Particle mesh Ewald: An N ⋅log( N ) method for Ewald sums in large systems

Lipid-Dependent Alternating Access Mechanism of a Bacterial Multidrug ABC Exporter

Immadisetty, K., Hettige, J., & Moradi, M. (2019) · ACS Central Science · doi:10.1021/acscentsci.8b00480 · Cited by 38

Biological and Computational Evaluation of Resveratrol Inhibitors against Alzheimer's Disease

Koukoulitsa, C., Villalonga-Barber, C., Csonka, R., Alexi, X., Leonis, G., Dellis, D., Hamelink, E., Belda, O., Steele, B. R., Micha-Screttas, M., et al. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2014.1003928 · Cited by 37

Understanding the specificity of a docking interaction between JNK1 and the scaffolding protein JIP1

Yan, C., Kaoud, T., Lee, S., Dalby, K. N., & Ren, P. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp1073522 · Cited by 36

Breakage of the oligomeric CaMKII hub by the regulatory segment of the kinase

Karandur, D., Bhattacharyya, M., Xia, Z., Lee, Y. K., Muratcioglu, S., McAffee, D., McSpadden, E. D., Qiu, B., Groves, J. T., Williams, E. R., et al. (2020) · eLife · doi:10.7554/elife.57784 · Cited by 35

Thin Water Films at Multifaceted Hematite Particle Surfaces

Boily, J.-F., Yeşilbaş, M., Md. Musleh Uddin, M., Baiqing, L., Trushkina, Y., & Salazar-Alvarez, G. (2015) · Langmuir · doi:10.1021/acs.langmuir.5b03167 · Cited by 34

Pharmacological hallmarks of allostery at the M4 muscarinic receptor elucidated through structure and dynamics

Vuckovic, Z., Wang, J., Pham, V., Mobbs, J. I., Belousoff, M. J., Bhattarai, A., Burger, W. A., Thompson, G., Yeasmin, M., Nawaratne, V., et al. (2023) · eLife · doi:10.7554/elife.83477 · Cited by 34

Autism-associated SHANK3 missense point mutations impact conformational fluctuations and protein turnover at synapses

Bucher, M., Niebling, S., Han, Y., Molodenskiy, D., Hassani Nia, F., Kreienkamp, H.-J., Svergun, D., Kim, E., Kostyukova, A. S., Kreutz, M. R., et al. (2021) · eLife · doi:10.7554/elife.66165 · Cited by 33

Quantum simulation of exact electron dynamics can be more efficient than classical mean-field methods

Babbush, R., Huggins, W. J., Berry, D. W., Ung, S. F., Zhao, A., Reichman, D. R., Neven, H., Baczewski, A. D., & Lee, J. (2023) · Nature Communications · doi:10.1038/s41467-023-39024-0 · Cited by 32

Revealing druggable cryptic pockets in the Nsp1 of SARS-CoV-2 and other β-coronaviruses by simulations and crystallography

Borsatto, A., Akkad, O., Galdadas, I., Ma, S., Damfo, S., Haider, S., Kozielski, F., Estarellas, C., & Gervasio, F. L. (2022) · eLife · doi:10.7554/elife.81167 · Cited by 32

A molecular propeller effect for chiral separation and analysis

Clemens, J. B., Kibar, O., & Chachisvilis, M. (2015) · Nature Communications · doi:10.1038/ncomms8868 · Cited by 31

Differentiable molecular simulation can learn all the parameters in a coarse-grained force field for proteins

Greener, J. G., & Jones, D. T. (2021) · PLOS ONE · doi:10.1371/journal.pone.0256990 · Cited by 29

Molecular Mechanism of Brassinosteroid Perception by the Plant Growth Receptor BRI1

Aldukhi, F., Deb, A., Zhao, C., Moffett, A. S., & Shukla, D. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b09377 · Cited by 29

Apolipoprotein A1 Forms 5/5 and 5/4 Antiparallel Dimers in Human High-density Lipoprotein

