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

The Protein Data Bank

Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723

Robust Regression and Outlier Detection

Piepel, G. F., Rousseeuw, P. J., & Leroy, A. M. (1989) · Technometrics · doi:10.2307/1268828 · Cited by 6,183

Robust Regression and Outlier Detection

Rousseeuw, P. J., & Leroy, A. M. (1987) · Wiley Series in Probability and Statistics · doi:10.1002/0471725382 · Cited by 5,609

Small Angle X-ray Scattering

Hart, M., & Deutsch, M. (1983) · Physics Bulletin · doi:10.1088/0031-9112/34/7/032 · Cited by 4,600

Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877

Small-Angle X-Ray Scattering

Bhushan, B. (2016) · Springer eBooks · doi:10.1007/978-94-017-9780-1_101037 · Cited by 3,800

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

Svergun, D. I., Barberato, C., & Koch, M. (1995) · Journal of Applied Crystallography · doi:10.1107/s0021889895007047 · Cited by 3,388

Linking Crystallographic Model and Data Quality

Karplus, P. A., & Diederichs, K. (2012) · Science · doi:10.1126/science.1218231 · Cited by 1,781

Light scattering and the absolute characterization of macromolecules

Wyatt, P. J. (1993) · Analytica Chimica Acta · doi:10.1016/0003-2670(93)80373-s · Cited by 1,433

Structural Characterisation of Non-Deamidated Acidic Variants of Erwinia chrysanthemi L-asparaginase Using Small-Angle X-ray Scattering and Ion-Mobility Mass Spectrometry

Gervais, D., King, D., Kanda, P., Foote, N., Elliott, L., Brown, P. J., Lee, N. O., Thalassinos, K., Pizzey, C. L., Rambo, R. P., et al. (2015) · Pharmaceutical Research · doi:10.1007/s11095-015-1722-2 · Cited by 14

Atypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA Binding

Barta, M. L., Hickey, J. M., Anbanandam, A., Dyer, K. N., Hammel, M., & Hefty, P. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091760 · Cited by 14

Distinct Structural Features of the Peroxide Response Regulator from Group A Streptococcus Drive DNA Binding

Lin, C. S., Chao, S.-Y., Hammel, M., Nix, J. C., Tseng, H.-L., Tsou, C.-C., Fei, C.-H., Ciou, H. S., Jeng, U., Lin, Y., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089027 · Cited by 14

Evolution of the substrate specificity of an RNA ligase ribozyme from phosphorimidazole to triphosphate activation

DasGupta, S., Weiss, Z., Nisler, C. R., & Szostak, J. W. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2407325121 · Cited by 13

Solution Structure of an Intramembrane Aspartyl Protease via Small Angle Neutron Scattering

Naing, S.-H., Oliver, R. C., Weiss, K. L., Urban, V. S., & Lieberman, R. L. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.12.017 · Cited by 13

Massively parallel, computationally guided design of a proenzyme

Yachnin, B. J., Azouz, L. R., White, R. E., Minetti, C. A. S. A., Remeta, D. P., Tan, V. M., Drake, J. M., & Khare, S. D. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2116097119 · Cited by 13

Chemical screening by time-resolved X-ray scattering to discover allosteric probes

Brosey, C. A., Link, T. M., Shen, R., Moiani, D., Burnett, K. H., Hura, G. L., Jones, D. E., & Tainer, J. A. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01609-1 · Cited by 13

Protein-Protein Interactions: Structures and Druggability

Ascher, D. B., Jubb, H. C., Pires, D. E. V., Ochi, T., Higueruelo, A. P., & Blundell, T. L. (2015) · NATO science for peace and security series. A, Chemistry and biology · doi:10.1007/978-94-017-9719-1_12 · Cited by 13

Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20–21

Seppälä, J., Tossavainen, H., Rodić, N., Permi, P., Pentikäinen, U., & Ylänne, J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136969 · Cited by 13

Unravelling the shape and structural assembly of the photosynthetic GAPDH–CP12–PRK complex fromArabidopsis thalianaby small-angle X-ray scattering analysis

Giudice, A. D., Pavel, N. V., Galantini, L., Falini, G., Trost, P., Fermani, S., & Sparla, F. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004715018520 · Cited by 13

Structural and mechanistic insights into Mycothiol Disulphide Reductase and the Mycoredoxin-1-alkylhydroperoxide reductase E assembly of Mycobacterium tuberculosis

