UCSF Chimera—A visualization system for exploratory research and analysis

PROSITE: a documented database using patterns and profiles as motif descriptors

Sigrist, C. J. A. (2002) · Briefings in Bioinformatics · doi:10.1093/bib/3.3.265 · Cited by 913

The Role of Mass Spectrometry in Structural Studies of Flavin-Based Electron Bifurcating Enzymes

Tokmina-Lukaszewska, M., Patterson, A., Berry, L., Scott, L., Balasubramanian, N., & Bothner, B. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01397 · Cited by 15

Structural basis of conformational transitions in the active site and 80′s loop in the FK506-binding protein FKBP12

Mustafi, S. M., Brecher, M., Zhang, J., Li, H., Lemaster, D. M., & Hernández, G. (2014) · Biochemical Journal · doi:10.1042/bj20131429 · Cited by 15

Molecular Basis for the Evolution of Species-Specific Hemoglobin Capture by Staphylococcus aureus

Choby, J. E., Buechi, H. B., Farrand, A. J., Skaar, E. P., & Barber, M. F. (2018) · mBio · doi:10.1128/mbio.01524-18 · Cited by 15

Structure of a Rhs effector clade domain provides mechanistic insights into type VI secretion system toxin delivery

Hayes, B. K., Harper, M., Venugopal, H., Lewis, J. M., Wright, A., Lee, H.-C., Steele, J. R., Steer, D. L., Schittenhelm, R. B., Boyce, J. D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52950-x · Cited by 15

A Noncoding A-to-U Kozak Site Change Related to the High Transmissibility of Alpha, Delta, and Omicron VOCs

Yang, J., Cui, Y., Yu, D., Zhang, G., Cao, R., Gu, Z., Dai, G., Wu, X., Ling, Y., Yi, C., et al. (2023) · Molecular Biology and Evolution · doi:10.1093/molbev/msad142 · Cited by 15

EGOC inhibits TOROID polymerization by structurally activating TORC1

Prouteau, M., Bourgoint, C., Felix, J., Bonadei, L., Sadian, Y., Gabus, C., Savvides, S. N., Gutsche, I., Desfosses, A., & Loewith, R. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00912-6 · Cited by 15

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

Validation of an Allosteric Binding Site of Src Kinase Identified by Unbiased Ligand Binding Simulations

Mingione, V. R., Foda, Z. H., Paung, Y., Philipose, H., Rangwala, A. M., Shan, Y., & Seeliger, M. A. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167628 · Cited by 13

Structural basis of microtubule-mediated signal transduction

Choi, S. R., Blum, T. B., Giono, M., Roy, B., Vakonakis, I., Schmid, D., Oelgarth, N., Ranganathan, A., Gossert, A. D., Shivashankar, G. V., et al. (2026) · Cell · doi:10.1016/j.cell.2025.11.011 · Cited by 14

The conserved HIV-1 spacer peptide 2 triggers matrix lattice maturation

(2025) · doi:10.1038/s41586-025-08624-9 · Cited by 14

Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410

(2023) · doi:10.1038/s41467-023-42073-0 · Cited by 14

The structure of a Plasmodium vivax Tryptophan Rich Antigen domain suggests a lipid binding function for a pan-Plasmodium multi-gene family

Kundu, P., Naskar, D., McKie, S. J., Dass, S., Kanjee, U., Introini, V., Ferreira, M. U., Cicuta, P., Duraisingh, M., Deane, J. E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40885-8 · Cited by 14

Structural and functional properties of the transporter SLC26A6 reveal mechanism of coupled anion exchange

Tippett, D. N., Breen, C., Butler, S. J., Sawicka, M., & Dutzler, R. (2023) · eLife · doi:10.7554/elife.87178 · Cited by 14

Base excision repair pathways of bacteria: New promise for an old problem

Kurthkoti, K., Kumar, P., Sang, P. B., & Varshney, U. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0267 · Cited by 12

Utilizing Genome-Wide mRNA Profiling to Identify the Cytotoxic Chemotherapeutic Mechanism of Triazoloacridone C-1305 as Direct Microtubule Stabilization