He, Y., Song, H. D., Anantharamaiah, G. M., Palgunachari, M. N., Bornfeldt, K. E., Segrest, J. P., & Heinecke, J. W. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000878 · Cited by 29

Equilibrium Conformational Ensemble of the Intrinsically Disordered Peptide n16N: Linking Subdomain Structures and Function in Nacre

Brown, A. H., Rodger, P. M., Evans, J. S., & Walsh, T. R. (2014) · Biomacromolecules · doi:10.1021/bm501263s · Cited by 28

Mutant thermal proteome profiling for characterization of missense protein variants and their associated phenotypes within the proteome

Peck Justice, S. A., Barron, M. P., Qi, G. D., Wijeratne, H. R. S., Victorino, J. F., Simpson, E. R., Vilseck, J. Z., Wijeratne, A. B., & Mosley, A. L. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014576 · Cited by 28

Temperature sensitive Mutant Proteome Profiling: a novel tool for the characterization of the global impact of missense mutations on the proteome

Peck Justice, S. A., Qi, G., Wijeratne, H. R. S., Victorino, J. F., Simpson, E. R., Wijeratne, A. B., & Mosley, A. L. (2019) · doi:10.1101/2019.12.30.891267 · Cited by 28

Anisotropic Dielectric Relaxation of the Water Confined in Nanotubes for Terahertz Spectroscopy Studied by Molecular Dynamics Simulations

Qi, W., Chen, J., Yang, J., Lei, X., Song, B., & Fang, H. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp3120435 · Cited by 28

Design, synthesis, and in vitro and in vivo characterization of new memantine analogs for Alzheimer’s disease

Turcu, A. L., Companys-Alemany, J., Phillips, M. B., Patel, D. S., Griñán-Ferré, C., Loza, M. I., Brea, J. M., Pérez, B., Soto, D., Sureda, F. X., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114354 · Cited by 27

Oncogenic KEAP1 mutations activate TRAF2-NFκB signaling to prevent apoptosis in lung cancer cells

Deen, A. J., Adinolfi, S., Härkönen, J., Patinen, T., Liu, X., Laitinen, T., Takabe, P., Kainulainen, K., Pasonen-Seppänen, S., Gawriyski, L. M., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103031 · Cited by 27

Orchestrated actin nucleation by the Candida albicans polarisome complex enables filamentous growth

Xie, Y., Loh, Z. Y., Xue, J., Zhou, F., Sun, J., Qiao, Z., Jin, S., Deng, Y., Li, H., Wang, Y., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013890 · Cited by 26

Palbociclib can overcome mutations in cyclin dependent kinase 6 that break hydrogen bonds between the drug and the protein

Hernandez Maganhi, S., Jensen, P., Caracelli, I., Zukerman Schpector, J., Fröhling, S., & Friedman, R. (2017) · Protein Science · doi:10.1002/pro.3135 · Cited by 25

Phosphorylation of the retinoic acid receptor alpha induces a mechanical allosteric regulation and changes in internal dynamics

Chebaro, Y., Amal, I., Rochel, N., Rochette-Egly, C., Stote, R. H., & Dejaegere, A. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003012 · Cited by 25

Structure and dynamics of differential ligand binding in the human ρ-type GABAA receptor

Cowgill, J., Fan, C., Haloi, N., Tobiasson, V., Zhuang, Y., Howard, R. J., & Lindahl, E. (2023) · Neuron · doi:10.1016/j.neuron.2023.08.006 · Cited by 25

Insight into the Interaction of Furfural with Metallic Surfaces in the Electrochemical Hydrogenation Process

Lenk, T., Rabet, S., Sprick, M., Raabe, G., & Schröder, U. (2023) · ChemPhysChem · doi:10.1002/cphc.202200614 · Cited by 26

Evidence for a trap-and-flip mechanism in a proton-dependent lipid transporter

Lambert, E., Mehdipour, A. R., Schmidt, A., Hummer, G., & Perez, C. (2022) · Nature Communications · doi:10.1038/s41467-022-28361-1 · Cited by 24