Kumar, A., Nartey, W., Shin, J. S., Manimekalai, M. S. S., & Grüber, G. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.05.007 · Cited by 13

Conformational switch of harmonin, a submembrane scaffold protein of the hair cell mechanoelectrical transduction machinery

Bahloul, A., Pepermans, E., Raynal, B. D. E., Wolff, N., Cordier, F., England, P., Nouaille, S., Baron, B., El‐Amraoui, A., Hardelin, J., et al. (2017) · FEBS Letters · doi:10.1002/1873-3468.12729 · Cited by 13

Structural Diversity of Native Major Ampullate, Minor Ampullate, Cylindriform, and Flagelliform Silk Proteins in Solution

Greving, I., Terry, A., Holland, C., Boulet-Audet, M., Grillo, I., Vollrath, F., & Dicko, C. (2020) · Biomacromolecules · doi:10.1021/acs.biomac.0c00819 · Cited by 13

A common SNP risk variant MT1-MMP causative for Dupuytren's disease has a specific defect in collagenolytic activity

Itoh, Y., Ng, M., Wiberg, A., Inoue, K., Hirata, N., Paiva, K. B. S., Ito, N., Dzobo, K. E., Sato, N., Gifford, V., et al. (2021) · Matrix Biology · doi:10.1016/j.matbio.2021.02.003 · Cited by 13

RAD51AP1 mediates RAD51 activity through nucleosome interaction

Pires, E., Sharma, N., Selemenakis, P., Wu, B., Huang, Y., Alimbetov, D. S., Zhao, W., & Wiese, C. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100844 · Cited by 15

The DNA binding domain of the Vibrio vulnificus SmcR transcription factor is flexible and binds diverse DNA sequences

Newman, J. D., Russell, M. M., Fan, L., Wang, Y., González-Gutiérrez, G., & van Kessel, J. C. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab387 · Cited by 13

The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau

Lyu, C., Vela, S. D., Al‐Hilaly, Y. K., Marshall, K. E., Thorogate, R., Svergun, D. I., Serpell, L. C., Pastore, A., & Hanger, D. P. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.779240 · Cited by 13

In Situ Monitoring of Protein Unfolding/Structural States under Cold High-Pressure Stress

Gomes, D. C., Teixeira, S. C. M., Leão, J. B., Razinkov, V. I., Qi, W., Rodrigues, M. Â., & Roberts, C. J. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.1c00604 · Cited by 13

Recent Advances in Understanding the Structures of Translesion Synthesis DNA Polymerases

Ling, J. A., Frevert, Z., & Washington, M. T. (2022) · Genes · doi:10.3390/genes13050915 · Cited by 15

Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-β-synthase domain

Imamura, A., Okada, T., Mase, H., Otani, T., Kobayashi, T., Tamura, M., Kubata, B. K., Inoue, K., Rambo, R. P., Uchiyama, S., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15611-3 · Cited by 13

Serine 298 Phosphorylation in Linker 2 of UHRF1 Regulates Ligand-Binding Property of Its Tandem Tudor Domain

Kori, S., Jimenji, T., Ekimoto, T., Sato, M., Kusano, F., Oda, T., Unoki, M., Ikeguchi, M., & Arita, K. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.05.006 · Cited by 13

Functional and structural characterization of a novel putative cysteine protease cell wall-modifying multi-domain enzyme selected from a microbial metagenome

Faheem, M. Q., Martins-de-Sa, D., Vidal, J. F. D., Álvares, A. D. C. M., Brandão-Neto, J., Bird, L. E., Tully, M. D., von Delft, F., Souto, B. M., Quirino, B. F., et al. (2016) · Scientific Reports · doi:10.1038/srep38031 · Cited by 13

Structural analysis of pathogenic mutations targeting Glu427 of ALDH7A1, the hot spot residue of pyridoxine‐dependent epilepsy

Laciak, A. R., Korasick, D. A., Gates, K. S., & Tanner, J. J. (2019) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12184 · Cited by 13

The Intrinsically Disordered Domain of the Antitoxin Phd Chaperones the Toxin Doc against Irreversible Inactivation and Misfolding

Gieter, S. D., Konijnenberg, A., Talavera, A., Butterer, A., Haesaerts, S., Greve, H. D., Sobott, F., Loris, R., & Garcia‐Pino, A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.572396 · Cited by 12