Króliczewski, J., Bartoszewska, S., Dudkowska, M., Janiszewska, D., Biernatowska, A., Crossman, D. K., Krzymiński, K., Wysocka, M., Romanowska, A., Baginski, M., et al. (2020) · Cancers · doi:10.3390/cancers12040864 · Cited by 13

Majority of the Highly Variable NLRs in Maize Share Genomic Location and Contain Additional Target-Binding Domains

Prigozhin, D. M., Sutherland, C. A., Rangavajjhala, S., & Krasileva, K. V. (2025) · Molecular Plant-Microbe Interactions® · doi:10.1094/mpmi-05-24-0047-fi · Cited by 13

Structure of Mycobacterial NDH-2 Bound to a 2-Mercapto-Quinazolinone Inhibitor

Liang, Y., Bueler, S. A., Cook, G. M., & Rubinstein, J. L. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00049 · Cited by 13

Dissecting the molecular basis for the modulation of neurotransmitter GPCR signaling by GINIP

Luebbers, A., Gonzalez-Hernandez, A. J., Zhou, M., Eyles, S. J., Levitz, J., & Garcia-Marcos, M. (2024) · Structure · doi:10.1016/j.str.2023.10.010 · Cited by 13

Spatial N-glycan rearrangement on α5β1 integrin nucleates galectin-3 oligomers to determine endocytic fate

Shafaq-Zadah, M., Dransart, E., Hamitouche, I., Wunder, C., Chambon, V., Valades-Cruz, C. A., Leconte, L., Sarangi, N. K., Robinson, J., Bai, S.-K., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64523-7 · Cited by 12

High-affinity PQQ import is widespread in Gram-negative bacteria

Munder, F., Voutsinos, M., Hantke, K., Venugopal, H., & Grinter, R. (2025) · Science Advances · doi:10.1126/sciadv.adr2753 · Cited by 12

Fisetin as a Blueprint for Senotherapeutic Agents – Elucidating Geroprotective and Senolytic Properties with Molecular Modeling

Spiegel, M. (2025) · Chemistry – A European Journal · doi:10.1002/chem.202403755 · Cited by 12

HIV-1 Intasomes Assembled with Excess Integrase C-Terminal Domain Protein Facilitate Structural Studies by Cryo-EM and Reveal the Role of the Integrase C-Terminal Tail in HIV-1 Integration

Li, M., Li, Z., Chen, X., Cui, Y., Engelman, A. N., & Craigie, R. (2024) · Viruses · doi:10.3390/v16071166 · Cited by 12

Human Gut Metagenomes Encode Diverse GH156 Sialidases

Mann, E., Shekarriz, S., & Surette, M. G. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.01755-22 · Cited by 12

Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation

Hernandez, G., Martins, M. L., Fernandes, N. P., Veloso, T., Lopes, J., Gomes, T., & Cordeiro, T. N. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf502 · Cited by 12

Multienzyme deep learning models improve peptide de novo sequencing by mass spectrometry proteomics

Gueto-Tettay, C., Tang, D., Happonen, L., Heusel, M., Khakzad, H., Malmström, J., & Malmström, L. (2023) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1010457 · Cited by 12

Structural basis of RECQL5-induced RNA polymerase II transcription braking and subsequent reactivation

Zhang, L., Gordiyenko, Y., Morgan, T., Franco, C., Tufegdžić Vidaković, A., & Zhang, S. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01586-6 · Cited by 12

Harmonin homology domain-mediated interaction of RTEL1 helicase with RPA and DNA provides insights into its recruitment to DNA repair sites

Kumar, N., Taneja, A., Ghosh, M., Rothweiler, U., Sundaresan, N. R., & Singh, M. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkad1208 · Cited by 12

Archaeal type six secretion system mediates contact-dependent antagonism

Zachs, T., Malit, J. J. L., Xu, J., Schürch, A., Sivabalasarma, S., Nußbaum, P., Albers, S.-V., & Pilhofer, M. (2024) · Science Advances · doi:10.1126/sciadv.adp7088 · Cited by 12