‘Asynchronous reciprocal coupling of Martini 2.2 coarse-grained and CHARMM36 all-atom simulations in an automated multiscale framework’

López, C. A., Zhang, X., Aydin, F., Shrestha, R., Van, Q. N., Stanley, C. B., Carpenter, T. S., Nguyen, K., Patel, L. A., Chen, D., et al. (2022) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c00168 · Cited by 18

Short-Sequence Superadhesive Peptides with Topologically Enhanced Cation−π Interactions

Chang, H., Adibnia, V., Li, C., Su, R., Qi, W., & Banquy, X. (2021) · Chemistry of Materials · doi:10.1021/acs.chemmater.1c01171 · Cited by 22

Structural delineation and computational design of SARS-CoV-2-neutralizing antibodies against Omicron subvariants

Moriyama, S., Anraku, Y., Taminishi, S., Adachi, Y., Kuroda, D., Kita, S., Higuchi, Y., Kirita, Y., Kotaki, R., Tonouchi, K., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39890-8 · Cited by 22

Predicting improved protein conformations with a temporal deep recurrent neural network

Pfeiffenberger, E., & Bates, P. A. (2018) · PLOS ONE · doi:10.1371/journal.pone.0202652 · Cited by 21

Exploring the Alternative Conformation of a Known Protein Structure Based on Contact Map Prediction

(2023) · doi:10.1021/acs.jcim.3c01381 · Cited by 21

Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation

Bartesaghi, S., Herrera, D., Martinez, D. M., Petruk, A., Demicheli, V., Trujillo, M., Martí, M. A., Estrín, D. A., & Radi, R. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.04.006 · Cited by 18

Cyclophilin A Inhibition: Targeting Transition-State-Bound Enzyme Conformations for Structure-Based Drug Design

Nagaraju, M., McGowan, L. C., & Hamelberg, D. (2013) · Journal of Chemical Information and Modeling · doi:10.1021/ci300432w · Cited by 18

Mutations at the Qo Site of the Cytochrome bc1 Complex Strongly Affect Oxygen Binding

Husen, P., & Solov’yov, I. A. (2017) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b08226 · Cited by 17

Rational design of 19F NMR labelling sites to probe protein structure and interactions

Streit, J. O., Chan, S. H. S., Daya, S., & Christodoulou, J. (2025) · Nature Communications · doi:10.1038/s41467-025-59105-6 · Cited by 17

The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing

Pfoh, R., Subramanian, A. S., Huang, J., Little, D. J., Forman, A., DiFrancesco, B. R., Balouchestani-Asli, N., Kitova, E. N., Klassen, J. S., Pomès, R., et al. (2022) · PLOS Pathogens · doi:10.1371/journal.ppat.1010750 · Cited by 17

KIDINS220 and InsP8 safeguard the stepwise regulation of phosphate exporter XPR1

(2025) · doi:10.1016/j.molcel.2025.08.003 · Cited by 17

Understanding the good and poor cell targeting activity of gold nanostructures functionalized with molecular units for the epidermal growth factor receptor

Mazzuca, C., Di Napoli, B., Biscaglia, F., Ripani, G., Rajendran, S., Braga, A., Benna, C., Mocellin, S., Gobbo, M., Meneghetti, M., et al. (2019) · Nanoscale Advances · doi:10.1039/c9na00096h · Cited by 16

Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration

Copley, K. E., Mauna, J. C., Danielson, H. L., Chen, Q., Ozguney, B., Ngo, M., Xie, L., Smirnov, A., Davis, M., Mayne, L., et al. (2026) · Science · doi:10.1126/science.adv3301 · Cited by 16

Insights into the structure and function of the human organic anion transporter 1 in lipid bilayer membranes

Janaszkiewicz, A., Tóth, Á., Faucher, Q., Martin, M., Chantemargue, B., Barin-Le Guellec, C., Marquet, P., & Di Meo, F. (2022) · Scientific Reports · doi:10.1038/s41598-022-10755-2 · Cited by 15

