Restoring Low Resolution Structure of Biological Macromolecules from Solution Scattering Using Simulated Annealing

DAMMIF , a program for rapid ab-initio shape determination in small-angle scattering

Franke, D., & Svergun, D. I. (2009) · Journal of Applied Crystallography · doi:10.1107/s0021889809000338 · Cited by 2,021

X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution

Putnam, C. D., Hammel, M., Hura, G. L., & Tainer, J. A. (2007) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583507004635 · Cited by 1,184

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

Integrating diverse data for structure determination of macromolecular assemblies

Alber, F., Förster, F., Korkin, D., Topf, M., & Sali, A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.060407.135530 · Cited by 206

Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90

Krukenberg, K. A., Förster, F., Rice, L. M., Sali, A., & Agard, D. A. (2008) · Structure · doi:10.1016/j.str.2008.01.021 · Cited by 160

Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2

Pádua, R. A. P., Sun, Y., Marko, I., Pitsawong, W., Stiller, J. B., Otten, R., & Kern, D. (2018) · Nature Communications · doi:10.1038/s41467-018-06814-w · Cited by 133

Histone Core Phosphorylation Regulates DNA Accessibility

Brehove, M., Wang, T., North, J., Luo, Y., Dreher, S. J., Shimko, J. C., Ottesen, J. J., Luger, K., & Poirier, M. G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.661363 · Cited by 93

Structural and Functional Integration of the PLCγ Interaction Domains Critical for Regulatory Mechanisms and Signaling Deregulation

Bunney, T. D., Esposito, D., Mas-Droux, C., Lamber, E., Baxendale, R. W., Martins, M., Cole, A., Svergun, D., Driscoll, P. C., & Katan, M. (2012) · Structure · doi:10.1016/j.str.2012.09.005 · Cited by 88

Assembly and solution structure of the core retromer protein complex

Norwood, S. J., Shaw, D. J., Cowieson, N. P., Owen, D. J., Teasdale, R. D., & Collins, B. M. (2011) · Traffic · doi:10.1111/j.1600-0854.2010.01124.x · Cited by 84

Antiviral signalling by a cyclic nucleotide activated CRISPR protease

Rouillon, C., Schneberger, N., Chi, H., Blumenstock, K., Da Vela, S., Ackermann, K., Moecking, J., Peter, M. F., Boenigk, W., Seifert, R., et al. (2023) · Nature · doi:10.1038/s41586-022-05571-7 · Cited by 66

An ensemble of flexible conformations underlies mechanotransduction by the cadherin–catenin adhesion complex

Bush, M., Alhanshali, B. M., Qian, S., Stanley, C. B., Heller, W. T., Matsui, T., Weiss, T. M., Nicholl, I. D., Walz, T., Callaway, D. J. E., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911489116 · Cited by 42

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

Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies

Ko, K.-T., Lennartz, F., Mekhaiel, D., Guloglu, B., Marini, A., Deuker, D. J., Long, C. A., Jore, M. M., Miura, K., Biswas, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33379-6 · Cited by 32

Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane

Park, S. H., Han, J., Jeong, B.-C., Song, J. H., Jang, S. H., Jeong, H., Kim, B. H., Ko, Y.-G., Park, Z.-Y., Lee, K. E., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01111-7 · Cited by 31

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

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

Structural basis for IL-33 recognition and its antagonism by the helminth effector protein HpARI2

Jamwal, A., Colomb, F., McSorley, H. J., & Higgins, M. K. (2024) · Nature Communications · doi:10.1038/s41467-024-49550-0 · Cited by 15

Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase

Bulvas, O., Knejzlík, Z., Sýs, J., Filimoněnko, A., Čížková, M., Clarová, K., Rejman, D., Kouba, T., & Pichová, I. (2024) · Nature Communications · doi:10.1038/s41467-024-50933-6 · Cited by 13

Comparison of angiopoietin-like protein 3 and 4 reveals structural and mechanistic similarities

Gunn, K. H., Gutgsell, A. R., Xu, Y., Johnson, C. V., Liu, J., & Neher, S. B. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100312 · Cited by 12

The structure of a Type III-A CRISPR-Cas effector complex reveals conserved and idiosyncratic contacts to target RNA and crRNA among Type III-A systems

(2023) · doi:10.1371/journal.pone.0287461 · Cited by 10

Fitting high-resolution electron density maps from atomic models to solution scattering data

Chamberlain, S. R., Moore, S., & Grant, T. D. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.10.034 · Cited by 10

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

Structural basis for the recognition and ubiquitylation of type-2 N-degron substrate by PRT1 plant N-recognin

Yang, W. S., Kim, S. H., Kim, M., Shin, H., Lee, J., Sandmann, A., Park, O. K., Dissmeyer, N., & Song, H. K. (2025) · Nature Communications · doi:10.1038/s41467-025-63282-9 · Cited by 4

Structure Characterization of Bacterial Microcompartment Shells via X-ray Scattering and Coordinate Modeling: Evidence for Adventitious Capture of Cytoplasmic Proteins

(2025) · doi:10.1021/acsabm.4c01621 · Cited by 3

Structural enzymological studies of the long chain fatty acyl-CoA synthetase FadD5 from the mce1 operon of Mycobacterium tuberculosis

Rahman, M. A., Dalwani, S., & Venkatesan, R. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151960 · Cited by 3

Identification of an Intrinsically Disordered Region (IDR) in Arginyltransferase 1 (ATE1)

Cartwright, M., Parakra, R., Oduwole, A., Zhang, F., Deredge, D. J., & Smith, A. T. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00512 · Cited by 3

Nanobodies against the myelin enzyme CNPase as tools for structural and functional studies

Markusson, S., Raasakka, A., Schröder, M., Sograte‐Idrissi, S., Rahimi, A. M., Asadpour, O., Körner, H., Lodygin, D., Eichel‐Vogel, M. A., Chowdhury, R., et al. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.16274 · Cited by 1

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

(2022) · doi:10.1101/2022.06.23.497309 · Cited by 1

Analysis of Plasmodium falciparum myosin B ATPase activity and structure in complex with the calmodulin-like domain of its light chain MLC-B

Pires, I., Hung, Y.-F., Bergmann, U., Molloy, J. E., & Kursula, I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102634 · Cited by 1

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. (2022) · doi:10.1101/2022.09.09.507262