Structural analyses of the Haemophilus influenzae peptidoglycan synthase activator LpoA suggest multiple conformations in solution

Sathiyamoorthy, K., Vijayalakshmi, J., Tirupati, B., Fan, L., & Saper, M. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.804997 · Cited by 12

Structural analysis of the complex between influenza B nucleoprotein and human importin-α

Labaronne, A., Milles, S., Donchet, A., Jensen, M. R., Blackledge, M. J., Bourhis, J., Ruigrok, R. W. H., & Crépin, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-17458-z · Cited by 14

Temperature induced conformational changes in the elastin-like peptide GVG(VPGVG) 3

Matt, A., Kuttich, B., Grillo, I., Weißheit, S., Thiele, C. M., & Stühn, B. (2019) · Soft Matter · doi:10.1039/c9sm00583h · Cited by 12

RovC - a novel type of hexameric transcriptional activator promoting type VI secretion gene expression

Knittel, V., Sadana, P., Seekircher, S., Stolle, A.-S., Körner, B., Volk, M., Jeffries, C. M., Svergun, D. I., Heroven, A. K., Scrima, A., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008552 · Cited by 13

Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets

Sagar, A., Herranz-Trillo, F., Langkilde, A. E., Vestergaard, B., & Bernadó, P. (2021) · Structure · doi:10.1016/j.str.2021.03.017 · Cited by 12

Structural basis of cyclic oligoadenylate binding to the transcription factor Csa3 outlines cross talk between type III and type I CRISPR systems

Xia, P., Dutta, A., Gupta, K., Batish, M., & Parashar, V. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101591 · Cited by 12

The Disordered Amino Terminus of the Circadian Enzyme Nocturnin Modulates Its NADP(H) Phosphatase Activity by Changing Protein Dynamics

Wickramaratne, A. C., Li, L., Hopkins, J. B., Joachimiak, Ł. A., & Green, C. B. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00072 · Cited by 12

Structural insights into 3Fe–4S ferredoxins diversity in M. tuberculosis highlighted by a first redox complex with P450

Gilep, A. A., Varaksa, T., Bukhdruker, S. S., Kavaleuski, A., Ryzhykau, Y. L., Smolskaya, S. V., Sushko, T. A., Tsumoto, K., Grabovec, I. P., Kapranov, I., et al. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1100032 · Cited by 12

The Crystal Structure and Small-Angle X-Ray Analysis of CsdL/TcdA Reveal a New tRNA Binding Motif in the MoeB/E1 Superfamily

López-Estepa, M., Ardá, A., Savko, M., Round, A. R., Shepard, W., Bruix, M., Coll, M., Fernández, F. J., Jiménez‐Barbero, J., & Vega, M. C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118606 · Cited by 12

The Salmonella Type III Secretion System Virulence Effector Forms a New Hexameric Chaperone Assembly for Export of Effector/Chaperone Complexes

Tsai, C.-L., Burkinshaw, B. J., Strynadka, N. C. J., & Tainer, J. A. (2014) · Journal of Bacteriology · doi:10.1128/jb.02524-14 · Cited by 12

Achieving selectivity in space and time with DNA double-strand-break response and repair: molecular stages and scaffolds come with strings attached

Liang, S., Esswein, S. R., Ochi, T., Wu, Q., Ascher, D. B., Chirgadze, D. Y., Sibanda, B. L., & Blundell, T. L. (2016) · Structural Chemistry · doi:10.1007/s11224-016-0841-7 · Cited by 12

N-terminal half of transportin SR2 interacts with HIV integrase

Tsirkone, V. G., Blokken, J., Wit, F. D., Breemans, J., Houwer, S. D., Debyser, Z., Christ, F., & Strelkov, S. V. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.777029 · Cited by 13

Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe–S cluster assembly centers

Galeano, B. K., Ranatunga, W. K., Gakh, O., Smith, D. Y., Thompson, J. R., & Isaya, G. (2017) · Metallomics · doi:10.1039/c7mt00089h · Cited by 12

Complementary uses of small angle X-ray scattering and X-ray crystallography

Pillon, M. C., & Guarné, A. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.07.013 · Cited by 13

Hybrid Methods for Macromolecular Modeling by Molecular Mechanics Simulations with Experimental Data

Miyashita, O., & Tama, F. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-2200-6_13 · Cited by 12