Structural insights into E. coli porphobilinogen deaminase during synthesis and exit of 1-hydroxymethylbilane

Bung, N., Pradhan, M., Srinivasan, H., & Bulusu, G. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003484 · Cited by 14

Unveiling the Conformational Dynamics of the Histone Tails Using Markov State Modeling

Patel, R., & Loverde, S. M. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5c00196 · Cited by 13

European Robin Cryptochrome-4a Associates with Lipid Bilayers in an Ordered Manner, Fulfilling a Molecular-Level Condition for Magnetoreception

(2025) · doi:10.1021/acschembio.4c00576 · Cited by 12

Amino acid sequence encodes protein abundance shaped by protein stability at reduced synthesis cost

(2024) · doi:10.1002/pro.5239 · Cited by 12

AI-driven prediction of SARS-CoV-2 variant binding trends from atomistic simulations

Capponi, S., Wang, S., Navarro, E. J., & Bianco, S. (2021) · The European Physical Journal E · doi:10.1140/epje/s10189-021-00119-5 · Cited by 12

Association of Both Inhibitory and Stimulatory Gα Subunits Implies Adenylyl Cyclase 5 Deactivation

van Keulen, S. C., Narzi, D., & Rothlisberger, U. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00662 · Cited by 11

LassoPred: a tool to predict the 3D structure of lasso peptides

Ouyang, X., Ran, X., Xu, H., Al-Abssi, R., Zhao, Y.-L., Link, A. J., & Yang, Z. J. (2025) · Nature Communications · doi:10.1038/s41467-025-60544-4 · Cited by 11

Probing the Microscopic Behavior of PFOS Clustering and Adsorption at LNAPL Interfaces; a PFOS–Water–Cyclohexane System

Sookhak Lari, K., Reinhardt, A., Warden, A. C., Rayner, J. L., & Davis, G. B. (2025) · Environmental Science & Technology · doi:10.1021/acs.est.5c01748 · Cited by 11

Interfacial water confers transcription factors with dinucleotide specificity

(2025) · doi:10.1038/s41594-024-01449-6 · Cited by 11

Investigation of the interactions between the EphB2 receptor and SNEW peptide variants

Ma, B., Kolb, S., Diprima, M., Karna, M., Tosato, G., Yang, Q., Huang, Q., & Nussinov, R. (2014) · Growth Factors · doi:10.3109/08977194.2014.985786 · Cited by 10

Structure of the Human Signal Peptidase Complex Reveals the Determinants for Signal Peptide Cleavage

Liaci, A. M., Steigenberger, B., Tamara, S., de Souza, P. C. T., Gröllers-Mulderij, M., Ogrissek, P., Marrink, S. J., Scheltema, R. A., & Förster, F. (2020) · doi:10.1101/2020.11.11.378711 · Cited by 10

Resolving the conformational ensemble of a membrane protein by integrating small-angle scattering with AlphaFold

Lidbrink, S. E., Howard, R. J., Haloi, N., & Lindahl, E. (2025) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1013187 · Cited by 9

Cosolvent and Dynamic Effects in Binding Pocket Search by Docking Simulations

(2021) · doi:10.1021/acs.jcim.1c00924 · Cited by 9

Free Energy of Membrane Pore Formation and Stability from Molecular Dynamics Simulations

Rivel, T., Biriukov, D., Kabelka, I., & Vácha, R. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01960 · Cited by 9

Human Carboxylesterase 2 in Cocaine Metabolism

Figueiredo, P. R., González, R. D., & Carvalho, A. T. P. (2021) · Molecular Catalysis · doi:10.1016/j.mcat.2021.111938 · Cited by 9

Allosteric Regulation in the Ligand Binding Domain of Retinoic Acid Receptorγ

Chebaro, Y., Sirigu, S., Amal, I., Lutzing, R., Stote, R. H., Rochette-Egly, C., Rochel, N., & Dejaegere, A. (2017) · PLOS ONE · doi:10.1371/journal.pone.0171043 · Cited by 8

Multiscale Computational Study of the Conformation of the Full-Length Intrinsically Disordered Protein MeCP2