Phytoecdysteroids and Anabolic Effect of Atriplex dimorphostegia: UPLC-PDA-MS/MS Profiling, In Silico and In Vivo Models

Zaghloul, E., Handousa, H., Singab, A. N. B., Elmazar, M. M., Ayoub, I. M., & Swilam, N. (2023) · Plants · doi:10.3390/plants12010206 · Cited by 11

Convergent molecular evolution of thermogenesis and circadian rhythm in Arctic ruminants

Li, M., Li, X., Wu, Z., Zhang, G., Wang, N., Dou, M., Liu, S., Yang, C., Meng, G., Sun, H., et al. (2023) · Proceedings of the Royal Society B: Biological Sciences · doi:10.1098/rspb.2023.0538 · Cited by 12

Phylogenetic and Protein Structure Analyses Provide Insight into the Evolution and Diversification of the CD36 Domain “Apex” among Scavenger Receptor Class B Proteins across Eukarya

(2023) · doi:10.1093/gbe/evad218 · Cited by 11

Novel Insulin-Like Growth Factor 1 Gene Mutation: Broadening of the Phenotype and Implications for Insulin Resistance

Giacomozzi, C., Martin, A., Fernández, M. C., Gutiérrez, M., Iascone, M., Domené, H. M., Dominici, F. P., Bergadá, I., Cangiano, B., Persani, L., et al. (2023) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgac738 · Cited by 10

Identification and characterisation of the tegument-expressed aldehyde dehydrogenase SmALDH_312 of Schistosoma mansoni, a target of disulfiram

Beutler, M., Harnischfeger, J., Weber, M. H. W., Hahnel, S. R., Quack, T., Blohm, A., Ueberall, M. E., Timm, T., Lochnit, G., Rennar, G. A., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115179 · Cited by 10

Structural mimicry of UM171 and neomorphic cancer mutants co-opts E3 ligase KBTBD4 for HDAC1/2 recruitment

Chen, Z., Chi, G., Balo, T., Chen, X., Montes, B. R., Clifford, S. C., D’Angiolella, V., Szabo, T., Kiss, A., Novak, T., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58350-z · Cited by 10

Ancient pangenomic origins of noncanonical NLR genes underlying the recent evolutionary rescue of a staple crop

VanGessel, C. J., Felderhoff, T. J., Prigozhin, D. M., Cui, M., Pressoir, G., Healey, A. L., Lovell, J. T., Nalam, V. J., Nishimura, M. T., & Morris, G. P. (2025) · Science Advances · doi:10.1126/sciadv.ady1667 · 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

Structural foundation for the role of enterococcal PrgB in conjugation, biofilm formation, and virulence

Sun, W.-S., Lassinantti, L., Järvå, M., Schmitt, A., ter Beek, J., & Berntsson, R. P.-A. (2023) · eLife · doi:10.7554/elife.84427.3 · Cited by 10

Distinct pathways for evolution of enhanced receptor binding and cell entry in SARS-like bat coronaviruses

(2024) · doi:10.1371/journal.ppat.1012704 · Cited by 10

Discovery of novel replication proteins for large plasmids in cyanobacteria and their potential applications in genetic engineering

Ohdate, K., Sakata, M., Maeda, K., Sakamaki, Y., Nimura-Matsune, K., Ohbayashi, R., Hess, W. R., & Watanabe, S. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1311290 · Cited by 9

Structural journey of an insecticidal protein against western corn rootworm

Marini, G., Poland, B., Leininger, C., Lukoyanova, N., Spielbauer, D., Barry, J. K., Altier, D., Lum, A., Scolaro, E., Ortega, C. P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39891-7 · Cited by 9

Proteolytic cleavage and inactivation of the TRMT1 tRNA modification enzyme by SARS-CoV-2 main protease

Zhang, K., Eldin, P., Ciesla, J. H., Briant, L., Lentini, J. M., Ramos, J., Cobb, J., Munger, J., & Fu, D. (2024) · eLife · doi:10.7554/elife.90316.3 · Cited by 9