SAXSMoW 3.0: New advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale

Neto, M. D. O., Fernandes, A. D. F., Piiadov, V., Craievich, A. F., de Araújo, E. A., & Polikarpov, I. (2021) · Protein Science · doi:10.1002/pro.4227 · Cited by 12

Combining NMR, SAXS and SANS to characterize the structure and dynamics of protein complexes

Delhommel, F., Martínez‐Lumbreras, S., & Sattler, M. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.09.020 · Cited by 11

Farnesylation of human guanylate‐binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization

Lorenz, C., Ince, S., Zhang, T., Cousin, A., Batra, R., Nagel‐Steger, L., Herrmann, C., & Stadler, A. M. (2019) · FEBS Journal · doi:10.1111/febs.15015 · Cited by 11

SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique

Stachowski, T. R., Snell, M. E., & Snell, E. H. (2020) · PLoS ONE · doi:10.1371/journal.pone.0239702 · Cited by 11

Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing

Tarbouriech, N., Chenavier, F., Kawasaki, J., Bachiri, K., Bourhis, J., Legrand, P., Freslon, L.-L., Laurent, E. M. N., Suberbielle, E., Ruigrok, R. W. H., et al. (2022) · Viruses · doi:10.3390/v14112358 · Cited by 13

Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410–DNA interaction using small angle X-ray scattering

Kaur, G., Ren, R., Hammel, M., Horton, J. R., Yang, J., Cao, Y. J., He, C., Lan, F., Lan, X., Blobel, G. A., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkac1274 · Cited by 11

Crystal structures and solution conformations of HtrA from Helicobacter pylori reveal pH-dependent oligomeric conversion and conformational rearrangements

Cui, L., Shi, X., Li, H., Wang, S., Guo, L., Lan, Z., Dai, Y., Zhang, Q., Wu, Y., & Liu, W. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.125274 · Cited by 12

Structures of the troponin core domain containing the cardiomyopathy-causing mutants studied by small-angle X-ray scattering

Matsuo, T., Takeda, S., Oda, T., & Fujiwara, S. (2015) · Biophysics and Physicobiology · doi:10.2142/biophysico.12.0_145 · Cited by 11

Structures of Class Id Ribonucleotide Reductase Catalytic Subunits Reveal a Minimal Architecture for Deoxynucleotide Biosynthesis

Rose, H. R., Maggiolo, A. O., McBride, M. J., Palowitch, G. M., Pandelia, M., Davis, K. M., Yennawar, N. H., & Boal, A. K. (2019) · Biochemistry · doi:10.1021/acs.biochem.8b01252 · Cited by 11

High-Throughput Studies of Protein Shapes and Interactions by Synchrotron Small-Angle X-Ray Scattering

Jeffries, C. M., & Svergun, D. I. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2230-7_15 · Cited by 11

Conformational flexibility in the enterovirus RNA replication platform

Warden, M. S., Cai, K., Cornilescu, G., Burke, J. E., Ponniah, K., Butcher, S. E., & Pascal, S. M. (2018) · RNA · doi:10.1261/rna.069476.118 · Cited by 11

Combined Solution and Crystal Methods Reveal the Electrostatic Tethers That Provide a Flexible Platform for Replication Activities in the Bacteriophage T7 Replisome

Foster, B. M., Rosenberg, D. J., Salvo, H., Stephens, K. L., Bintz, B. J., Hammel, M., Ellenberger, T., Gainey, M. D., & Wallen, J. R. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00525 · Cited by 11

Probing the Average Local Structure of Biomolecules Using Small-Angle Scattering and Scaling Laws

Watson, M. C., & Curtis, J. E. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.03.050 · Cited by 11

Structural control of caspase-generated glutamyl-tRNA synthetase by appended noncatalytic WHEP domains

Halawani, D., Gogonea, V., DiDonato, J. A., Pipich, V., Yao, P., China, A., Topbas, C., Vasu, K., Arif, A., Hazen, S. L., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.807503 · Cited by 11

Modeling Conformationally Flexible Proteins With X-ray Scattering and Molecular Simulations

Powers, K. T., Gildenberg, M. S., & Washington, M. T. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.04.011 · Cited by 13

Deciphering cellular and molecular determinants of human DPCD protein in complex with RUVBL1/RUVBL2 AAA-ATPases