Chávez-García, C., Hénin, J., & Karttunen, M. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c01354 · Cited by 8

Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase

Fraser, A., Sokolova, M. L., Drobysheva, A. V., Gordeeva, J. V., Borukhov, S., Jumper, J., Severinov, K. V., & Leiman, P. G. (2022) · Nature Communications · doi:10.1038/s41467-022-31214-6 · Cited by 7

Unveiling the Catalytic Mechanism and Conformational Dynamics of Guinea Pig l -Asparaginase Type 1 for Leukemia Drug Design

Andjelkovic, M., Zinovjev, K., Ruiz-Pernía, J. J., & Tuñón, I. (2025) · ACS Catalysis · doi:10.1021/acscatal.4c07791 · Cited by 7

Identification and characterization of substrate- and product-selective nylon hydrolases

Drufva, E. E., Cahill, J. F., Saint-Vincent, P. M. B., Williams, A. N., Bocharova, V., Capra, N., Meilleur, F., Carper, D. L., Bourgery, C., Miyazaki, K., et al. (2025) · Chem Catalysis · doi:10.1016/j.checat.2025.101418 · Cited by 7

DNA Wrapping by a tetrameric bacterial histone

(2025) · doi:10.1038/s41467-025-67425-w · Cited by 7

Continuous millisecond conformational cycle of a DEAH box helicase reveals control of domain motions by atomic-scale transitions

Becker, R. A., & Hub, J. S. (2023) · Communications Biology · doi:10.1038/s42003-023-04751-z · Cited by 7

An allosteric network governs Tom70 conformational dynamics to coordinate mitochondrial import

Bachochin, M. J., McGuire, K. L., Cook, B. D., Ye, Q., Silletti, S., Corbett, K. D., Komives, E. A., & Herzik, M. A. (2026) · Structure · doi:10.1016/j.str.2025.11.011 · Cited by 7

TMEM63 proteins act as mechanically activated cholesterol modulated lipid scramblases contributing to membrane mechano-resilience

Lin, Y., Zhou, Z., Han, Y., Cheng, D., Wang, H. J., Ju, L. A., Zhang, Y., Cox, C. D., & Corry, B. (2026) · Nature Communications · doi:10.1038/s41467-026-68919-x · Cited by 7

Prediction of Kv11.1 potassium channel PAS-domain variants trafficking via machine learning

Immadisetty, K., Fang, X., Ramon, G. S., Hartle, C. M., McCoy, T. P., Center, R. G., Mirshahi, T., Delisle, B. P., & Kekenes-Huskey, P. M. (2023) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2023.05.002 · Cited by 5

Molecular insights into the role of Estrogen Receptor Beta in Ecdysterone Mediated Anabolic Activity

Tariq, S. S., Sardar, M., Shafiq, M., Heinz, H., Nur-e-Alam, M., Ahmed, A., & Ul-Haq, Z. (2025) · PLoS One · doi:10.1371/journal.pone.0320865 · Cited by 4

Mapping structural and dynamic divergence across the MBOAT family

Ansell, T. B., Healy, M., Coupland, C. E., Sansom, M. S. P., & Siebold, C. (2024) · Structure · doi:10.1016/j.str.2024.03.014 · Cited by 4

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) · doi:10.1101/2022.05.24.493318 · Cited by 4

Conformational dynamics of a histidine molecular switch in a cation/proton antiporter

(2025) · doi:10.1016/j.bbabio.2025.149563 · Cited by 4

A novel model for proton transport mediated by uncoupling protein 1

Jacobsen, L., Menon, S., Gaudry, M. J., Hakami Zanjani, A. A., Reinholdt, P., Jastroch, M., & Khandelia, H. (2025) · Protein Science · doi:10.1002/pro.70357 · Cited by 3

Employing steered MD simulations for effective virtual screening: Active pharmacophore search by dynamic corrections to target MKK3-MYC interactions

Ulug, M. E., Ikram, S., Sayyah, E., & Durdağı, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142602 · Cited by 3