Non-canonical Staphylococcus aureus pathogenicity island repression

Miguel-Romero, L., Alqasmi, M., Bacarizo, J., Tan, J. A., Cogdell, R. J., Chen, J., Byron, O., Christie, G. E., Marina, A., & Penadés, J. R. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac855 · Cited by 9

Structure of the F-tractin–F-actin complex

Shatskiy, D., Sivan, A., Wedlich-Söldner, R., & Belyy, A. (2025) · Journal of Cell Biology · doi:10.1083/jcb.202409192 · Cited by 9

An integrated structural model of the DNA damage-responsive H3K4me3 binding WDR76:SPIN1 complex with the nucleosome

Liu, X., Zhang, Y., Wen, Z., Hao, Y., Banks, C. A. S., Cesare, J., Bhattacharya, S., Arvindekar, S., Lange, J. J., Xie, Y., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318601121 · Cited by 9

Production and characterisation of stabilised PV-3 virus-like particles using Pichia pastoris

Sherry, L., Grehan, K., Swanson, J. J., Bahar, M. W., Porta, C., Fry, E. E., Stuart, D. I., Rowlands, D. J., & Stonehouse, N. J. (2022) · doi:10.1101/2022.09.16.508282 · Cited by 18

Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures

Conley, M., Emmott, E., Orton, R., Taylor, D., Carneiro, D. G., Murata, K., Goodfellow, I. G., Hansman, G. S., & Bhella, D. (2017) · Journal of General Virology · doi:10.1099/jgv.0.000658 · Cited by 8

Computational investigation unveils pathogenic LIG3 non-synonymous mutations and therapeutic targets in acute myeloid leukemia

Hossen, M. A., Jahan, U. M. S., Hossain, M. A., Asif, K. H., Rahman, A., Ahmed, S., Uddin, M. M., Amin, M. F., Barik, M. A., Islam, M. J., et al. (2025) · PLOS One · doi:10.1371/journal.pone.0320550 · Cited by 8

A unified analysis of evolutionary and population constraint in protein domains highlights structural features and pathogenic sites

MacGowan, S. A., Madeira, F., Britto-Borges, T., & Barton, G. J. (2024) · Communications Biology · doi:10.1038/s42003-024-06117-5 · Cited by 8

Structure of the Drosophila melanogaster Flight Muscle Myosin Filament at 4.7 Å Resolution Reveals New Details of Non-Myosin Proteins

(2023) · doi:10.3390/ijms241914936 · Cited by 8

Structure and regulation of full-length human leucine-rich repeat kinase 1

Metcalfe, R. D., Martinez Fiesco, J. A., Bonet-Ponce, L., Kluss, J. H., Cookson, M. R., & Zhang, P. (2023) · Nature Communications · doi:10.1038/s41467-023-40532-2 · Cited by 8

Structural similarities between the metacyclic and bloodstream form variant surface glycoproteins of the African trypanosome

Chandra, M., Đaković, S., Foti, K., Zeelen, J. P., van Straaten, M., Aresta-Branco, F., Tihon, E., Lübbehusen, N., Ruppert, T., Glover, L., et al. (2023) · PLOS Neglected Tropical Diseases · doi:10.1371/journal.pntd.0011093 · Cited by 8

Molecular insights into RNA recognition and gene regulation by the TRIM-NHL protein Mei-P26

Salerno-Kochan, A., Horn, A., Ghosh, P., Nithin, C., Kościelniak, A., Meindl, A., Strauss, D., Krutyhołowa, R., Rossbach, O., Bujnicki, J. M., et al. (2022) · Life Science Alliance · doi:10.26508/lsa.202201418 · Cited by 8

Cryo-EM structure of native honey bee vitellogenin

Montserrat-Canals, M., Schnelle, K., Leipart, V., Halskau, Ø., Amdam, G. V., Moeller, A., Cunha, E. S., & Luecke, H. (2025) · Nature Communications · doi:10.1038/s41467-025-58575-y · Cited by 7

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

Comprehensive analysis of insertion sequences within rRNA genes of CPR bacteria and biochemical characterization of a homing endonuclease encoded by these sequences