Morais, R. D. S., Santo, P. E., Ley, M., Schelcher, C., Abel, Y., Plassart, L., Deslignière, E., Chagot, M.-E., Quinternet, M., Paiva, A. C. F., et al. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167760 · Cited by 11

Determination of upper limit of Guinier approximation on dilute polydisperse system in SAXS

Chen, R., Li, Z., & He, J. (2024) · Nuclear Instruments and Methods in Physics Research Section B Beam Interactions with Materials and Atoms · doi:10.1016/j.nimb.2024.165377 · Cited by 10

Autoinhibition of ubiquitin-specific protease 8: Insights into domain interactions and mechanisms of regulation

Caba, C., Black, M. K., Liu, Y., DaDalt, A. A., Mallare, J., Fan, L., Harding, R., Wang, Y., Vacratsis, P. O., Huang, R., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107727 · Cited by 11

The MLL1 trimeric catalytic complex is a dynamic conformational ensemble stabilized by multiple weak interactions

Kaustov, L., Lemak, A. S., Wu, H., Faini, M., Fan, L., Fang, X., Zeng, H., Duan, S., Allali‐Hassani, A., Li, F., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz697 · Cited by 10

From Protein Design to the Energy Landscape of a Cold Unfolding Protein

Pulavarti, S. V. S. R. K., Maguire, J. B., Yuen, S., Harrison, J. S., Griffin, J. R., Premkumar, L., Esposito, E. A., Makhatadze, G. I., Garcı́a, A. E., Weiss, T. M., et al. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c10750 · Cited by 10

Novel interaction interfaces mediate the interaction between the NEIL1 DNA glycosylase and mitochondrial transcription factor A

Sharma, N., Thompson, M. K., Arrington, J. F., Terry, D. M., Chakravarthy, S., Prevelige, P. E., & Prakash, A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.893806 · Cited by 11

Describing small-angle scattering profiles by a limited set of intensities

Grant, T. D. (2022) · Journal of Applied Crystallography · doi:10.1107/s1600576722006598 · Cited by 10

Fine-tuning of the Hsc70-based Human Protein Disaggregase Machinery by the Distinctive C-terminal Extension of Apg2

Cabrera, Y., Bernardo‐Seisdedos, G., Dublang, L., Albesa-Jové, D., Orozco, N., Viguera, A. R., Millet, Ó., Muga, A., & Moro, F. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167841 · Cited by 10

Structural insights into translation regulation by the THF-II riboswitch

Xu, L., Xiao, Y., Zhang, J., & Fang, X. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkac1257 · Cited by 10

14‐3‐3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C‐terminal helices

Petrvalská, O., Honzejková, K., Koupilova, N., Heřman, P., Obšilová, V., & Obšil, T. (2023) · Protein Science · doi:10.1002/pro.4805 · Cited by 10

Structural properties of the HNF-1A transactivation domain

Kind, L., Driver, M., Raasakka, A., Onck, P. R., Njølstad, P. R., Arnesen, T., & Kursula, P. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1249939 · Cited by 10

DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island

Heilers, J.-H., Reiners, J., Heller, E.-M., Golzer, A., Smits, S. H. J., & van der Does, C. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz577 · Cited by 12

BEES: Bayesian Ensemble Estimation from SAS

Bowerman, S., Curtis, J. E., Clayton, J., Brookes, E., & Wereszczynski, J. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.06.024 · Cited by 10

Regulation of Protein Kinase R by Epstein-Barr Virus EBER1 RNA

Zerbe, C. M., & Cole, J. L. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00088 · Cited by 10

Predicting RNA structure and dynamics with deep learning and solution scattering

Patt, E., Classen, S., Hammel, M., & Schneidman‐Duhovny, D. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.12.024 · Cited by 9

FlbB forms a distinctive ring essential for periplasmic flagellar assembly and motility in Borrelia burgdorferi

Botting, J. M., Rahman, M. K., Xu, H., Yue, J., Guo, W., Mundo, J. T. D., Hammel, M., Motaleb, M. A., & Liu, J. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012812 · Cited by 9

Inhibition of oligomeric BAX by an anti-apoptotic dimer

Newman, C. E., Gygi, M. A., Alimohamadi, H., DeAngelo, T. M., Camara, C. M., Mintseris, J., Yu, E., Harvey, E. P., Hauseman, Z. J., Fan, L., et al. (2025) · Cell · doi:10.1016/j.cell.2025.10.037 · Cited by 9

