integrase Inhibitors Promote Formation of Inactive Branched Polymers via Homomeric Carboxy-Terminal Domain Interactions

Gupta, K., Allen, A., Giraldo, C., Eilers, G., Sharp, R., Hwang, Y., Murali, H., Cruz, K., Janmey, P., Bushman, F., et al. (2021) · Structure · doi:10.1016/j.str.2020.12.001 · Cited by 19

Characterization of Protein Flexibility Using Small-Angle X-Ray Scattering and Amplified Collective Motion Simulations

Wen, B., Peng, J., Zuo, X., Gong, Q., & Zhang, Z. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.07.005 · Cited by 20

Structure of SALL4 zinc finger domain reveals link between AT-rich DNA binding and Okihiro syndrome

Watson, J. A., Pantier, R., Jayachandran, U., Chhatbar, K., Alexander-Howden, B., Kruusvee, V., Prendecki, M., Bird, A., & Cook, A. G. (2023) · Life Science Alliance · doi:10.26508/lsa.202201588 · Cited by 14

SOP-MULTI: A Self-Organized Polymer-Based Coarse-Grained Model for Multidomain and Intrinsically Disordered Proteins with Conformation Ensemble Consistent with Experimental Scattering Data

Baratam, K., & Srivastava, A. (2024) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c00579 · Cited by 9

Conserved intramolecular networks in GDAP1 are closely connected to CMT-linked mutations and protein stability

Sutinen, A., Paffenholz, D., Nguyen, G. T. T., Ruskamo, S., Torda, A. E., & Kursula, P. (2023) · PLOS ONE · doi:10.1371/journal.pone.0284532 · Cited by 8

Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains

Hay, I. M., Shamin, M., Caroe, E. R., Mohammed, A. S. A., Svergun, D. I., Jeffries, C. M., Graham, S. C., Sharpe, H. J., & Deane, J. E. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102750 · Cited by 7

Atomic-Resolution Prediction of Degrader-mediated Ternary Complex Structures by Combining Molecular Simulations with Hydrogen Deuterium Exchange

Dixon, T., MacPherson, D., Mostofian, B., Dauzhenka, T., Lotz, S., McGee, D., Shechter, S., Shrestha, U. R., Wiewiora, R., McDargh, Z. A., et al. (2021) · doi:10.1101/2021.09.26.461830 · Cited by 7

A Novel Biosensor for Ferrous Iron Developed via CoBiSe: A Computational Method for Rapid Biosensor Design

Papadopoulos, A., Anlauf, M. T., Reiners, J., Paik, S.-H., Krüger, A., Lückel, B., Bott, M., Drepper, T., Frunzke, J., Gohlke, H., et al. (2026) · ACS Sensors · doi:10.1021/acssensors.5c02481 · Cited by 5

luxA Gene From Enhygromyxa salina Encodes a Functional Homodimeric Luciferase

Yudenko, A., Bazhenov, S. V., Aleksenko, V. A., Goncharov, I. M., Semenov, O., Remeeva, A., Nazarenko, V. V., Kuznetsova, E., Fomin, V. V., Konopleva, M. N., et al. (2024) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26739 · Cited by 5

Protein Quaternary Structures in Solution are a Mixture of Multiple forms

Marciano, S., Dey, D., Listov, D., Fleishman, S. J., Sonn-Segev, A., Mertens, H., Busch, F., Kim, Y., Harvey, S. R., Wysocki, V. H., et al. (2022) · doi:10.1101/2022.03.30.486392 · Cited by 3

SAXS data based glycosylated models of human alpha-1-acid glycorprotein, a key player in health, disease and drug circulation

Kalidas, N., Peddada, N., Pandey, K., & Ashish (2026) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2025.2475244 · Cited by 2

Asymmetric horseshoe-like assembly of peroxisomal Yeast Oxalyl-CoA synthetase

Bürgi, J., Lill, P., Giannopoulou, E.-A., Jeffries, C. M., Chojnowski, G., Raunser, S., Gatsogiannis, C., & Wilmanns, M. (2022) · doi:10.1101/2022.08.30.505785 · Cited by 1

Investigating the quaternary structure of a homomultimeric catechol 1,2-dioxygenase: An integrative structural biology study

(2025) · doi:10.1371/journal.pone.0315992 · Cited by 1

A novel biosensor for ferrous iron developed via CoBiSe: A computational method for rapid biosensor design

Papadopoulos, A., Anlauf, M. T., Reiners, J., Paik, S.-H., Krüger, A., Lückel, B., Bott, M., Drepper, T., Frunzke, J., Gohlke, H., et al. (2025) · doi:10.1101/2025.07.16.665043