(2024) · doi:10.1128/jb.00074-24 · Cited by 7

Hidden GPCR structural transitions addressed by multiple walker supervised molecular dynamics (mwSuMD)

Deganutti, G., Pipito, L., Rujan, R. M., Weizmann, T., Griffin, P., Ciancetta, A., Moro, S., & Reynolds, C. A. (2025) · eLife · doi:10.7554/elife.96513 · Cited by 7

Substrate recruitment via eIF2γ enhances catalytic efficiency of a holophosphatase that terminates the integrated stress response

Yan, Y., Shetty, M., Harding, H. P., George, G., Zyryanova, A., Labbé, K., Mafi, A., Hao, Q., Sidrauski, C., & Ron, D. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2320013121 · Cited by 7

Tracing Potential Covalent Inhibitors of an E3 Ubiquitin Ligase through Target-Focused Modelling

Bjij, I., Ramharack, P., Khan, S., Cherqaoui, D., & Soliman, M. E. S. (2019) · Molecules · doi:10.3390/molecules24173125 · Cited by 6

AlphaFold2 Reveals Structural Patterns of Seasonal Haplotype Diversification in SARS-CoV-2 Nucleocapsid Protein Variants

Ali, M. A., & Caetano-Anollés, G. (2024) · Viruses · doi:10.3390/v16091358 · Cited by 6

Cryo-EM structures reveal the activation and substrate recognition mechanism of human enteropeptidase

Yang, X., Ding, Z., Peng, L., Song, Q., Zhang, D., Cui, F., Xia, C., Li, K., Yin, H., Li, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34364-9 · Cited by 6

Selective Inhibition of Deamidated Triosephosphate Isomerase by Disulfiram, Curcumin, and Sodium Dichloroacetate: Synergistic Therapeutic Strategies for T-Cell Acute Lymphoblastic Leukemia in Jurkat Cells

Flores-López, L. A., De la Mora-De la Mora, I., Malagón-Reyes, C. M., García-Torres, I., Martínez-Pérez, Y., López-Herrera, G., Hernández-Alcántara, G., León-Avila, G., López-Velázquez, G., Olaya-Vargas, A., et al. (2024) · Biomolecules · doi:10.3390/biom14101295 · Cited by 6

RECQ4-MUS81 interaction contributes to telomere maintenance with implications to Rothmund-Thomson syndrome

Ashraf, R., Polasek-Sedlackova, H., Marini, V., Prochazkova, J., Hasanova, Z., Zacpalova, M., Boudova, M., & Krejci, L. (2025) · Nature Communications · doi:10.1038/s41467-025-56518-1 · Cited by 6

Single-dose avian influenza A(H5N1) Clade 2.3.4.4b hemagglutinin–Matrix-M® nanoparticle vaccine induces neutralizing responses in nonhuman primates

Patel, N., Rehman, A., Trost, J. F., Flores, R., Longacre, Z., Guebre-Xabier, M., Zhou, H., Zhou, B., Jacobson, K., Jiang, D., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61964-y · Cited by 6

Asymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase

(2023) · doi:10.1515/hsz-2022-0273 · Cited by 6

In silico docking yields small molecule negative allosteric modulators targeting the core of Frizzled 7

Scharf, M. M., Kinsolving, J., Grätz, L., Voss, J. H., Carrasco-Busturia, D., Forsberg, B., Kolb, P., & Schulte, G. (2025) · Nature Communications · doi:10.1038/s41467-025-67147-z · Cited by 6

Human metabolism and pharmacological profiling of protonitazepyne and metonitazepyne, two highly potent nitazenes: prediction of main metabolite activity based on µ-opioid receptor docking simulations

Berardinelli, D., Taoussi, O., Ovat, D. Y., Pichini, S., Pulver, B., Auwärter, V., Busardò, F. P., Basile, G., Laudadio, E., & Carlier, J. (2026) · Archives of Toxicology · doi:10.1007/s00204-025-04163-4 · Cited by 5

Expanding the clinical and molecular Spectrum of PSMD12-related neurodevelopmental syndrome: an additional patient and review