An Integrative Structural Biology Analysis of Von Willebrand Factor Binding and Processing by ADAMTS-13 in Solution

del Amo-Maestro, L., Sagar, A., Pompach, P., Goulas, T., Scavenius, C., Ferrero, D. S., Castrillo-Briceño, M., Taulés, M., Enghild, J. J., Bernadó, P., et al. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166954 · Cited by 9

Mechanism of dimerization and structural features of human LI-cadherin

Yui, A., Caaveiro, J. M. M., Kuroda, D., Nakakido, M., Nagatoishi, S., Goda, S., Maruno, T., Uchiyama, S., & Tsumoto, K. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101054 · Cited by 10

Structural and biophysical properties of FopA, a major outer membrane protein of Francisella tularensis

(2022) · doi:10.1371/journal.pone.0267370 · Cited by 9

Transient Prenyltransferase–Cyclase Association in Fusicoccadiene Synthase, an Assembly-Line Terpene Synthase

Faylo, J., van Eeuwen, T., Gupta, K., Murakami, K., & Christianson, D. W. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00509 · Cited by 9

Response regulator PorX coordinates oligonucleotide signalling and gene expression to control the secretion of virulence factors

Schmitz, C., Madej, M., Nowakowska, Z., Cuppari, A., Jacuła, A., Książęk, M., Mikruta, K., Wiśniewski, J. Ł., Pudełko‐Malik, N., Saran, A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1103 · Cited by 9

Structural and functional studies reveal the molecular basis of substrate promiscuity of a glycosyltransferase originating from a major agricultural pest

Arriaza, R. H., Abiskaroon, B., Patel, M., Daneshian, L., Kluza, A., Snoeck, S., Watkins, M. B., Hopkins, J. B., Leeuwen, T. V., Grbić, M., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105421 · Cited by 9

Shape-specific nanostructured protein mimics from de novo designed chimeric peptides

Jiang, L., Yang, S., Lund, R., & Dong, H. (2017) · Biomaterials Science · doi:10.1039/c7bm00906b · Cited by 9

Hexameric assembly of the AAA+ protein McrB is necessary for GTPase activity

Nirwan, N., Singh, P. K., Mishra, G. G., Johnson, C. M., Szczelkun, M. D., Inoue, K., Vinothkumar, K. R., & Saikrishnan, K. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1170 · Cited by 9

Vesicular Stomatitis Virus Phosphoprotein Dimerization Domain Is Dispensable for Virus Growth

Gérard, F. C. A., Jamin, M., Blackledge, M. J., Blondel, D., & Bourhis, J. (2019) · Journal of Virology · doi:10.1128/jvi.01789-19 · Cited by 9

Revisiting the Molecular Interactions between the Tumor Protein TCTP and the Drugs Sertraline/Thioridazine

Malard, F., Jacquet, E., Nhiri, N., Sizun, C., Chabrier, A., Messaoudi, S., Dejeu, J., Betzi, S., Zhang, X., Thureau, A., et al. (2021) · ChemMedChem · doi:10.1002/cmdc.202100528 · Cited by 9

Structure and ensemble refinement against SAXS data: Combining MD simulations with Bayesian inference or with the maximum entropy principle

Chatzimagas, L., & Hub, J. S. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.09.014 · Cited by 9

Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP, and Dok1

Vish, K. J., Stiegler, A. L., & Boggon, T. J. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105098 · Cited by 9

The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil

de Opakua, A. I., Merino, N., Villate, M., Cordeiro, T. N., Ormaza, G., Sänchez‐Carbayo, M., Diercks, T., Bernadó, P., & Blanco, F. J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172507 · Cited by 9

Recombinant production of A1S_0222 from Acinetobacter baumannii ATCC 17978 and confirmation of its DNA-(adenine N6)-methyltransferase activity

Blaschke, U., Suwono, B., Zafari, S., Ebersberger, I., Skiebe, E., Jeffries, C. M., Svergun, D. I., & Wilharm, G. (2018) · Protein Expression and Purification · doi:10.1016/j.pep.2018.06.009 · Cited by 9

Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers

Rahman, S. K., Okazawa, H., & Chen, Y. W. (2019) · Journal of Structural Biology · doi:10.1016/j.jsb.2019.04.003 · Cited by 9

Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling

Ge, J., Remesh, S. G., Hammel, M., Pan, S. Y., Mahan, A. D., Wang, S., & Wang, X. (2019) · Structure · doi:10.1016/j.str.2019.05.011 · Cited by 9

Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56

Lisboa, J., Pereira, C., Pinto, R. D., Rodrigues, I. S., Pereira, L. M. G., Pinheiro, B., Oliveira, P., Pereira, P. J. B., Azevedo, J. E., Durand, D., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43054-z · Cited by 9

Correlating Conformational Equilibria with Catalysis in the Electron Bifurcating EtfABCX of Thermotoga maritima

Murray, D. T., Ge, X., Schut, G. J., Rosenberg, D. J., Hammel, M., Bierma, J. C., Hille, R., Adams, M. W. W., & Hura, G. L. (2023) · Biochemistry · doi:10.1021/acs.biochem.3c00472 · Cited by 8

Small-angle neutron scattering differentiates molecular-level structural models of nanoparticle interfaces

Wu, Y., Liu, X., Rădulescu, A., Porcar, L., Krause‐Heuer, A. M., Jiang, H., Yang, H., Ke, Y., Darwish, T. A., & Luo, Z. (2024) · Nanoscale · doi:10.1039/d4nr04365k · Cited by 8

Ultrafast structural dynamics of carbon–carbon single-bond rotation in transient radical species at non-equilibrium

Lee, S., Ki, H., Im, D., Kim, J., Lee, Y., Gu, J., Segalina, A., Heo, J. N., Cha, Y., Lee, K. W., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57279-7 · Cited by 8

Isoleucine Binding and Regulation of Escherichia coli and Staphylococcus aureus Threonine Dehydratase (IlvA)

Yun, M., Subramanian, C., Miller, K., Jackson, P. D., Radka, C. D., & Rock, C. O. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00168 · Cited by 8

Unraveling low-resolution structural data of large biomolecules by constructing atomic models with experiment-targeted parallel cascade selection simulations

Peng, J., & Zhang, Z. (2016) · Scientific Reports · doi:10.1038/srep29360 · Cited by 8

Biophysical Characterization of Cancer-Related Carbonic Anhydrase IX

Koruza, K., Murray, A. B., Mahon, B. P., Hopkins, J. B., Knecht, W., McKENNA, R. V., & Fisher, S. Z. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155277 · Cited by 8

Styrene–Maleic Acid Copolymer Nanodiscs to Determine the Shape of Membrane Proteins

Jeong, C., Franklin, R., Edler, K. J., Vanommeslaeghe, K., Krueger, S., & Curtis, J. E. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c05050 · Cited by 8

Reconstruction of 3D density from solution scattering

Grant, T. D. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.09.018 · Cited by 8

Structural insights into the formation of repulsive netrin guidance complexes

Priest, J. M., Nichols, E. L., Smock, R. G., Hopkins, J. B., Mendoza, J. L., Meijers, R., Shen, K., & Özkan, E. (2024) · Science Advances · doi:10.1126/sciadv.adj8083 · Cited by 8

Conformational characterization of full-length X-chromosome-linked inhibitor of apoptosis protein (XIAP) through an integrated approach

Polykretis, P., Luchinat, E., Bonucci, A., Giachetti, A., Graewert, M. A., Svergun, D. I., & Banci, L. (2019) · IUCrJ · doi:10.1107/s205225251901073x · Cited by 9

Heparin-mediated dimerization of follistatin

Walker, R. G., Kattamuri, C., Goebel, E. J., Zhang, F., Hammel, M., Tainer, J. A., Linhardt, R. J., & Thompson, T. B. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370220966296 · Cited by 8

SEC-SAXS: Experimental set-up and software developments build up a powerful tool

Pérez, J., Thureau, A., & Vachette, P. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.08.024 · Cited by 8

SAS, refined

Breidenbach, M. A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2634 · Cited by 1

Resolution and validation of SAS-based structural models

Tuukkanen, A. T., Kleywegt, G. J., & Svergun, D. I. (2017) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s2053273317089161

Resolution ofab initioshapes determined from small-angle scattering

Tuukkanen, A. T., Kleywegt, G. J., & Svergun, D. I. (2016) · IUCrJ · doi:10.1107/s2052252516016018 · Cited by 91

Quality control of protein standards for molecular mass determinations by SAXS

Akiyama, S. (2011) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767311099053

Joint use of SAXS and SANS with high-resolution methods for macromolecular solutions

Svergun, D. I. (2008) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767308097080