The Oncogenic EGFR–SHC1 Fusion Confers Insensitivity to EGFR-TKIs via Dual Activation of N-EGFR Kinase Domain and C-SHC1 Phosphorylation Sites in Lung Cancer

Zheng, J., Zhao, S., Zhan, J., Zhuang, W., Chen, M., Jiang, W., Huang, Y., He, J., Hu, L., Pang, L., et al. (2026) · Cancer Discovery · doi:10.1158/2159-8290.cd-25-1936 · Cited by 2

The flexible stalk domain of sTREM2 modulates its interactions with brain-based phospholipids

(2025) · doi:10.7554/elife.102269.3 · Cited by 2

EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery

Wijeratne, H. R. S., Runnebohm, A. M., Barron, M. P., Hampton, A. J., Li, R., Peck Justice, S. A., Lenceski, S. H., Rooney, J. D., Smith-Kinnaman, W. R., Chang, G. S., et al. (2026) · doi:10.64898/2026.01.26.701775 · Cited by 1

Structural implications of glycosylation on the voltage-gated sodium channel β3-subunit

Beaudoin, C. A., Hayes, J., Liu, H., Namadurai, S., Deery, M. J., August, E. A., Krasner, S., Hamaia, S. W., Salvage, S. C., Huang, C. L.-H., et al. (2026) · Journal of Structural Biology · doi:10.1016/j.jsb.2026.108321 · Cited by 1

On the Role of VP3-PI3P Interaction in Birnavirus Endosomal Membrane Targeting

(2024) · doi:10.1101/2024.02.20.581221 · Cited by 1

Disulfide bridge-dependent dimerization triggers FGF2 membrane translocation into the extracellular space

Lolicato, F., Steringer, J., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H., et al. (2023) · doi:10.7554/elife.88579.2 · Cited by 1

The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing

(2023) · doi:10.32920/24746796 · Cited by 1

On the curvature and relaxation of microtubule plus-end tips

Skóra, T., Wu, J., Beckett, D., Xue, W., Voth, G. A., & Bidone, T. C. (2026) · Biophysical Journal · doi:10.1016/j.bpj.2025.07.003 · Cited by 1

A computational model for lipid-anchored polysaccharide export by the outer membrane protein GfcD

Fruet, C., Martinez-Goikoetxea, M., Merino, F., & Lupas, A. N. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.08.012 · Cited by 1

Free Energy Landscapes and Residue Network Analysis for Six SARS-CoV-2 Targets in Complex with Plausible Phytochemical Inhibitors from Withania Somnifera: 1 µS Molecular Dynamics Simulations

Parida, P. K., Paul, D., & Chakravorty, D. (2021) · doi:10.26434/chemrxiv.14499306.v1

The impact of glycosylation on the conformational ensembles of β-, δ-, and γ-sarcoglycans

Fazelpour, E., Cook, G. A., & McCullagh, M. (2026) · Biophysical Journal · doi:10.1016/j.bpj.2026.04.018

Disulfide bridge-dependent dimerization triggers FGF2 membrane translocation into the extracellular space

Lolicato, F., Steringer, J. P., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H.-M., et al. (2024) · eLife · doi:10.7554/elife.88579.3

The Impact of Glycosylation on the Conformational Ensembles of β -, δ -, and γ Sarcoglycans

Fazelpour, E., Cook, G. A., & McCullagh, M. (2026) · doi:10.64898/2026.01.13.699269

Computational optimization of DEK1 calpain domain solubility through integrated structural modelling and data-driven targeted mutagenesis

Dabiri, M., Levarski, Z., Struhárňanská, E., Demko, V., Beneš, V., Turňa, J., & Stuchlík, S. (2026) · Scientific Reports · doi:10.1038/s41598-026-38805-z

SMC complex unidirectionally translocates DNA by coupling segment capture with an asymmetric kleisin path

Yamauchi, M., Brandani, G. B., Terakawa, T., & Takada, S. (2026) · eLife · doi:10.7554/elife.106752