Palumbo, P., Palumbo, O., Di Muro, E., Pia Leone, M., Castellana, S., Biagini, T., Mazza, T., Leotta, V., Carella, M., & Bukvic, N. (2019) · Archives of Clinical and Medical Case Reports · doi:10.26502/acmcr.96550088 · Cited by 5

Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology

Piccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395

A curated list of targeted optimized promiscuous ketoreductases (TOP-K)

Shanbhag, A. P., Rajagopal, S., Ghatak, A., Katagihallimath, N., Subramanian, R., & Datta, S. (2023) · Biochemical Journal · doi:10.1042/bcj20230051 · Cited by 5

Cryo-EM structure of histidyl-tRNA synthetase-like domain reveals activating crossed helices at the core of GCN2

Solorio-Kirpichyan, K., Fan, X., Golovenko, D., Korostelev, A. A., Yan, N., & Korennykh, A. (2024) · PNAS Nexus · doi:10.1093/pnasnexus/pgae528 · Cited by 5

Nucleosome structural variations in interphase and metaphase chromosomes

Arimura, Y., Shih, R. M., Froom, R., & Funabiki, H. (2020) · doi:10.1101/2020.11.12.380386 · Cited by 5

Discovery and Heterologous Expression of Functional 4- O -Dimethylallyl- l -tyrosine Synthases from Lichen-Forming Fungi

Iacovelli, R., He, S., Sokolova, N., Lokhorst, I., Borg, M., Fodran, P., & Haslinger, K. (2024) · Journal of Natural Products · doi:10.1021/acs.jnatprod.4c00619 · Cited by 5

Cryo-EM structure of the diapause chaperone artemin

Parvate, A. D., Powell, S. M., Brookreson, J. T., Moser, T. H., Novikova, I. V., Zhou, M., & Evans, J. E. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.998562 · Cited by 5

Insulin Docking Within the Open Hemichannel of Connexin 43 May Reduce Risk of Amyotrophic Lateral Sclerosis

LEHRER, S., & RHEINSTEIN, P. H. (2023) · In Vivo · doi:10.21873/invivo.13112 · 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

The Spc105/Kre28 complex promotes mitotic error correction by outer kinetochore recruitment of Ipl1/Sli15

Dudziak, A., Pleuger, R., Schmidt, J., Hamm, F., Tendulkar, S., Jänen, K., Vetter, I. R., Singh, S., Fischböck, J., Herzog, F., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00437-w · Cited by 4

Light-induced structural adaptation of the bundle-shaped phycobilisome from thylakoid-lacking cyanobacterium Gloeobacter violaceus

(2025) · doi:10.1038/s41467-025-60673-w · Cited by 4

THE PALISADE LAYER OF THE POXVIRUS CORE IS COMPOSED OF FLEXIBLE A10-TRIMERS

Liu, J., Corroyer-Dulmont, S., Pražák, V., Khusainov, I., Bahrami, K., Welsch, S., Vasishtan, D., Obarska-Kosińska, A., Thorkelsson, S. R., Grunewald, K., et al. (2023) · doi:10.1101/2023.05.24.542031 · Cited by 4

Disulfiram and disulfiram-loaded poly-[lactide-co-glycolic acid] nanoparticles modulate metastatic markers and proteasomal activity in hepatocarcinoma Hep3b cell line

Hoda, M., Cavuturu, B. M., Iqbal, S., Shakya, G., & Rajagopalan, R. (2017) · European Journal of Nanomedicine · doi:10.1515/ejnm-2017-0013 · Cited by 3

Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus

Burmeister, W. P., Boutin, L., Balestra, A. C., Gröger, H., Ballandras-Colas, A., Hutin, S., Kraft, C., Grimm, C., Böttcher, B., Fischer, U., et al. (2024) · PLOS Pathogens · doi:10.1371/journal.ppat.1011652 · Cited by 3

Discovery of antimicrobial peptides clostrisin and cellulosin from Clostridium: insights into their structures, co-localized biosynthetic gene clusters, and antibiotic activity

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